UniProt Accession

 RFWD3_HUMAN; Q6PCD5; A8K585; B2RE35; D3DUJ8; Q5XKR3; Q9H9Q3; Q9NVT4 

Genbank Protein ID

 AK001382; AK022673; AK291200; AK315786; AC109599; CH471114; CH471114; BC002574; BC059371 

Genbank Nucleotide ID

 BAA91662.1; BAB14169.1; BAF83889.1; BAG38132.1; EAW95680.1; EAW95681.1; AAH02574.2; AAH59371.2 

Protein Name

 E3 ubiquitin-protein ligase RFWD3 

Protein Synonyms/Alias

 RING finger and WD repeat domain-containing protein 3; RING finger protein 201 

Gene Name

 RFWD3 

Gene Synonyms/Alias

 RNF201 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
321	RCISTWLKGQVRKCP	ubiquitination	[1, 2]
359	TSEQERMKSSLLKEQ	ubiquitination	[2]
364	RMKSSLLKEQMLRKQ	ubiquitination	[1, 2, 3, 4, 5]
370	LKEQMLRKQAELESA	ubiquitination	[2, 5]
389	QLQVLTDKCTRLQRR	ubiquitination	[1, 2, 3, 5, 6]
402	RRVQDLQKLTSHQSQ	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9]
433	PSSQGQHKHKYHFQK	ubiquitination	[1, 2, 8]
435	SQGQHKHKYHFQKTF	ubiquitination	[2]
440	KHKYHFQKTFTVSQA	ubiquitination	[1, 2, 5, 8]
488	MLSTANMKSSQYIPM	ubiquitination	[2, 5]
498	QYIPMHGKQIRGLAF	ubiquitination	[2, 3, 5]
583	VQELVAQKARCPLVS	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9]
658	LVTYRPDKNHTTIRS	ubiquitination	[1, 2, 5, 8]
697	FFGGPTCKLLTKNAI	ubiquitination	[1, 2, 5, 8]
766	YLATLTEKMVHIYKW	ubiquitination	[2, 5, 7, 8, 9]
772	EKMVHIYKWE*****	ubiquitination	[1, 2]

Reference

 [1] 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]
 [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] 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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] 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]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] 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]
 [8] 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]
 [9] 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

 E3 ubiquitin-protein ligase that mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53. Plays a role in RPA-mediated DNA damage signaling and repair. 

Sequence Annotation

 REPEAT 495 537 WD 1.
 REPEAT 539 577 WD 2.
 REPEAT 583 628 WD 3.
 ZN_FING 287 331 RING-type; degenerate.
 MOD_RES 46 46 Phosphoserine; by ATM and ATR.
 MOD_RES 63 63 Phosphoserine; by ATM and ATR.  

Keyword

 Coiled coil; Complete proteome; Cytoplasm; DNA damage; DNA repair; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 774 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:UniProtKB.
 GO:0010212; P:response to ionizing radiation; IDA:UniProtKB. 

Interpro

 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 

Pfam

 PF00400; WD40
 PF13639; zf-RING_2 

SMART

 SM00184; RING
 SM00320; WD40 

PROSITE

 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 

PRINTS