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Database: UniProt
Entry: Q01518
LinkDB: Q01518
Original site: Q01518 
ID   CAP1_HUMAN              Reviewed;         475 AA.
AC   Q01518; Q53HR7; Q5T0S1; Q5T0S2; Q6I9U6;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 5.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=Adenylyl cyclase-associated protein 1;
DE            Short=CAP 1;
GN   Name=CAP1; Synonyms=CAP;
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] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
RP   SER-245; GLY-247; ASP-249 AND ALA-256.
RX   PubMed=1406678; DOI=10.1128/mcb.12.11.5033-5040.1992;
RA   Matviw H., Yu G., Young D.;
RT   "Identification of a human cDNA encoding a protein that is structurally and
RT   functionally related to the yeast adenylyl cyclase-associated CAP
RT   proteins.";
RL   Mol. Cell. Biol. 12:5033-5040(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
RP   SER-245; GLY-247; ASP-249 AND ALA-256.
RA   Kawamukai M., O'Neill K., Rodgers L., Riggs M., Schaller H.C., Chalfie M.,
RA   Field J., Wigler M.;
RT   "Genes from metazoans encoding homologs of yeast adenylyl cyclase-
RT   associated proteins.";
RL   Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-229;
RP   GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-229;
RP   GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-229;
RP   GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC   TISSUE=Adipose tissue;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-229;
RP   GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC   TISSUE=Kidney;
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   [8]
RP   PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using sequential
RT   IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-308 AND SER-310, AND
RP   IDENTIFICATION BY 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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; SER-308 AND SER-310, AND
RP   IDENTIFICATION BY 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   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-290; SER-295;
RP   SER-301; SER-308 AND SER-310, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-310, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [24]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [25]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 319-475.
RX   PubMed=15311924; DOI=10.1021/bi049071r;
RA   Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
RA   Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T., Godzik A.,
RA   Almo S.C.;
RT   "Crystal structure of the actin binding domain of the cyclase-associated
RT   protein.";
RL   Biochemistry 43:10628-10641(2004).
CC   -!- FUNCTION: Directly regulates filament dynamics and has been implicated
CC       in a number of complex developmental and morphological processes,
CC       including mRNA localization and the establishment of cell polarity.
CC   -!- SUBUNIT: Homodimer. Binds actin monomers.
CC   -!- INTERACTION:
CC       Q01518; P13569: CFTR; NbExp=14; IntAct=EBI-2808398, EBI-349854;
CC       Q01518; P0DTC3: 3a; Xeno; NbExp=3; IntAct=EBI-2808398, EBI-25475894;
CC       Q01518; Q2GHU2: ECH_0166; Xeno; NbExp=4; IntAct=EBI-2808398, EBI-26585631;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q01518-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q01518-2; Sequence=VSP_036038;
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR   EMBL; M98474; AAA35648.1; -; mRNA.
DR   EMBL; L12168; AAA35507.1; -; mRNA.
DR   EMBL; BT007152; AAP35816.1; -; mRNA.
DR   EMBL; CR457409; CAG33690.1; -; mRNA.
DR   EMBL; AK222513; BAD96233.1; -; mRNA.
DR   EMBL; AL512599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013963; AAH13963.1; -; mRNA.
DR   EMBL; BC095440; AAH95440.1; -; mRNA.
DR   CCDS; CCDS41309.1; -. [Q01518-1]
DR   CCDS; CCDS81304.1; -. [Q01518-2]
DR   PIR; A48120; A48120.
DR   RefSeq; NP_001099000.1; NM_001105530.1. [Q01518-1]
DR   RefSeq; NP_006358.1; NM_006367.3. [Q01518-1]
DR   RefSeq; XP_005270425.1; XM_005270368.1.
DR   RefSeq; XP_011538811.1; XM_011540509.1.
DR   RefSeq; XP_011538812.1; XM_011540510.1. [Q01518-1]
DR   RefSeq; XP_011538813.1; XM_011540511.1.
