Full text data of CAPZB
CAPZB
[Confidence: high (present in two of the MS resources)]
F-actin-capping protein subunit beta (CapZ beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
F-actin-capping protein subunit beta (CapZ beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00026185
IPI00026185 Splice isoform 1 of P47756 F-actin capping protein beta subunit Splice isoform 1 of P47756 F-actin capping protein beta subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 cytoskeleton associated SIDAIPDNQK, ELSQVLTQR found at its expected molecular weight found at molecular weight
IPI00026185 Splice isoform 1 of P47756 F-actin capping protein beta subunit Splice isoform 1 of P47756 F-actin capping protein beta subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 cytoskeleton associated SIDAIPDNQK, ELSQVLTQR found at its expected molecular weight found at molecular weight
UniProt
P47756
ID CAPZB_HUMAN Reviewed; 277 AA.
AC P47756; Q32Q68; Q5U0L4; Q8TB49; Q9NUC4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=CapZ beta;
GN Name=CAPZB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=7665558; DOI=10.1074/jbc.270.37.21472;
RA Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q.,
RA Tsui L.-C., Casella J.F.;
RT "Sequence analysis and chromosomal localization of human Cap Z.
RT Conserved residues within the actin-binding domain may link Cap Z to
RT gelsolin/severin and profilin protein families.";
RL J. Biol. Chem. 270:21472-21479(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 95-108, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP INTERACTION WITH RCSD1/CAPZIP, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15850461; DOI=10.1042/BJ20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C.,
RA Cuenda A., Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [9]
RP INTERACTION WITH ARHGAP17.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC manner to the fast growing ends of actin filaments (barbed end)
CC thereby blocking the exchange of subunits at these ends. Unlike
CC other capping proteins (such as gelsolin and severin), these
CC proteins do not sever actin filaments. Plays a role in the
CC regulation of cell morphology and cytoskeletal organization.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
CC with ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex,
CC composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2
CC or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH
CC (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A,
CC FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cytoplasm, myofibril, sarcomere (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P47756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47756-2; Sequence=VSP_000767;
CC Name=3;
CC IsoId=P47756-3; Sequence=Not described;
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit
CC family.
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DR EMBL; U03271; AAA87395.1; -; mRNA.
DR EMBL; BT019470; AAV38277.1; -; mRNA.
DR EMBL; BT019471; AAV38278.1; -; mRNA.
DR EMBL; AL035413; CAI22231.1; -; Genomic_DNA.
DR EMBL; AL359199; CAI22231.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAI22231.1; JOINED; Genomic_DNA.
DR EMBL; AL359199; CAH72124.1; -; Genomic_DNA.
DR EMBL; AL035413; CAH72124.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAH72124.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAH71392.1; -; Genomic_DNA.
DR EMBL; AL035413; CAH71392.1; JOINED; Genomic_DNA.
DR EMBL; AL359199; CAH71392.1; JOINED; Genomic_DNA.
DR EMBL; CH471134; EAW94890.1; -; Genomic_DNA.
DR EMBL; BC024601; AAH24601.1; -; mRNA.
DR EMBL; BC107752; AAI07753.1; -; mRNA.
DR EMBL; BC109241; AAI09242.1; -; mRNA.
DR EMBL; BC109242; AAI09243.1; -; mRNA.
DR RefSeq; NP_001193469.1; NM_001206540.2.
DR RefSeq; NP_001269091.1; NM_001282162.1.
DR RefSeq; NP_004921.1; NM_004930.4.
DR UniGene; Hs.432760; -.
DR ProteinModelPortal; P47756; -.
DR SMR; P47756; 2-251.
DR IntAct; P47756; 17.
DR MINT; MINT-254051; -.
DR STRING; 9606.ENSP00000364287; -.
DR PhosphoSite; P47756; -.
DR DMDM; 13124696; -.
DR DOSAC-COBS-2DPAGE; P47756; -.
