Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

F-actin-capping protein subunit alpha-1

Gene

CAPZA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  1. barbed-end actin filament capping Source: InterPro
  2. blood coagulation Source: Reactome
  3. innate immune response Source: Reactome
  4. movement of cell or subcellular component Source: UniProtKB
  5. 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: UniProtKB
  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 – 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.
ExpressionAtlasiP52907. baseline and differential.
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. 51 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 – 2755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000006476.
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

        10         20         30         40         50
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH
110 120 130 140 150
LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG
160 170 180 190 200
QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVVG VLKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
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 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi107279. 51 interactions.
IntActiP52907. 16 interactions.
MINTiMINT-5001076.
STRINGi9606.ENSP00000263168.

PTM databases

PhosphoSiteiP52907.

2D gel databases

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

Proteomic databases

MaxQBiP52907.
PaxDbiP52907.
PeptideAtlasiP52907.
PRIDEiP52907.

Protocols and materials databases

DNASUi829.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi829.
GeneCardsiGC01P113161.
HGNCiHGNC:1488. CAPZA1.
HPAiCAB045963.
MIMi601580. gene.
neXtProtiNX_P52907.
PharmGKBiPA26069.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261759.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP52907.
KOiK10364.
OMAiACDSALR.
OrthoDBiEOG71ZP25.
PhylomeDBiP52907.
TreeFamiTF314822.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiCAPZA1. human.
EvolutionaryTraceiP52907.
GenomeRNAii829.
NextBioi3414.
PROiP52907.
SOURCEiSearch...

Gene expression databases

BgeeiP52907.
CleanExiHS_CAPZA1.
ExpressionAtlasiP52907. baseline and differential.
GenevestigatoriP52907.

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]
ProtoNetiSearch...

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], CLEAVAGE OF INITIATOR METHIONINE [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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.
  14. "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: March 4, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.