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Protein

F-actin-capping protein subunit beta

Gene

Capzb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Alternative name(s):
CapZ beta
Gene namesi
Name:Capzb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1359099. Capzb.

Subcellular locationi

GO - Cellular componenti

  • dendritic spine Source: RGD
  • F-actin capping protein complex Source: InterPro
  • neuronal cell body Source: RGD
  • sarcomere Source: UniProtKB-SubCell
  • WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 272271F-actin-capping protein subunit betaPRO_0000289720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei235 – 2351N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XI32.
PRIDEiQ5XI32.

2D gel databases

World-2DPAGE0004:Q5XI32.

PTM databases

iPTMnetiQ5XI32.
PhosphoSiteiQ5XI32.

Expressioni

Gene expression databases

ExpressionAtlasiQ5XI32. baseline.
GenevisibleiQ5XI32. RN.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MtpnP627753EBI-2128068,EBI-2128047

Protein-protein interaction databases

BioGridi255949. 2 interactions.
IntActiQ5XI32. 1 interaction.
STRINGi10116.ENSRNOP00000010308.

Structurei

3D structure databases

ProteinModelPortaliQ5XI32.
SMRiQ5XI32. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili210 – 27263Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiQ5XI32.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.

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.

Q5XI32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA
60 70 80 90 100
RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA
110 120 130 140 150
NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS
160 170 180 190 200
IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KSGSGTMNLG GSLTRQMEKD
210 220 230 240 250
ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSVQTFA
260 270
DKSKQEALKN DLVEALKRKQ QC
Length:272
Mass (Da):30,629
Last modified:November 23, 2004 - v1
Checksum:iE6466A68B1254FD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083861 mRNA. Translation: AAH83861.1.
RefSeqiNP_001005903.1. NM_001005903.1.
UniGeneiRn.105999.

Genome annotation databases

EnsembliENSRNOT00000010308; ENSRNOP00000010308; ENSRNOG00000007330.
GeneIDi298584.
KEGGirno:298584.
UCSCiRGD:1359099. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083861 mRNA. Translation: AAH83861.1.
RefSeqiNP_001005903.1. NM_001005903.1.
UniGeneiRn.105999.

3D structure databases

ProteinModelPortaliQ5XI32.
SMRiQ5XI32. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi255949. 2 interactions.
IntActiQ5XI32. 1 interaction.
STRINGi10116.ENSRNOP00000010308.

PTM databases

iPTMnetiQ5XI32.
PhosphoSiteiQ5XI32.

2D gel databases

World-2DPAGE0004:Q5XI32.

Proteomic databases

PaxDbiQ5XI32.
PRIDEiQ5XI32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010308; ENSRNOP00000010308; ENSRNOG00000007330.
GeneIDi298584.
KEGGirno:298584.
UCSCiRGD:1359099. rat.

Organism-specific databases

CTDi832.
RGDi1359099. Capzb.

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiQ5XI32.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.

Enzyme and pathway databases

ReactomeiR-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiQ5XI32.

Gene expression databases

ExpressionAtlasiQ5XI32. baseline.
GenevisibleiQ5XI32. RN.

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. "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].
    Tissue: Kidney.
  2. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 95-108, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  3. "Proteome profile of the mature rat olfactory bulb."
    Maurya D.K., Sundaram C.S., Bhargava P.
    Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPZB_RAT
AccessioniPrimary (citable) accession number: Q5XI32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 85 of the entry and version 1 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. 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.