protein_name
stringlengths 7
11
| species
stringclasses 238
values | sequence
stringlengths 2
34.4k
| annotation
stringlengths 6
11.5k
⌀ |
|---|---|---|---|
UBXN7_HUMAN | Homo sapiens | MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN | Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
Subcellular locations: Nucleus |
UBXN7_PONAB | Pongo abelii | MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN | Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates (By similarity).
Subcellular locations: Nucleus |
UBXN8_HUMAN | Homo sapiens | MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN | Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction.
Subcellular locations: Endoplasmic reticulum membrane
Expressed abundantly in ovary and testis, and weakly in all other tissues tested. |
UDB10_HUMAN | Homo sapiens | MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD | UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane |
UDB11_HUMAN | Homo sapiens | MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSASILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELYDIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTIERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVLGRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTMSSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAAHDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD | UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane
Widely expressed. |
UDB15_HUMAN | Homo sapiens | MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSASTLVNASKSSAIKLEVYPTSLTKNYLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEYYDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYTFEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile ( ). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds . Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens) ( ). Displays glucuronidation activity toward several classes of xenobiotic substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4-hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins) . Catalyzes the glucuronidation of monoterpenoid alcohols such as borneol, menthol and isomenthol, a class of natural compounds used in essential oils (By similarity).
Subcellular locations: Endoplasmic reticulum membrane
Expressed in many tissues. Present in liver, prostate and testis. |
UDB17_HUMAN | Homo sapiens | MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile ( ). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol) ( ).
Subcellular locations: Endoplasmic reticulum membrane
Expressed in various tissues including the liver, kidney, testis, uterus, placenta, mammary gland, adrenal gland, skin and prostate. |
UDB18_MACFA | Macaca fascicularis | MSVKWTSVILLIQLSFYFSSGSCGKVLVWAAEYSHWMNMKTILEELVQRGHEVTVLASSASILFDPNNSSALKIEVFPTSLTKTEFENIIRQQIKRWSELPKDTFWLYFSQMQEIMWKFGDITRNFCKDVVSNKKLMKKLQKSRFDVVFADAIFPCSELLAELLNTPLVYSLRFTPGYNFEKHCGGFLFPPSYVPVVMSELSDHMTFMERVKNMIYMLYFDFCFQIYAMKKWDQFYSEVLGRPTTLSETMGKADIWLIRNSWNFQFPHPLLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVTNMKEERANVIASALAQIPQKVLWRFDGKKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGSNGIYEAIYHGVPMVGIPLFADQPDNIAHMKAKGAAVRLDFDTMSSTDLVNALKTVINDPLYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWFQYHSLDVIGFLLACVATVIFIIMKCCLFCFWKFARKGKKGKSD | UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward 3-hydroxyandrogens. It is principally active on C19 steroids having a hydroxyl group at position 3-alpha of the steroid molecule and also active on planar phenols and bile acids.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane
Expressed in liver, prostate, kidney, testis, adrenal, bile duct, bladder, colon, small intestine, cerebellum and pancreas. |
UDB19_MACFA | Macaca fascicularis | MSMKWTSALLLIQLSCYLSFGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLAYSTSILPDPNNPSPLKFEICPTSLTETEFQDSVTQLVKRWSDIRKDTFWPHFLHVQEMMWTYGDMIRKFCKDVVSNKKLMKKLQESRFDVVLADAISPCGELLAELLKIPFVYSLRFSPGYALEKHGGGFLFPPSYVPVTMSELRDQMTFMERVQNMIYMVYFDFWFQVWDVKNWDQFYSKVLGRPTTLFEIMAKAEIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSGDNGVVVFSLGSMVSNMSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTQLYKWLPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVRLDFDTMSSTDLLNALKTVINDPIYKENAMKLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLACVATVIFIITKCLFCVWKFVRTRKKGKRD | UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward several classes of xenobiotic substrates: eugenol, 4-methyllumbelliferone, p-nitrophenol, 1-naphthol, p,p'-biphenol, naringenin and o,o'-biphenol. Active also on 3a-hydroxy and 17b-hydroxy positions of steroids.
Contributes to the formation of androgen glucuronide in extrahepatic steroid target tissues such as the prostate.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane
Expressed in liver, ovary, prostate, colon, kidney, pancreas, brain, cerebellum, mammary gland and epididymis. Not expressed in small intestine, spleen, bladder, adrenal gland and testis. |
UDB20_MACFA | Macaca fascicularis | MSLKWTSVFLLLQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVRRRHEVTVLTSSASTFVNDSKSSAIKFEVYPTSLTKNDMEDSLMKLLDIWTYSISNSTFLSYFSKLQELCWEYYYYSEKLCKDAVLNKKLMTKLKETKFDVILADALNPCGELLAELFNIPFVYSLRFTVGYTFEKNGGGFLFPPSYVPVVMSELSDQMTFTERIKNMIHKLYFDFWFQIHDIKKWDQFYSEVLGRPTTLFETMRKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMISNMSEERANMIASALAQIPQKVLWKFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIVHMKVKGAALSVDIRTMSSRDLLNALKSVINEPIYKENAMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVAAVIFIITKCCLFCFRKLAKTGKKKKWD | UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity with androgens, such as testosterone, dihydrotestosterone (DHT) and 3-alpha-diol. It is also active on catecholoestrogens including 1,3,5,10-oestratriene-3,4-diol-17-one.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane |
UDB23_MACFA | Macaca fascicularis | MSVKWTSVILLIQLSFYFSSGSCGKVLVWAAEYSHWMNMKTILEELVQRGHEVTALASSASILFDPNNSSALKIEVFPTSLPKPEFENIVTQEIKRWIELPKDTFWLYFSQMQEIMWKFGDIFRNFCKDVVSNKKLMKKLQESRFDVVFADPIFPCSELLAELFNIPLVYSLRFTPGYVFEKHCGGFLFPPSYVPVVMSELSDQMTFMERVKNMIYMLYFDFCFQIYDMKKWDQFYTEVLGRHTTLSEIMGKADIWLIRNSWNFQFPHPLLPNVDFIGGLLCKPAKPLPKEMEEFVQSSGENGVVVFTLGSMITNMKEERANVIASALAQIPQKVLWRFDGNKPDTLGVNTRLYKWIPQNDLLGHPKTKAFITHGGANGIYEAIYHGVPMVGIPLFADQPDNIAHMKTRGAAVQLDFDTMSSTDLVNALKTVINDPLYKENVMKLSRIQRDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWFQYHSFDVIGFLLACVATVIFIIMKCCLFCFWKFARKGKKGKSD | UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity on 6 steroids and the bile acid, hyodeoxycholic acid. May potentially play an important role in estrogen and androgen catabolism in peripheral steroid target tissues.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane
Expressed in several tissues, including the prostate, mammary gland, epididymis, testis and ovary. |
UDB28_HUMAN | Homo sapiens | MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSASILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFHDIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTIERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVLGRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTMSSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAARDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile . Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds . Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (androsterone, 3alpha-androstanediol) and estrogens (estradiol, estrone) . Catalyzes the glucuronidation of bile acid substrates, which are natural detergents for dietary lipids absorption . Displays glucuronidation activity toward the phenolic compounds eugenol .
Lack UDP-glucuronosyltransferase (UGT) activity.
Subcellular locations: Endoplasmic reticulum membrane, Cytoplasm, Perinuclear region
Expressed in the liver, breast and kidney. |
UDB30_MACFA | Macaca fascicularis | MSMKWTSALLLIQLSCYLSSGNCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLAYSPSILPGPNNPSALKFEICPTSLTETEFEDSVTQLVKRWSDIPKDTFWPHFLQVQEMMWTYGDMIRKFCKDVVSNKKLMKKLQESRFDVVLADAISPCGELLAELLKIPFVYSLRFSPGYAIEKHGGGFLFPPSYVPVVMSEFSDQMTFMERVKNMIYMVYFDFWFQAWDTKKWDQFYSEVLGRPTTLFETMAKAEIWLIRNYWDFQFPHPLLPHVELVGGLHCKPAKPLPKEMEGFVQSSGDNGVVVFSLGSMVSNMSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTQLYKWLPQNDLLGHPKTRAFITHGGANAIYEAIYHGIPMVGVPLFADQLDNIAHMKAKGARVSLDFNTMSSTDLLHALKTVINDPFYKENAMKLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAYDLTWFQYHSLDVIGFLLACVATVIFIITKCLFCVLKFVRTGKKGKRD | UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity on testosterone, dihydrotestosterone, 5-alpha-androstane-3-alpha,17-beta-diol, androsterone, oestradiol, tetrahydroaldosterone and tetrahydrocortisone. This enzyme is essential to inactivation of several steroids.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane
Expressed in several tissues, including prostate, testis, mammary gland, kidney, adrenals and intestine. |
UDB33_MACMU | Macaca mulatta | MSVKWTSIILLIQLSFYFSSGSCGKVLVWAAEYSHWMNMKTILEELVQRGHEVTVLASSASILFDPNNSSALKIEVFPTSLTKTEFENIIRQQIKRWSELPKDTFWLYFSQIQEIMWRFGDISIKFCKDVVSNKKLMKKLQESRFDVVLADPIFPCSELLAELFNIPLVYSLRFTPGYVFEKHCGGFLFPPSYVPVVMSELSDQMTFMERVKNMIYVLYFDFCFQLYDMKKWDQFYSEVLGRHTTLSEIMGKADIWLIRNSWNFQFPHPLLPNVDFIGGLLCKPAKPLPKEMEEFVQSSGENGVVVFTLGSMITNMKEERANVIASALAQIPQKVLWRFDGNKPDTLGVNTRLYKWIPQNDLLGHPKTKAFITHGGANGIYEAIYHGVPMVGIPLFADQPDNIAHMKTRGAAVQLDFDTMSSTDLANALKTVINDPLYKENVMKLSRIQRDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWFQYHSLDVIGFLLACVATVIFIIMKCCLFCFWKFTRKGKKGKSD | UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity on estriol and does not catalyze the glucuronidation of beta-estradiol. Capable of conjugating 4-hydroxyestrone, androsterone, diclofenac, and hyodeoxycholic acid.
