CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014246
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
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
21SSGRSCSKDPSGAHPacetylation[1]
96PSATAAVKMEPENKYacetylation[2]
102VKMEPENKYLPELMAacetylation[2]
102VKMEPENKYLPELMAubiquitination[3]
152YLDLFSHKNMKLKERubiquitination[3]
165ERVLIPVKQYPKFNFubiquitination[3]
169IPVKQYPKFNFVGKIubiquitination[3]
175PKFNFVGKILGPQGNacetylation[2, 4]
175PKFNFVGKILGPQGNubiquitination[3]
185GPQGNTIKRLQEETGubiquitination[3]
194LQEETGAKISVLGKGubiquitination[3]
432APPARPVKGAYREHPubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] 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
 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.
 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; Direct protein sequencing; 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
MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG PRGGARASPA 60
TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE 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 YDDTYAEQSY EGYEGYYSQS QGESEYYDYG HGELQDSYEA YGQDDWNGTR 420
PSLKAPPARP VKGAYREHPY GRY 443 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0070618; C:Grb2-Sos complex; IEA:Compara.
 GO:0016020; C:membrane; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
 GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
 GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS