KHDR1_CHICK
ID KHDR1_CHICK Reviewed; 433 AA.
AC Q8UUW7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 1;
DE AltName: Full=Src-associated in mitosis 68 kDa protein;
DE Short=Sam68;
GN Name=KHDRBS1 {ECO:0000250|UniProtKB:Q07666};
GN Synonyms=SAM68 {ECO:0000312|EMBL:AAL30071.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL30071.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=B-cell {ECO:0000269|PubMed:12163178};
RX PubMed=12163178; DOI=10.1016/s0014-5793(02)03103-4;
RA Li Q.H., Haga I., Shimizu T., Itoh M., Kurosaki T., Fujisawa J.;
RT "Retardation of the G2-M phase progression on gene disruption of RNA
RT binding protein Sam68 in the DT40 cell line.";
RL FEBS Lett. 525:145-150(2002).
CC -!- FUNCTION: Recruited and tyrosine phosphorylated by several receptor
CC systems, for example the T-cell, leptin and insulin receptors. Once
CC phosphorylated, functions as an adapter protein in signal transduction
CC cascades by binding to SH2 and SH3 domain-containing proteins. Role in
CC G2-M progression in the cell cycle. Represses CBP-dependent
CC transcriptional activation apparently by competing with other nuclear
CC factors for binding to CBP. Also acts as a putative regulator of mRNA
CC stability and/or translation rates and mediates mRNA nuclear export.
CC Plays a role in the regulation of alternative splicing and influences
CC mRNA splice site selection and exon inclusion.
CC {ECO:0000250|UniProtKB:Q07666, ECO:0000250|UniProtKB:Q60749,
CC ECO:0000269|PubMed:12163178}.
CC -!- SUBUNIT: Self-associates to form homooligomers when bound to RNA,
CC oligomerization appears to be limited when binding to proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07666}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q07666}. Membrane
CC {ECO:0000250|UniProtKB:Q07666}. Note=Predominantly located in the
CC nucleus but also located partially in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q07666}.
CC -!- DOMAIN: The KH domain is required for binding to RNA.
CC {ECO:0000250|UniProtKB:Q60749}.
CC -!- PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases
CC including LCK, FYN and JAK3. {ECO:0000250|UniProtKB:Q07666}.
CC -!- PTM: Acetylated. Positively correlates with ability to bind RNA (By
CC similarity). {ECO:0000250|UniProtKB:Q07666}.
CC -!- PTM: Methylated by HRMT1L2. Required for nuclear localization (By
CC similarity). {ECO:0000250|UniProtKB:Q07666}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}.
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DR EMBL; AY057837; AAL30071.1; -; mRNA.
DR RefSeq; NP_989561.1; NM_204230.1.
DR AlphaFoldDB; Q8UUW7; -.
DR SMR; Q8UUW7; -.
DR STRING; 9031.ENSGALP00000005166; -.
DR PaxDb; Q8UUW7; -.
DR PRIDE; Q8UUW7; -.
DR GeneID; 374071; -.
DR KEGG; gga:374071; -.
DR CTD; 10657; -.
DR VEuPathDB; HostDB:geneid_374071; -.
DR eggNOG; KOG1588; Eukaryota.
DR InParanoid; Q8UUW7; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; Q8UUW7; -.
DR PRO; PR:Q8UUW7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0046831; P:regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cytoplasm; Membrane; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW SH3-binding; Transcription; Transcription regulation.
FT CHAIN 1..433
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 1"
FT /id="PRO_0000050127"
FT DOMAIN 171..197
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..243
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT REGION 259..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 46504 MW; 7DEAE27358C8EAA8 CRC64;
MQRRDDSSAR MGRGPGGPGS ARQGGPNPRR SPRGGGGRGA GAQHPQPLLT GGAAAGSSGA
QGPAAANPAP LLPGGAVKME PENKYLPELM AEKDSLDPSS THAMQLLSAE IEKIQKGETT
KKDEEENYLD LFSHKNMKLK ERVLIPVKQY PKFNFVGKIL GPQGNTIKRL QEETGAKISV
LGKGSMRDKA KEEELRKGGD PKYAHLNMDL HVFIEVFGPP CEAYALMAHA MEEVKKFLVP
DMMDDICQEQ FLELSYLNGV PEPTRGRGGP VRGRGAAPPP PPPVPRGRGV GPPPPPPPPR
GALVRGAPVR GAIARGAAVA RGVPPPPAVR GAPAPRARAA GIQRIPLPPP PAPETYEEYG
YDDAYADQSY EGYEGYYSQG QGDTEYYDYG HGEAQETYEA YGQDDWNGTR PSLKAPPARP
VKGAYREHPY GRY