Subcellular locations: Microsome membrane, Endoplasmic reticulum membrane |
UL17C_HUMAN | Homo sapiens | MEEDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSNRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKMLTLLTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQPNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLKLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ | Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection.
Subcellular locations: Nucleus, Endoplasmic reticulum |
UMAD1_HUMAN | Homo sapiens | MFHFFRKPPESKKPSVPETEADGFVLLGDTTDEQRMTARGKTSDIEANQPLETNKENSSSVTVSDPEMENKAGQTLENSSLMAELLSDVPFTLAPHVLAVQGTITDLPDHLLSYDGSENLSRFWYDFTLENSVLCDS | null |
UMAS1_HUMAN | Homo sapiens | MAWGLPCHQNTAGANPHLFLGCYSTSSLQGLEYGGQRGDAHGKPGVLHGELEPHDHTSRLERHDLHSQLPTSVQVRHHWWEGALDLAKKRQQQTSINVFTTIKQGSRCDRWMVLGAISLLYNQEEAPDDRPLRARREVRSQHLSWAFPGTAGPGLVCAGDSQ | null |
UST_HUMAN | Homo sapiens | MKKKQQHPGGGADPWPHGAPMGGAPPGLGSWKRRVPLLPFLRFSLRDYGFCMATLLVFCLGSLLYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVNRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVKKTVPSPEAVQILYQRMRYEYEFYHYVKEQFHLLKRKFGLKSHVSKPPLRPHFFIPTPLETEEPIDDEEQDDEKWLEDIYKR | Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.
Subcellular locations: Golgi apparatus membrane
Widely expressed. |
UTS2B_HUMAN | Homo sapiens | MNKILSSTVCFGLLTLLSVLSFLQSVHGRPYLTQGNEIFPDKKYTNREELLLALLNKNFDFQRPFNTDLALPNKLEELNQLEKLKEQLVEEKDSETSYAVDGLFSSHPSKRACFWKYCV | Potent vasoconstrictor.
Subcellular locations: Secreted |
UTS2_HUMAN | Homo sapiens | MYKLASCCLLFIGFLNPLLSLPLLDSREISFQLSAPHEDARLTPEELERASLLQILPEMLGAERGDILRKADSSTNIFNPRGNLRKFQDFSGQDPNILLSHLLARIWKPYKKRETPDCFWKYCV | Highly potent vasoconstrictor.
Subcellular locations: Secreted
Brain specific. |
UTS2_MACMU | Macaca mulatta | MYKLASCCLLFIGFLNPLFSLPLLDSGEVSLQLSAPHEDAPLTSEELERASLLQILPEMLLGAERGDSLRKADSSTNIFNPRGNLRKFQDFSGQDPDILLSHLLARIRKPYKKRETPDCFWKYCV | Highly potent vasoconstrictor.
Subcellular locations: Secreted |
UTY_HUMAN | Homo sapiens | MKSCAVSLTTAAVAFGDEAKKMAEGKASRESEEESVSLTVEEREALGGMDSRLFGFVRLHEDGARTKTLLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKRCSNTSTLAARIKFLQNGSDNWNGGQSLSHHPVQQVYSLCLTPQKLQHLEQLRANRDNLNPAQKHQLEQLESQFVLMQQMRHKEVAQVRTTGIHNGAITDSSLPTNSVSNRQPHGALTRVSSVSQPGVRPACVEKLLSSGAFSAGCIPCGTSKILGSTDTILLGSNCIAGSESNGNVPYLQQNTHTLPHNHTDLNSSTEEPWRKQLSNSAQGLHKSQSSCLSGPNEEQPLFSTGSAQYHQATSTGIKKANEHLTLPSNSVPQGDADSHLSCHTATSGGQQGIMFTKESKPSKNRSLVPETSRHTGDTSNGCADVKGLSNHVHQLIADAVSSPNHGDSPNLLIADNPQLSALLIGKANGNVGTGTCDKVNNIHPAVHTKTDHSVASSPSSAISTATPSPKSTEQRSINSVTSLNSPHSGLHTVNGEGLGKSQSSTKVDLPLASHRSTSQILPSMSVSICPSSTEVLKACRNPGKNGLSNSCILLDKCPPPRPPTSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWRCESNRSHTTIAKYAQYQASSFQESLREENEKRTQHKDHSDNESTSSENSGRRRKGPFKTIKFGTNIDLSDNKKWKLQLHELTKLPAFARVVSAGNLLTHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNNLNFLMSSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNVGPLTACQYKLAVERYEWNKLKSVKSPVPMVHLSWNMARNIKVSDPKLFEMIKYCLLKILKQYQTLREALVAAGKEVIWHGRTNDEPAHYCSICEVEVFNLLFVTNESNTQKTYIVHCHDCARKTSKSLENFVVLEQYKMEDLIQVYDQFTLALSLSSSS | Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity.
Subcellular locations: Nucleus |
UTY_PANTR | Pan troglodytes | MKSCGVSLTTAAVAFGDEAKKMAAGKASREGEEEPLSLTVEEREALGDMDSRLFGFVRLHEDGARTKTLLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSSAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIPYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFVSYRQSIDRSEASADTWCSIGVLYQQQNQPIDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKRCSNTSTLAARIKFLQNGSDNWNGGQSLSHHPVQQVYSLCLTPQKLQHLEQLRANRDNLNPAQKHQLEQLESQFVLMQQMRHKEVAQVRTTGIHNGAIADSSLPTNSVSNRQPHAALTRVSSVSQPGVRPACVEKLLSNGAFSAGCIPCGTSKILGSTDTILLGSNCIAGSESNGNVPYLQQNTHTLPHSHTDLNSSTEEPWRKQLSNSTQGLHKSQSSCLSGPNEEQPLFSTGSAQYHQATSTGIKKSNEHLTLPSNSVPQGDADSHLSSHTATSGGQQGIMFTKESKPSKNRSLVPETSRHTGDPSNGCADVKGLSNHVHQLIADAVSSPNHGDSPNLLIADNPQLSALLIGKANGNVGTGTCDKVNNIHPAVHTKTDHSVASSPSSAISTATPSPKSTEQRSINSVTSLNSPHSGLHTVNGEGLGNSQSSTKVDLPLVSHRSTSQIIPSMSVSICPSSTEVLKACRNPGKNGLSNSCILLDKCPPPRPPTSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHIVEVRTQLLQPADENWDPTGTKKIWRCESNRSHTTIAKYAQYQASSFQESLRAGMQWCDLSSLQPPPPGFKRFSHLSLPNSWNYRHLPSCPTNFCIFVETGFHHVGQAHLELLTSGGLLASASQSAGITGVSHHAR | Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity.
Subcellular locations: Nucleus |
VATC1_HUMAN | Homo sapiens | MTEFWLISAPGEKTCQQTWEKLHAATSKNNNLAVTSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLANGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFRKAVDDFRHKARENKFIVRDFQYNEEEMKADKEEMNRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHVKALRVFVESVLRYGLPVNFQAMLLQPNKKTLKKLREVLHELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular locations: Cytoplasmic vesicle, Secretory vesicle, Synaptic vesicle membrane, Cytoplasmic vesicle, Clathrin-coated vesicle membrane
Ubiquitous. |
VATC1_MACFA | Macaca fascicularis | MTEFWLISAPGEKTCQQTWEKLHAATSKNNNLAVTSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLANGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFRKAVDDFRHKARENKFIVRDFQYNEEEMKADKEEMNRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHVKALRVFVESVLRYGLPVNFQAMLLQPNKKTLKKLREVLHELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular locations: Cytoplasmic vesicle, Secretory vesicle, Synaptic vesicle membrane, Cytoplasmic vesicle, Clathrin-coated vesicle membrane |
VATC1_PONAB | Pongo abelii | MTEFWLISAPGEKTCQQTWEKLHAATSKNNNLAVTSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLANGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFRKAVDDFRHKARENKFIVRDFQYNEEEMKADKEEMNRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHVKALRVFVESVLRYGLPVNFQAMLLQPNKKTLKKLREVLHELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular locations: Cytoplasmic vesicle, Secretory vesicle, Synaptic vesicle membrane, Cytoplasmic vesicle, Clathrin-coated vesicle membrane |
VBPC1_HUMAN | Homo sapiens | MEEVIQAGLAQWSRQKGLALPWDRTRGHPDVPWRNLTSSPTRPLAQPAGSCMPAEPSPAAHYHQLHVHLQLLPSDLSERPGLRLAPLALVEVGMTLPVPQTPLPHVTQQQKLAPGRQLCPW | null |
VENTX_HUMAN | Homo sapiens | MRLSSSPPRGPQQLSSFGSVDWLSQSSCSGPTHTPRPADFSLGSLPGPGQTSGAREPPQAVSIKEAAGSSNLPAPERTMAGLSKEPNTLRAPRVRTAFTMEQVRTLEGVFQHHQYLSPLERKRLAREMQLSEVQIKTWFQNRRMKHKRQMQDPQLHSPFSGSLHAPPAFYSTSSGLANGLQLLCPWAPLSGPQALMLPPGSFWGLCQVAQEALASAGASCCGQPLASHPPTPGRPSLGPALSTGPRGLCAMPQTGDAF | May be involved in ventralization.
