CAP1_HUMAN
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 03-AUG-2022, entry version 207.
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; 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; 86.
DR CORUM; Q01518; -.
DR DIP; DIP-62063N; -.
DR IntAct; Q01518; 36.
DR MINT; Q01518; -.
DR STRING; 9606.ENSP00000361883; -.
DR CarbonylDB; Q01518; -.
DR GlyGen; Q01518; 2 sites, 2 O-linked glycans (2 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; Q01518; -.
DR PeptideAtlas; Q01518; -.
DR PRIDE; Q01518; -.
DR ProteomicsDB; 57962; -. [Q01518-1]
DR ProteomicsDB; 57963; -. [Q01518-2]
DR Antibodypedia; 32000; 216 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 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; LDGNKWI; -.
DR OrthoDB; 1098760at2759; -.
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; 304 hits in 1075 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 210 other 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:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
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:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.330; -; 1.
DR Gene3D; 2.160.20.70; -; 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; IPR028415; CAP1.
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; PTHR10652; 1.
DR PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 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