DR OGP; P47756; -.
DR REPRODUCTION-2DPAGE; IPI00026185; -.
DR SWISS-2DPAGE; P47756; -.
DR PaxDb; P47756; -.
DR PRIDE; P47756; -.
DR DNASU; 832; -.
DR Ensembl; ENST00000264202; ENSP00000264202; ENSG00000077549.
DR Ensembl; ENST00000375142; ENSP00000364284; ENSG00000077549.
DR Ensembl; ENST00000401084; ENSP00000383862; ENSG00000077549.
DR GeneID; 832; -.
DR KEGG; hsa:832; -.
DR UCSC; uc021ohr.1; human.
DR CTD; 832; -.
DR GeneCards; GC01M019665; -.
DR HGNC; HGNC:1491; CAPZB.
DR HPA; HPA031531; -.
DR MIM; 601572; gene.
DR neXtProt; NX_P47756; -.
DR PharmGKB; PA26072; -.
DR eggNOG; NOG291067; -.
DR HOGENOM; HOG000041208; -.
DR HOVERGEN; HBG050789; -.
DR KO; K10365; -.
DR OMA; FDTYREM; -.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CAPZB; human.
DR GeneWiki; CAPZB; -.
DR GenomeRNAi; 832; -.
DR NextBio; 3446; -.
DR PRO; PR:P47756; -.
DR ArrayExpress; P47756; -.
DR Bgee; P47756; -.
DR CleanEx; HS_CAPZB; -.
DR Genevestigator; P47756; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; TAS:ProtInc.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR001698; CapZ_beta.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative splicing;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 277 F-actin-capping protein subunit beta.
FT /FTId=PRO_0000204634.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 235 235 N6-acetyllysine.
FT VAR_SEQ 246 277 IDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN -> VQTFA
FT DKSKQEALKNDLVEALKRKQQC (in isoform 2).
FT /FTId=VSP_000767.
SQ SEQUENCE 277 AA; 31350 MW; ABA1621F9E0152A6 CRC64;
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
NGLRSIDAIP DNQKFKQLQR ELSQVLTQRQ IYIQPDN
//
ID CAPZB_HUMAN Reviewed; 277 AA.
AC P47756; Q32Q68; Q5U0L4; Q8TB49; Q9NUC4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=CapZ beta;
GN Name=CAPZB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=7665558; DOI=10.1074/jbc.270.37.21472;
RA Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q.,
RA Tsui L.-C., Casella J.F.;
RT "Sequence analysis and chromosomal localization of human Cap Z.
RT Conserved residues within the actin-binding domain may link Cap Z to
RT gelsolin/severin and profilin protein families.";
RL J. Biol. Chem. 270:21472-21479(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 95-108, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP INTERACTION WITH RCSD1/CAPZIP, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15850461; DOI=10.1042/BJ20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C.,
RA Cuenda A., Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [9]
RP INTERACTION WITH ARHGAP17.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC manner to the fast growing ends of actin filaments (barbed end)
CC thereby blocking the exchange of subunits at these ends. Unlike
CC other capping proteins (such as gelsolin and severin), these
CC proteins do not sever actin filaments. Plays a role in the
CC regulation of cell morphology and cytoskeletal organization.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
CC with ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex,
CC composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2
CC or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH
CC (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A,
CC FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cytoplasm, myofibril, sarcomere (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P47756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47756-2; Sequence=VSP_000767;
CC Name=3;
CC IsoId=P47756-3; Sequence=Not described;
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit
CC family.
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DR EMBL; U03271; AAA87395.1; -; mRNA.
DR EMBL; BT019470; AAV38277.1; -; mRNA.
DR EMBL; BT019471; AAV38278.1; -; mRNA.
DR EMBL; AL035413; CAI22231.1; -; Genomic_DNA.
DR EMBL; AL359199; CAI22231.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAI22231.1; JOINED; Genomic_DNA.