DR   RefSeq; XP_011538814.1; XM_011540512.1.
DR   RefSeq; XP_011538815.1; XM_011540513.2.
DR   RefSeq; XP_011538816.1; XM_011540514.1.
DR   RefSeq; XP_011538817.1; XM_011540515.1. [Q01518-2]
DR   RefSeq; XP_016855556.1; XM_017000067.1.
DR   RefSeq; XP_016855557.1; XM_017000068.1.
DR   RefSeq; XP_016855558.1; XM_017000069.1. [Q01518-1]
DR   RefSeq; XP_016855559.1; XM_017000070.1.
DR   RefSeq; XP_016855560.1; XM_017000071.1.
DR   RefSeq; XP_016855561.1; XM_017000072.1.
DR   PDB; 1K8F; X-ray; 2.80 A; A/B/C/D=319-475.
DR   PDBsum; 1K8F; -.
DR   AlphaFoldDB; Q01518; -.
DR   SMR; Q01518; -.
DR   BioGRID; 115750; 177.
DR   CORUM; Q01518; -.
DR   DIP; DIP-62063N; -.
DR   IntAct; Q01518; 37.
DR   MINT; Q01518; -.
DR   STRING; 9606.ENSP00000361883; -.
DR   CarbonylDB; Q01518; -.
DR   GlyCosmos; Q01518; 2 sites, 2 glycans.
DR   GlyGen; Q01518; 3 sites, 2 O-linked glycans (3 sites).
DR   iPTMnet; Q01518; -.
DR   MetOSite; Q01518; -.
DR   PhosphoSitePlus; Q01518; -.
DR   SwissPalm; Q01518; -.
DR   BioMuta; CAP1; -.
DR   DMDM; 308153681; -.
DR   OGP; Q01518; -.
DR   REPRODUCTION-2DPAGE; IPI00639931; -.
DR   CPTAC; CPTAC-325; -.
DR   CPTAC; CPTAC-326; -.
DR   EPD; Q01518; -.
DR   jPOST; Q01518; -.
DR   MassIVE; Q01518; -.
DR   MaxQB; Q01518; -.
DR   PaxDb; 9606-ENSP00000361883; -.
DR   PeptideAtlas; Q01518; -.
DR   PRIDE; Q01518; -.
DR   ProteomicsDB; 57962; -. [Q01518-1]
DR   ProteomicsDB; 57963; -. [Q01518-2]
DR   Pumba; Q01518; -.
DR   Antibodypedia; 32000; 239 antibodies from 30 providers.
DR   DNASU; 10487; -.
DR   Ensembl; ENST00000340450.7; ENSP00000344832.3; ENSG00000131236.18. [Q01518-2]
DR   Ensembl; ENST00000372792.7; ENSP00000361878.2; ENSG00000131236.18. [Q01518-1]
DR   Ensembl; ENST00000372797.7; ENSP00000361883.3; ENSG00000131236.18. [Q01518-1]
DR   Ensembl; ENST00000372798.5; ENSP00000361884.1; ENSG00000131236.18. [Q01518-2]
DR   Ensembl; ENST00000372802.5; ENSP00000361888.1; ENSG00000131236.18. [Q01518-2]
DR   Ensembl; ENST00000372805.8; ENSP00000361891.3; ENSG00000131236.18. [Q01518-1]
DR   GeneID; 10487; -.
DR   KEGG; hsa:10487; -.
DR   MANE-Select; ENST00000372805.8; ENSP00000361891.3; NM_006367.4; NP_006358.2.
DR   UCSC; uc001cey.5; human. [Q01518-1]
DR   AGR; HGNC:20040; -.
DR   CTD; 10487; -.
DR   DisGeNET; 10487; -.
DR   GeneCards; CAP1; -.
DR   HGNC; HGNC:20040; CAP1.
DR   HPA; ENSG00000131236; Low tissue specificity.
DR   MIM; 617801; gene.
DR   neXtProt; NX_Q01518; -.
