GAK_RAT
ID GAK_RAT Reviewed; 1305 AA.
AC P97874;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cyclin-G-associated kinase;
DE EC=2.7.11.1;
GN Name=Gak;
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].
RC TISSUE=Kidney;
RX PubMed=9013862; DOI=10.1016/s0014-5793(96)01484-6;
RA Kanaoka Y., Kimura S.H., Okazaki I., Ikeda M., Nojima H.;
RT "GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain.";
RL FEBS Lett. 402:73-80(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-16; SER-809; SER-824
RP AND SER-827, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin
CC homolog that is involved in the uncoating of clathrin-coated vesicles
CC by Hsc70 in non-neuronal cells. Expression oscillates slightly during
CC the cell cycle, peaking at G1 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell junction,
CC focal adhesion {ECO:0000250}. Note=Localizes to the perinuclear area
CC and to the trans-Golgi network. Also seen on the plasma membrane,
CC probably at focal adhesions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D38560; BAA18911.1; -; mRNA.
DR PIR; T31096; T31096.
DR RefSeq; NP_112292.1; NM_031030.2.
DR AlphaFoldDB; P97874; -.
DR SMR; P97874; -.
DR BioGRID; 249559; 1.
DR IntAct; P97874; 2.
DR MINT; P97874; -.
DR STRING; 10116.ENSRNOP00000000064; -.
DR iPTMnet; P97874; -.
DR PhosphoSitePlus; P97874; -.
DR jPOST; P97874; -.
DR PaxDb; P97874; -.
DR PRIDE; P97874; -.
DR GeneID; 81659; -.
DR KEGG; rno:81659; -.
DR UCSC; RGD:621589; rat.
DR CTD; 2580; -.
DR RGD; 621589; Gak.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; P97874; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; P97874; -.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P97874; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0030332; F:cyclin binding; IDA:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0072318; P:clathrin coat disassembly; ISO:RGD.
DR GO; GO:1905224; P:clathrin-coated pit assembly; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0009913; P:epidermal cell differentiation; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0048853; P:forebrain morphogenesis; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:RGD.
DR GO; GO:0035622; P:intrahepatic bile duct development; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00226; DnaJ; 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; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell junction; Cytoplasm;
KW Golgi apparatus; Kinase; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT CHAIN 2..1305
FT /note="Cyclin-G-associated kinase"
FT /id="PRO_0000085960"
FT DOMAIN 40..315
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 397..564
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 570..708
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1241..1305
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 1122
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99KY4"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
SQ SEQUENCE 1305 AA; 143703 MW; 6D36BD38011C44EE CRC64;
MSLLQSALDF LAGPGSLGGA AGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDL
GSGREYALKR LLSNEEEKNR AIIQEVCFLK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
LLTELCKGQL VEFLRRVECK GPLSCDSILK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
LSNQGTIKLC DFGSATTISH YPDYSWSAQK RAMVEEEITR NTTPMYRTPE IVDLYSNFPI
GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPV NDTRYTVFHD LIRGMLKVNP
EERLSIAEVV RQLQEIAAAR NVNPKAPITE LLEQNGGYGN SGPSRAQPPS GGPVNSSGVL
ALAEYDQPYG GFLDILRGGT ERLFTNLKDT SSKVIQSVAN YAKGDLDISY ITSRIAVMSF
PAEGVESAIK NNIEDVRLFL DAKHPGHYAV YNLSPRIYRA SKFHNRVTEC GWAVRRAPHL
HSLYTLCRSM HAWLREDHRN VCVVHCMDGR AASAVAVCAF LCFCRLFSTA EAAVYMFSMK
RCPPGIWPSH KRYIEYVCDM VAEEPITPHS KPMLVKSVVM TPVPLFSKQR NGCRPFCEVY
VGEERVTTTS QEYDRMKEFK IEDGKAVIPL GITVQGDVLT IIYHARSTLG GRLQAKMASM
KMFQIQFHTG FVPRNATTVK FAKYDLDACD IQEKYPDLFQ VNLEVEVEPR DRPSRDVPPW
ENTSLRGLNP KILFSNREEQ QDILSKFGKP ELPRQPGSTA QYDAEAGSPE AEITESDSPQ
SSSTDTNHFL HTLDWQEEKD PETGVDNTSP KESQSNLIAD GDGSEVSDEE EASCPSEERK
PGAGEDTPRL AAGTRQQDLI FDVGMLAAPQ EPVQPEEGVD LLGLHSEGDL RPAAPLQASG
VQSSNTDLLS SLLEPSDASQ VGPPGDLLGG ETPLLLASPV SLLGVQSNLQ GKVPDTVDPF
DQFLLPSSSD TQPCSKPDLF GEFLNSDSVA SSTAFPSTHS APPPSCSTAF LHLGDLPAEP
NKVIASSSHP DLLGGWDTWA ETALPGPASM PVPEGTLFSS AGHPAPPGPN PSQTKSQNPD
PFADLSDLSS SLQGLPAGLP AGSFVGTSAT THKSNSSWQT TRPTAPGTSW PPQAKPAPRA
SEQLRSHFSV IGAREERGVR APSFAQKPKV SENDFEDLLP NQGFSKSDKK GPKTMAEMRK
QELARDTDPF KLKLLDWIEG KERNIRALLS TLHTVLWDGE SRWTPVSMAD LVTPEQVKKQ
YRRAVLVVHP DKATGQPYEQ SAKMIFMELN DAWSEFENQG SRPLF
