CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001508
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 19 
Protein Synonyms/Alias
 Deubiquitinating enzyme 19; Ubiquitin thioesterase 19; Ubiquitin-specific-processing protease 19; Zinc finger MYND domain-containing protein 9 
Gene Name
 USP19 
Gene Synonyms/Alias
 KIAA0891; ZMYND9 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
610DLNRIQNKPYTETVDubiquitination[1, 2]
651DLFQGQYKSKLVCPVubiquitination[1, 3]
653FQGQYKSKLVCPVCAubiquitination[2]
735LRLAEVIKNRFHRVFubiquitination[2]
823YCNQLCQKTHWPDHKubiquitination[2]
1120RSFIWRDKINDLVEFubiquitination[1, 2, 3, 4]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional 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. 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. 
Sequence Annotation
 DOMAIN 113 202 CS 1.
 DOMAIN 282 384 CS 2.
 ZN_FING 791 833 MYND-type.
 ACT_SITE 506 506 Nucleophile (By similarity).
 ACT_SITE 1165 1165 Proton acceptor (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Polymorphism; Protease; Reference proteome; Repeat; Thiol protease; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1318 AA 
Protein Sequence
MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ AGLEPLASGD 60
PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG ACEDPHDLLA TPTPELLLDW 120
RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR 180
KGSLLHLTLP KKVPMLTWPS LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN 240
DPVSPAMVRS RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH 300
VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL RNLIEPEQCT 360
FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG PTPLDSTPPG GAPHPLTGQE 420
EARAVEKDKS KARSEDTGLD SVATRTPMEH VTPKPETHLA SPKPTCMVPP MPHSPVSGDS 480
VEEEEEEEKK VCLPGFTGLV NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL 540
GTGGRLAIGF AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL 600
HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY KSKLVCPVCA 660
KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL VSVSKENSTA SEVLDSLSQS 720
VHVKPENLRL AEVIKNRFHR VFLPSHSLDT VSPSDTLLCF ELLSSELAKE RVVVLEVQQR 780
PQVPSVPISK CAACQRKQQS EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY 840
PFLVSVPASR LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA 900
GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA SGPIEVGSLP 960
AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE QRLEDKGDTP LELGDDCSLA 1020
LVWRNNERLQ EFVLVASKEL ECAEDPGSAG EAARAGHFTL DQCLNLFTRP EVLAPEEAWY 1080
CPQCKQHREA SKQLLLWRLP NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG 1140
QKEEQLPSYD LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ 1200
VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE LEAEEEPVPE 1260
GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL VALVLNVFYP LVSQSRWR 1318 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030433; P:ER-associated protein catabolic process; IDA:UniProtKB.
 GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
 GO:0090068; P:positive regulation of cell cycle process; ISS:UniProtKB.
 GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
 GO:1900037; P:regulation of cellular response to hypoxia; IMP:UniProtKB.
 GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
 GO:0034976; P:response to endoplasmic reticulum stress; IEP:UniProtKB.
 GO:0014732; P:skeletal muscle atrophy; ISS:UniProtKB. 
Interpro
 IPR007052; CS-like_domain.
 IPR017447; CS_domain.
 IPR015054; DUF1872.
 IPR008978; HSP20-like_chaperone.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR002893; Znf_MYND. 
Pfam
 PF04969; CS
 PF08959; DUF1872
 PF00443; UCH
 PF01753; zf-MYND 
SMART
  
PROSITE
 PS51203; CS
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS01360; ZF_MYND_1
 PS50865; ZF_MYND_2 
PRINTS