Q01518 (CAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylyl cyclase-associated protein 1
Short name=CAP 1

Gene names

Name:	CAP1
Synonyms:	CAP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Homodimer. Binds actin monomers.
Subcellular location	Cell membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the CAP family. Contains 1 C-CAP/cofactor C-like domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	activation of adenylate cyclase activity Traceable author statement. Source: ProtInc axon guidance Traceable author statement. Source: Reactome establishment or maintenance of cell polarity Traceable author statement. Source: ProtInc platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome signal transduction Traceable author statement. Source: ProtInc
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q01518-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q01518-2)

The sequence of this isoform differs from the canonical sequence as follows:
     38-38: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 475

474

Adenylyl cyclase-associated protein 1

PRO_0000205696

Regions

Domain

319 – 453

135

C-CAP/cofactor C-like

Compositional bias

218 – 256

39

Ala/Pro/Ser-rich

Compositional bias

230 – 241

12

Poly-Pro

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.14

Modified residue

81

1

N6-acetyllysine Ref.16

Modified residue

164

1

Phosphotyrosine Ref.9

Modified residue

209

1

N6-acetyllysine Ref.16

Modified residue

290

1

Phosphoserine Ref.13

Modified residue

295

1

Phosphoserine Ref.13

Modified residue

301

1

Phosphoserine Ref.13

Modified residue

307

1

Phosphothreonine Ref.10 Ref.13

Modified residue

308

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

310

1

Phosphoserine Ref.10 Ref.11 Ref.13 Ref.15

Natural variations

Alternative sequence

38

1

Missing in isoform 2.

VSP_036038

Natural variant

229

1

C → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs11207440 [ dbSNP | Ensembl ].

VAR_028419

Natural variant

236

1

C → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs6665926 [ dbSNP | Ensembl ].

VAR_028420

Natural variant

245

1

I → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs6665933 [ dbSNP | Ensembl ].

VAR_028421

Natural variant

247

1

C → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs6665936 [ dbSNP | Ensembl ].

VAR_028422

Natural variant

249

1

Y → D. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs6665937 [ dbSNP | Ensembl ].

VAR_028423

Natural variant

256

1

S → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs6665944 [ dbSNP | Ensembl ].

VAR_028424

Experimental info

Sequence conflict

374

1

N → S in BAD96233. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

475

Helix Strand Turn

Details...

