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USP19

Gene
Usp19
Protein
Ubiquitin carboxyl-terminal hydrolase 19
Organism
Mus musculus
Length
1360 amino acids
Function
Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates (By similarity). Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity). Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis.
Mass
150.549 kDa
Sequence
MSAGASATGPRRGPPGLEEATSKKKQKDRANLESKDGDARRVSLPRKEPTKDELLLDWRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGRQWGGVFFAEIQSSCTKVQARKGGLLQLVLPKKVPLLTWPSLLKPLGTQELVPGLQCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGAGPGTQAGPSAKRAVHLRRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEKLCAPPMNTQTSLLSSEKSLALLTVEKTVSPRNDPVAPVMVQDRDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVAPKPDPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIFYFAREPHSKPIKFLVSVSKENSSASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEEEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRVWPPADRGPVPSTSGLSSEMLASGPIEGCPLLAGERVSRPEAAVPGYQHSSESVNTHTPQFFIYKIDASNREQRLEDKGETPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRASHSEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR

Gene
Usp19
Protein
Ubiquitin carboxyl-terminal hydrolase 19
Organism
Rattus norvegicus
Length
1357 amino acids
Function
Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity).
Mass
150.302 kDa
Sequence
MSAGTSATGPRRGPPGLEEATSKKKQKDRANQESKDGDPRRVSMPRKEPTKDELLLDWRQSSDKVVVKLRVGTGPICLEEVDAAFTDTDCVVRLPDGRQWGGVFFAKIQSSCTKVQTRKGGLLQLALPKKVPLLTWPSLLKKPLGTQELVPGLRCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGASPGAQAGPSAKRAVHLCRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEQLHVPPVNPQTSLLGSEKNLALLTVEKTVSPRSDSVSPVMIRNRDPEKDDHFKEEMAVGADPAALADEPESMVNLAFVKNDSYEKGPDSVVVHVYVKESRRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRVGGAKVAVPTGPTPLDSTPPGGGPLPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVTPKPEPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIYYFAREPHSKPIKFLVSVSKENSSASEVLESLSQSVHVKPESLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRMWPPADRGPVPSTSGISSEMLASGPMEGCSLLAGERVSRPEAAVPGYQHSRESVSAHTPQFFIYKIDASSREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPSDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAAHAEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTSDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR

Gene
USP19
Protein
Ubiquitin carboxyl-terminal hydrolase 19
Organism
Homo sapiens
Length
1318 amino acids
Function
Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains.
Similarity
Belongs to the peptidase C19 family.
Mass
145.651 kDa
Sequence
MSGGASATGPRRGPPGLEDTTSKKKQKDRANQESKDGDPRKETGSRYVAQAGLEPLASGDPSASASHAAGITGSRHRTRLFFPSSSGSASTPQEEQTKEGACEDPHDLLATPTPELLLDWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQWGGVFYAEIKSSCAKVQTRKGSLLHLTLPKKVPMLTWPSLLVEADEQLCIPPLNSQTCLLGSEENLAPLAGEKAVPPGNDPVSPAMVRSRNPGKDDCAKEEMAVAADAATLVDEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTTFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPAARVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVTPKPETHLASPKPTCMVPPMPHSPVSGDSVEEEEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPVFYFAREPHSKPIKFLVSVSKENSTASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDTVSPSDTLLCFELLSSELAKERVVVLEVQQRPQVPSVPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTGSLEAGDSERDPIQPPELQLVTPMAEGDTGLPRVWAAPDRGPVPSTSGISSEMLASGPIEVGSLPAGERVSRPEAAVPGYQHPSEAMNAHTPQFFIYKIDSSNREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAGHSEHHPDLGPAAEAAASQASRIWQELEAEEEPVPEGSGPLGPWGPQDWVGPLPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR