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Protein

Adenylyl cyclase-associated protein 1

Gene

Cap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • ameboidal-type cell migration Source: MGI
  • cell morphogenesis Source: MGI
  • receptor-mediated endocytosis Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylyl cyclase-associated protein 1
Short name:
CAP 1
Gene namesi
Name:Cap1
Synonyms:Cap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88262. Cap1.

Subcellular locationi

GO - Cellular componenti

  • cortical actin cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular region Source: Reactome
  • focal adhesion Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 474473Adenylyl cyclase-associated protein 1PRO_0000205697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei31 – 311PhosphotyrosineCombined sources
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei80 – 801N6-acetyllysineBy similarity
Modified residuei289 – 2891PhosphoserineBy similarity
Modified residuei294 – 2941PhosphoserineBy similarity
Modified residuei300 – 3001PhosphoserineBy similarity
Modified residuei306 – 3061PhosphothreonineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP40124.
MaxQBiP40124.
PaxDbiP40124.
PRIDEiP40124.

2D gel databases

REPRODUCTION-2DPAGEP40124.

PTM databases

iPTMnetiP40124.
PhosphoSiteiP40124.
SwissPalmiP40124.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP40124.
ExpressionAtlasiP40124. baseline and differential.
GenevisibleiP40124. MM.

Interactioni

Subunit structurei

Homodimer. Binds actin monomers (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Mcf2Q99N723EBI-641927,EBI-641874

Protein-protein interaction databases

BioGridi198468. 1 interaction.
DIPiDIP-49641N.
IntActiP40124. 7 interactions.
MINTiMINT-1591929.
STRINGi10090.ENSMUSP00000068260.

Structurei

3D structure databases

ProteinModelPortaliP40124.
SMRiP40124. Positions 43-214, 318-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini312 – 452141C-CAP/cofactor C-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi217 – 25539Ala/Pro/Ser-richAdd
BLAST
Compositional biasi229 – 24012Poly-ProAdd
BLAST

Sequence similaritiesi

Belongs to the CAP family.Curated
Contains 1 C-CAP/cofactor C-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2675. Eukaryota.
ENOG410XPXJ. LUCA.
GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
HOVERGENiHBG003080.
InParanoidiP40124.
KOiK17261.
OMAiLIRIKQT.
OrthoDBiEOG7DNNTH.
TreeFamiTF313791.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR001837. 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.
IPR028415. CAP1.
IPR028417. CAP_CS_C.
IPR018106. CAP_CS_N.
IPR006599. CARP_motif.
[Graphical view]
PANTHERiPTHR10652. PTHR10652. 1 hit.
PTHR10652:SF1. PTHR10652:SF1. 1 hit.
PfamiPF08603. CAP_C. 1 hit.
PF01213. CAP_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
SUPFAMiSSF101278. SSF101278. 1 hit.
SSF69340. SSF69340. 1 hit.
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
PS01088. CAP_1. 1 hit.
PS01089. CAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADMQNLVER LERAVGRLEA VSHTSDMHCG YGDSPSKGAV PYVQAFDSLL
60 70 80 90 100
ANPVAEYLKM SKEIGGDVQK HAEMVHTGLK LERALLATAS QCQQPAGNKL
110 120 130 140 150
SDLLAPISEQ IQEVITFREK NRGSKFFNHL SAVSESIQAL GWVALAAKPG
160 170 180 190 200
PFVKEMNDAA MFYTNRVLKE YRDVDKKHVD WVRAYLSIWT ELQAYIKEFH
210 220 230 240 250
TTGLAWSKTG PVAKELSGLP SGPSVGSGPP PPPPGPPPPP ISTSSGSDDS
260 270 280 290 300
ASRSALFAQI NQGESITHAL KHVSDDMKTH KNPALKAQSG PVRSGPKPFS
310 320 330 340 350
APKPQTSPSP KPATKKEPAL LELEGKKWRV ENQENVSNLV IDDTELKQVA
360 370 380 390 400
YIYKCVNTTL QIKGKINSIT VDNCKKLGLV FDDVVGIVEI INSRDVKVQV
410 420 430 440 450
MGKVPTISIN KTDGCHAYLS KNSLDCEIVS AKSSEMNVLI PTEGGDFNEF
460 470
PVPEQFKTLW NGQKLVTTVT EIAG
Length:474
Mass (Da):51,565
Last modified:July 27, 2011 - v4
Checksum:i076863277E7AF2F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421S → P in AAC37610 (PubMed:7691848).Curated
Sequence conflicti242 – 2421S → P in AAH05446 (PubMed:15489334).Curated
Sequence conflicti242 – 2421S → P in AAH05472 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12367 mRNA. Translation: AAC37610.1.
AK053351 mRNA. Translation: BAC35357.1.
AL606906, BX545849 Genomic DNA. Translation: CAM13994.1.
BX545849, AL606906 Genomic DNA. Translation: CAM18197.1.
BC005446 mRNA. Translation: AAH05446.1.
BC005472 mRNA. Translation: AAH05472.1.
CCDSiCCDS18604.1.
PIRiI49572.
RefSeqiNP_001287996.1. NM_001301067.1.
NP_031624.2. NM_007598.4.
XP_006502758.1. XM_006502695.1.
XP_006502760.1. XM_006502697.2.
UniGeneiMm.8687.

