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GKAP1_HUMAN
ID   GKAP1_HUMAN             Reviewed;         366 AA.
AC   Q5VSY0; Q96LI0; Q9BYI1; Q9BYI2; Q9H225;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=G kinase-anchoring protein 1;
DE   AltName: Full=cGMP-dependent protein kinase-anchoring protein of 42 kDa;
GN   Name=GKAP1; Synonyms=GKAP42; ORFNames=FKSG21;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=10671526; DOI=10.1074/jbc.275.7.4897;
RA   Yuasa K., Omori K., Yanaka N.;
RT   "Binding and phosphorylation of a novel male germ cell-specific cGMP-
RT   dependent protein kinase-anchoring protein by cGMP-dependent protein kinase
RT   Ialpha.";
RL   J. Biol. Chem. 275:4897-4905(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Wang Y.-G., Gong L.;
RT   "Cloning of FKSG21, a novel gene located on human chromosome 9.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-366 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=16015647; DOI=10.1002/gcc.20236;
RA   Sweetser D.A., Peniket A.J., Haaland C., Blomberg A.A., Zhang Y.,
RA   Zaidi S.T., Dayyani F., Zhao Z., Heerema N.A., Boultwood J., Dewald G.W.,
RA   Paietta E., Slovak M.L., Willman C.L., Wainscoat J.S., Bernstein I.D.,
RA   Daly S.B.;
RT   "Delineation of the minimal commonly deleted segment and identification of
RT   candidate tumor-suppressor genes in del(9q) acute myeloid leukemia.";
RL   Genes Chromosomes Cancer 44:279-291(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Regulates insulin-dependent IRS1 tyrosine phosphorylation in
CC       adipocytes by modulating the availability of IRS1 to IR tyrosine
CC       kinase. Its association with IRS1 is required for insulin-induced
CC       translocation of SLC2A4 to the cell membrane. Involved in TNF-induced
CC       impairment of insulin-dependent IRS1 tyrosine phosphorylation.
CC       {ECO:0000250|UniProtKB:Q9JMB0}.
CC   -!- SUBUNIT: Interacts with PRKG1 and IRS1. {ECO:0000250|UniProtKB:Q9JMB0}.
CC   -!- INTERACTION:
CC       Q5VSY0; B0YJ76: DYR; NbExp=3; IntAct=EBI-743722, EBI-10175413;
CC       Q5VSY0; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-743722, EBI-11986315;
CC       Q5VSY0; Q5VSY0: GKAP1; NbExp=4; IntAct=EBI-743722, EBI-743722;
CC       Q5VSY0; Q8N4P3: HDDC3; NbExp=3; IntAct=EBI-743722, EBI-750003;
CC       Q5VSY0; Q63ZY3: KANK2; NbExp=5; IntAct=EBI-743722, EBI-2556193;
CC       Q5VSY0; Q92993: KAT5; NbExp=3; IntAct=EBI-743722, EBI-399080;
CC       Q5VSY0; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-743722, EBI-739909;
CC       Q5VSY0; P55081: MFAP1; NbExp=3; IntAct=EBI-743722, EBI-1048159;
CC       Q5VSY0; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-743722, EBI-742459;
CC       Q5VSY0; Q8TCD6: PHOSPHO2; NbExp=3; IntAct=EBI-743722, EBI-2861380;
CC       Q5VSY0; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-743722, EBI-1504830;
CC       Q5VSY0; O00560: SDCBP; NbExp=3; IntAct=EBI-743722, EBI-727004;
CC       Q5VSY0; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-743722, EBI-597063;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9JMB0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5VSY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5VSY0-2; Sequence=VSP_030596;
CC   -!- SIMILARITY: Belongs to the GKAP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAW62665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB033131; BAB40454.1; -; mRNA.
DR   EMBL; AB033132; BAB40455.1; -; mRNA.
DR   EMBL; AF319476; AAG40320.1; -; mRNA.
DR   EMBL; AL354733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62665.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471089; EAW62666.1; -; Genomic_DNA.
DR   EMBL; BC014476; AAH14476.1; -; mRNA.
DR   EMBL; AK058198; BAB71712.1; ALT_INIT; mRNA.
DR   CCDS; CCDS35049.1; -. [Q5VSY0-1]
DR   CCDS; CCDS47988.1; -. [Q5VSY0-2]
DR   RefSeq; NP_001129425.1; NM_001135953.1. [Q5VSY0-2]
DR   RefSeq; NP_079487.2; NM_025211.3. [Q5VSY0-1]
DR   RefSeq; XP_005252298.1; XM_005252241.2. [Q5VSY0-1]
DR   RefSeq; XP_011517360.1; XM_011519058.2. [Q5VSY0-1]
DR   AlphaFoldDB; Q5VSY0; -.
DR   SMR; Q5VSY0; -.
DR   BioGRID; 123231; 49.
DR   DIP; DIP-47324N; -.
DR   IntAct; Q5VSY0; 29.
DR   MINT; Q5VSY0; -.
DR   STRING; 9606.ENSP00000365550; -.
DR   iPTMnet; Q5VSY0; -.
DR   PhosphoSitePlus; Q5VSY0; -.
DR   BioMuta; GKAP1; -.
DR   DMDM; 166224631; -.
DR   EPD; Q5VSY0; -.
DR   jPOST; Q5VSY0; -.
DR   MassIVE; Q5VSY0; -.
DR   MaxQB; Q5VSY0; -.
DR   PaxDb; Q5VSY0; -.
DR   PeptideAtlas; Q5VSY0; -.
DR   PRIDE; Q5VSY0; -.
DR   ProteomicsDB; 65286; -. [Q5VSY0-1]
DR   ProteomicsDB; 65287; -. [Q5VSY0-2]
DR   Antibodypedia; 27552; 171 antibodies from 23 providers.
DR   DNASU; 80318; -.
DR   Ensembl; ENST00000376365.7; ENSP00000365544.3; ENSG00000165113.13. [Q5VSY0-2]
DR   Ensembl; ENST00000376371.7; ENSP00000365550.2; ENSG00000165113.13. [Q5VSY0-1]
DR   GeneID; 80318; -.
DR   KEGG; hsa:80318; -.
DR   MANE-Select; ENST00000376371.7; ENSP00000365550.2; NM_025211.4; NP_079487.2.
DR   UCSC; uc004amy.4; human. [Q5VSY0-1]
DR   CTD; 80318; -.
DR   DisGeNET; 80318; -.
DR   GeneCards; GKAP1; -.
DR   HGNC; HGNC:17496; GKAP1.
DR   HPA; ENSG00000165113; Group enriched (skeletal muscle, testis).
DR   MIM; 611356; gene.
DR   neXtProt; NX_Q5VSY0; -.
DR   OpenTargets; ENSG00000165113; -.
DR   PharmGKB; PA134880503; -.
DR   VEuPathDB; HostDB:ENSG00000165113; -.
DR   eggNOG; ENOG502QUT6; Eukaryota.
DR   GeneTree; ENSGT00390000008742; -.
DR   HOGENOM; CLU_065161_1_0_1; -.
DR   InParanoid; Q5VSY0; -.
DR   OMA; RKNHQGR; -.
DR   OrthoDB; 1595194at2759; -.
DR   PhylomeDB; Q5VSY0; -.
DR   TreeFam; TF328459; -.
DR   PathwayCommons; Q5VSY0; -.
DR   SignaLink; Q5VSY0; -.
DR   SIGNOR; Q5VSY0; -.
DR   BioGRID-ORCS; 80318; 21 hits in 1080 CRISPR screens.
DR   ChiTaRS; GKAP1; human.
DR   GenomeRNAi; 80318; -.
DR   Pharos; Q5VSY0; Tdark.
DR   PRO; PR:Q5VSY0; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q5VSY0; protein.
DR   Bgee; ENSG00000165113; Expressed in sperm and 183 other tissues.
DR   ExpressionAtlas; Q5VSY0; baseline and differential.
DR   Genevisible; Q5VSY0; HS.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   InterPro; IPR026109; GKAP1.
DR   PANTHER; PTHR14899; PTHR14899; 1.
DR   PRINTS; PR02083; GKINASEAP1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Golgi apparatus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..366
FT                   /note="G kinase-anchoring protein 1"
FT                   /id="PRO_0000315654"
FT   REGION          1..95
FT                   /note="Interaction with IRS1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMB0"
FT   REGION          20..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..77
FT                   /evidence="ECO:0000255"
FT   COILED          128..160
FT                   /evidence="ECO:0000255"
FT   COILED          243..353
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        86..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMB0"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMB0"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         106
FT                   /note="Phosphoserine; by PKG"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMB0"
FT   VAR_SEQ         196..246
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10671526"
FT                   /id="VSP_030596"
FT   CONFLICT        325
FT                   /note="Q -> R (in Ref. 2; AAG40320)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  42078 MW;  973D16361756691B CRC64;
     MASAVLSSVP TTASRFALLQ VDSGSGSDSE PGKGKGRNTG KSQTLGSKST TNEKKREKRR
     KKKEQQQSEA NELRNLAFKK IPQKSSHAVC NAQHDLPLSN PVQKDSREEN WQEWRQRDEQ
     LTSEMFEADL EKALLLSKLE YEEHKKEYED AENTSTQSKV MNKKDKRKNH QGKDRPLTVS
     LKDFHSEDHI SKKTEELSSS QTLSHDGGFF NRLEDDVHKI LIREKRREQL TEYNGTDNCT
     AHEHNQEVVL KDGRIERLKL ELERKDAEIQ KLKNVITQWE AKYKEVKARN AQLLKMLQEG
     EMKDKAEILL QVDESQSIKN ELTIQVTSLH AALEQERSKV KVLQAELAKY QGGRKGKRNS
     ESDQCR
 
 
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