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P52907

- CAZA1_HUMAN

UniProt

P52907 - CAZA1_HUMAN

Protein

F-actin-capping protein subunit alpha-1

Gene

CAPZA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (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.

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. actin filament capping Source: UniProtKB-KW
    3. blood coagulation Source: Reactome
    4. cellular component movement Source: UniProtKB
    5. innate immune response Source: Reactome
    6. protein complex assembly Source: ProtInc

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-actin-capping protein subunit alpha-1
    Alternative name(s):
    CapZ alpha-1
    Gene namesi
    Name:CAPZA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1488. CAPZA1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. F-actin capping protein complex Source: ProtInc
    7. WASH complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26069.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 286285F-actin-capping protein subunit alpha-1PRO_0000208624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei19 – 191N6-acetyllysine1 Publication
    Modified residuei97 – 971N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP52907.
    PaxDbiP52907.
    PeptideAtlasiP52907.
    PRIDEiP52907.

    2D gel databases

    OGPiP52907.
    REPRODUCTION-2DPAGEIPI00005969.
    P52907.
    SWISS-2DPAGEP52907.

    PTM databases

    PhosphoSiteiP52907.

    Expressioni

    Gene expression databases

    BgeeiP52907.
    CleanExiHS_CAPZA1.
    GenevestigatoriP52907.

    Organism-specific databases

    HPAiCAB045963.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Interacts with S100A By similarity. 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. Interacts with S100B.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SH3KBP1Q96B972EBI-355586,EBI-346595

    Protein-protein interaction databases

    BioGridi107279. 43 interactions.
    IntActiP52907. 16 interactions.
    MINTiMINT-5001076.
    STRINGi9606.ENSP00000263168.

    Structurei

    Secondary structure

    1
    286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi271 – 2755

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MQ1NMR-C/D265-276[»]
    1MWNNMR-X/Y265-276[»]
    ProteinModelPortaliP52907.
    SMRiP52907. Positions 7-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52907.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG261759.
    HOGENOMiHOG000036539.
    HOVERGENiHBG050810.
    InParanoidiP52907.
    KOiK10364.
    OMAiACDSALR.
    OrthoDBiEOG71ZP25.
    PhylomeDBiP52907.
    TreeFamiTF314822.

    Family and domain databases

    InterProiIPR002189. CapZ_alpha.
    IPR017865. F-actin_cap_asu_CS.
    [Graphical view]
    PANTHERiPTHR10653. PTHR10653. 1 hit.
    PfamiPF01267. F-actin_cap_A. 1 hit.
    [Graphical view]
    PRINTSiPR00191. FACTINCAPA.
    PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
    PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52907-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA    50
    AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH 100
    LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG 150
    QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVVG VLKIQVHYYE 200
    DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ TAISENYQTM 250
    SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA 286
    Length:286
    Mass (Da):32,923
    Last modified:January 23, 2007 - v3
    Checksum:i0F47ADAB6A3689DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921L → P in BAD96946. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56637 mRNA. Translation: AAC00533.1.
    CR407657 mRNA. Translation: CAG28585.1.
    CR541819 mRNA. Translation: CAG46618.1.
    BT019364 mRNA. Translation: AAV38171.1.
    AK223226 mRNA. Translation: BAD96946.1.
    AL603832, AL929470 Genomic DNA. Translation: CAI14054.1.
    AL929470, AL603832 Genomic DNA. Translation: CAI16528.1.
    BC000144 mRNA. Translation: AAH00144.1.
    CCDSiCCDS30805.1.
    PIRiG02639.
    RefSeqiNP_006126.1. NM_006135.2.
    UniGeneiHs.744974.

    Genome annotation databases

    EnsembliENST00000263168; ENSP00000263168; ENSG00000116489.
    GeneIDi829.
    KEGGihsa:829.
    UCSCiuc001ecj.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56637 mRNA. Translation: AAC00533.1 .
    CR407657 mRNA. Translation: CAG28585.1 .
    CR541819 mRNA. Translation: CAG46618.1 .
    BT019364 mRNA. Translation: AAV38171.1 .
    AK223226 mRNA. Translation: BAD96946.1 .
    AL603832 , AL929470 Genomic DNA. Translation: CAI14054.1 .
    AL929470 , AL603832 Genomic DNA. Translation: CAI16528.1 .
    BC000144 mRNA. Translation: AAH00144.1 .
    CCDSi CCDS30805.1.
    PIRi G02639.
    RefSeqi NP_006126.1. NM_006135.2.
    UniGenei Hs.744974.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MQ1 NMR - C/D 265-276 [» ]
    1MWN NMR - X/Y 265-276 [» ]
    ProteinModelPortali P52907.
    SMRi P52907. Positions 7-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107279. 43 interactions.
    IntActi P52907. 16 interactions.
    MINTi MINT-5001076.
    STRINGi 9606.ENSP00000263168.

    PTM databases

    PhosphoSitei P52907.

    2D gel databases

    OGPi P52907.
    REPRODUCTION-2DPAGE IPI00005969.
    P52907.
    SWISS-2DPAGE P52907.

    Proteomic databases

    MaxQBi P52907.
    PaxDbi P52907.
    PeptideAtlasi P52907.
    PRIDEi P52907.

    Protocols and materials databases

    DNASUi 829.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263168 ; ENSP00000263168 ; ENSG00000116489 .
    GeneIDi 829.
    KEGGi hsa:829.
    UCSCi uc001ecj.1. human.

    Organism-specific databases

    CTDi 829.
    GeneCardsi GC01P113161.
    HGNCi HGNC:1488. CAPZA1.
    HPAi CAB045963.
    MIMi 601580. gene.
    neXtProti NX_P52907.
    PharmGKBi PA26069.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261759.
    HOGENOMi HOG000036539.
    HOVERGENi HBG050810.
    InParanoidi P52907.
    KOi K10364.
    OMAi ACDSALR.
    OrthoDBi EOG71ZP25.
    PhylomeDBi P52907.
    TreeFami TF314822.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.

    Miscellaneous databases

    ChiTaRSi CAPZA1. human.
    EvolutionaryTracei P52907.
    GenomeRNAii 829.
    NextBioi 3414.
    PROi P52907.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52907.
    CleanExi HS_CAPZA1.
    Genevestigatori P52907.

    Family and domain databases

    InterProi IPR002189. CapZ_alpha.
    IPR017865. F-actin_cap_asu_CS.
    [Graphical view ]
    PANTHERi PTHR10653. PTHR10653. 1 hit.
    Pfami PF01267. F-actin_cap_A. 1 hit.
    [Graphical view ]
    PRINTSi PR00191. FACTINCAPA.
    PROSITEi PS00748. F_ACTIN_CAPPING_A_1. 1 hit.
    PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns."
      Hart M.C., Korshunova Y.O., Cooper J.A.
      Cell Motil. Cytoskeleton 38:120-132(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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].
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Gastric mucosa.
    5. "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].
    6. "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: Cervix.
    7. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    8. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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.
    10. "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-19 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12."
      Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M., Weber D.J.
      J. Mol. Biol. 324:1003-1014(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
    13. "A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex."
      McClintock K.A., Shaw G.S.
      J. Biol. Chem. 278:6251-6257(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.

    Entry informationi

    Entry nameiCAZA1_HUMAN
    AccessioniPrimary (citable) accession number: P52907
    Secondary accession number(s): Q53FQ6, Q6FHD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3