CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014008
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein 26 
Protein Synonyms/Alias
 CTCL tumor antigen se70-2; RNA-binding motif protein 26 
Gene Name
 RBM26 
Gene Synonyms/Alias
 C13orf10; PRO1777 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71ETQIFVEKLFDAVNTubiquitination[1]
510TKKTWFDKPNFNRTNacetylation[2, 3, 4, 5]
510TKKTWFDKPNFNRTNubiquitination[1, 6]
678DRLGFVSKPSVSATEacetylation[3, 4]
709AALKAAQKTLLVSTSubiquitination[1, 6]
Reference
 [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] 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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] 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
  
Sequence Annotation
 DOMAIN 532 606 RRM 1.
 DOMAIN 891 960 RRM 2.
 ZN_FING 288 316 C3H1-type.
 MOD_RES 127 127 Phosphoserine.
 MOD_RES 510 510 N6-acetyllysine.
 MOD_RES 518 518 Phosphoserine.
 MOD_RES 616 616 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1007 AA 
Protein Sequence
MVSKMIIENF EALKSWLSKT LEPICDADPS ALAKYVLALV KKDKSEKELK ALCIDQLDVF 60
LQKETQIFVE KLFDAVNTKS YLPPPEQPSS GSLKVEFFPH QEKDIKKEEI TKEEEREKKF 120
SRRLNHSPPQ SSSRYRENRS RDERKKDDRS RKRDYDRNPP RRDSYRDRYN RRRGRSRSYS 180
RSRSRSWSKE RLRERDRDRS RTRSRSRTRS RERDLVKPKY DLDRTDPLEN NYTPVSSVPS 240
ISSGHYPVPT LSSTITVIAP THHGNNTTES WSEFHEDQVD HNSYVRPPMP KKRCRDYDEK 300
GFCMRGDMCP FDHGSDPVVV EDVNLPGMLP FPAQPPVVEG PPPPGLPPPP PILTPPPVNL 360
RPPVPPPGPL PPSLPPVTGP PPPLPPLQPS GMDAPPNSAT SSVPTVVTTG IHHQPPPAPP 420
SLFTADTYDT DGYNPEAPSI TNTSRPMYRH RVHAQRPNLI GLTSGDMDLP PREKPPNKSS 480
MRIVVDSESR KRTIGSGEPG VPTKKTWFDK PNFNRTNSPG FQKKVQFGNE NTKLELRKVP 540
PELNNISKLN EHFSRFGTLV NLQVAYNGDP EGALIQFATY EEAKKAISST EAVLNNRFIK 600
VYWHREGSTQ QLQTTSPKVM QPLVQQPILP VVKQSVKERL GPVPSSTIEP AEAQSASSDL 660
PQNVTKLSVK DRLGFVSKPS VSATEKVLST STGLTKTVYN PAALKAAQKT LLVSTSAVDN 720
NEAQKKKQEA LKLQQDVRKR KQEILEKHIE TQKMLISKLE KNKTMKSEDK AEIMKTLEVL 780
TKNITKLKDE VKAASPGRCL PKSIKTKTQM QKELLDTELD LYKKMQAGEE VTELRRKYTE 840
LQLEAAKRGI LSSGRGRGIH SRGRGAVHGR GRGRGRGRGV PGHAVVDHRP RALEISAFTE 900
SDREDLLPHF AQYGEIEDCQ IDDSSLHAVI TFKTRAEAEA AAVHGARFKG QDLKLAWNKP 960
VTNISAVETE EVEPDEEEFQ EESLVDDSLL QDDDEEEEDN ESRSWRR 1007 
Gene Ontology
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:InterPro.
 GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR002483; PWI_dom.
 IPR000504; RRM_dom.
 IPR000571; Znf_CCCH. 
Pfam
 PF01480; PWI 
SMART
 SM00360; RRM
 SM00356; ZnF_C3H1 
PROSITE
 PS50102; RRM
 PS50103; ZF_C3H1 
PRINTS