UniProt Accession

 TRI13_HUMAN; O60858; B2RB49; Q5UBW0; Q5W0U8; Q5W0U9; Q9BQ47; Q9C021 

Genbank Protein ID

 AJ224819; AF279660; AF220127; AF220128; AY191002; AF241849; AF241850; AY455758; AY764035; AK314496; AL137060; AL137060; AL137060; CH471075; CH471075; BC003579; BC063407 

Genbank Nucleotide ID

 CAA12136.1; AAK13059.1; AAG53500.1; AAG53501.1; AAO38979.1; AAK51624.1; AAF91315.1; AAR31110.1; AAV51406.1; BAG37096.1; CAC43391.1; CAH72825.1; CAH72826.1; EAX08844.1; EAX08845.1; AAH03579.1; AAH63407.1 

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
35	CSHNFCKKCLEGILE	ubiquitination	[1]
56	LWRPAPFKCPTCRKE	ubiquitination	[1]
128	ATRGEHTKHVFCSIE	ubiquitination	[1]
171	LDTLETSKRKSLQLL	ubiquitination	[1]
173	TLETSKRKSLQLLTK	ubiquitination	[1]
186	TKDSDKVKEFFEKLQ	ubiquitination	[1]
224	AYDPEINKLNTILQE	ubiquitination	[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] 

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

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