Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P47756 (CAPZB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-actin-capping protein subunit beta
Alternative name(s):
CapZ beta
Gene names
Name:CAPZB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

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), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmmyofibrilsarcomere By similarity.

Sequence similarities

Belongs to the F-actin-capping protein beta subunit family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Molecular functionActin capping
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

barbed-end actin filament capping

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

cytoskeleton organization

Inferred from mutant phenotype Ref.13. Source: UniProtKB

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

muscle fiber development

Inferred from electronic annotation. Source: Ensembl

negative regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

regulation of cell morphogenesis

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of protein kinase C signaling

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentF-actin capping protein complex

Traceable author statement Ref.1. Source: ProtInc

WASH complex

Inferred from direct assay Ref.11. Source: UniProtKB

Z disc

Inferred from electronic annotation. Source: Ensembl

acrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

intercalated disc

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P47756-1)

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: P47756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     246-277: IDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC
Isoform 3 (identifier: P47756-3)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 277276F-actin-capping protein subunit beta
PRO_0000204634

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.10 Ref.16 Ref.17
Modified residue2351N6-acetyllysine Ref.12

Natural variations

Alternative sequence246 – 27732IDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2.
VSP_000767

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: ABA1621F9E0152A6

FASTA27731,350
        10         20         30         40         50         60 
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL 

        70         80         90        100        110        120 
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY 

       130        140        150        160        170        180 
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN 

       190        200        210        220        230        240 
KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV 

       250        260        270 
NGLRSIDAIP DNQKFKQLQR ELSQVLTQRQ IYIQPDN 

« Hide

Isoform 2 [UniParc].

Checksum: E6466A68B1254FD0
Show »

FASTA27230,629
Isoform 3 (Sequence not available).

References

« Hide 'large scale' references
[1]"Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families."
Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q., Tsui L.-C., Casella J.F.
J. Biol. Chem. 270:21472-21479(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retina.
[2]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2).
Tissue: Ovary.
[6]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14, ACETYLATION AT SER-2.
Tissue: Platelet.
[7]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 95-108, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ."
Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A., Cohen P.
Biochem. J. 389:127-135(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RCSD1/CAPZIP, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP17.
[10]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex."
Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.
Dev. Cell 17:712-723(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE WASH COMPLEX.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03271 mRNA. Translation: AAA87395.1.
BT019470 mRNA. Translation: AAV38277.1.
BT019471 mRNA. Translation: AAV38278.1.
AL035413, AL359199, AL445163 Genomic DNA. Translation: CAI22231.1.
AL359199, AL035413, AL445163 Genomic DNA. Translation: CAH72124.1.
AL445163, AL035413, AL359199 Genomic DNA. Translation: CAH71392.1.
CH471134 Genomic DNA. Translation: EAW94890.1.
BC024601 mRNA. Translation: AAH24601.1.
BC107752 mRNA. Translation: AAI07753.1.
BC109241 mRNA. Translation: AAI09242.1.
BC109242 mRNA. Translation: AAI09243.1.
CCDSCCDS41277.1. [P47756-2]
CCDS55579.1. [P47756-1]
RefSeqNP_001193469.1. NM_001206540.2. [P47756-1]
NP_001269091.1. NM_001282162.1.
NP_004921.1. NM_004930.4. [P47756-2]
UniGeneHs.432760.

3D structure databases

ProteinModelPortalP47756.
SMRP47756. Positions 2-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107282. 44 interactions.
IntActP47756. 17 interactions.
MINTMINT-254051.
STRING9606.ENSP00000364287.

PTM databases

PhosphoSiteP47756.

Polymorphism databases

DMDM13124696.

2D gel databases

DOSAC-COBS-2DPAGEP47756.
OGPP47756.
REPRODUCTION-2DPAGEIPI00026185.
SWISS-2DPAGEP47756.

Proteomic databases

MaxQBP47756.
PaxDbP47756.
PRIDEP47756.

Protocols and materials databases

DNASU832.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264202; ENSP00000264202; ENSG00000077549. [P47756-1]
ENST00000375142; ENSP00000364284; ENSG00000077549. [P47756-1]
ENST00000401084; ENSP00000383862; ENSG00000077549. [P47756-2]
GeneID832.
KEGGhsa:832.
UCSCuc001bce.3. human. [P47756-2]
uc021ohr.1. human. [P47756-1]

Organism-specific databases

CTD832.
GeneCardsGC01M019665.
HGNCHGNC:1491. CAPZB.
HPAHPA031531.
HPA056066.
MIM601572. gene.
neXtProtNX_P47756.
PharmGKBPA26072.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291067.
HOGENOMHOG000041208.
HOVERGENHBG050789.
KOK10365.
OMAFDTYREM.
PhylomeDBP47756.
TreeFamTF105732.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP47756.
BgeeP47756.
CleanExHS_CAPZB.
GenevestigatorP47756.

Family and domain databases

InterProIPR001698. CapZ_beta.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERPTHR10619. PTHR10619. 1 hit.
PfamPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSPR00192. FACTINCAPB.
PROSITEPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPZB. human.
GeneWikiCAPZB.
GenomeRNAi832.
NextBio3446.
PROP47756.
SOURCESearch...

Entry information

Entry nameCAPZB_HUMAN
AccessionPrimary (citable) accession number: P47756
Secondary accession number(s): Q32Q68 expand/collapse secondary AC list , Q5U0L4, Q8TB49, Q9NUC4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM