Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Adenylyl cyclase-associated protein 1  

UniProtKB / Swiss-Prot ID :  CAP1_HUMAN

Gene Name (Synonyms) : 
CAP1, CAP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Peripheral membrane protein (By similarity). 

Protein 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. 

Protein Sequence MADMQNLVERLERAVGRLEAVSHTSDMHRGYADSPSKAGAAPYVQAFDSLLAGPVAEYLKISKEIGGDVQ...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
229C -> G (in dbSNP:rs11207440). VAR_028419
236C -> G (in dbSNP:rs6665926). VAR_028420
245I -> S (in dbSNP:rs6665933). VAR_028421
247C -> G (in dbSNP:rs6665936). VAR_028422
249Y -> D (in dbSNP:rs6665937). VAR_028423
256S -> A (in dbSNP:rs6665944). VAR_028424
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADMQN
---CHHHHH
22.45UniProtKB
Link-
31PhosphotyrosineMHRGYADSP
CCCCCCCCC
13.75Phosphositeplus
Link-
34PhosphoserineGYADSPSKA
CCCCCCCCC
23.93HPRD
Link-
34PhosphoserineGYADSPSKA
CCCCCCCCC
23.93Phosphositeplus
Link-
36PhosphoserineADSPSKAGA
CCCCCCCCC
38.80HPRD
Link-
36PhosphoserineADSPSKAGA
CCCCCCCCC
38.80Phosphositeplus
Link-
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDVQKHAEM
HHHHHHHHH
44.63Phosphositeplus
Link-
81N6-acetyllysineHTGLKLERA
HHHHHHHHH
50.04HPRD
Link-
81N6-acetyllysineHTGLKLERA
HHHHHHHHH
50.04Phosphositeplus
Link-
81N6-acetyllysine.HTGLKLERA
HHHHHHHHH
50.04UniProtKB
Link-
93S-nitrosocysteineTASQCQQPA
HHHHHCCCC
3.62dbSNO
Link-
164PhosphotyrosineAAMFYTNRV
HHHHHHHHH
7.04HPRD
Link-
164PhosphotyrosineAAMFYTNRV
HHHHHHHHH
7.04Phosphositeplus
Link-
164PhosphotyrosineAAMFYTNRV
HHHHHHHHH
7.04SysPTM
Link-
164Phosphotyrosine.AAMFYTNRV
HHHHHHHHH
7.04UniProtKB
Link-
165PhosphothreonineAMFYTNRVL
HHHHHHHHH
12.79HPRD
Link-
165PhosphothreonineAMFYTNRVL
HHHHHHHHH
12.79Phosphositeplus
Link-
172PhosphotyrosineVLKEYKDVD
HHHHHHCCC
15.76HPRD
Link-
209N6-acetyllysineLAWSKTGPV
CEECCCCCH
46.96HPRD
Link-
209N6-acetyllysineLAWSKTGPV
CEECCCCCH
46.96Phosphositeplus
Link-
209N6-acetyllysine.LAWSKTGPV
CEECCCCCH
46.96UniProtKB
Link-
280PhosphothreonineDDMKTHKNP
HHHHHCCCH
31.29HPRD
Link-
280PhosphothreonineDDMKTHKNP
HHHHHCCCH
31.29Phosphositeplus
Link-
290PhosphoserineLKAQSGPVR
HHCCCCCCC
50.34HPRD
Link-
290PhosphoserineLKAQSGPVR
HHCCCCCCC
50.34PhosphoELM
Link-
290PhosphoserineLKAQSGPVR
HHCCCCCCC
50.34Phosphositeplus
Link-
290PhosphoserineLKAQSGPVR
HHCCCCCCC
50.34SysPTM
Link-
290Phosphoserine.LKAQSGPVR
HHCCCCCCC
50.34UniProtKB
Link-
295PhosphoserineGPVRSGPKP
CCCCCCCCC
60.73HPRD
Link-
295PhosphoserineGPVRSGPKP
CCCCCCCCC
60.73PhosphoELM
Link-
295PhosphoserineGPVRSGPKP
CCCCCCCCC
60.73Phosphositeplus
Link-
295PhosphoserineGPVRSGPKP
CCCCCCCCC
60.73SysPTM
Link-
295Phosphoserine.GPVRSGPKP
CCCCCCCCC
60.73UniProtKB
Link-
301PhosphoserinePKPFSAPKP
CCCCCCCCC
52.79HPRD
Link-
301PhosphoserinePKPFSAPKP
CCCCCCCCC
52.79PhosphoELM
Link-
301PhosphoserinePKPFSAPKP
CCCCCCCCC
52.79Phosphositeplus
Link-
301PhosphoserinePKPFSAPKP
CCCCCCCCC
52.79SysPTM
Link-
301Phosphoserine.PKPFSAPKP
CCCCCCCCC
52.79UniProtKB
Link-
307PhosphothreoninePKPQTSPSP
CCCCCCCCC
51.65HPRD
Link-
307PhosphothreoninePKPQTSPSP
CCCCCCCCC
51.65PhosphoELM
Link-
307PhosphothreoninePKPQTSPSP
CCCCCCCCC
51.65Phosphositeplus
Link-
307PhosphothreoninePKPQTSPSP
CCCCCCCCC
51.65SysPTM
Link-
307Phosphothreonine.PKPQTSPSP
CCCCCCCCC
51.65UniProtKB
Link-
308PhosphoserineKPQTSPSPK
CCCCCCCCC
20.38HPRD
Link-
308PhosphoserineKPQTSPSPK
CCCCCCCCC
20.38PhosphoELM
Link-
308PhosphoserineKPQTSPSPK
CCCCCCCCC
20.38Phosphositeplus
Link-
308PhosphoserineKPQTSPSPK
CCCCCCCCC
20.38SysPTM
Link-
308Phosphoserine.KPQTSPSPK
CCCCCCCCC
20.38UniProtKB
Link-
310PhosphoserineQTSPSPKRA
CCCCCCCCC
42.70HPRD
Link-
310PhosphoserineQTSPSPKRA
CCCCCCCCC
42.70PhosphoELM
Link-
310PhosphoserineQTSPSPKRA
CCCCCCCCC
42.70Phosphositeplus
Link-
310PhosphoserineQTSPSPKRA
CCCCCCCCC
42.70SysPTM
Link-
310Phosphoserine.QTSPSPKRA
CCCCCCCCC
42.70UniProtKB
Link-
354PhosphotyrosineVAYIYKCVN
EEEEEEEEE
5.90Phosphositeplus
Link
412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISINKTDGC
EEEECCCCC
46.45Phosphositeplus
Link
419PhosphotyrosineGCHAYLSKN
CCEEEECCC
6.45Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACTB_HUMANin vivo
yeast 2-hybrid
HPRD:09869HPRD8761950
SPB8_HUMANin vivo
yeast 2-hybrid
HPRD:09869HPRD8761950
CAP1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:09869HPRD8761950
CAP2_HUMANENSP00000344832STRING
SPB8_HUMANENSP00000344832STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-308, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81 AND LYS-209, AND MASSSPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307 AND SER-310, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-295; SER-301;THR-307; SER-308 AND SER-310, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-308, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-164, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures