Tag | Content |
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CPLM ID | CPLM-018446 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | KH domain-containing, RNA-binding, signal transduction-associated protein 1 |
Protein Synonyms/Alias | GAP-associated tyrosine phosphoprotein p62; Src-associated in mitosis 68 kDa protein; Sam68; p21 Ras GTPase-activating protein-associated p62; p68 |
Gene Name | Khdrbs1 |
Gene Synonyms/Alias | Sam68 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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96 | PSATAAAKMEPENKY | acetylation | [1] | 169 | IPVKQYPKFNFVGKI | acetylation | [1] | 175 | PKFNFVGKILGPQGN | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain- containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)- containing RNA species. |
Sequence Annotation | DOMAIN 171 197 KH. MOD_RES 20 20 Phosphoserine (By similarity). MOD_RES 29 29 Phosphoserine (By similarity). MOD_RES 45 45 Asymmetric dimethylarginine; alternate MOD_RES 45 45 Omega-N-methylated arginine; by PRMT1; MOD_RES 52 52 Asymmetric dimethylarginine; alternate MOD_RES 52 52 Omega-N-methylated arginine; by PRMT1; MOD_RES 58 58 Phosphoserine (By similarity). MOD_RES 113 113 Phosphoserine (By similarity). MOD_RES 175 175 N6-acetyllysine (By similarity). MOD_RES 291 291 Omega-N-methylated arginine; by PRMT1 (By MOD_RES 304 304 Asymmetric dimethylarginine; alternate MOD_RES 304 304 Omega-N-methylated arginine; by PRMT1; MOD_RES 310 310 Omega-N-methylarginine; alternate (By MOD_RES 310 310 Omega-N-methylated arginine; by PRMT1; MOD_RES 315 315 Omega-N-methylarginine; alternate (By MOD_RES 315 315 Omega-N-methylated arginine; by PRMT1; MOD_RES 320 320 Dimethylated arginine; alternate (By MOD_RES 320 320 Omega-N-methylarginine; alternate (By MOD_RES 320 320 Omega-N-methylated arginine; by PRMT1; MOD_RES 325 325 Omega-N-methylarginine; alternate (By MOD_RES 325 325 Omega-N-methylated arginine; by PRMT1; MOD_RES 331 331 Dimethylated arginine; alternate (By MOD_RES 331 331 Omega-N-methylated arginine; by PRMT1; MOD_RES 340 340 Omega-N-methylarginine; alternate (By MOD_RES 340 340 Omega-N-methylated arginine; by PRMT1; MOD_RES 346 346 Omega-N-methylated arginine; by PRMT1 (By MOD_RES 435 435 Phosphotyrosine; by PTK6 (By similarity). MOD_RES 440 440 Phosphotyrosine; by PTK6 (By similarity). MOD_RES 443 443 Phosphotyrosine; by PTK6 (By similarity). |
Keyword | Acetylation; Cell cycle; Complete proteome; Membrane; Methylation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; SH3-binding; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 443 AA |
Protein Sequence | MQRRDDPAAR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRSRGGGGG PRGGARASPA 60 TQPPPLLPPS NPGPDATVVG SAPTPLLPPS ATAAAKMEPE NKYLPELMAE KDSLDPSFTH 120 AMQLLSVEIE KIQKGESKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ 180 GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA 240 YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV 300 PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA GIQRIPLPPT 360 PAPETYEDYG YDDSYAEQSY EGYEGYYSQS QGESEYYDYG HGELQDSYEA YGQDDWNGTR 420 PSLKAPPARP VKGAYREHPY GRY 443 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:RGD. GO:0070618; C:Grb2-Sos complex; IDA:RGD. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0032403; F:protein complex binding; IDA:RGD. GO:0003723; F:RNA binding; ISS:UniProtKB. GO:0017124; F:SH3 domain binding; IDA:RGD. GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB. GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB. GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB. GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB. GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB. GO:0009966; P:regulation of signal transduction; NAS:RGD. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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