UniProt Accession

 RBM5_HUMAN; P52756; B2RA45; B4DM16; B4DMF9; B4DZ63; Q93021; Q9BU14; Q9HDA6; Q9UKY8; Q9UL24 

Genbank Protein ID

 U23946; AF091263; AF103802; AF107493; AK297249; AK297445; AK302766; AK314032; CH471055; CH471055; U73168 

Genbank Nucleotide ID

 AAA99715.1; AAD04159.1; AAF02422.2; AAF99551.1; BAG59728.1; BAG59871.1; BAG63975.1; BAG36742.1; EAW65040.1; EAW65041.1; AAB42216.1 

Protein Name

 RNA-binding protein 5 

Protein Synonyms/Alias

 Protein G15; Putative tumor suppressor LUCA15; RNA-binding motif protein 5; Renal carcinoma antigen NY-REN-9 

Gene Name

 RBM5 

Gene Synonyms/Alias

 H37; LUCA15 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
314	TIGVDFAKSARKDLV	ubiquitination	[1]
542	KTAQQIAKDMERWAK	acetylation	[2, 3, 4]

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]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] 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

 Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis. 

Sequence Annotation

 DOMAIN 98 178 RRM 1.
 DOMAIN 231 315 RRM 2.
 DOMAIN 743 789 G-patch.
 ZN_FING 181 210 RanBP2-type.
 ZN_FING 647 677 C2H2-type; atypical.
 REGION 321 809 Required for interaction with U2AF2.
 REGION 452 535 Sufficient for interaction with ACIN1,
 MOD_RES 69 69 Phosphoserine (By similarity).
 MOD_RES 78 78 Phosphoserine (By similarity).
 MOD_RES 621 621 Phosphoserine.
 MOD_RES 624 624 Phosphoserine.  

Keyword

 3D-structure; Alternative splicing; Apoptosis; Complete proteome; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 815 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005681; C:spliceosomal complex; TAS:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003729; F:mRNA binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0008285; P:negative regulation of cell proliferation; TAS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB. 

Interpro

 IPR000467; G_patch_dom.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR001876; Znf_RanBP2. 

Pfam

 PF01585; G-patch
 PF00641; zf-RanBP 

SMART

 SM00443; G_patch
 SM00360; RRM
 SM00355; ZnF_C2H2
 SM00547; ZnF_RBZ 

PROSITE

 PS50174; G_PATCH
 PS50102; RRM
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 

PRINTS