DR EMBL; AL359199; CAH72124.1; -; Genomic_DNA.
DR EMBL; AL035413; CAH72124.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAH72124.1; JOINED; Genomic_DNA.
DR EMBL; AL445163; CAH71392.1; -; Genomic_DNA.
DR EMBL; AL035413; CAH71392.1; JOINED; Genomic_DNA.
DR EMBL; AL359199; CAH71392.1; JOINED; Genomic_DNA.
DR EMBL; CH471134; EAW94890.1; -; Genomic_DNA.
DR EMBL; BC024601; AAH24601.1; -; mRNA.
DR EMBL; BC107752; AAI07753.1; -; mRNA.
DR EMBL; BC109241; AAI09242.1; -; mRNA.
DR EMBL; BC109242; AAI09243.1; -; mRNA.
DR RefSeq; NP_001193469.1; NM_001206540.2.
DR RefSeq; NP_001269091.1; NM_001282162.1.
DR RefSeq; NP_004921.1; NM_004930.4.
DR UniGene; Hs.432760; -.
DR ProteinModelPortal; P47756; -.
DR SMR; P47756; 2-251.
DR IntAct; P47756; 17.
DR MINT; MINT-254051; -.
DR STRING; 9606.ENSP00000364287; -.
DR PhosphoSite; P47756; -.
DR DMDM; 13124696; -.
DR DOSAC-COBS-2DPAGE; P47756; -.
DR OGP; P47756; -.
DR REPRODUCTION-2DPAGE; IPI00026185; -.
DR SWISS-2DPAGE; P47756; -.
DR PaxDb; P47756; -.
DR PRIDE; P47756; -.
DR DNASU; 832; -.
DR Ensembl; ENST00000264202; ENSP00000264202; ENSG00000077549.
DR Ensembl; ENST00000375142; ENSP00000364284; ENSG00000077549.
DR Ensembl; ENST00000401084; ENSP00000383862; ENSG00000077549.
DR GeneID; 832; -.
DR KEGG; hsa:832; -.
DR UCSC; uc021ohr.1; human.
DR CTD; 832; -.
DR GeneCards; GC01M019665; -.
DR HGNC; HGNC:1491; CAPZB.
DR HPA; HPA031531; -.
DR MIM; 601572; gene.
DR neXtProt; NX_P47756; -.
DR PharmGKB; PA26072; -.
DR eggNOG; NOG291067; -.
DR HOGENOM; HOG000041208; -.
DR HOVERGEN; HBG050789; -.
DR KO; K10365; -.
DR OMA; FDTYREM; -.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CAPZB; human.
DR GeneWiki; CAPZB; -.
DR GenomeRNAi; 832; -.
DR NextBio; 3446; -.
DR PRO; PR:P47756; -.
DR ArrayExpress; P47756; -.
DR Bgee; P47756; -.
DR CleanEx; HS_CAPZB; -.
DR Genevestigator; P47756; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; TAS:ProtInc.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR001698; CapZ_beta.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative splicing;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 277 F-actin-capping protein subunit beta.
FT /FTId=PRO_0000204634.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 235 235 N6-acetyllysine.
FT VAR_SEQ 246 277 IDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN -> VQTFA
FT DKSKQEALKNDLVEALKRKQQC (in isoform 2).
FT /FTId=VSP_000767.
SQ SEQUENCE 277 AA; 31350 MW; ABA1621F9E0152A6 CRC64;
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
NGLRSIDAIP DNQKFKQLQR ELSQVLTQRQ IYIQPDN
//
MIM
601572
*RECORD*
*FIELD* NO
601572
*FIELD* TI
*601572 CAPPING PROTEIN, BETA; CAPZB
;;CAP PROTEIN, ACTIN, BETA; CAPPB
*FIELD* TX
read moreCLONING
CapZ was identified in chicken as an actin-binding protein composed of
alpha (see 601580) and beta subunits. From a human retina cDNA library,
Barron-Casella et al. (1995) isolated cDNAs homologous for the beta
subunit of chicken CapZ.
MAPPING
Barron-Casella et al. (1995) mapped the CAPZB gene to chromosome 1p36.1
by fluorescence in situ hybridization.
HISTORY
In the course of mapping 39 ESTs on chromosome 6p24-p23, Olavesen et al.
(1997) concluded that CAPZB is located in that region flanked by EDN1
(131240) on the centromeric side and TFAP2 (107580) on the telomeric
side. However, Cooper (1999) stated that a 'simple clerical error'
occurred at the outset of this project; the EST in question does not
share sequence similarity with the CAPZB gene and, therefore, the
mapping of the CAPZB gene to chromosome 6p24-p23 is incorrect.
*FIELD* RF
1. Barron-Casella, E. A.; Torres, M. A.; Scherer, S. W.; Heng, H.
H. Q.; Tsui, L.-C.; Casella, J. F.: 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. J.
Biol. Chem. 270: 21472-21479, 1995.
2. Cooper, J. A.: Personal Communication. St. Louis, Mo. 3/8/1999.
3. Olavesen, M. G.; Bentley, E.; Mason, R. V. F.; Stephens, R. J.;
Ragoussis, J.: Fine mapping of 39 ESTs on human chromosome 6p23-p25. Genomics 46:
303-306, 1997.
*FIELD* CN
Patti M. Sherman - updated: 9/8/2000
Victor A. McKusick - updated: 2/11/1998
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
mgross: 11/21/2012
terry: 10/26/2012
joanna: 6/10/2004
mgross: 6/10/2004
mcapotos: 9/12/2000
psherman: 9/8/2000
mark: 2/11/1998
mark: 12/17/1996
mark: 12/16/1996
*RECORD*
*FIELD* NO
601572
*FIELD* TI
*601572 CAPPING PROTEIN, BETA; CAPZB
;;CAP PROTEIN, ACTIN, BETA; CAPPB
*FIELD* TX
read moreCLONING
CapZ was identified in chicken as an actin-binding protein composed of
alpha (see 601580) and beta subunits. From a human retina cDNA library,
Barron-Casella et al. (1995) isolated cDNAs homologous for the beta
subunit of chicken CapZ.
MAPPING
Barron-Casella et al. (1995) mapped the CAPZB gene to chromosome 1p36.1
by fluorescence in situ hybridization.
HISTORY
In the course of mapping 39 ESTs on chromosome 6p24-p23, Olavesen et al.
(1997) concluded that CAPZB is located in that region flanked by EDN1
(131240) on the centromeric side and TFAP2 (107580) on the telomeric
side. However, Cooper (1999) stated that a 'simple clerical error'
occurred at the outset of this project; the EST in question does not
share sequence similarity with the CAPZB gene and, therefore, the
mapping of the CAPZB gene to chromosome 6p24-p23 is incorrect.
*FIELD* RF
1. Barron-Casella, E. A.; Torres, M. A.; Scherer, S. W.; Heng, H.
H. Q.; Tsui, L.-C.; Casella, J. F.: 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. J.
Biol. Chem. 270: 21472-21479, 1995.
2. Cooper, J. A.: Personal Communication. St. Louis, Mo. 3/8/1999.
3. Olavesen, M. G.; Bentley, E.; Mason, R. V. F.; Stephens, R. J.;
Ragoussis, J.: Fine mapping of 39 ESTs on human chromosome 6p23-p25. Genomics 46:
303-306, 1997.
*FIELD* CN
Patti M. Sherman - updated: 9/8/2000
Victor A. McKusick - updated: 2/11/1998
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
mgross: 11/21/2012
terry: 10/26/2012
joanna: 6/10/2004
mgross: 6/10/2004
mcapotos: 9/12/2000
psherman: 9/8/2000
mark: 2/11/1998
mark: 12/17/1996
mark: 12/16/1996