ID A0A2K5MTI5_CERAT Unreviewed; 1311 AA.
AC A0A2K5MTI5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cyclin G associated kinase {ECO:0000313|Ensembl:ENSCATP00000028553.1};
GN Name=GAK {ECO:0000313|Ensembl:ENSCATP00000028553.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000028553.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000028553.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011914720.1; XM_012059330.1.
DR STRING; 9531.ENSCATP00000028553; -.
DR Ensembl; ENSCATT00000052808.1; ENSCATP00000028553.1; ENSCATG00000037531.1.
DR GeneID; 105585505; -.
DR CTD; 2580; -.
DR GeneTree; ENSGT00940000159527; -.
DR OrthoDB; 103262at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037531; Expressed in thymus and 12 other cell types or tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IEA:Ensembl.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
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:UP000233060}.
FT DOMAIN 40..314
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 399..566
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 572..710
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1247..1311
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 710..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 143066 MW; A55CB3AA70B30012 CRC64;
MSLLQSALDF LAGPGSLGGA SGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDV
GSGREYALKR LLSNEEEKNR AIIQEVCFMK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
LLTELCKGQL VEFLKKMESR GPLSCDTVLK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
LSNQGTIKLC DFGSATTISH YPDYSWSAQR RALVEEEITR NTTPMYRTPE IIDLYSNFPI
GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPP HDTQYTVFHS LIRAMLQVNP
EERLSIAEVV HQLQEIAAAR NVNPKSPITE LLEQNGGYGS TVLSRGPPPL VGPAGSGYSG
GLALAEYDQP YGGFLDILRG GTERLFTNLK DTSSKVIQSV ANYAKGDLDI SYITSRIAVM
SFPAEGVESA LKNNIEDVRL FLDSKHPGHY AVYNLSPRTY RPSRFHNRVS ECGWAARRAP
HLHTLYNICR NMHAWLRQDH KNVCIVHCMD GRAASAVAVC SFLCFCRLFS TAEAAVYMFS
MKRCPPGIWP SHKRYIEYMC DMVAEEPITP HSKPILVRAV VMTPVPLFSK QRSGCRPFCE
VYVGDERVAS TSQEYDKMRD FKIEDGKAVI PLGVTVQGDV LIVIYHARST LGGRLQAKMA
SMKMFQIQFH TGFVPRNATT VKFAKYDLDA CDIQEKYPDL FQVNLEVEVE PRDRLSREAP
PWENSSMRGL NPKILFSSRE EQQDILSKFG KPELPRQPGS TAQYDAGAGS PEAEPTDSDS
PPSSSADASR FLHTLDWQEE KEAETGAANA SPKESESALM EDRDESEVSD EGGSPVSSEG
QEPRADPEHP GLAAGLVQQD VVFEVGTPAV LPEPVPQEDG VDLLGLHSEV GAGPAVALQA
LQAPSSNTDL LCCLLGPPEA TSQGPPEDLL GEARLLLASP APPLSMQSTP GGGPPAAADP
FGPLLLSSDS DSQPCSNPDL FGEFLNSDSA AVPPSFPSAH SAPPPSCSAD FLQLGDLPGE
PSKMTASSSN PDLLGGWAAW TETAASAVAP TPATEGPLFS PGGQPAPCGP QASWTKSQNP
DPFADLGDLS SGLQGSPAGF PPGGFIPKTA TTAKGSGSWQ TSRPPAQGAS WPPQAKPPLK
ACTQPRPNYA ANFSVIGARE ERGVRAPSFA QKPKVSENDF EDLLPNQGFS SRSDKKGPKT
IAEMRKQDLA KDTDPLKLKL LDWIEGKERN IRALLSTLHT VLWDGESRWT PVGMADLVAP
EQVKKHYRRA VLAVHPDKAA GQPYEQHAKM IFMELNDAWS EFENQGSRPL F
//
