| Tag | Content |
|---|
| CPLM ID | CPLM-010723 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RNA-binding protein 10 |
Protein Synonyms/Alias | G patch domain-containing protein 9; RNA-binding motif protein 10; RNA-binding protein S1-1; S1-1 |
Gene Name | RBM10 |
Gene Synonyms/Alias | DXS8237E; GPATC9; GPATCH9; KIAA0122 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 383 | TINVEFAKGSKRDMA | acetylation | [1] |
|
Reference | [1] 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] |
Functional Description | May be involved in post-transcriptional processing, most probably in mRNA splicing. 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.
MOD_RES 89 89 Phosphoserine.
MOD_RES 383 383 N6-acetyllysine.
MOD_RES 718 718 Phosphoserine.
MOD_RES 723 723 Phosphoserine.
MOD_RES 733 733 Phosphoserine.
MOD_RES 736 736 Phosphoserine.
MOD_RES 738 738 Phosphoserine.
MOD_RES 781 781 Phosphoserine.
MOD_RES 797 797 Phosphoserine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Complete proteome; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 930 AA |
Protein Sequence | MEYERRGGRG DRTGRYGATD RSQDDGGENR SRDHDYRDMD YRSYPREYGS QEGKHDYDDS 60
SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG DYRDQDYRTE QGEEEEEEED 120
EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ SHGVQAREVR LMRNKSSGQS RGFAFVEFSH 180
LQDATRWMEA NQHSLNILGQ KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK 240
SEAEQKLPLG TRLDQQTLPL GGRELSQGLL PLPQPYQAQG VLASQALSQG SEPSSENAND 300
TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL STIVEAAQLL 360
QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRISAA SVASTAIAAA QWAISQASQG 420
GEGTWATSEE PPVDYSYYQQ DEGYGNSQGT ESSLYAHGYL KGTKGPGITG TKGDPTGAGP 480
EASLEPGADS VSMQAFSRAQ PGAAPGIYQQ SAEASSSQGT AANSQSYTIM SPAVLKSELQ 540
SPTHPSSALP PATSPTAQES YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA 600
QSQQYLYWDG ERRTYVPALE QSADGHKETG APSKEGKEKK EKHKTKTAQQ IAKDMERWAR 660
SLNKQKENFK NSFQPISSLR DDERRESATA DAGYAILEKK GALAERQHTS MDLPKLASDD 720
RPSPPRGLVA AYSGESDSEE EQERGGPERE EKLTDWQKLA CLLCRRQFPS KEALIRHQQL 780
SGLHKQNLEI HRRAHLSENE LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG 840
ISTASVDFEQ PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG 900
ARGSSYGVTS TESYKETLHK TMVTRFNEAQ 930 |
Gene Ontology | GO:0005634; C:nucleus; NAS:UniProtKB. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0003723; F:RNA binding; NAS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0070935; P:3'-UTR-mediated mRNA stabilization; IEA:Compara. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0008285; P:negative regulation of cell proliferation; IEA:Compara. GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara. GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IEA:Compara. GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |