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Protein

F-actin-capping protein subunit beta

Gene

CAP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.1 Publication

GO - Molecular functioni

  • actin filament binding Source: SGD

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • barbed-end actin filament capping Source: SGD
  • filamentous growth Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31306-MONOMER.
ReactomeiREACT_312184. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Gene namesi
Name:CAP2
Ordered Locus Names:YIL034C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IX

Organism-specific databases

CYGDiYIL034c.
EuPathDBiFungiDB:YIL034C.
SGDiS000001296. CAP2.

Subcellular locationi

  • Cytoplasmcytoskeletonactin patch 1 Publication
  • Bud 1 Publication
  • Bud tip 1 Publication

  • Note: Found at cortical actin spots at the site of bud emergence and at the tips of growing buds and shmoos.

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • actin filament Source: SGD
  • cellular bud tip Source: UniProtKB-SubCell
  • F-actin capping protein complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 287286F-actin-capping protein subunit betaPRO_0000204642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei85 – 851Phosphoserine2 Publications
Modified residuei92 – 921Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13517.
PaxDbiP13517.
PeptideAtlasiP13517.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CAP1P284955EBI-4013,EBI-4003

Protein-protein interaction databases

BioGridi34956. 79 interactions.
DIPiDIP-836N.
IntActiP13517. 11 interactions.
MINTiMINT-482123.
STRINGi4932.YIL034C.

Structurei

3D structure databases

ProteinModelPortaliP13517.
SMRiP13517. Positions 2-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
InParanoidiP13517.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG78H45S.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAQFDAAL DLLRRLNPTT LQENLNNLIE LQPNLAQDLL SSVDVPLSTQ
60 70 80 90 100
KDSADSNREY LCCDYNRDID SFRSPWSNTY YPELSPKDLQ DSPFPSAPLR
110 120 130 140 150
KLEILANDSF DVYRDLYYEG GISSVYLWDL NEEDFNGHDF AGVVLFKKNQ
160 170 180 190 200
SDHSNWDSIH VFEVTTSPSS PDSFNYRVTT TIILHLDKTK TDQNSHMMLS
210 220 230 240 250
GNLTRQTEKD IAIDMSRPLD VIFTSHVANL GSLIEDIESQ MRNLLETVYF
260 270 280
EKTRDIFHQT KNAAIASSAE EANKDAQAEV IRGLQSL
Length:287
Mass (Da):32,629
Last modified:November 1, 1991 - v3
Checksum:i6E669023D1378778
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401F → Y in AAA66935 (PubMed:2823100).Curated
Sequence conflicti146 – 1472FK → I in AAA66935 (PubMed:2823100).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62630 Genomic DNA. Translation: CAA44497.1.
Z46861 Genomic DNA. Translation: CAA86917.1.
M17223 Genomic DNA. Translation: AAA66935.1.
BK006942 Genomic DNA. Translation: DAA08514.1.
PIRiS49944.
RefSeqiNP_012230.3. NM_001179384.3.

Genome annotation databases

EnsemblFungiiYIL034C; YIL034C; YIL034C.
GeneIDi854777.
KEGGisce:YIL034C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62630 Genomic DNA. Translation: CAA44497.1.
Z46861 Genomic DNA. Translation: CAA86917.1.
M17223 Genomic DNA. Translation: AAA66935.1.
BK006942 Genomic DNA. Translation: DAA08514.1.
PIRiS49944.
RefSeqiNP_012230.3. NM_001179384.3.

3D structure databases

ProteinModelPortaliP13517.
SMRiP13517. Positions 2-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34956. 79 interactions.
DIPiDIP-836N.
IntActiP13517. 11 interactions.
MINTiMINT-482123.
STRINGi4932.YIL034C.

Proteomic databases

MaxQBiP13517.
PaxDbiP13517.
PeptideAtlasiP13517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL034C; YIL034C; YIL034C.
GeneIDi854777.
KEGGisce:YIL034C.

Organism-specific databases

CYGDiYIL034c.
EuPathDBiFungiDB:YIL034C.
SGDiS000001296. CAP2.

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
InParanoidiP13517.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG78H45S.

Enzyme and pathway databases

BioCyciYEAST:G3O-31306-MONOMER.
ReactomeiREACT_312184. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

NextBioi977553.
PROiP13517.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of the actin cytoskeleton in yeast capping protein mutants."
    Amatruda J.F., Cannon J.F., Tatchell K., Hug C., Cooper J.A.
    Nature 344:352-354(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Amatruda J.F., Gattermeir D.J., Cooper J.A.
    Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase."
    Cannon J.F., Tatchell K.
    Mol. Cell. Biol. 7:2653-2663(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-195.
  6. "Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein."
    Amatruda J.F., Cooper J.A.
    J. Cell Biol. 117:1067-1076(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 149-156, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPZB_YEAST
AccessioniPrimary (citable) accession number: P13517
Secondary accession number(s): D6VVP8, Q07082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1991
Last modified: June 24, 2015
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6770 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

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 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.