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P52907 (CAZA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-actin-capping protein subunit alpha-1
Alternative name(s):
CapZ alpha-1
Gene names
Name:CAPZA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9

Subcellular location

Cytoplasmcytoskeleton By similarity.

Sequence similarities

Belongs to the F-actin-capping protein alpha subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SH3KBP1Q96B972EBI-355586,EBI-346595

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 286285F-actin-capping protein subunit alpha-1
PRO_0000208624

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.8
Modified residue191N6-acetyllysine Ref.10
Modified residue971N6-acetyllysine Ref.10

Experimental info

Sequence conflict1921L → P in BAD96946. Ref.4

Secondary structure

... 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52907 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0F47ADAB6A3689DD

FASTA28632,923
        10         20         30         40         50         60 
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD 

        70         80         90        100        110        120 
QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW 

       130        140        150        160        170        180 
RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT 

       190        200        210        220        230        240 
ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ 

       250        260        270        280 
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG02639.
RefSeqNP_006126.1. NM_006135.2.
UniGeneHs.744974.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ1NMR-C/D265-276[»]
1MWNNMR-X/Y265-276[»]
ProteinModelPortalP52907.
SMRP52907. Positions 7-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107279. 39 interactions.
IntActP52907. 15 interactions.
MINTMINT-5001076.
STRING9606.ENSP00000263168.

PTM databases

PhosphoSiteP52907.

2D gel databases

OGPP52907.
REPRODUCTION-2DPAGEIPI00005969.
P52907.
SWISS-2DPAGEP52907.

Proteomic databases

PaxDbP52907.
PeptideAtlasP52907.
PRIDEP52907.

Protocols and materials databases

DNASU829.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263168; ENSP00000263168; ENSG00000116489.
GeneID829.
KEGGhsa:829.
UCSCuc001ecj.1. human.

Organism-specific databases

CTD829.
GeneCardsGC01P113161.
HGNCHGNC:1488. CAPZA1.
HPACAB045963.
MIM601580. gene.
neXtProtNX_P52907.
PharmGKBPA26069.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261759.
HOGENOMHOG000036539.
HOVERGENHBG050810.
InParanoidP52907.
KOK10364.
OMAACDSALR.
OrthoDBEOG71ZP25.
PhylomeDBP52907.
TreeFamTF314822.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

BgeeP52907.
CleanExHS_CAPZA1.
GenevestigatorP52907.

Family and domain databases

InterProIPR002189. CapZ_alpha.
IPR017865. F-actin_cap_asu_CS.
[Graphical view]
PANTHERPTHR10653. PTHR10653. 1 hit.
PfamPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSPR00191. FACTINCAPA.
PROSITEPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPZA1. human.
EvolutionaryTraceP52907.
GenomeRNAi829.
NextBio3414.
PROP52907.
SOURCESearch...

Entry information

Entry nameCAZA1_HUMAN
AccessionPrimary (citable) accession number: P52907
Secondary accession number(s): Q53FQ6, Q6FHD5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM