CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018567
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein 5 
Protein Synonyms/Alias
 Putative tumor suppressor LUCA15; RNA-binding motif protein 5 
Gene Name
 Rbm5 
Gene Synonyms/Alias
 Luca15 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
542KTAQQIAKDMERWAKacetylation[1, 2]
787KGAGLGAKGSAYGLSacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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 production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity). 
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 647 672 C2H2-type.
 REGION 321 809 Required for interaction with U2AF2 (By
 REGION 452 535 Sufficient for interaction with ACIN1,
 MOD_RES 69 69 Phosphoserine.
 MOD_RES 78 78 Phosphoserine.
 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; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 815 AA 
Protein Sequence
MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 60
ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 120
FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP 180
KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESAQSVDYYC DTIILRNIAP 240
HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP 300
LKIDGKTIGV DFAKSARKDL VLPDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY 360
MQPGQDGYTQ YTQYSQDYQQ FYQQQAGGLE SDTSATSGTT VTTTSAAVVS QSPQLYNQTS 420
NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY 480
DPNSQYYYNS LTQQYLYWDG EKETYVPAAE ASSNQQTGLP STKEGKEKKE KPKSKTAQQI 540
AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLLP 600
ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNRD 660
ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP 720
KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK 780
GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME 815 
Gene Ontology
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; ISS: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:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0000245; P:spliceosomal complex assembly; ISS: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