Genome annotation databases

EnsembliENSMUST00000069533; ENSMUSP00000068260; ENSMUSG00000028656.
ENSMUST00000106255; ENSMUSP00000101862; ENSMUSG00000028656.
ENSMUST00000106257; ENSMUSP00000101864; ENSMUSG00000028656.
GeneIDi12331.
KEGGimmu:12331.
UCSCiuc008uok.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12367 mRNA. Translation: AAC37610.1.
AK053351 mRNA. Translation: BAC35357.1.
AL606906, BX545849 Genomic DNA. Translation: CAM13994.1.
BX545849, AL606906 Genomic DNA. Translation: CAM18197.1.
BC005446 mRNA. Translation: AAH05446.1.
BC005472 mRNA. Translation: AAH05472.1.
CCDSiCCDS18604.1.
PIRiI49572.
RefSeqiNP_001287996.1. NM_001301067.1.
NP_031624.2. NM_007598.4.
XP_006502758.1. XM_006502695.1.
XP_006502760.1. XM_006502697.2.
UniGeneiMm.8687.

3D structure databases

ProteinModelPortaliP40124.
SMRiP40124. Positions 43-214, 318-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198468. 1 interaction.
DIPiDIP-49641N.
IntActiP40124. 7 interactions.
MINTiMINT-1591929.
STRINGi10090.ENSMUSP00000068260.

PTM databases

iPTMnetiP40124.
PhosphoSiteiP40124.
SwissPalmiP40124.

2D gel databases

REPRODUCTION-2DPAGEP40124.

Proteomic databases

EPDiP40124.
MaxQBiP40124.
PaxDbiP40124.
PRIDEiP40124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069533; ENSMUSP00000068260; ENSMUSG00000028656.
ENSMUST00000106255; ENSMUSP00000101862; ENSMUSG00000028656.
ENSMUST00000106257; ENSMUSP00000101864; ENSMUSG00000028656.
GeneIDi12331.
KEGGimmu:12331.
UCSCiuc008uok.3. mouse.

Organism-specific databases

CTDi10487.
MGIiMGI:88262. Cap1.

Phylogenomic databases

eggNOGiKOG2675. Eukaryota.
ENOG410XPXJ. LUCA.
GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
HOVERGENiHBG003080.
InParanoidiP40124.
KOiK17261.
OMAiLIRIKQT.
OrthoDBiEOG7DNNTH.
TreeFamiTF313791.

Miscellaneous databases

ChiTaRSiCap1. mouse.
NextBioi280930.
PROiP40124.
SOURCEiSearch...

Gene expression databases

BgeeiP40124.
ExpressionAtlasiP40124. baseline and differential.
GenevisibleiP40124. MM.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR001837. 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.
IPR028415. CAP1.
IPR028417. CAP_CS_C.
IPR018106. CAP_CS_N.
IPR006599. CARP_motif.
[Graphical view]
PANTHERiPTHR10652. PTHR10652. 1 hit.
PTHR10652:SF1. PTHR10652:SF1. 1 hit.
PfamiPF08603. CAP_C. 1 hit.
PF01213. CAP_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
SUPFAMiSSF101278. SSF101278. 1 hit.
SSF69340. SSF69340. 1 hit.
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
PS01088. CAP_1. 1 hit.
PS01089. CAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein."
    Vojtek A.B., Cooper J.A.
    J. Cell Sci. 105:777-785(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 254-271, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCAP1_MOUSE
AccessioniPrimary (citable) accession number: P40124
Secondary accession number(s): Q8BPT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.