CPLM-022235

Genbank Nucleotide ID

E3 ubiquitin-protein ligase RLIM

Protein Synonyms/Alias

LIM domain-interacting RING finger protein; RING finger LIM domain-binding protein; R-LIM; RING finger protein 12; Renal carcinoma antigen NY-REN-43

Homo sapiens (Human)

Position	Peptide	Type	References
9	ENSDSNDKGSGDQSA	ubiquitination	[1, 2, 3]
72	LRRLQQIKEGPPPQN	ubiquitination	[4]
550	DQPRGLTKEQIDNLA	ubiquitination	[2, 3, 4, 5]
568	FGENDALKTCSVCIT	ubiquitination	[2]
582	TEYTEGNKLRKLPCS	ubiquitination	[1, 2, 3]
585	TEGNKLRKLPCSHEY	ubiquitination	[2, 3]

[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] 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]
[4] 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]
[5] 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-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex- related dosage differences of X-encoded genes in somatic cells of female placental mammals.

ZN_FING 570 611 RING-type.
MOTIF 621 624 PDZ-binding (Potential).
MOD_RES 228 228 Phosphoserine (By similarity).
MOD_RES 230 230 Phosphoserine.

Complete proteome; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0017053; C:transcriptional repressor complex; NAS:UniProtKB.
GO:0003714; F:transcription corepressor activity; NAS:UniProtKB.
GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0045892; P:negative regulation of transcription, DNA-dependent; NAS:UniProtKB.
GO:0060816; P:random inactivation of X chromosome; IDA:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.

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

PS00518; ZF_RING_1
PS50089; ZF_RING_2