DOK1_BOVIN
ID DOK1_BOVIN Reviewed; 483 AA.
AC Q5EA84;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Docking protein 1;
DE AltName: Full=Downstream of tyrosine kinase 1;
GN Name=DOK1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding
CC proteins. They provide a docking platform for the assembly of
CC multimolecular signaling complexes. DOK1 appears to be a negative
CC regulator of the insulin signaling pathway. Modulates integrin
CC activation by competing with talin for the same binding site on ITGB3
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts
CC directly with phosphorylated ITGB3 (By similarity). Interacts with SRMS
CC (via the SH2 and SH3 domains) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Constitutively tyrosine-phosphorylated (By similarity).
CC Phosphorylated by TEC. Phosphorylated by LYN (By similarity).
CC Phosphorylated on tyrosine residues by the insulin receptor kinase.
CC Results in the negative regulation of the insulin signaling pathway (By
CC similarity). Phosphorylated on tyrosine residues by SRMS (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR EMBL; BT020685; AAX08702.1; -; mRNA.
DR RefSeq; NP_001019714.2; NM_001024543.2.
DR AlphaFoldDB; Q5EA84; -.
DR SMR; Q5EA84; -.
DR STRING; 9913.ENSBTAP00000024727; -.
DR PaxDb; Q5EA84; -.
DR GeneID; 514962; -.
DR KEGG; bta:514962; -.
DR CTD; 1796; -.
DR eggNOG; KOG4047; Eukaryota.
DR InParanoid; Q5EA84; -.
DR OrthoDB; 378139at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR037751; Dok1/2/3_PTB.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..483
FT /note="Docking protein 1"
FT /id="PRO_0000187267"
FT DOMAIN 4..119
FT /note="PH"
FT DOMAIN 151..259
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 293..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 296
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 377
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 398
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 451
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
SQ SEQUENCE 483 AA; 52206 MW; 46A4BCFEFC0B3696 CRC64;
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS GGGRGSSRRL
DCKVIRLAEC VSVAPVAVES PPEPGAASFR LDTAQRSHLL AADAPSSAAW VQTLCQNAFP
KGSWALAPAE NPPKLSALEM LENSLYSPSW EGSQFWVTVQ KTEAAERCGL HGSYVLRVEA
ERLTLLAPGA QRQILEPLLF WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND
IFQAVETAIH RQKIQGKAGQ GQDVLRADSH EGEVADGKLA SLAAPLELPG SPPALYSEPL
DSLRIPPGPS QDSLYSDPLD STPARAGEGT QLKKALYWDL CEHVQQKLIK AKLTDPKEDP
IYDEPEGLAP ATLRGLYDLP QEPKDAWWCQ ARVKEEGYEL PYNPAMDDYA VPPPRSTKPF
PAPKPQGLAL SESGAATGSG SQGHSSDTAL YSQVQKSGAS GSWDCGLSGV VTDRTGAKSE
GST
