CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000731
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF13 
Protein Synonyms/Alias
 RING finger protein 13 
Gene Name
 RNF13 
Gene Synonyms/Alias
 RZF 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107LDCNFDIKVLNAQRAubiquitination[1]
232KLPVHKFKKGDEYDVubiquitination[2]
233LPVHKFKKGDEYDVCubiquitination[1, 2]
273CVDPWLTKTKKTCPVubiquitination[1, 2]
276PWLTKTKKTCPVCKQubiquitination[1]
Reference
 [1] 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]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. 
Sequence Annotation
 DOMAIN 65 160 PA.
 ZN_FING 240 282 RING-type; atypical.
 MOD_RES 292 292 Phosphoserine (By similarity).
 MOD_RES 294 294 Phosphoserine (By similarity).
 MOD_RES 296 296 Phosphothreonine (By similarity).
 MOD_RES 298 298 Phosphoserine (By similarity).
 MOD_RES 299 299 Phosphoserine (By similarity).
 CARBOHYD 88 88 N-linked (GlcNAc...).  
Keyword
 Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Ligase; Lysosome; Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Signal; Transmembrane; Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 381 AA 
Protein Sequence
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFDD LPARFGYRLP 60
AEGLKGFLIN SKPENACEPI VPPPVKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI 120
VHNVDSDDLI SMGSNDIEVL KKIDIPSVFI GESSANSLKD EFTYEKGGHL ILVPEFSLPL 180
EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC 240
AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ 300
EENEVTEHTP LLRPLASVSA QSFGALSESR SHQNMTESSD YEEDDNEDTD SSDAENEINE 360
HDVVVQLQPN GERDYNIANT V 381 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031902; C:late endosome membrane; ISS:UniProtKB.
 GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. 
Interpro
 IPR003137; Protease-assoc_domain.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02225; PA
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS