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P52907

- CAZA1_HUMAN

UniProt

P52907 - CAZA1_HUMAN

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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

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
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.
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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26069.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
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.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107279. 43 interactions.
IntActiP52907. 15 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.

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

Sequence conflict

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

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. 15 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

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