CPLM-004224

Genbank Nucleotide ID

Zinc finger protein RFP

Protein Synonyms/Alias

RING finger protein 76; Ret finger protein; Tripartite motif-containing protein 27

Homo sapiens (Human)

Position	Peptide	Type	References
79	ANVTQLVKQLRTERP	ubiquitination	[1, 2, 3, 4, 5]
140	EEAVEGFKEQIQNQL	ubiquitination	[5]
181	LTQMEREKIVWEFEQ	ubiquitination	[5]
194	EQLYHSLKEHEYRLL	ubiquitination	[5]
283	KIHIFAQKCLFLTES	ubiquitination	[5]
292	LFLTESLKQFTEKMQ	ubiquitination	[5, 6, 7, 8]
297	SLKQFTEKMQSDMEK	ubiquitination	[2, 5]
304	KMQSDMEKIQELREA	ubiquitination	[5, 8]
380	WEVEVGDKAKWTIGV	ubiquitination	[3, 5, 7]
382	VEVGDKAKWTIGVCE	ubiquitination	[5]

[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] 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]
[3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]

Functional Description

Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA (By similarity). E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation.

DOMAIN 298 492 B30.2/SPRY.
ZN_FING 16 57 RING-type.
ZN_FING 96 127 B box-type.

Alternative splicing; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Ligase; Metal-binding; Nucleus; Proto-oncogene; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
GO:0031965; C:nuclear membrane; IDA:MGI.
GO:0005654; C:nucleoplasm; IDA:MGI.
GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0046872; F:metal ion binding; TAS:ProtInc.
GO:0003676; F:nucleic acid binding; TAS:ProtInc.
GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0008283; P:cell proliferation; TAS:ProtInc.
GO:0072643; P:interferon-gamma secretion; IMP:UniProtKB.
GO:0002820; P:negative regulation of adaptive immune response; IMP:UniProtKB.
GO:0090281; P:negative regulation of calcium ion import; IMP:UniProtKB.
GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
GO:1900041; P:negative regulation of interleukin-2 secretion; IMP:UniProtKB.
GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO:0070206; P:protein trimerization; IDA:UniProtKB.
GO:0007283; P:spermatogenesis; TAS:ProtInc.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR001870; B30.2/SPRY.
IPR003879; Butyrophylin.
IPR008985; ConA-like_lec_gl_sf.
IPR006574; PRY.
IPR018355; SPla/RYanodine_receptor_subgr.
IPR003877; SPRY_rcpt.
IPR000315; Znf_B-box.
IPR020457; Znf_B-box_chordata.
IPR018957; Znf_C3HC4_RING-type.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR017907; Znf_RING_CS.

PF00622; SPRY
PF00643; zf-B_box
PF00097; zf-C3HC4

SM00336; BBOX
SM00589; PRY
SM00184; RING
SM00449; SPRY

PS50188; B302_SPRY
PS50119; ZF_BBOX
PS00518; ZF_RING_1
PS50089; ZF_RING_2

PR01406; BBOXZNFINGER.
PR01407; BUTYPHLNCDUF.