ID F1MIB2_BOVIN Unreviewed; 1268 AA.
AC F1MIB2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cyclin G associated kinase {ECO:0000313|Ensembl:ENSBTAP00000025537.5};
GN Name=GAK {ECO:0000313|Ensembl:ENSBTAP00000025537.5,
GN ECO:0000313|VGNC:VGNC:29211};
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 {ECO:0000313|Ensembl:ENSBTAP00000025537.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000025537.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025537.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000025537.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025537.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; F1MIB2; -.
DR SMR; F1MIB2; -.
DR STRING; 9913.ENSBTAP00000025537; -.
DR PaxDb; 9913-ENSBTAP00000025537; -.
DR Ensembl; ENSBTAT00000025537.5; ENSBTAP00000025537.5; ENSBTAG00000019188.5.
DR VEuPathDB; HostDB:ENSBTAG00000019188; -.
DR VGNC; VGNC:29211; GAK.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000159527; -.
DR HOGENOM; CLU_007537_0_0_1; -.
DR InParanoid; F1MIB2; -.
DR OMA; HYKNTNL; -.
DR TreeFam; TF105165; -.
DR Reactome; R-BTA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-BTA-8856828; Clathrin-mediated endocytosis.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000019188; Expressed in spermatid and 107 other cell types or tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0072318; P:clathrin coat disassembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0090160; P:Golgi to lysosome transport; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:1905443; P:regulation of clathrin coat assembly; IEA:Ensembl.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd14564; PTP_GAK; 1.
DR CDD; cd14036; STKc_GAK; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR PANTHER; PTHR22967:SF105; CYCLIN-G-ASSOCIATED KINASE; 1.
DR PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 40..317
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 388..555
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 561..699
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1204..1268
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 738..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 138075 MW; ED67E6ECE7AA2B85 CRC64;
MSLLQSALDF LAGPGSLGGA AGRDQTDFVG QTVEMGELRL RVRRVLAEGG FAFVYEAQDL
GSGREYALKR LLSNEEEKNR AIIQEVCFMK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
LLMELCRGQL VEFLKKVESK GPLSCDTVLK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
LSNQGTIKLC DFGSATTISH YPDYSWSAQR RALVEEEITR NTTPMYRTPE IVDLYSNFPI
GEKQDIWALG CILYLLCFGQ HPFEDGAKLR IVNGKYAIPA DDTRYSVFHS LIRSMLKVNP
EERLSVTELV NQLQEIAAAR NVNPKSPITE LLEQNGGYGH AAPPGSTGSS LVVTEYEQPY
GGFLDILRGG TERLFTNIKD TSSKVIQSVA NYAKGDLDIS YITSRIAVMS FPAEGVESAI
KNNIEDVRLF LDSKHPGRYA VYNLSPRTYR PSKFHNRVSD CGWVARRAPS LRSLYSLCRN
MHAWLRRDPG NVCVVHCMDG RAVSAVAVCS FLCFCRLFST AEAAVYMFSM KRCPPGIWPS
HKRYIEYMCD MVAEEPVTPH SKPILVKAVV MTPVPLFSKQ RSGCRPFCEV YVGDERVTTT
SQEYDKMRDF KIEDGKAVIP LGITVQGDVL IIIYHARSTL GGRLQAKMAS MKMFQIQFHT
GFVPRNAATV KFAKYDLDAC DIQEKYPDLF QVSLEVEVEP RDRPGHEAPP WEGAGMRGLN
PKILFSSREE QQDVLSKFGK PELPRQPGST AQYDAEAGPA DAEPPESDSP HSSVDADHFL
HTLDWREDRD SSVGPEGHLA EEGPSAVAED GCVSEPSDEE APTPSAESGD TGDEDVPAPA
APQDDSVDLL GLHAEAGPVP APQAPGGPPS NADLLGCLLG APGPAPEGAV GGLLDGDAAL
VFSSPAPAPC TQTTAPAADP FGPLLLPPDV DTPPSSQPDL FGEFLNSDAP AAQPAPFPST
HSAPPPACST DFLHLGDLPA EPSKMTASAS HPDLLGAWDA WAEAPAPALA ADGTFFSPGD
QPAPSGLPAG QTKSQSQDPF ADLGDLSAGL QGSPAAAAPG GFGPKAAPPP KASSSWQTSR
PPAQGTPWPP QAKPPPKASV PPRPNYTSSF SVIGSREERG VRAPSFGPKP RVSENDFEDL
LSNQGFSSRA DRKGPRTIAE MRRQDQARDL DPLKLKLLEW TEGKERNIRA LLSTLHTALW
DGESRWTPVG MADLVTPAQV KKHYRRAVLV VHPDKARGQP YEQYARMIFM ELNDAWAEFE
SQGSRPLF
//
