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Adenylyl cyclase-associated protein 1 (CAP 1)

 CAP1_HUMAN              Reviewed;         475 AA.
Q01518; Q53HR7; Q5T0S1; Q5T0S2; Q6I9U6;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 5.
22-NOV-2017, entry version 176.
RecName: Full=Adenylyl cyclase-associated protein 1;
Short=CAP 1;
Name=CAP1; Synonyms=CAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
SER-245; GLY-247; ASP-249 AND ALA-256.
PubMed=1406678; DOI=10.1128/MCB.12.11.5033;
Matviw H., Yu G., Young D.;
"Identification of a human cDNA encoding a protein that is
structurally and functionally related to the yeast adenylyl cyclase-
associated CAP proteins.";
Mol. Cell. Biol. 12:5033-5040(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
SER-245; GLY-247; ASP-249 AND ALA-256.
Kawamukai M., O'Neill K., Rodgers L., Riggs M., Schaller H.C.,
Chalfie M., Field J., Wigler M.;
"Genes from metazoans encoding homologs of yeast adenylyl cyclase-
associated proteins.";
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-308 AND
SER-310, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; SER-308 AND
SER-310, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-290; SER-295;
SER-301; SER-308 AND SER-310, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-310, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 319-475.
PubMed=15311924; DOI=10.1021/bi049071r;
Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T.,
Godzik A., Almo S.C.;
"Crystal structure of the actin binding domain of the cyclase-
associated protein.";
Biochemistry 43:10628-10641(2004).
-!- FUNCTION: Directly regulates filament dynamics and has been
implicated in a number of complex developmental and morphological
processes, including mRNA localization and the establishment of
cell polarity.
-!- SUBUNIT: Homodimer. Binds actin monomers.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q01518-1; Sequence=Displayed;
Name=2;
IsoId=Q01518-2; Sequence=VSP_036038;
-!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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EMBL; M98474; AAA35648.1; -; mRNA.
EMBL; L12168; AAA35507.1; -; mRNA.
EMBL; BT007152; AAP35816.1; -; mRNA.
EMBL; CR457409; CAG33690.1; -; mRNA.
EMBL; AK222513; BAD96233.1; -; mRNA.
EMBL; AL512599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013963; AAH13963.1; -; mRNA.
EMBL; BC095440; AAH95440.1; -; mRNA.
CCDS; CCDS41309.1; -. [Q01518-1]
CCDS; CCDS81304.1; -. [Q01518-2]
PIR; A48120; A48120.
RefSeq; NP_001099000.1; NM_001105530.1.
RefSeq; NP_006358.1; NM_006367.3.
RefSeq; XP_005270425.1; XM_005270368.1.
RefSeq; XP_011538811.1; XM_011540509.1.
RefSeq; XP_011538812.1; XM_011540510.1. [Q01518-1]
RefSeq; XP_011538813.1; XM_011540511.1.
RefSeq; XP_011538814.1; XM_011540512.1.
RefSeq; XP_011538815.1; XM_011540513.2.
RefSeq; XP_011538816.1; XM_011540514.1.
RefSeq; XP_011538817.1; XM_011540515.1. [Q01518-2]
RefSeq; XP_016855556.1; XM_017000067.1.
RefSeq; XP_016855557.1; XM_017000068.1.
RefSeq; XP_016855558.1; XM_017000069.1. [Q01518-1]
RefSeq; XP_016855559.1; XM_017000070.1.
RefSeq; XP_016855560.1; XM_017000071.1.
RefSeq; XP_016855561.1; XM_017000072.1.
UniGene; Hs.370581; -.
UniGene; Hs.733189; -.
PDB; 1K8F; X-ray; 2.80 A; A/B/C/D=319-475.
PDBsum; 1K8F; -.
ProteinModelPortal; Q01518; -.
SMR; Q01518; -.
BioGrid; 115750; 54.
CORUM; Q01518; -.
DIP; DIP-62063N; -.
IntAct; Q01518; 8.
MINT; MINT-3024327; -.
STRING; 9606.ENSP00000361878; -.
iPTMnet; Q01518; -.
PhosphoSitePlus; Q01518; -.
SwissPalm; Q01518; -.
BioMuta; CAP1; -.
DMDM; 308153681; -.
OGP; Q01518; -.
REPRODUCTION-2DPAGE; IPI00639931; -.
EPD; Q01518; -.
MaxQB; Q01518; -.
PaxDb; Q01518; -.
PeptideAtlas; Q01518; -.
PRIDE; Q01518; -.
Ensembl; ENST00000340450; ENSP00000344832; ENSG00000131236. [Q01518-2]
Ensembl; ENST00000372792; ENSP00000361878; ENSG00000131236. [Q01518-1]
Ensembl; ENST00000372797; ENSP00000361883; ENSG00000131236. [Q01518-1]
Ensembl; ENST00000372798; ENSP00000361884; ENSG00000131236. [Q01518-2]
Ensembl; ENST00000372802; ENSP00000361888; ENSG00000131236. [Q01518-2]
Ensembl; ENST00000372805; ENSP00000361891; ENSG00000131236. [Q01518-1]
GeneID; 10487; -.
KEGG; hsa:10487; -.
UCSC; uc001cey.5; human. [Q01518-1]
CTD; 10487; -.
DisGeNET; 10487; -.
EuPathDB; HostDB:ENSG00000131236.16; -.
GeneCards; CAP1; -.
HGNC; HGNC:20040; CAP1.
HPA; HPA030124; -.
neXtProt; NX_Q01518; -.
OpenTargets; ENSG00000131236; -.
PharmGKB; PA399; -.
eggNOG; KOG2675; Eukaryota.
eggNOG; ENOG410XPXJ; LUCA.
GeneTree; ENSGT00390000017955; -.
HOGENOM; HOG000206192; -.
HOVERGEN; HBG003080; -.
InParanoid; Q01518; -.
KO; K17261; -.
OMA; HCGYGDS; -.
OrthoDB; EOG091G0DLX; -.
PhylomeDB; Q01518; -.
TreeFam; TF313791; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CAP1; human.
EvolutionaryTrace; Q01518; -.
GeneWiki; CAP1; -.
GenomeRNAi; 10487; -.
PRO; PR:Q01518; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000131236; -.
CleanEx; HS_CAP1; -.
ExpressionAtlas; Q01518; baseline and differential.
Genevisible; Q01518; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IBA:GO_Central.
GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
InterPro; IPR017901; C-CAP_CF_C-like.
InterPro; IPR028415; CAP1.
InterPro; IPR036223; CAP_C_sf.
InterPro; IPR028417; CAP_CS_C.
InterPro; IPR018106; CAP_CS_N.
InterPro; IPR036222; CAP_N_sf.
InterPro; IPR006599; CARP_motif.
PANTHER; PTHR10652; PTHR10652; 1.
PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
Pfam; PF08603; CAP_C; 1.
Pfam; PF01213; CAP_N; 1.
SMART; SM00673; CARP; 2.
SUPFAM; SSF101278; SSF101278; 1.
SUPFAM; SSF69340; SSF69340; 1.
PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PROSITE; PS01088; CAP_1; 1.
PROSITE; PS01089; CAP_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Cell membrane; Complete proteome; Direct protein sequencing;
Isopeptide bond; Membrane; Methylation; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
CHAIN 2 475 Adenylyl cyclase-associated protein 1.
/FTId=PRO_0000205696.
DOMAIN 319 453 C-CAP/cofactor C-like.
{ECO:0000255|PROSITE-ProRule:PRU00659}.
COMPBIAS 218 256 Ala/Pro/Ser-rich.
COMPBIAS 230 241 Poly-Pro.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 31 31 Phosphotyrosine.
{ECO:0000250|UniProtKB:P40124}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 287 287 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 307 307 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 348 348 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 38 38 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_036038.
VARIANT 229 229 C -> G (in dbSNP:rs11207440).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028419.
VARIANT 236 236 C -> G (in dbSNP:rs6665926).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028420.
VARIANT 245 245 I -> S (in dbSNP:rs6665933).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028421.
VARIANT 247 247 C -> G (in dbSNP:rs6665936).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028422.
VARIANT 249 249 Y -> D (in dbSNP:rs6665937).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028423.
VARIANT 256 256 S -> A (in dbSNP:rs6665944).
{ECO:0000269|PubMed:1406678,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_028424.
CONFLICT 374 374 N -> S (in Ref. 5; BAD96233).
{ECO:0000305}.
STRAND 321 325 {ECO:0000244|PDB:1K8F}.
STRAND 328 333 {ECO:0000244|PDB:1K8F}.
STRAND 340 342 {ECO:0000244|PDB:1K8F}.
STRAND 350 355 {ECO:0000244|PDB:1K8F}.
STRAND 360 374 {ECO:0000244|PDB:1K8F}.
STRAND 376 393 {ECO:0000244|PDB:1K8F}.
STRAND 395 403 {ECO:0000244|PDB:1K8F}.
STRAND 406 412 {ECO:0000244|PDB:1K8F}.
STRAND 414 419 {ECO:0000244|PDB:1K8F}.
STRAND 428 433 {ECO:0000244|PDB:1K8F}.
STRAND 435 443 {ECO:0000244|PDB:1K8F}.
TURN 444 446 {ECO:0000244|PDB:1K8F}.
STRAND 447 452 {ECO:0000244|PDB:1K8F}.
STRAND 456 461 {ECO:0000244|PDB:1K8F}.
STRAND 463 471 {ECO:0000244|PDB:1K8F}.
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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