KHDR2_RAT
ID KHDR2_RAT Reviewed; 349 AA.
AC Q920F3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 2;
DE AltName: Full=Sam68-like mammalian protein 1;
DE Short=SLM-1;
DE Short=rSLM-1;
GN Name=Khdrbs2; Synonyms=Slm1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH RBMX; SAFB;
RP SFRS9 AND YTHDC1, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15345239; DOI=10.1016/j.mcn.2004.04.011;
RA Stoss O., Novoyatleva T., Gencheva M., Olbrich M., Benderska N., Stamm S.;
RT "p59(fyn)-mediated phosphorylation regulates the activity of the tissue-
RT specific splicing factor rSLM-1.";
RL Mol. Cell. Neurosci. 27:8-21(2004).
RN [2]
RP FUNCTION, AND INTERACTION WITH RBMX.
RX PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC alternative splicing and influences mRNA splice site selection and exon
CC inclusion. Its phosphorylation by FYN inhibits its ability to regulate
CC splice site selection. Induces an increased concentration-dependent
CC incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich
CC exonic enhancer. May function as an adapter protein for Src kinases
CC during mitosis (By similarity). Binds both poly(A) and poly(U)
CC homopolymers (By similarity). Phosphorylation by PTK6 inhibits its RNA-
CC binding ability (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15345239}.
CC -!- SUBUNIT: Self-associates to form homooligomers. Interacts with SAFB,
CC SFRS9 and YTHDC1. Found in a complex with KHDRBS1, KHDRBS2 and KHDRBS3.
CC Interacts with RBMX (By similarity). Interacts with the SH3 domains of
CC FYN and PLCG1 (By similarity). Interacts with the SH2 domains of FYN,
CC GRAP2, PLCG1 and RASA1 (By similarity). Interacts with RBMX.
CC {ECO:0000250, ECO:0000269|PubMed:15345239,
CC ECO:0000269|PubMed:19282290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9WU01}.
CC -!- TISSUE SPECIFICITY: Expressed in the cortex, cerebellum, striatum,
CC midbrain, brainstem and thalamus of the brain (at protein level).
CC Expressed in neurons (at protein level). Expressed in brain and testis.
CC Expressed in the dentate gyrus of the hippocampus.
CC {ECO:0000269|PubMed:15345239}.
CC -!- PTM: Methylated. {ECO:0000250|UniProtKB:Q5VWX1}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN. Tyrosine
CC phosphorylated by PTK6 and SRC (By similarity). Tyrosine phosphorylated
CC by SRC during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9WU01}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}.
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DR EMBL; AF305618; AAL09360.1; -; mRNA.
DR RefSeq; NP_579852.1; NM_133318.1.
DR AlphaFoldDB; Q920F3; -.
DR SMR; Q920F3; -.
DR STRING; 10116.ENSRNOP00000016579; -.
DR CarbonylDB; Q920F3; -.
DR iPTMnet; Q920F3; -.
DR PhosphoSitePlus; Q920F3; -.
DR jPOST; Q920F3; -.
DR PaxDb; Q920F3; -.
DR PRIDE; Q920F3; -.
DR Ensembl; ENSRNOT00000016578; ENSRNOP00000016579; ENSRNOG00000012284.
DR GeneID; 170843; -.
DR KEGG; rno:170843; -.
DR UCSC; RGD:621738; rat.
DR CTD; 202559; -.
DR RGD; 621738; Khdrbs2.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000157134; -.
DR HOGENOM; CLU_034976_0_0_1; -.
DR InParanoid; Q920F3; -.
DR OMA; HETYEEY; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; Q920F3; -.
DR TreeFam; TF314878; -.
DR Reactome; R-RNO-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR PRO; PR:Q920F3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000012284; Expressed in frontal cortex and 2 other tissues.
DR Genevisible; Q920F3; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; ISO:RGD.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:RGD.
DR GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032571; Qua1_dom.
DR InterPro; IPR032335; Sam68-YY.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16274; Qua1; 1.
DR Pfam; PF16568; Sam68-YY; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; SH3-binding; Transcription; Transcription regulation.
FT CHAIN 1..349
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 2"
FT /id="PRO_0000308955"
FT DOMAIN 65..135
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 181..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU01"
FT MOD_RES 240
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU01"
SQ SEQUENCE 349 AA; 38854 MW; B8566F0211C1D942 CRC64;
MGEEKYLPEL MAEKDSLDPS FVHASRLLAE EIEKFQGSDG RKEDEEKKYL DVISNKNIKL
SERVLIPVKQ YPKFNFVGKL LGPRGNSLKR LQEETGAKMS ILGKGSMRDK AKEEELRKSG
EAKYAHLSDE LHVLIEVFAP PGEAYSRMSH ALEEIKKFLV PDYNDEIRQE QLRELSYLNG
SEESGRGRGI RGRGIRITPT APSRGRGGAV PPPPPPGRGV LTPRGTTVTR GALPVPPVAR
GVPTPRARGT AAVPGYRAPP PPAPEAYEEY GYDDGYGGEY DDQTYEAYDN SYVTPTQSVP
EYYDYGHGVN EDAYDSYAPE EWTTTRSSLK APPPRSARGG YREHPYGRY
