UBP19_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBP19_MOUSE
• UniProt AC: Q3UJD6
• Protein Name: Ubiquitin carboxyl-terminal hydrolase 19
• Gene Name: Usp19
• Organism: Mus musculus (Mouse).
• Sequence Length: 1360
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass membrane protein.
• Protein Description: 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..
• Protein Sequence: MSAGASATGPRRGPPGLEEATSKKKQKDRANLESKDGDARRVSLPRKEPTKDELLLDWRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGRQWGGVFFAEIQSSCTKVQARKGGLLQLVLPKKVPLLTWPSLLKPLGTQELVPGLQCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGAGPGTQAGPSAKRAVHLRRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEKLCAPPMNTQTSLLSSEKSLALLTVEKTVSPRNDPVAPVMVQDRDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVAPKPDPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIFYFAREPHSKPIKFLVSVSKENSSASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEEEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRVWPPADRGPVPSTSGLSSEMLASGPIEGCPLLAGERVSRPEAAVPGYQHSSESVNTHTPQFFIYKIDASNREQRLEDKGETPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRASHSEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	KDRANLESKDGDARR HHHHCCCCCCCCCCC	38.93	22705319
43	Phosphorylation	DGDARRVSLPRKEPT CCCCCCCCCCCCCCC	30.74	24719451
162	Phosphorylation	QENGQELSPIALEPG CCCCEECCCEECCCC	17.32	26745281
220	Phosphorylation	RGPEGEGSMDGPGPQ CCCCCCCCCCCCCCC	14.92	25521595
232	Phosphorylation	GPQGDAPSFLSDSAT CCCCCCCHHHCCCCC	40.31	27742792
264	Phosphorylation	SLLSSEKSLALLTVE HHHCCHHHEEEEEEE	18.15	29899451
441	Phosphorylation	GAKVAVPTGPTPLDS CCEEEECCCCCCCCC	49.55	25293948
444	Phosphorylation	VAVPTGPTPLDSTPP EEECCCCCCCCCCCC	37.52	25293948
448	Phosphorylation	TGPTPLDSTPPGGGP CCCCCCCCCCCCCCC	50.96	26745281
449	Phosphorylation	GPTPLDSTPPGGGPH CCCCCCCCCCCCCCC	32.92	26239621
459	Phosphorylation	GGGPHPLTGQEEARA CCCCCCCCCHHHHHH	41.07	25293948
476	Phosphorylation	KEKPKARSEDSGLDG HHCCCCCCCCCCCCC	51.09	-
488	Phosphorylation	LDGVVARTPLEHVAP CCCEEECCCHHHCCC	23.61	21454597
503	Phosphorylation	KPDPHLASPKPTCMV CCCCCCCCCCCCEEC	39.55	26060331
516	Phosphorylation	MVPPMPHSPVSGDSV ECCCCCCCCCCCCCC	22.56	30352176
519	Phosphorylation	PMPHSPVSGDSVEED CCCCCCCCCCCCCCC	40.02	26643407
522	Phosphorylation	HSPVSGDSVEEDEEE CCCCCCCCCCCCHHH	34.65	26643407
652	Ubiquitination	DLNRIQNKPYTETVD HHHHHHCCCCCCEEC	24.03	22790023
693	Ubiquitination	DLFQGQYKSKLVCPV HHHCCCCCCCEECCC	32.97	22790023
721	Ubiquitination	LPVPLPQKQKVLPIF CCCCCCCCCCEEEEE	50.58	-
777	Ubiquitination	LRLAEVIKNRFHRVF CHHHHHHHHCCCEEE	47.44	22790023
1153	Phosphorylation	IVQLKRFSFRSFIWR EEEECCCCCHHHHHH	24.63	24719451
1162	Ubiquitination	RSFIWRDKINDLVEF HHHHHHHHCCHHEEC	34.53	22790023
1178	Ubiquitination	VRNLDLSKFCIGQKE CCCCCHHHHHCCCCC	52.10	22790023
1191	Phosphorylation	KEEQLPSYDLYAVIN CCCCCCCCCHHEEHH	14.18	28494245
1194	Phosphorylation	QLPSYDLYAVINHYG CCCCCCHHEEHHHCC	8.91	28494245
1200	Phosphorylation	LYAVINHYGGMIGGH HHEEHHHCCCCCCCE	15.75	28494245
1258	Phosphorylation	LFYRRRNSPVERPPR EEECCCCCCCCCCCC	28.63	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of UBP19_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBP19_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of UBP19_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RN123_MOUSE	Rnf123	physical	19015242
MARH6_HUMAN	MARCH6	physical	25088257
UBC_HUMAN	UBC	physical	25088257

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.