UniProt Accession

 RNF5_HUMAN; Q99942; A2BFI6; B2R4K3; Q0VDB7; Q9UMQ2 

Genbank Protein ID

 AB056869; AJ243936; AK311859; BT007105; U89336; AL845464; AL662884; AL662830; BX284686; BX927239; CR812478; CR933878; BC004155; BC111392; BC119741; BC119742; BC127651; BC127652; BC148255 

Genbank Nucleotide ID

 BAB39359.1; CAB51286.1; BAG34800.1; AAP35769.1; AAB47492.1; CAI41808.1; CAI18351.1; CAI17532.1; CAM26222.1; CAQ06594.1; CAQ10698.1; CAQ09623.1; AAH04155.1; AAI11393.1; AAI19742.1; AAI19743.1; AAI27652.1; AAI27653.1; AAI48256.1 

Protein Name

 E3 ubiquitin-protein ligase RNF5 

Protein Synonyms/Alias

 Protein G16; RING finger protein 5; Ram1 homolog; HsRma1 

Gene Name

 RNF5 

Gene Synonyms/Alias

 G16; NG2; RMA1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
68	RQECPVCKAGISREK	ubiquitination	[1, 2]
75	KAGISREKVVPLYGR	ubiquitination	[1, 2, 3]
86	LYGRGSQKPQDPRLK	ubiquitination	[1, 2, 3]
93	KPQDPRLKTPPRPQG	ubiquitination	[1, 2, 3]

Reference

 [1] 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]
 [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]
 [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] 

Functional Description

 Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurrs in mitochondria after viral transfection and regulates antiviral responses. 

Sequence Annotation

 ZN_FING 27 68 RING-type.
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 Acetylation; Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 180 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; TAS:ProtInc.
 GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB.
 GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
 GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. 

Interpro

 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 

Pfam

  

SMART

 SM00184; RING 

PROSITE

 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 

PRINTS