DR   OpenTargets; ENSG00000131236; -.
DR   PharmGKB; PA399; -.
DR   VEuPathDB; HostDB:ENSG00000131236; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   GeneTree; ENSGT00390000017955; -.
DR   HOGENOM; CLU_015780_1_1_1; -.
DR   InParanoid; Q01518; -.
DR   OMA; KSQQTHK; -.
DR   OrthoDB; 1453907at2759; -.
DR   PhylomeDB; Q01518; -.
DR   TreeFam; TF313791; -.
DR   PathwayCommons; Q01518; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q01518; -.
DR   SIGNOR; Q01518; -.
DR   BioGRID-ORCS; 10487; 322 hits in 1147 CRISPR screens.
DR   ChiTaRS; CAP1; human.
DR   EvolutionaryTrace; Q01518; -.
DR   GeneWiki; CAP1; -.
DR   GenomeRNAi; 10487; -.
DR   Pharos; Q01518; Tbio.
DR   PRO; PR:Q01518; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q01518; Protein.
DR   Bgee; ENSG00000131236; Expressed in blood and 212 other cell types or tissues.
DR   ExpressionAtlas; Q01518; baseline and differential.
DR   Genevisible; Q01518; HS.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR   GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 1.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR028417; CAP_CS_C.
DR   InterPro; IPR018106; CAP_CS_N.
DR   InterPro; IPR036222; CAP_N_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR10652:SF1; ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   Pfam; PF01213; CAP_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR   SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW   Cell membrane; Direct protein sequencing; Isopeptide bond; Membrane;
KW   Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..475
FT                   /note="Adenylyl cyclase-associated protein 1"
FT                   /id="PRO_0000205696"
FT   DOMAIN          319..453
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          216..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         31
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P40124"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         287
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         307
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   CROSSLNK        348
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   VAR_SEQ         38
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036038"
FT   VARIANT         229
FT                   /note="C -> G (in dbSNP:rs11207440)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028419"
FT   VARIANT         236
FT                   /note="C -> G (in dbSNP:rs6665926)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028420"
FT   VARIANT         245
FT                   /note="I -> S (in dbSNP:rs6665933)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028421"
FT   VARIANT         247
FT                   /note="C -> G (in dbSNP:rs6665936)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028422"
FT   VARIANT         249
FT                   /note="Y -> D (in dbSNP:rs6665937)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028423"
FT   VARIANT         256
FT                   /note="S -> A (in dbSNP:rs6665944)"
FT                   /evidence="ECO:0000269|PubMed:1406678,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_028424"
FT   CONFLICT        374
FT                   /note="N -> S (in Ref. 5; BAD96233)"
FT                   /evidence="ECO:0000305"
FT   STRAND          321..325
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          340..342
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          350..355
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          360..374
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          376..393
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          395..403
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          406..412
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          414..419
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          428..433
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          435..443
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   TURN            444..446
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          447..452
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          456..461
FT                   /evidence="ECO:0007829|PDB:1K8F"
FT   STRAND          463..471
FT                   /evidence="ECO:0007829|PDB:1K8F"
SQ   SEQUENCE   475 AA;  51901 MW;  7789D1FAC0D1AB7B CRC64;
     MADMQNLVER LERAVGRLEA VSHTSDMHRG YADSPSKAGA APYVQAFDSL LAGPVAEYLK
     ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAENK LSDLLAPISE QIKEVITFRE
     KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
     DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAKELSGL PSGPSAGSCP PPPPPCPPPP
     PVSTISCSYE SASRSSLFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPVRSGPKPF
     SAPKPQTSPS PKRATKKEPA VLELEGKKWR VENQENVSNL VIEDTELKQV AYIYKCVNTT
     LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSKDVKVQ VMGKVPTISI NKTDGCHAYL
     SKNSLDCEIV SAKSSEMNVL IPTEGGDFNE FPVPEQFKTL WNGQKLVTTV TEIAG
//
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