P47756 (CAPZB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-actin-capping protein subunit beta

Alternative name(s):
CapZ beta

Gene names

Name:

CAPZB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Plays a role in the regulation of cell morphology and cytoskeletal organization. Ref.12
Subunit structure	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. Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the F-actin-capping protein beta subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding
Molecular function	Actin capping
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Traceable author statement. Source: Reactome cellular component movement Traceable author statement PubMed 16130169. Source: UniProtKB cytoskeleton organization Inferred from mutant phenotype Ref.12. Source: UniProtKB lamellipodium assembly Inferred from electronic annotation. Source: Compara regulation of cell morphogenesis Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	F-actin capping protein complex Traceable author statement Ref.1. Source: ProtInc WASH complex Inferred from direct assay Ref.10. Source: UniProtKB cortical cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from electronic annotation. Source: Compara membrane Inferred from electronic annotation. Source: Compara
Molecular_function	actin binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P47756-1)

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.

Isoform 2 (identifier: P47756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     246-277: IDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC

Isoform 3 (identifier: P47756-3)

The sequence of this isoform is not available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 277	276	F-actin-capping protein subunit beta		PRO_0000204634
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.6
	Modified residue	182	1	Phosphoserine By similarity
	Modified residue	235	1	N6-acetyllysine Ref.11
Natural variations
	Alternative sequence	246 – 277	32	IDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2.		VSP_000767

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: ABA1621F9E0152A6	FASTA	277	31,350
	10 20 30 40 50 60 MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL 70 80 90 100 110 120 LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY 130 140 150 160 170 180 LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN 190 200 210 220 230 240 KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV 250 260 270 NGLRSIDAIP DNQKFKQLQR ELSQVLTQRQ IYIQPDN
	Isoform 2 [UniParc]. Checksum: E6466A68B1254FD0	FASTA	272	30,629
	10 20 30 40 50 60 MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL 70 80 90 100 110 120 LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY 130 140 150 160 170 180 LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN 190 200 210 220 230 240 KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV 250 260 270 NGLRSVQTFA DKSKQEALKN DLVEALKRKQ QC
	Isoform 3 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"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.
[11]	"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, MASS SPECTROMETRY.
[12]	"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.
[13]	"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].
[14]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00026185. IPI00642256.
RefSeq	NP_001193469.1. NM_001206540.1. NP_004921.1. NM_004930.3.
UniGene	Hs.432760.
3D structure databases
ProteinModelPortal	P47756.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47756. 15 interactions.
MINT	MINT-254051.
STRING	9606.ENSP00000364287.
PTM databases
PhosphoSite	P47756.
Polymorphism databases
DMDM	13124696.
2D gel databases
DOSAC-COBS-2DPAGE	P47756.
OGP	P47756.
REPRODUCTION-2DPAGE	IPI00026185.
SWISS-2DPAGE	P47756.
Proteomic databases
PaxDb	P47756.
PRIDE	P47756.
Protocols and materials databases
DNASU	832.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264202; ENSP00000264202; ENSG00000077549. ENST00000375142; ENSP00000364284; ENSG00000077549. ENST00000401084; ENSP00000383862; ENSG00000077549.
GeneID	832.
KEGG	hsa:832.
UCSC	uc001bce.3. human. uc021ohr.1. human.
Organism-specific databases
CTD	832.
GeneCards	GC01M019665.
HGNC	HGNC:1491. CAPZB.
HPA	HPA031531.
MIM	601572. gene.
neXtProt	NX_P47756.
PharmGKB	PA26072.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291067.
HOGENOM	HOG000041208.
HOVERGEN	HBG050789.
KO	K10365.
OMA	NLLQEVY.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P47756.
Bgee	P47756.
CleanEx	HS_CAPZB.
Genevestigator	P47756.
GermOnline	ENSG00000077549. Homo sapiens.
Family and domain databases
InterPro	IPR019771. F-actin_capping_bsu_CS. IPR001698. WASH_F-actin_cap_beta. [Graphical view]
PANTHER	PTHR10619. PTHR10619. 1 hit.
Pfam	PF01115. F_actin_cap_B. 1 hit. [Graphical view]
PRINTS	PR00192. FACTINCAPB.
PROSITE	PS00231. F_ACTIN_CAPPING_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CAPZB. human.
GenomeRNAi	832.
NextBio	3446.
SOURCE	Search...

Entry information

Entry name

CAPZB_HUMAN

Accession

Primary (citable) accession number: P47756
Secondary accession number(s): Q32Q68 , Q5U0L4, Q8TB49, Q9NUC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 128 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.