CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019894
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein 10 
Protein Synonyms/Alias
 RNA-binding motif protein 10 
Gene Name
 Rbm10 
Gene Synonyms/Alias
 Kiaa0122 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
54EYGSQEGKHEYDDSSacetylation[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
Functional Description
 Not known. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). 
Sequence Annotation
 DOMAIN 129 209 RRM 1.
 DOMAIN 300 384 RRM 2.
 DOMAIN 858 904 G-patch.
 ZN_FING 212 242 RanBP2-type.
 ZN_FING 759 784 C2H2-type; atypical.
 MOD_RES 61 61 Phosphoserine (By similarity).
 MOD_RES 89 89 Phosphoserine (By similarity).
 MOD_RES 383 383 N6-acetyllysine (By similarity).
 MOD_RES 718 718 Phosphoserine (By similarity).
 MOD_RES 723 723 Phosphoserine (By similarity).
 MOD_RES 733 733 Phosphoserine.
 MOD_RES 736 736 Phosphoserine.
 MOD_RES 738 738 Phosphoserine.
 MOD_RES 781 781 Phosphoserine (By similarity).
 MOD_RES 797 797 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 930 AA 
Protein Sequence
MEYERRGGRG DRTGRYGATD RSQDDSGENR SRDHDYRDMD YRSYPREYGS QEGKHEYDDS 60
SEEQSAEIRG QLQSHGVQAR EVRLMRNKSS GQSRGFAFVE FSHLQDATRW MEANQHSLNI 120
LGQKVSMHYS DPKPKINEDW LCNKCGVQNF KRREKCFKCG VPKSEAEQKL PLGTRLDQQA 180
LPLGGRELSQ GLLPLPQPYQ AQGVLTSQAL SQGSEPSSEN ANDTIILRNL NPHSTMDSIL 240
GALAPYAVLS SSNVRVIKDK QTQLNRGFAF IQLSTIVEAA QLLQILQALH PPLTIDGKTI 300
NVEFAKGSKR DMASNEGSRI NAASVASTAI AAAQWAISQA SQGGESAWAA PEEPPVDYSY 360
YQQDEGYGSS QGTDSLYAHG YLKNSKGPGM TGTKGDPAGT GPEASLEAGA DSVSLQAFSR 420
AQPGAAPGLY QQSAEGSSGQ STATNSQSYT IISPAVLKAE LQSPTQPSSS AFPPATSPTA 480
PEAYSQYPVP DVSTYQYDET SGYYYDPQTG LYYDPNSQYY YNAQSQQYLY WDGERRTYIP 540
ALEQSADGHK DTGASSKEGK EKKEKHKTKT AQQIAKDMER WARSLNKQKE NFKNSFQPIS 600
ALRDDERRES ATADAGYAIL EKKGALAERQ HTSMDLPKLA SDDRPSPPRG LVAAYSGESD 660
SEEEQERGGP EREEKLTDWQ KLACLLCRRQ FPSKEALIRH QQLSGLHKQN LEIHRRAHLS 720
ENELEALEKN DMEQMKYRDR AAERREKYGI PEPPEPKRRK YGGISTASVD FEQPTRDGLG 780
SDNIGSRMLQ AMGWKEGSGL GRKKQGIVTP IEAQTRVRGS GLGARGSSYG VTSTESYKET 840
LHKTMVTRFN EAQ 853 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:MGI.
 GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:MGI. 
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
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS