CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001011
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM13 
Protein Synonyms/Alias
 B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Leukemia-associated protein 5; Putative tumor suppressor RFP2; RING finger protein 77; Ret finger protein 2; Tripartite motif-containing protein 13 
Gene Name
 TRIM13 
Gene Synonyms/Alias
 LEU5; RFP2; RNF77 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32CSHNFCKKCLEGILEubiquitination[1, 2]
53LWRPAPFKCPTCRKEubiquitination[1]
90NKIKISPKMPVCKGHubiquitination[2]
125ATRGEHTKHVFCSIEubiquitination[1]
168LDTLETSKRKSLQLLubiquitination[1, 3]
170TLETSKRKSLQLLTKubiquitination[1]
183TKDSDKVKEFFEKLQubiquitination[1]
221AYDPEINKLNTILQEubiquitination[1, 3, 4]
279LPASPLMKNFDTSQWubiquitination[3]
290TSQWEDIKLVDVDKLubiquitination[3]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. 
Sequence Annotation
 ZN_FING 10 58 RING-type.
 ZN_FING 89 131 B box-type.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 407 AA 
Protein Sequence
MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE 60
TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR 120
GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD 180
KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK 240
DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP 300
QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC LSNFSSYLTK 360
TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF VCKYKLL 407 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0030433; P:ER-associated protein catabolic process; IDA:UniProtKB.
 GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0016239; P:positive regulation of macroautophagy; IDA:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
 GO:0010332; P:response to gamma radiation; IEP:UniProtKB. 
Interpro
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00643; zf-B_box 
SMART
 SM00336; BBOX
 SM00184; RING 
PROSITE
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS