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Database: UniProt
Entry: A0A2R9AD78_PANPA
LinkDB: A0A2R9AD78_PANPA
Original site: A0A2R9AD78_PANPA 
ID   A0A2R9AD78_PANPA        Unreviewed;      1232 AA.
AC   A0A2R9AD78;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Cyclin G associated kinase {ECO:0000313|Ensembl:ENSPPAP00000015259.1};
GN   Name=GAK {ECO:0000313|Ensembl:ENSPPAP00000015259.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000015259.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000015259.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000015259.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR   EMBL; AJFE02035447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02035448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02035449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9AD78; -.
DR   Ensembl; ENSPPAT00000037949.1; ENSPPAP00000015259.1; ENSPPAG00000030635.1.
DR   GeneTree; ENSGT00940000159527; -.
DR   OMA; HYKNTNL; -.
DR   Proteomes; UP000240080; Chromosome 4.
DR   Bgee; ENSPPAG00000030635; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd14564; PTP_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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT   DOMAIN          1..235
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          320..487
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          493..631
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1168..1232
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          630..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1049
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1065
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1232 AA;  134415 MW;  18AFA82632644C61 CRC64;
     MSLLQSALDF LAGPGSLGGA SGRDQSDFVG QTVELGELRL RVRRVLAEGQ LVEFLKKMES
     RGPLSCDTVL KIFYQTCRAV QHMHRQKPPI IHRDLKVENL LLSNQGTIKL CDFGSATTIS
     HYPDYSWSAQ RRALVEEEIT RNTTPMYRTP EIIDLYSNFP IGEKQDIWAL GCILYLLCFR
     QHPFEDGAKL RIVNGKYSIP PHDTQYTVFH SLIRAMLQVN PEERLSIAEV VHQLQEIAAA
     RNVNPKSPIT ELLEQNGGYG SATLSRGPPP PVGPAGSGYS GGLALAEYDQ PYGGFLDILR
     GGTERLFTNL KDTSSKVIQS VANYAKGDLD ISYITSRIAV MSFPAEGVES ALKNNIEDVR
     LFLDSKHPGH YAVYNLSPRT YRPSRFHNRV SECGWAARRA PHLHTLYNIC RNMHAWLRQD
     HKNVCVVHCM DGRAASAVAV CSFLCFCRLF STAEAAVYMF SMKRCPPGIW PSHKRYIEYM
     CDMVAEEPIT PHSKPILVRA VVMTPVPLFS KQRSGCRPFC EVYVGDERVA STSQEYDKMR
     DFKIEDGKAV IPLGVTVQGD VLIVIYHARS TLGGRLQAKM ASMKMFQIQF HTGFVPRNAT
     TVKFAKYDLD ACDIQEKYPD LFQVNLEVEV EPRDRPSREA PPWENSSMRG LNPKILFSSR
     EEQQDILSKF GKPELPRQPG STAQYDAGAG SPEAEPTDSD SPPSSSADAS HFLHTLDWQE
     EKEAETGAEN ASPKESESAL MEDRDESEVS DDGGSPISSE GQEPRADPEP PGLAAGPVQQ
     DLVFEVETPA VLPEPVPQED GVDLLGLHSE VGAGPAVPPQ ACKAPSSNTD LLSCLLGPPE
     AASQGPPEDL LSEDPLLLAS PAPPLSVQST PRGGPPAAAD PFGPLLPSSG NNSQPCSNPD
     LFGEFLNSDS VTVPPSFPSA HSAPPPSCSA DFLHLGDLPG EPSKMTASSS NPDLLGGWAA
     WTETAASAVA PTPATEGPLF SSGGQPAPCG SQASWTKSQN PDPFADLGDL SSGLQGSPAG
     FPPGGFIPKT ATTPKGSSSW QTSRPPAQGA SWPPQAKPPP KACTQPRPNY ASNFSVIGAR
     EERGVRAPSF AQKPKVSEND FEDLLSNQGF SSRSDKKGPK TIAEMRKQDL AKDTDPLKLK
     LLDWIEGKER NIRALLSTLH TVLWDGESRW TPVGMADLVA PEQVKKHYRR AVLAVHPDKA
     AGQPYEQHAK MIFMELNDAW SEFENQGSRP LF
//
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