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P47756

- CAPZB_HUMAN

UniProt

P47756 - CAPZB_HUMAN

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
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26072.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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. 3 PublicationsVSP_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]
    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 ]
    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

    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: October 1, 2014
    This is version 143 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