Beta strand

321 – 325

5

Beta strand

328 – 333

6

Beta strand

340 – 342

3

Beta strand

350 – 355

6

Beta strand

360 – 374

15

Beta strand

376 – 393

18

Beta strand

395 – 403

9

Beta strand

406 – 412

7

Beta strand

414 – 419

6

Beta strand

428 – 433

6

Beta strand

435 – 443

9

Turn

444 – 446

3

Beta strand

447 – 452

6

Beta strand

456 – 461

6

Beta strand

463 – 471

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 5. Checksum: 7789D1FAC0D1AB7B	FASTA	475	51,901
	10 20 30 40 50 60 MADMQNLVER LERAVGRLEA VSHTSDMHRG YADSPSKAGA APYVQAFDSL LAGPVAEYLK 70 80 90 100 110 120 ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAENK LSDLLAPISE QIKEVITFRE 130 140 150 160 170 180 KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV 190 200 210 220 230 240 DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAKELSGL PSGPSAGSCP PPPPPCPPPP 250 260 270 280 290 300 PVSTISCSYE SASRSSLFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPVRSGPKPF 310 320 330 340 350 360 SAPKPQTSPS PKRATKKEPA VLELEGKKWR VENQENVSNL VIEDTELKQV AYIYKCVNTT 370 380 390 400 410 420 LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSKDVKVQ VMGKVPTISI NKTDGCHAYL 430 440 450 460 470 SKNSLDCEIV SAKSSEMNVL IPTEGGDFNE FPVPEQFKTL WNGQKLVTTV TEIAG
	Isoform 2 [UniParc]. Checksum: E0CD26F4975A39A0	FASTA	474	51,830
	10 20 30 40 50 60 MADMQNLVER LERAVGRLEA VSHTSDMHRG YADSPSKGAA PYVQAFDSLL AGPVAEYLKI 70 80 90 100 110 120 SKEIGGDVQK HAEMVHTGLK LERALLVTAS QCQQPAENKL SDLLAPISEQ IKEVITFREK 130 140 150 160 170 180 NRGSKLFNHL SAVSESIQAL GWVAMAPKPG PYVKEMNDAA MFYTNRVLKE YKDVDKKHVD 190 200 210 220 230 240 WVKAYLSIWT ELQAYIKEFH TTGLAWSKTG PVAKELSGLP SGPSAGSCPP PPPPCPPPPP 250 260 270 280 290 300 VSTISCSYES ASRSSLFAQI NQGESITHAL KHVSDDMKTH KNPALKAQSG PVRSGPKPFS 310 320 330 340 350 360 APKPQTSPSP KRATKKEPAV LELEGKKWRV ENQENVSNLV IEDTELKQVA YIYKCVNTTL 370 380 390 400 410 420 QIKGKINSIT VDNCKKLGLV FDDVVGIVEI INSKDVKVQV MGKVPTISIN KTDGCHAYLS 430 440 450 460 470 KNSLDCEIVS AKSSEMNVLI PTEGGDFNEF PVPEQFKTLW NGQKLVTTVT EIAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human cDNA encoding a protein that is structurally and functionally related to the yeast adenylyl cyclase-associated CAP proteins." Matviw H., Yu G., Young D. Mol. Cell. Biol. 12:5033-5040(1992) [PubMed: 1406678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
[2]	"Genes from metazoans encoding homologs of yeast adenylyl cyclase-associated proteins." Kawamukai M., O'Neill K., Rodgers L., Riggs M., Schaller H.C., Chalfie M., Field J., Wigler M. Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256. Tissue: Adipose tissue.
[6]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256. Tissue: Kidney.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric 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) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2. Tissue: Platelet.
[9]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-164, MASS SPECTROMETRY. Tissue: Pituitary.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells 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) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307 AND SER-310, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-295; SER-301; THR-307; SER-308 AND SER-310, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81 AND LYS-209, MASS SPECTROMETRY.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Crystal structure of the actin binding domain of the cyclase-associated protein." 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. Biochemistry 43:10628-10641(2004) [PubMed: 15311924] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 319-475.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M98474 mRNA. Translation: AAA35648.1.
L12168 mRNA. Translation: AAA35507.1.
BT007152 mRNA. Translation: AAP35816.1.
CR457409 mRNA. Translation: CAG33690.1.
AK222513 mRNA. Translation: BAD96233.1.
AL512599 Genomic DNA. Translation: CAI11021.1.
AL512599 Genomic DNA. Translation: CAI11022.1.
BC013963 mRNA. Translation: AAH13963.1.
BC095440 mRNA. Translation: AAH95440.1.

IPI

IPI00008274.
IPI00639931.

PIR

A48120.

RefSeq

NP_001099000.1. NM_001105530.1.
NP_006358.1. NM_006367.3.

UniGene

Hs.370581.
Hs.713078.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K8F	X-ray	2.80	A/B/C/D	319-475	[»]

ProteinModelPortal

Q01518.

SMR

Q01518. Positions 35-218, 319-475.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01518. 3 interactions.

STRING

Q01518.

PTM databases

PhosphoSite

Q01518.

Polymorphism databases

DMDM

308153681.

2D gel databases

OGP

Q01518.

REPRODUCTION-2DPAGE

IPI00639931.

Proteomic databases

PRIDE

Q01518.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372792; ENSP00000361878; ENSG00000131236.
ENST00000372797; ENSP00000361883; ENSG00000131236.
ENST00000372805; ENSP00000361891; ENSG00000131236.

GeneID

10487.

KEGG

hsa:10487.

UCSC

uc001cey.2. human.

Organism-specific databases

CTD

10487.

GeneCards

GC01P040505.

HGNC

HGNC:20040. CAP1.

HPA

HPA030124.

neXtProt

NX_Q01518.

PharmGKB

PA399.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05476.

HOGENOM

HBG444917.

HOVERGEN

HBG003080.

InParanoid

Q01518.

OMA

YLSIWTE.

OrthoDB

EOG49S669.

PhylomeDB

Q01518.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q01518.

Bgee

Q01518.

CleanEx

HS_CAP1.

Genevestigator

Q01518.

GermOnline

ENSG00000131236. Homo sapiens.

Family and domain databases

InterPro

IPR001837. Adenylate_cyclase-assoc_CAP.
IPR013912. Adenylate_cyclase-assoc_CAP_C.
IPR013992. Adenylate_cyclase-assoc_CAP_N.
IPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR018106. CAP_CS.
IPR006599. CARP_motif.
[Graphical view]

Gene3D

G3DSA:2.160.20.70. CAP/MinC_C. 1 hit.

PANTHER

PTHR10652. CAP. 1 hit.

Pfam

PF08603. CAP_C. 1 hit.
PF01213. CAP_N. 1 hit.
[Graphical view]

SMART

SM00673. CARP. 2 hits.
[Graphical view]

SUPFAM

SSF101278. Adenylate_cyclase-assoc_CAP_N. 1 hit.
SSF69340. CARP. 1 hit.

PROSITE

PS51329. C_CAP_COFACTOR_C. 1 hit.
PS01088. CAP_1. 1 hit.
PS01089. CAP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

39792.

Entry information

Entry name

CAP1_HUMAN

Accession

Primary (citable) accession number: Q01518
Secondary accession number(s): Q53HR7 , Q5T0S1, Q5T0S2, Q6I9U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 5, 2010
Last modified:	January 25, 2012
This is version 118 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.