Subcellular locations: Nucleus
Expressed in bone marrow of patients recovering from chemotherapy. Also expressed in an erythroleukemia cell line. |
VIAAT_HUMAN | Homo sapiens | MATLLRSKLSNVATSVSNKSQAKMSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKAEGEPCGDEGAEAPVEGDIHYQRGSGAPLPPSGSKDQVGGGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNIFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYSGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED | Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals. The transport is equally dependent on the chemical and electrical components of the proton gradient (By similarity). May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (By similarity).
Subcellular locations: Cytoplasmic vesicle membrane, Presynapse
Presents in glycine-, GABA- or GABA- and glycine-containing boutons.
Retina. Expressed throughout the horizontal cells or more specifically at the terminals. |
VIAAT_MACFA | Macaca fascicularis | MATLLRSKLSNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKAEGEPCGDEGAEPPVEGDIHYQRGSGAPLPPSGSKDQVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNIFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED | Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals. The transport is equally dependent on the chemical and electrical components of the proton gradient (By similarity). May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (By similarity).
Subcellular locations: Cytoplasmic vesicle membrane, Presynapse
Presents in glycine-, GABA- or GABA- and glycine-containing boutons. |
VISL1_MACFA | Macaca fascicularis | MGKQNSKLAPEVMEDLVKSTEFNEHELKQWYKGFLKDCPSGRLNLEEFQQLYVKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEIIEAIYKMVGTVIMMKMNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPSIVLLLQCDIQK | Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner. |
VISL1_PONAB | Pongo abelii | MGKQNSKLAPEVMEDLVKSTEFNEHELKQWYKGFLKDCPSGRLNLEEFQQLYVKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEIIEAIYKMVGTVIMMKMNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPSIVLLLQCDIQK | Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner. |
VISTA_HUMAN | Homo sapiens | MGVPTALEAGSWRWGSLLFALFLAASLGPVAAFKVATPYSLYVCPEGQNVTLTCRLLGPVDKGHDVTFYKTWYRSSRGEVQTCSERRPIRNLTFQDLHLHHGGHQAANTSHDLAQRHGLESASDHHGNFSITMRNLTLLDSGLYCCLVVEIRHHHSEHRVHGAMELQVQTGKDAPSNCVVYPSSSQDSENITAAALATGACIVGILCLPLILLLVYKQRQAASNRRAQELVRMDSNIQGIENPGFEASPPAQGIPEAKVRHPLSYVAQRQPSESGRHLLSEPSTPLSPPGPGDVFFPSLDPVPDSPNFEVI | Immunoregulatory receptor which inhibits the T-cell response . May promote differentiation of embryonic stem cells, by inhibiting BMP4 signaling (By similarity). May stimulate MMP14-mediated MMP2 activation .
Subcellular locations: Cell membrane
Expressed in spleen. Detected on a number of myeloid cells including CD11b monocytes, CD66b+ neutrophils, at low levels on CD4+ and CD8+ T-cells, and in a subset of NK cells. Not detected on B cells (at protein level). Expressed at high levels in placenta, spleen, plasma blood leukocytes, and lung. Expressed at moderate levels in lymph node, bone marrow, fat, uterus, and trachea. Has low expression levels in other tissues. |
VMO1_HUMAN | Homo sapiens | MERGAGAKLLPLLLLLRATGFTCAQTDGRNGYTAVIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIPGDDTALNGIRLHCARGNVLGNTHVVESQSGSWGEWSEPLWCRGGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWSDHCPKGACGLQTKIQGPRGLGDDTALNDARLFCCRS | Subcellular locations: Secreted |
VP33A_HUMAN | Homo sapiens | MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF | Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations ( , ). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39 . The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG .
Subcellular locations: Cytoplasmic vesicle, Late endosome membrane, Lysosome membrane, Early endosome, Cytoplasmic vesicle, Autophagosome, Cytoplasmic vesicle, Clathrin-coated vesicle |
VP33B_HUMAN | Homo sapiens | MAFPHRPDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKPALSSNEQLCFLVRPRIKNMRYIASLVNADKLAGRTRKYKVIFSPQKFYACEMVLEEEGIYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCAKMAYELWRNLEEEEDGETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFNEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQAPGDTLTAVESKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFGGAYVPLSCRIIEQVLERRSWQGLDEVVRLLNCSDFAFTDMTKEDKASSESLRLILVVFLGGCTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKA | May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Required for proper trafficking and targeting of the collagen-modifying enzyme lysyl hydroxylase 3 (LH3) to intracellular collagen . Mediates phagolysosomal fusion in macrophages . Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity . Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity).
Subcellular locations: Late endosome membrane, Lysosome membrane, Early endosome, Cytoplasmic vesicle, Clathrin-coated vesicle, Recycling endosome
Colocalizes in clusters with VIPAS39 at cytoplasmic organelles (, ). Colocalizes with RAB11A and VIPAS39 on recycling endosomes . Colocalizes with AP-3, clathrin, Rab5 and Rab7b . Colocalizes with M.tuberculosis PtpA in the cytosol of tuberculosis-infected macrophages and associates with phagosomes .
Ubiquitous; highly expressed in testis and low expression in the lung. |
VP9D1_HUMAN | Homo sapiens | MAAAAGDGTVKPLQSAMKLANGAIELDTGNRPREAYTEYLRSIHYISQVLLEEVETTKEAGETVPPDTSKMLKLAQQCLERAQSTAAKLGKTRLKPTMPAAAPIPQPAGRHRRVYSDEGGKLSPFLPPEIFQKLQGAESQSCKKELTPLEEASLQNQKLKAAYEARMARLDPSQAMQKTSLTLSLQRQMMENLVIAKAREETLQRKMEERRLRLQEAANRRFCSQVALTPEEREQRALYAAILEYEQDHDWPKHWKAKLKRNPGDLSLVTSLVSHLLSLPDHPIAQLLRRLQCSVYSALYPAVSRAAAPAPGCCPPTPNPGSRRLRPSQSLHCMLSPPEPSAAPRPQDSPPTPPLQPGPVGSPSPLGDTASGLPDKDSSFEDLEQFLGTSERQGRGRGVQPEPQLQQLKTAVEEIHNAVDRLLSLTLLAFEGLNTAASKDRCLACIEEPFFSPLWPLLLALYRSVHRAREAALSRSMELYRNAPPTAIGIPTKLLPQNPEAKGATGYPYCAAAQELGLLVLESCPQKKLECIVRTLRIICVCAEDYCPTPEATPQAGPPPIAAAAIGADDLLPILSFVVLRSGLPQLVSECAALEEFIHEGYLIGEEGYCLTSLQSALSYVELLPRGGLAK | Ubiquitous. |
VPS4B_PONAB | Pongo abelii | MSSTSPNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAQCTEYLDRAEKLKEYLKNKEKKAQKPVKEGQPSPADEKGNDSDGEGESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMRGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEPHARAAMFKLHLGTTQNSLTEADFRELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNHLVDDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMSDMLRSLSNTKPTVNEHDLLKLKKFTEDFGQEG | Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
(Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (lentiviruses).
Subcellular locations: Late endosome membrane
Membrane-associated in the prevacuolar endosomal compartment. |
VPS50_HUMAN | Homo sapiens | MQKIKSLMTRQGLKSPQESLSDLGAIESLRVPGKEEFRELREQPSDPQAEQELINSIEQVYFSVDSFDIVKYELEKLPPVLNLQELEAYRDKLKQQQAAVSKKVADLILEKQPAYVKELERVTSLQTGLQLAAVICTNGRRHLNIAKEGFTQASLGLLANQRKRQLLIGLLKSLRTIKTLQRTDVRLSEMLEEEDYPGAIQLCLECQKAASTFKHYSCISELNSKLQDTLEQIEEQLDVALSKICKNFDINHYTKVQQAYRLLGKTQTAMDQLHMHFTQAIHNTVFQVVLGYVELCAGNTDTKFQKLQYKDLCTHVTPDSYIPCLADLCKALWEVMLSYYRTMEWHEKHDNEDTASASEGSNMIGTEETNFDRGYIKKKLEHGLTRIWQDVQLKVKTYLLGTDLSIFKYDDFIFVLDIISRLMQVGEEFCGSKSEVLQESIRKQSVNYFKNYHRTRLDELRMFLENETWELCPVKSNFSILQLHEFKFMEQSRSPSVSPSKQPVSTSSKTVTLFEQYCSGGNPFEIQANHKDEETEDVLASNGYESDEQEKSAYQEYDSDSDVPEELKRDYVDEQTGDGPVKSVSRETLKSRKKSDYSLNKVNAPILTNTTLNVIRLVGKYMQMMNILKPIAFDVIHFMSQLFDYYLYAIYTFFGRNDSLESTGLGLSSSRLRTTLNRIQESLIDLEVSADPTATLTAAEERKEKVPSPHLSHLVVLTSGDTLYGLAERVVATESLVFLAEQFEFLQPHLDAVMPAVKKPFLQQFYSQTVSTASELRKPIYWIVAGKALDYEQMLLLMANVKWDVKEIMSQHNIYVDALLKEFEQFNRRLNEVSKRVRIPLPVSNILWEHCIRLANRTIVEGYANVKKCSNEGRALMQLDFQQFLMKLEKLTDIRPIPDKEFVETYIKAYYLTENDMERWIKEHREYSTKQLTNLVNVCLGSHINKKARQKLLAAIDDIDRPKR | Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Subcellular locations: Recycling endosome, Membrane
Associates with membranes in an EIPR1-dependent manner.
Ubiquitous, with higher expression in brain and skeletal muscle. |
VPS51_HUMAN | Homo sapiens | MAAAAAAGPSPGSGPGDSPEGPEGEAPERRRKAHGMLKLYYGLSEGEAAGRPAGPDPLDPTDLNGAHFDPEVYLDKLRRECPLAQLMDSETDMVRQIRALDSDMQTLVYENYNKFISATDTIRKMKNDFRKMEDEMDRLATNMAVITDFSARISATLQDRHERITKLAGVHALLRKLQFLFELPSRLTKCVELGAYGQAVRYQGRAQAVLQQYQHLPSFRAIQDDCQVITARLAQQLRQRFREGGSGAPEQAECVELLLALGEPAEELCEEFLAHARGRLEKELRNLEAELGPSPPAPDVLEFTDHGGSGFVGGLCQVAAAYQELFAAQGPAGAEKLAAFARQLGSRYFALVERRLAQEQGGGDNSLLVRALDRFHRRLRAPGALLAAAGLADAATEIVERVARERLGHHLQGLRAAFLGCLTDVRQALAAPRVAGKEGPGLAELLANVASSILSHIKASLAAVHLFTAKEVSFSNKPYFRGEFCSQGVREGLIVGFVHSMCQTAQSFCDSPGEKGGATPPALLLLLSRLCLDYETATISYILTLTDEQFLVQDQFPVTPVSTLCAEARETARRLLTHYVKVQGLVISQMLRKSVETRDWLSTLEPRNVRAVMKRVVEDTTAIDVQVGLLYEEGVRKAQSSDSSKRTFSVYSSSRQQGRYAPSYTPSAPMDTNLLSNIQKLFSERIDVFSPVEFNKVSVLTGIIKISLKTLLECVRLRTFGRFGLQQVQVDCHFLQLYLWRFVADEELVHLLLDEVVASAALRCPDPVPMEPSVVEVICERG | Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN . Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane .
Subcellular locations: Golgi apparatus, Trans-Golgi network, Recycling endosome
Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex . |
VRK1_HUMAN | Homo sapiens | MPRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAKKEWKVGLPIGQGGFGCIYLADMNSSESVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHNGVAPSRRGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPEKNKPGEIAKYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKKRKKEIEESKEPGVEDTEWSNTQTEEAIQTRSRTRKRVQK | Serine/threonine kinase involved in cell cycle, nuclear condensation and transcription regulation ( ). Involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation . Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2 . Phosphorylates KAT5 in response to DNA damage, promoting KAT5 association with chromatin and histone acetyltransferase activity . Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm . Phosphorylates ATF2 which activates its transcriptional activity .
Subcellular locations: Nucleus, Cytoplasm
Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis.
Widely expressed. Highly expressed in fetal liver, testis and thymus. |
VTCN1_HUMAN | Homo sapiens | MASLGQILFWSIISIIIILAGAIALIIGFGISGRHSITVTTVASAGNIGEDGILSCTFEPDIKLSDIVIQWLKEGVLGLVHEFKEGKDELSEQDEMFRGRTAVFADQVIVGNASLRLKNVQLTDAGTYKCYIITSKGKGNANLEYKTGAFSMPEVNVDYNASSETLRCEAPRWFPQPTVVWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTESEIKRRSHLQLLNSKASLCVSSFFAISWALLPLSPYLMLK | Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor-associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation.
Subcellular locations: Cell membrane
Expressed at the cell surface. A soluble form has also been detected.
Overexpressed in breast, ovarian, endometrial, renal cell (RCC) and non-small-cell lung cancers (NSCLC). Expressed on activated T- and B-cells, monocytes and dendritic cells, but not expressed in most normal tissues (at protein level). Widely expressed, including in kidney, liver, lung, ovary, placenta, spleen and testis. |
VTDB_HUMAN | Homo sapiens | MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL | Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Subcellular locations: Secreted
Expressed in the liver. Found in plasma, ascites, cerebrospinal fluid and urine. |
WDR19_HUMAN | Homo sapiens | MKRIFSLLEKTWLGAPIQFAWQKTSGNYLAVTGADYIVKIFDRHGQKRSEINLPGNCVAMDWDKDGDVLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAENLLALGGEDKMITVSNQEGDTIRQTQVRSEPSNMQFFLMKMDDRTSAAESMISVVLGKKTLFFLNLNEPDNPADLEFQQDFGNIVCYNWYGDGRIMIGFSCGHFVVISTHTGELGQEIFQARNHKDNLTSIAVSQTLNKVATCGDNCIKIQDLVDLKDMYVILNLDEENKGLGTLSWTDDGQLLALSTQRGSLHVFLTKLPILGDACSTRIAYLTSLLEVTVANPVEGELPITVSVDVEPNFVAVGLYHLAVGMNNRAWFYVLGENAVKKLKDMEYLGTVASICLHSDYAAALFEGKVQLHLIESEILDAQEERETRLFPAVDDKCRILCHALTSDFLIYGTDTGVVQYFYIEDWQFVNDYRHPVSVKKIFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWENWPMDKGVFIAYDDDKVYTYVFHKDTIQGAKVILAGSTKVPFAHKPLLLYNGELTCQTQSGKVNNIYLSTHGFLSNLKDTGPDELRPMLAQNLMLKRFSDAWEMCRILNDEAAWNELARACLHHMEVEFAIRVYRRIGNVGIVMSLEQIKGIEDYNLLAGHLAMFTNDYNLAQDLYLASSCPIAALEMRRDLQHWDSALQLAKHLAPDQIPFISKEYAIQLEFAGDYVNALAHYEKGITGDNKEHDEACLAGVAQMSIRMGDIRRGVNQALKHPSRVLKRDCGAILENMKQFSEAAQLYEKGLYYDKAASVYIRSKNWAKVGDLLPHVSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWQSVIRIYLDHLNNPEKAVNIVRETQSLDGAKMVARFFLQLGDYGSAIQFLVMSKCNNEAFTLAQQHNKMEIYADIIGSEDTTNEDYQSIALYFEGEKRYLQAGKFFLLCGQYSRALKHFLKCPSSEDNVAIEMAIETVGQAKDELLTNQLIDHLLGENDGMPKDAKYLFRLYMALKQYREAAQTAIIIAREEQSAGNYRNAHDVLFSMYAELKSQKIKIPSEMATNLMILHSYILVKIHVKNGDHMKGARMLIRVANNISKFPSHIVPILTSTVIECHRAGLKNSAFSFAAMLMRPEYRSKIDAKYKKKIEGMVRRPDISEIEEATTPCPFCKFLLPECELLCPGCKNSIPYCIATGRHMLKDDWTVCPHCDFPALYSELKIMLNTESTCPMCSERLNAAQLKKISDCTQYLRTEEEL | As component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in cilia function and/or assembly . Essential for functional IFT-A assembly and ciliary entry of GPCRs . Associates with the BBSome complex to mediate ciliary transport (By similarity).
Subcellular locations: Cell projection, Cilium, Cytoplasm, Cytoskeleton, Cilium basal body, Cell projection, Cilium, Photoreceptor outer segment, Cell projection, Cilium, Flagellum
Localizes to photoreceptor connecting cilia, to the base of motile cilia in brain ependymal cells and to the base of and along primary cilia in kidney cells. Localizes at the sperm neck and flagellum .
Some isoforms are tissue-specific. Highly expressed in the prostate. Lower expression in the cerebellum, pituitary gland, fetal lung, and pancreas. In normal prostate, expressed in both basal and luminal epithelial cells. No expression detected in fibromuscular stromal cells, endothelial cells, or infiltrating lymphocytes. Uniformed expression in prostate adenocarcinoma cells. |
WDR1_HUMAN | Homo sapiens | MPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYTEHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSVSLSGYINYLDRNNPSKPLHVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFAGKGHTNQVSRMTVDESGQLISCSMDDTVRYTSLMLRDYSGQGVVKLDVQPKCVAVGPGGYAVVVCIGQIVLLKDQRKCFSIDNPGYEPEVVAVHPGGDTVAIGGVDGNVRLYSILGTTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETRVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY | Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins ( ). Enhances cofilin-mediated actin severing (By similarity). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions . Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance (By similarity). Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension (By similarity). Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt .
Subcellular locations: Cytoplasm, Cytoplasm, Cytoskeleton, Cell projection, Podosome, Cell junction
Expressed in peripheral blood mononuclear cells (at protein level). |
WDR20_HUMAN | Homo sapiens | MATEGGGKEMNEIKTQFTTREGLYKLLPHSEYSRPNRVPFNSQGSNPVRVSFVNLNDQSGNGDRLCFNVGRELYFYIYKGVRKAADLSKPIDKRIYKGTQPTCHDFNHLTATAESVSLLVGFSAGQVQLIDPIKKETSKLFNEERLIDKSRVTCVKWVPGSESLFLVAHSSGNMYLYNVEHTCGTTAPHYQLLKQGESFAVHTCKSKSTRNPLLKWTVGEGALNEFAFSPDGKFLACVSQDGFLRVFNFDSVELHGTMKSYFGGLLCVCWSPDGKYIVTGGEDDLVTVWSFVDCRVIARGHGHKSWVSVVAFDPYTTSVEEGDPMEFSGSDEDFQDLLHFGRDRANSTQSRLSKRNSTDSRPVSVTYRFGSVGQDTQLCLWDLTEDILFPHQPLSRARTHTNVMNATSPPAGSNGNSVTTPGNSVPPPLPRSNSLPHSAVSNAGSKSSVMDGAIASGVSKFATLSLHDRKERHHEKDHKRNHSMGHISSKSSDKLNLVTKTKTDPAKTLGTPLCPRMEDVPLLEPLICKKIAHERLTVLIFLEDCIVTACQEGFICTWGRPGKVVSFNP | Regulator of deubiquitinating complexes. Activates deubiquitinating activity of complexes containing USP12 (, ). Anchors at the base of the ubiquitin-contacting loop of USP12 and remotely modulates the catalytic center of the enzyme . Regulates shuttling of the USP12 deubiquitinase complex between the plasma membrane, cytoplasm and nucleus .
Subcellular locations: Cytoplasm, Nucleus |
WDR91_HUMAN | Homo sapiens | MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRASSAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDNMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA | Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport . It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome . May play a role in meiosis (By similarity).
Subcellular locations: Early endosome membrane, Late endosome membrane |
WDR91_PONAB | Pongo abelii | MIFHCEVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECRRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQAQSSAKKESFGGQGTKGKDPTSGAKDGKGLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRTSLAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDDMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA | Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May play a role in meiosis.
Subcellular locations: Early endosome membrane, Late endosome membrane |
WDR93_HUMAN | Homo sapiens | MSFPRGSQTQKIKHPIGTRKGPLEVPPPTEKDWPKDDEQDHVLVDPDEELDSLPQPYRMINKLVNLLFDQSWEIIEERNALREAESSQIQPTVYPPLGEIQLNKMPNCMAVSQDYVFIGGAKGFSIYNLYSAKQIYAWEKLKVDVTSIWATDLGNEILIAPVDEMGIIRLFYFYKEGLYLVKAINEVDDTSKQTTCIKMEISQGGDFAAFLLQGAGDIWLDVYKLPKETWLKKLEHPQLTSNPKKKVRQPQLNSLGPISADPLEMDANVSFKGDIKLSLPVYIMKIKPPKPVTGTTFKSPLEVFAKIKDCYGLGSGQNHFIKDSQWEQQAEIFNASYKKYLDREWEEEPLSTATFYFLLPSCLFAMPPEVKGPSGMACVLGIHWTRSHNFFLYSLNRTLKDKADPEGVWPCAAPIAVSQLSCSSSYLVLACEDGVLTLWDLAKGFPLGVAALPQGCFCQSIHFLKYFSVHKGQNMYPEGQVKSQMKCVVLCTDASLHLVEASGTQGPTISVLVERPVKHLDKTICAVAPVPALPGMVLIFSKNGSVCLMDVAKREIICAFAPPGAFPLEVPWKPVFAVSPDHPCFLLRGDYSHETASTDDAGIQYSVFYFNFEACPLLENISKNCTIPQRDLDNMAFPQALPLEKRCERFLQKSYRKLEKNPEKEEEHWARLQRYSLSLQRENFKK | null |
WDR97_HUMAN | Homo sapiens | MEAEVWEAEGYNLVLDSDLYDADGYDVPDPGLLTEKNELTFTEPSQVLPFLTSSQQWQSLTPRARARRLWLLLRTSLHEVVEKEKRAELRAARLTHGLEPLRRLEVAAGLRSVAQDPVGGRFVVLDGAGRLHLHKEDGWAQETLLAPVRLTGLVTVLGPLGAVGRFVGWGPAGLAILRPNLSLLWLSEQGVGRAPGWAPTCCLPVPDLRLLLVAEMNSSLALWQFRSGGRRLVLRGSALHPPPSPTGRLMRLAVAPVPPHHVLRCFAAYGSAVLTFDLHAWTLVDVRRDLHKTTISDLAYCEEVEAMVTASRDSTVKVWEADWQIRMVFVGHTGPVTAMTVLPNTTLVLSASQDGTLRTWDLQAAAQVGEVALGFWGQDKLSRRVGRLLAPVRPGWPVLSLCASSMQLWRVRELYSPLAQLPAKVLHVQVAPALPAPAHQSLPTRLVCACADGSVYLLSAATGRIVSSLLLEPEDCAAAVAYCLPREALWLLTRAGHLVRANAARCPMSVLHRVCPPPPPAPQPCCLHLYSHLTDLEGAFSSWEIVRQHWGELRCSSVACAWKNKNRYLPVVGHTDGTLSVLEWLSSKTVFQTEAHSPGPVVAIASTWNSIVSSGGDLTVKMWRVFPYAEESLSLLRTFSCCYPAVALCALGRRVTAGFEDPDSATYGLVQFGLGDSPRLDHRPQDDPTDHITGLCCCPTLKLYACSSLDCTVRIWTAENRLLRLLQLNGAPQALAFCSNSGDLVLALGSRLCLVSHRLYLPTSYLVKKMCRKAPDVVDDPPLPLMSQESLTSAQLQRLTNLHGAASLSEALSLIHRRRATSQHLVPKEDLDAIVARDRDLQQLRLGLVVPAAQPPPSWQQRQEGFDNYLRLIYGSGLLGMQSGRGSQQWSAGTLRVERETRDVCAVPQAAHCLARAEVSTAAQTVPTALSPQDLGALGQHFSQSPRVTVPIPPTHRRVHSKASQLLARSSLSHYLGISLDLQLQLEQLRGRTTMALDLPSSHLQCRIPLLPKRWDKEPLSSLRGFFPATVQPHKHCLRPICFPGYVPNSAVLQQMWLNAEPGASQDALWLWRPRPSQTQWQRKLLQWMGEKPGEEGEEDKKEEEEEKEDEELDWALASLSPHSNQQLDSWELEDQSAVDWTQEPRRRSCKVARTHPHPWHRHGSLLLDEHYGHLPKFLHFFIYQTWFKKLFPIFSLQAYPEAGTIEGLASLLVALLEKTTWVDRVHILQVLLRLLPNMSSDLQGQLQGLLVHLLNLDQPPSLQDQTQKKFVILALQLLLACSLESRDVVLELMSYFLYSPVHCRPELKKLLHGLGLQDPEGFLFKEMMTWVQGPDLDSKAGLRTCCHQKLEDMIQELQETPSQTSVVSGAPTRASVIPSGTSWSASGIFGRLSQVSEVPLMVVSPAEPHSLAPELQAQRMLAPKRSWGTPQLRLRVLSETLKSFCLEPEARLHPAGPAQLPGEPPPLEETDWSHSQLLDLGPIDALNFFCEQLRAQQRSSLQEKAAHPHPPEPYTVAPVPDMVVPPPREHWYHPILRLQEAKPQRSARSAMRLRGPMRSRLCAGRTLDGPIRTLKLPLPRVEPQPFPLDWPMPPRPLPPRLLQPALQRYFLPADADPDTYS | null |
WDTC1_HUMAN | Homo sapiens | MAKVNITRDLIRRQIKERGALSFERRYHVTDPFIRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMHTGHTANIFSVKFLPHAGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPMWPNTFWSAAEDGLIRQYDLRENSKHSEVLIDLTEYCGQLVEAKCLTVNPQDNNCLAVGASGPFVRLYDIRMIHNHRKSMKQSPSAGVHTFCDRQKPLPDGAAQYYVAGHLPVKLPDYNNRLRVLVATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTFLLPRKCHSSGEVQNGKMSTNGVSNGVSNGLHLHSNGFRLPESRGHVSPQVELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKWDGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFKGKFPEQAHSSACDALGRDITAALFSKNDGEEKKGPGGGAPVRLRSTSRKDSISEDEMVLRERSYDYQFRYCGHCNTTTDIKEANFFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNADPLEVMLLNMGYRITGLSSGGAGASDDEDSSEGQVQCRPS | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. |
WFS1_HUMAN | Homo sapiens | MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIPTHHINALIFFFIVSNLTIDFFAFFIPLVIFYLSFISMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYAHFLLSVFFVIFSFPIASKDCIPCSELAVITGFFTVTSYLSLSTHAEPYTRRALATEVTAGLLSLLPSMPLNWPYLKVLGQTFITVPVGHLVVLNVSVPCLLYVYLLYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLESTGLGLLRASIGYFLFLFALPILVAGLALVGVLQFARWFTSLELTKIAVTVAVCSVPLLLRWWTKASFSVVGMVKSLTRSSMVKLILVWLTAIVLFCWFYVYRSEGMKVYNSTLTWQQYGALCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAESAINMLPFFIGDWMRCLYGEAYPACSPGNTSTAEEELCRLKLLAKHPCHIKKFDRYKFEITVGMPFSSGADGSRSREEDDVTKDIVLRASSEFKSVLLSLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMAQLSPTRRHVKIEHDWRSTVHGAVKFAFDFFFFPFLSAA | Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store . Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism .
Subcellular locations: Endoplasmic reticulum membrane, Cytoplasmic vesicle, Secretory vesicle
Co-localizes with ATP6V1A in the secretory granules in neuroblastoma cell lines.
Highly expressed in heart followed by brain, placenta, lung and pancreas. Weakly expressed in liver, kidney and skeletal muscle. Also expressed in islet and beta-cell insulinoma cell line. |
WHAL1_HUMAN | Homo sapiens | MMILVFWSNYPYEPVCLASHRNNMEASVPKYKKHLPQLGMQKEMEQDVKRFGQAAWATAIPRLEKLKLMLAQETLQLMRAKELCLNHKRAEIQGKMEDLPEQEKNINVVDELAIQFYEIQLELYEVKFEILKNKEILLTTQLDSLERLIKDEI | null |
WHAMM_HUMAN | Homo sapiens | MEDEQPDSLEGWVPVREGLFAEPERHRLRFLVAWNGAEGKFAVTCHDRTAQQRRLREGARLGPEPEPKPEAAVSPSSWAGLLSAAGLRGAHRQLAALWPPLERCFPRLPPELDVGGGGAWGLGLGLWALLWPTRAGPGEAALQELCGQLERYLGAAADGCGGATVRDALFPAEGGAADCESPREFRERALRARWVEADARLRQVIQGHGKANTMVALMNVYQEEDEAYQELVTVATMFFQYLLQPFRAMREVATLCKLDILKSLDEDDLGPRRVVALEKEAEEWTRRAEEAVVSIQDITVNYFKETVKALAGMQKEMEQDAKRFGQAAWATAIPRLEKLQLMLARETLQLMRAKELCLNHKRAEIQGKMEDLPEQEKNTNVVDELEIQFYEIQLELYEVKFEILKNEEILLTTQLDSLKRLIKEKQDEVVYYDPCENPEELKVIDCVVGLQDDKNLEVKELRRQCQQLESKRGRICAKRASLRSRKDQCKENHRFRLQQAEESIRYSRQHHSIQMKRDKIKEEEQKKKEWINQERQKTLQRLRSFKDKRLAQSVRNTSGSEPVAPNLPSDLSQQMCLPASHAVSVIHPSSRKTRGVPLSEAGNVKSPKCQNCHGNIPVQVFVPVGDQTHSKSSEELSLPPPPPPPPPPPPPPPPPPPPLRALSSSSQAATHQNLGFRAPVKDDQPRPLVCESPAERPRDSLESFSCPGSMDEVLASLRHGRAPLRKVEVPAVRPPHASINEHILAAIRQGVKLKKVHPDLGPNPSSKPTSNRRTSDLERSIKAALQRIKRVSADSEEDSDEQDPGQWDG | Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule-binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Involved as a regulator of Golgi positioning and morphology. Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration.
Subcellular locations: Cytoplasm, Endoplasmic reticulum-Golgi intermediate compartment, Cytoplasmic vesicle membrane, Golgi apparatus, Cis-Golgi network
Localized to a perinuclear compartment near the microtubule-organizing center (MTOC). Also detected on tubulo-vesicular structures in the cell periphery that frequently localized along microtubules.
Expressed in brain, lung, heart, colon and kidney (at protein level). |
WNT2B_HUMAN | Homo sapiens | MLRPGGAEEAAQLPLRRASAPVPVPSPAAPDGSRASARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRVMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVMATQDGANFTAARQGYRRATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT | Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a redundant role in embryonic lung development.
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted
Isoform 1 is expressed in adult heart, brain, placenta, lung, prostate, testis, ovary, small intestine and colon. In the adult brain, it is mainly found in the caudate nucleus, subthalamic nucleus and thalamus. Also detected in fetal brain, lung and kidney. Isoform 2 is expressed in fetal brain, fetal lung, fetal kidney, caudate nucleus, testis and cancer cell lines. |
WNT2_AOTNA | Aotus nancymaae | MNSPLRGIWLWLPLLLTWLTPEVSSSWWYMGATGGSARVMCDNVPGLVSSQRQLCHRHPDVMRAIGLGVTEWTSECQYQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSGKDSKGVFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKSVKRFLKQECKCHGVSGSCSLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDRETGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMIKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTSPT | Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as a upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT2_ATEGE | Ateles geoffroyi | MNSPLRGIWLWLPLLLTWLTPEVSSSWWYMGATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAIGLGVTEWTAECQYQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSGKDSKGVFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKSVKRFLKQECKCHGVSGSCSLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDRETGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMIKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTPT | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix |
WNT2_CALJA | Callithrix jacchus | MNSPLRGIWLWLPLLLTWLTPEVSSSWWYMGATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAIGLGVTEWTSECQYQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAVTRACSQGEVKSCSCDPKKMGSGKDSKGVFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKSVKRFLKQECKCHGVSGSCSLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDRETGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMIKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWKSPT | Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as a upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT2_CHLAE | Chlorocebus aethiops | MNAPLGGIWLWLPLLLTWLTPEVNSSWWYMRATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAISQGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSAKDSKGIFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTPT | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix |
WNT2_COLGU | Colobus guereza | MNAPLGGIWLWLPLLLTWLTPEVNSSWWYMRATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAISQGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSAKDSKGIFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTPT | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix |
WNT6_HUMAN | Homo sapiens | MLPPLPSRLGLLLLLLLCPAHVGGLWWAVGSPLVMDPTSICRKARRLAGRQAELCQAEPEVVAELARGARLGVRECQFQFRFRRWNCSSHSKAFGRILQQDIRETAFVFAITAAGASHAVTQACSMGELLQCGCQAPRGRAPPRPSGLPGTPGPPGPAGSPEGSAAWEWGGCGDDVDFGDEKSRLFMDARHKRGRGDIRALVQLHNNEAGRLAVRSHTRTECKCHGLSGSCALRTCWQKLPPFREVGARLLERFHGASRVMGTNDGKALLPAVRTLKPPGRADLLYAADSPDFCAPNRRTGSPGTRGRACNSSAPDLSGCDLLCCGRGHRQESVQLEENCLCRFHWCCVVQCHRCRVRKELSLCL | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. Together with CAV1 may promote chemoresistance of gastric cancer cells to DNA-damaging anthracycline drugs through the activation of the canonical Wnt receptor signaling pathway.
Subcellular locations: Secreted, Extracellular space, Extracellular matrix
Expressed in gastric cancer cell lines and gastric cancer tissues (at protein level). Detected in the apical gland region of the gastric foveolar epithelium (at protein level). |
WNT7A_AOTTR | Aotus trivirgatus | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT7A_CALJA | Callithrix jacchus | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT7A_CHLAE | Chlorocebus aethiops | MNRKARRCLGHLFLSLGMVYLRIGGFSTVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT7A_GORGO | Gorilla gorilla gorilla | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
WNT7A_HUMAN | Homo sapiens | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development . Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation . Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (By similarity). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (By similarity). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (By similarity). Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted
Expression is restricted to placenta, kidney, testis, uterus, fetal lung, and fetal and adult brain. |
WNT7A_MACFA | Macaca fascicularis | MNRKARRCLGHLFLSLGMVYLRIGGFSTVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).
Subcellular locations: Secreted, Extracellular space, Extracellular matrix, Secreted |
XAF1_HUMAN | Homo sapiens | MEGDFSVCRNCKRHVVSANFTLHEAYCLRFLVLCPECEEPVPKETMEEHCKLEHQQVGCTMCQQSMQKSSLEFHKANECQERPVECKFCKLDMQLSKLELHESYCGSRTELCQGCGQFIMHRMLAQHRDVCRSEQAQLGKGERISAPEREIYCHYCNQMIPENKYFHHMGKCCPDSEFKKHFPVGNPEILPSSLPSQAAENQTSTMEKDVRPKTRSINRFPLHSESSSKKAPRSKNKTLDPLLMSEPKPRTSSPRGDKAAYDILRRCSQCGILLPLPILNQHQEKCRWLASSKGKQVRNFS | Seems to function as a negative regulator of members of the IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase activity of BIRC4. Induces cleavage and inactivation of BIRC4 independent of caspase activation. Mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells. May inhibit BIRC4 indirectly by activating the mitochondrial apoptosis pathway. After translocation to mitochondria, promotes translocation of BAX to mitochondria and cytochrome c release from mitochondria. Seems to promote the redistribution of BIRC4 from the cytoplasm to the nucleus, probably independent of BIRC4 inactivation which seems to occur in the cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. Seems to be involved in cellular sensitivity to the proapoptotic actions of TRAIL. May be a tumor suppressor by mediating apoptosis resistance of cancer cells.
Subcellular locations: Cytoplasm, Nucleus, Mitochondrion
Found in the cytoplasm and nucleus of placental syncytiotrophoblasts. Translocates to mitochondria upon TNF-alpha treatment.
Subcellular locations: Nucleus
Subcellular locations: Nucleus
Widely expressed. Expression is frequently down-regulated in cancer cell lines. Isoform 5 is widely expressed. Expressed in placenta (at protein level). |
XAGE1_HUMAN | Homo sapiens | MESPKKKNQQLKVGILHLGSRQKKIRIQLRSQCATWKVICKSCISQTPGINLDLGSGVKVKIIPKEEHCKMPEAGEEQPQV | In normal tissues, highly expressed in testis. Expressed also in many different types of cancers: highly expressed in breast cancer, prostate cancer and many types of lung cancers, including squamous cell carcinoma, small cell carcinoma, non-small cell carcinoma, and adenocarcinoma, as well as in Ewing's cell lines, in some Ewing's sarcoma patient samples, and in one of one alveolar rhabdomyosarcoma patient sample. |
XAGE2_HUMAN | Homo sapiens | MSWRGRSTYRPRPRRSLQPPELIGAMLEPTDEEPKEEKPPTKSRNPTPDQKREDDQGAAEIQVPDLEADLQELCQTKTGDGCEGGTDVKGKILPKAEHFKMPEAGEGKSQV | null |
XAGE3_HUMAN | Homo sapiens | MIWRGRSTYRPRPRRSVPPPELIGPMLEPGDEEPQQEEPPTESRDPAPGQEREEDQGAAETQVPDLEADLQELSQSKTGGECGNGPDDQGKILPKSEQFKMPEGGDRQPQV | null |
XAGE5_HUMAN | Homo sapiens | MSWRGRRYRPRRCLRLAQLVGPMLEPSVPEPQQEEPPTESQDHTPGQKREDDQGAAEIQVPNLEADLQELSQSKTGDECGDSPDVQGKILPKSEQFKMPEGGEGKPQL | null |
XPP1_HUMAN | Homo sapiens | MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH | Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro ( ). Contributes to the degradation of bradykinin .
Subcellular locations: Cytoplasm, Cytosol
Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas. |
XPP2_HUMAN | Homo sapiens | MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV | Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin.
Subcellular locations: Cell membrane
Expressed in kidney, lung, heart, placenta, liver, small intestine and colon. No expression in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary. |
XPP3_HUMAN | Homo sapiens | MPWLLSAPKLVPAVANVRGLSGCMLCSQRRYSLQPVPERRIPNRYLGQPSPFTHPHLLRPGEVTPGLSQVEYALRRHKLMSLIQKEAQGQSGTDQTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCGFQEPDSILVLQSLPGKQLPSHKAILFVPRRDPSRELWDGPRSGTDGAIALTGVDEAYTLEEFQHLLPKMKAETNMVWYDWMRPSHAQLHSDYMQPLTEAKAKSKNKVRGVQQLIQRLRLIKSPAEIERMQIAGKLTSQAFIETMFTSKAPVEEAFLYAKFEFECRARGADILAYPPVVAGGNRSNTLHYVKNNQLIKDGEMVLLDGGCESSCYVSDITRTWPVNGRFTAPQAELYEAVLEIQRDCLALCFPGTSLENIYSMMLTLIGQKLKDLGIMKNIKENNAFKAARKYCPHHVGHYLGMDVHDTPDMPRSLPLQPGMVITIEPGIYIPEDDKDAPEKFRGLGVRIEDDVVVTQDSPLILSADCPKEMNDIEQICSQAS | Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala (, ). Also shows low activity towards peptides with Ala or Ser at the P1 position .
Promotes TNFRSF1B-mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling.
Subcellular locations: Mitochondrion, Cytoplasm
Mainly mitochondrial. Translocates to the cytoplasm following TNFRSF1B activation.
Subcellular locations: Cytoplasm
Isoform 1 and isoform 2 are widely expressed, with isoform 1 being more abundant. |
XPP3_PONAB | Pongo abelii | MPWLLSAPKLVPAVANVRGLSGCMLCSQRRYSLQPVPERRIPNRYLGQPSPFTHPHLLRPGEVTPGLSQVEYALRRHKLMSLIQKEAQGQSGTDQTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCGFQEPDSILVLQSLPGKQLPSHKAILFVPRRDPSRELWDGPRSGTDGAIALTGVDEAYTLEEFQHLLPKMKAETNMVWYDWMRPSHAQLHSDYMQPLTEAKAKSKNKVRGVQQLIQRLRLIKSPAEIERMQIAGKLTSQAFIETMFASKAPVEEGFLYAKFEFECRARGADILAYPPVVAGGNRSNTLHYVKNNQLIKDGEMVLLDGGCESSCYVSDITRTWPVNGRFTAPQAELYEAILEIQRDCLALCFPGTSLENIYSMMLTLIGQKLKDLGIMKNIKENNAFKAARKYCPHHVGHYLGMDVHDTPDMPRSLPLQPGMVITIEPGIYIPEDDKDAPEKFRGLGVRIEDDVVVTQDSPLILSADCPKEMNDIEQICSRAS | Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B-mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling.
Subcellular locations: Mitochondrion, Cytoplasm
Mainly mitochondrial. Translocates to the cytoplasm following TNFRSF1B activation. |
YA037_HUMAN | Homo sapiens | MQDVHTKSIACDGDLLPVLQENSISFQMLSLEMSGSFHSSPALENATITILHVSLLSFFRGIQAPCRGSPLLVTDSPGG | null |
YA043_HUMAN | Homo sapiens | MKGLRVAKAFQPSQGCSRQALGHLSGRGPSPRSEMNSSVGDLGVGGCSLWDDPARFIVVPAAYALALGLGLPANVAALAMFIRSGGRLGQALLLYLFNLALVDEFFTLTLQLWLTYYLGLARRPPATRPGPPTTCPPMRRWSSPRSSACAAAASYAVPGPGRLPAWPGAYGAPRALPAPSPGWRAWPLPAWSTAGQARGWPPPRWPSRPPSCWCSRPT | Subcellular locations: Membrane |
YC006_HUMAN | Homo sapiens | MPVYCKYQFHKTPVHKTKGEPHGTHVYFQDINVIFLGALHPSDLREYLEGPPMVVEVHDRDRKSEECSQKPVLFGEDPLDSYLNFQALISPRETENNPFESQNKMWYPYGIAQVSFADLLLGHKYLNLAVPIHSCEVQPTHCGQDSRRRKVVGLGVPRDGHQHGPMPRGNYLEADSQLKLRVDIAVPLRAGARAADPDLGGSQFGRIIFVFDFKKVSLLHSLLQDITMINAKALGLDSYPVRTLQQILSAFKVRVRVQEQQHLDVLTGFHLLDGKTHLFILEGLADQGLRQLWENHQSWIPRSEHRKYKVLYNSQLLFRSRLYGDLEAILYHVHLFQPTELLLQQAVFFLRDTERRRVFQALARIHDICYNSTTLWDVTVRDLLPSSAMIKDLSQEFGMPLSQEELTDEKLFALPPQPAPNLEDYHSRNSTLTLEIHAHQEPRKRFTYSQDYLSAMVEPLDLKEEEKKAQKKSRQAWLTARGFQVTGLQSDTESSFQDLKLPPIKELNEEWKENSLFANVLEPVLDRDRWSWDRHHVDFDLYKKPPPFLELLPSPAPKPVTVRKKKGNSPIS | null |
YC018_HUMAN | Homo sapiens | MLPVQRRKLDPLLKKYRHHKKATRTKRRRKEKMEAQCSPVPPTPSTPPQSEEDEAVDKKPTLLSAQEDTPDLLHEDRLQYLQEEGSGVMHQECQIQSCELSVAQKPRPSSPAVTSLASPPLCFGSFLSCVCQTFSRSRKQKPPRRKGNNQAEAGGDAEVLRPGPAKPELSLSKTCSHLKLIELSFVFSFIVLSVCHCSS | null |
YD022_HUMAN | Homo sapiens | MCMNTSIHAHTYARTHTHSVFMSSNVTVFQWMRLMRASSRSFTQAIPAGQLLQTACSHLFTTQNTCQNALGNNTRLQHTEKVRLSIGLADFGLPGIARNTFVVPDSISRYCREGSVIGKCCPSRKSALLNKQGSLKKFKITRGETQPGVTISVLELAEIDQRF | null |
YD023_HUMAN | Homo sapiens | MFARLCPVSETFGRLCPVSETFARLCPVSETFARLCPVSETFARLCPVSETFGRLCPVSEMFGRLSPVSETFGRLCPVSETFGRLCPVSEMFARLCPVSETFGRLSPVSEMFGRLCPVSEMFGRLCPVSEMFGRLCPVIT | null |
YDJC_HUMAN | Homo sapiens | MSRPRMRLVVTADDFGYCPRRDEGIVEAFLAGAVTSVSLLVNGAATESAAELARRHSIPTGLHANLSEGRPVGPARRGASSLLGPEGFFLGKMGFREAVAAGDVDLPQVREELEAQLSCFRELLGRAPTHADGHQHVHVLPGVCQVFAEALQAYGVRFTRLPLERGVGGCTWLEAPARAFACAVERDARAAVGPFSRHGLRWTDAFVGLSTCGRHMSAHRVSGALARVLEGTLAGHTLTAELMAHPGYPSVPPTGGCGEGPDAFSCSWERLHELRVLTAPTLRAQLAQDGVQLCALDDLDSKRPGEEVPCEPTLEPFLEPSLL | Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides. |
YJ012_HUMAN | Homo sapiens | MRLCLIPRNTGTPQRVLRPVVWSPPSRKKPVLSPHNSIMFGHLSPVRIPCLRGKFNLQLPSLDDQVIPARLPKTEVSAEEPKEATEVKDQVETQGQEDNKRGPCSNGEAASTSRPLETQGNLTSSWYNPRPLEGNVHLKSLTEKNQTDKAQVHAVSFYSKGHGVASSHSPAGGILPFGKPDPLPTVLPAPVPGCSLWPEKAALKVLGEDHLPSSPGLLMVGEDMQPKDPAALGSSRSSPPRAAGHRSHKRKLSGPPLQLQPTPPLQLRCDRDERPPPAKLPCLSPEALLVGQASQREGRLQHGNMRKNMRVLSRISKFRRLRQLLRRRKKTRQGRRGGSCL | null |
YJ013_HUMAN | Homo sapiens | MQPGGTAGPEEAPMREAEAGPPQVGLSRPTCSLPASSPGPALPPGCVSRPDSGLPTTSLDSAPAQLPAALVDPQLPEAKLPRPSSGLTVASPGSAPALRWHLQAPNGLRSVGSSRPSLGLPAASAGPKRPEVGLSRPSSGLPAAFAGPSRPQVGLELGLEEQQVSLSGPSSILSAASPGAKLPRVSLSRPSSSCLPLASFSPAQPSSWLSAAFPGPAFDFWRPLQAQNLPSSGPLQARPRPRPHSGLSTPS | null |
YJ016_HUMAN | Homo sapiens | MRAVSANYSTGSPAVKSRIELDRIQTIMESMGSKLSPGAQQLINMVRFQQWNCIPIEEQLQLVLGNAGYKQMTGLQCSSALGALDKLSSTPFPFRTGLTSGNVTENLQAYIDKSTQASSGENSTKLDECKIVPQNHSLLENDLKNATSPFLPKKANDNSNIPNSELLPFLQNLCSQVNYLLVGRKAE | null |
YJ018_HUMAN | Homo sapiens | MYNPWQVGASLAPARAGPRPFPTPRARPPDCSGGHAPSGFPALGLRTAQRPRPFSSSPRSASGRLRGPRPVARGPAHSSSPTGLPAYLPPAAALDSQTSAPTVSPVTRPRVVARGKTPRVSLAGLETLSSLLHQQQLFD | null |
YM017_HUMAN | Homo sapiens | MRLCLIPRNTGTPQRVLPPVVWSTPSRKKPVLSARNSMMFGHLSPMRIPHLRGKFNLQLPSLDEQVIPARLPKTEVRAEEPKEATEVKDQVETQEQEDNKRGPCSNGEAASTSRPLETQGNLTSSWYNPRPLEGNVHLKSLTEKNQTDKAQVHAVSFYSKGHGVASSHSPAGGILPFGRPDSLPTVLPAPVPGCSLWPEKAALKVLGKDYLPSSPGLLMVGEDMQPKDPAALGSSRSSPPKAAGHRSHKRKLSGPPLQLQPTPPLQLRWDRDEGPPPAKLPCLSPEALLVGQASQREGHLQQGNMHKNMRVLSRTSKFRRLRQLLRRRKKRRQGRCGGSRL | null |
YN009_HUMAN | Homo sapiens | MGKLRPSRGRGFADVSQQIRVRNRPSWACRRGGPLGTLLANAGPSTVPVTPTAGSCQPSPLSPGGSDPPPPPRAHVSPQEAPLGQVPGAEWLPPTRGLLCKDVSSSPGPSFHLGGPGLPGHAGPCGPRARPAQGLAGRGGNVGEGSESPLGTLPCSVPASQQLLRGRSHLQGSLAALGEARGGGAAFSWGQEGP | null |
YN010_HUMAN | Homo sapiens | MVRPHLLKKKILGRVWWLMPVVLALWEAEVGGSLEVRSLRPAWPTW | Subcellular locations: Secreted |
YS001_HUMAN | Homo sapiens | MEPWWPRGTGANAPWVLVAVPPGLFPSLLGACCTLTSSSWLQPRFWGLGWRVEVGLEGAGGSSQNYQAALPSFFCLAASPASRPAIFGILAAEPPSASPQAPWPKPGCASPHGSHWPSILIC | null |
YS002_HUMAN | Homo sapiens | MAALSRALGPLRTPAPPLWIGLFLVATGSQQSLAQPLPGNTTEATPRSLRASGSLCGPHAKAPYLCEATHEPAAARIRAQVPDTRWSRVGGQRFYSRVLSPLHRGPSGHTEASAQRSHMGKLKEPQPQDHKPGLGAS | Subcellular locations: Secreted |
YS006_HUMAN | Homo sapiens | MCEQLVCIFTYAYLKINLTKALGHHNPSYPVARAQPQTMFPSASECNAFPRVSKVPNRSGAAETALLVRVLPKPLKSQASLLSLPFIHITEQLSTHICVVLFKLFHVCLFTINNMNDCSMDAAERNAEGGLQLE | null |
YS014_HUMAN | Homo sapiens | MPDASLGSLGITWCFLESPLEVSSGRFGLARLLGSQDHGDDPAERGRTATDAWGPSRWGQSPGNGGGYCDASPPSALAPGDRAWALPASPSSGAPASQHCCLEKAGTRTKASPVWGRDGNTWN | null |
YS025_HUMAN | Homo sapiens | METANGEEPPAGPPVSLHGRRLLRVGGACPTPLPVLQRLPPSALHHTLHCVPRRVCVSPLGQVTRIPPVRTVRRAPSGLLPQRRGGPSWWPPSGVARGGPSWWPPSGVVRGGPSSWPPSGVAEPREALGLP | null |
YS039_HUMAN | Homo sapiens | MVPLFITSDSALTYSPLPEPPPTPALGGQRGPPTCQCPDFPYPVPPSEGCPSGRLLLSLHWDWGRGAGGSWSGGAWPGSPGWRLARGPAHGASAESLGPLGKALVTGWEGGWRGGQGGACSPWYFPIPAAL | null |
YT001_HUMAN | Homo sapiens | MESPKCLYSRITVNTAFGTKFSHISFIILFKVFLFPRITISKKTKLVTLSNYLNK | null |
YT009_HUMAN | Homo sapiens | MQLGEHTHPQKNPKSLAGCLLPNPHPQLQLRGKRAAGLLLRRNPWCHPQAPGGSSTWAPSLPPILAPQAYLNFAPPTLVPGGSPGTEAQPVAPANALGSRSKLNLTQPSCLSSGSHLPLPFPAGMCPHPANPTWALRKGAEVPQGPPLSHTRKALCLAASGVGALLLEVPRHPGWGQQSAAGFQQVFQEGAGTHFPSVRVQPGRGKLQGQR | null |
ZA2G_HUMAN | Homo sapiens | MVRMVPVLLSLLLLLGPAVPQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS | Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
Subcellular locations: Secreted
Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver. |
ZACN_HUMAN | Homo sapiens | MMALWSLLHLTFLGFSITLLLVHGQGFQGTAAIWPSLFNVNLSKKVQESIQIPNNGSAPLLVDVRVFVSNVFNVDILRYTMSSMLLLRLSWLDTRLAWNTSAHPRHAITLPWESLWTPRLTILEALWVDWRDQSPQARVDQDGHVKLNLALATETNCNFELLHFPRDHSNCSLSFYALSNTAMELEFQAHVVNEIVSVKREYVVYDLKTQVPPQQLVPCFQVTLRLKNTALKSIIALLVPAEALLLADVCGGLLPLRAIERIGYKVTLLLSYLVLHSSLVQALPSSSSCNPLLIYYFTILLLLLFLSTIETVLLAGLLARGNLGAKSGPSPAPRGEQREHGNPGPHPAEEPSRGVKGSQRSWPETADRIFFLVYVVGVLCTQFVFAGIWMWAACKSDAAPGEAAPHGRRPRL | Zinc-activated ligand-gated ion channel.
Subcellular locations: Cell membrane
Detected in pancreas, brain, liver, placenta, trachea, kidney, spinal cord, stomach and fetal brain. In the adult brain region expression is detected in the hippocampus, striatum, amygdala and thalamus. |
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