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P47756

- CAPZB_HUMAN

UniProt

P47756 - CAPZB_HUMAN

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Protein

F-actin-capping protein subunit beta

Gene
CAPZB
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Plays a role in the regulation of cell morphology and cytoskeletal organization.1 Publication

GO - Molecular functioni

  1. actin binding Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. barbed-end actin filament capping Source: Ensembl
  3. blood coagulation Source: Reactome
  4. cellular component movement Source: UniProtKB
  5. cytoskeleton organization Source: UniProtKB
  6. lamellipodium assembly Source: Ensembl
  7. muscle fiber development Source: Ensembl
  8. negative regulation of microtubule polymerization Source: Ensembl
  9. neuron projection development Source: Ensembl
  10. regulation of cell morphogenesis Source: UniProtKB
  11. regulation of protein kinase C signaling Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_24970. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1491. CAPZB.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cytoplasmmyofibrilsarcomere By similarity

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. actin cytoskeleton Source: ProtInc
  3. cortical cytoskeleton Source: Ensembl
  4. cytoskeleton Source: UniProtKB
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
  7. F-actin capping protein complex Source: ProtInc
  8. intercalated disc Source: Ensembl
  9. lamellipodium Source: Ensembl
  10. membrane Source: Ensembl
  11. WASH complex Source: UniProtKB
  12. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26072.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 277276F-actin-capping protein subunit betaPRO_0000204634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei235 – 2351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47756.
PaxDbiP47756.
PRIDEiP47756.

2D gel databases

DOSAC-COBS-2DPAGEP47756.
OGPiP47756.
REPRODUCTION-2DPAGEIPI00026185.
SWISS-2DPAGEP47756.

PTM databases

PhosphoSiteiP47756.

Expressioni

Gene expression databases

ArrayExpressiP47756.
BgeeiP47756.
CleanExiHS_CAPZB.
GenevestigatoriP47756.

Organism-specific databases

HPAiHPA031531.
HPA056066.

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), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53.3 Publications

Protein-protein interaction databases

BioGridi107282. 44 interactions.
IntActiP47756. 17 interactions.
MINTiMINT-254051.
STRINGi9606.ENSP00000364287.

Structurei

3D structure databases

ProteinModelPortaliP47756.
SMRiP47756. Positions 2-251.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG291067.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
KOiK10365.
OMAiFDTYREM.
PhylomeDBiP47756.
TreeFamiTF105732.

Family and domain databases

InterProiIPR001698. CapZ_beta.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P47756-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA    50
RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA 100
NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS 150
IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KSGSGTMNLG GSLTRQMEKD 200
ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSIDAIP 250
DNQKFKQLQR ELSQVLTQRQ IYIQPDN 277
Length:277
Mass (Da):31,350
Last modified:January 23, 2007 - v4
Checksum:iABA1621F9E0152A6
GO
Isoform 2 (identifier: P47756-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-277: IDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC

Show »
Length:272
Mass (Da):30,629
Checksum:iE6466A68B1254FD0
GO
Isoform 3 (identifier: P47756-3)

Sequence is not available
Length:
Mass (Da):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei246 – 27732IDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2. VSP_000767Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41277.1. [P47756-2]
CCDS55579.1. [P47756-1]
RefSeqiNP_001193469.1. NM_001206540.2. [P47756-1]
NP_001269091.1. NM_001282162.1.
NP_004921.1. NM_004930.4. [P47756-2]
UniGeneiHs.432760.

Genome annotation databases

EnsembliENST00000264202; ENSP00000264202; ENSG00000077549. [P47756-1]
ENST00000375142; ENSP00000364284; ENSG00000077549. [P47756-1]
ENST00000401084; ENSP00000383862; ENSG00000077549. [P47756-2]
GeneIDi832.
KEGGihsa:832.
UCSCiuc001bce.3. human. [P47756-2]
uc021ohr.1. human. [P47756-1]

Polymorphism databases

DMDMi13124696.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41277.1. [P47756-2 ]
CCDS55579.1. [P47756-1 ]
RefSeqi NP_001193469.1. NM_001206540.2. [P47756-1 ]
NP_001269091.1. NM_001282162.1.
NP_004921.1. NM_004930.4. [P47756-2 ]
UniGenei Hs.432760.

3D structure databases

ProteinModelPortali P47756.
SMRi P47756. Positions 2-251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107282. 44 interactions.
IntActi P47756. 17 interactions.
MINTi MINT-254051.
STRINGi 9606.ENSP00000364287.

PTM databases

PhosphoSitei P47756.

Polymorphism databases

DMDMi 13124696.

2D gel databases

DOSAC-COBS-2DPAGE P47756.
OGPi P47756.
REPRODUCTION-2DPAGE IPI00026185.
SWISS-2DPAGE P47756.

Proteomic databases

MaxQBi P47756.
PaxDbi P47756.
PRIDEi P47756.

Protocols and materials databases

DNASUi 832.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264202 ; ENSP00000264202 ; ENSG00000077549 . [P47756-1 ]
ENST00000375142 ; ENSP00000364284 ; ENSG00000077549 . [P47756-1 ]
ENST00000401084 ; ENSP00000383862 ; ENSG00000077549 . [P47756-2 ]
GeneIDi 832.
KEGGi hsa:832.
UCSCi uc001bce.3. human. [P47756-2 ]
uc021ohr.1. human. [P47756-1 ]

Organism-specific databases

CTDi 832.
GeneCardsi GC01M019665.
HGNCi HGNC:1491. CAPZB.
HPAi HPA031531.
HPA056066.
MIMi 601572. gene.
neXtProti NX_P47756.
PharmGKBi PA26072.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291067.
HOGENOMi HOG000041208.
HOVERGENi HBG050789.
KOi K10365.
OMAi FDTYREM.
PhylomeDBi P47756.
TreeFami TF105732.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi CAPZB. human.
GeneWikii CAPZB.
GenomeRNAii 832.
NextBioi 3446.
PROi P47756.
SOURCEi Search...

Gene expression databases

ArrayExpressi P47756.
Bgeei P47756.
CleanExi HS_CAPZB.
Genevestigatori P47756.

Family and domain databases

InterProi IPR001698. CapZ_beta.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view ]
PANTHERi PTHR10619. PTHR10619. 1 hit.
Pfami PF01115. F_actin_cap_B. 1 hit.
[Graphical view ]
PRINTSi PR00192. FACTINCAPB.
PROSITEi PS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPZB_HUMAN
AccessioniPrimary (citable) accession number: P47756
Secondary accession number(s): Q32Q68
, Q5U0L4, Q8TB49, Q9NUC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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