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Protein

F-actin-capping protein subunit beta

Gene

CAPZB

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. Plays a role in the regulation of cell morphology and cytoskeletal organization.1 Publication

GO - Molecular functioni

  • actin binding Source: ProtInc
  • actin filament binding Source: GO_Central

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • barbed-end actin filament capping Source: GO_Central
  • blood coagulation Source: Reactome
  • cell morphogenesis Source: GO_Central
  • cytoskeleton organization Source: UniProtKB
  • movement of cell or subcellular component Source: UniProtKB
  • negative regulation of filopodium assembly Source: GO_Central
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of lamellipodium assembly Source: GO_Central
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.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Alternative name(s):
CapZ beta
Gene namesi
Name:CAPZB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1491. CAPZB.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • actin filament Source: GO_Central
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • F-actin capping protein complex Source: ProtInc
  • sarcomere Source: UniProtKB-SubCell
  • WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26072.

Polymorphism and mutation databases

DMDMi13124696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 277276F-actin-capping protein subunit betaPRO_0000204634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei235 – 2351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47756.
PaxDbiP47756.
PRIDEiP47756.

2D gel databases

DOSAC-COBS-2DPAGEP47756.
OGPiP47756.
REPRODUCTION-2DPAGEIPI00026185.
SWISS-2DPAGEP47756.

PTM databases

PhosphoSiteiP47756.

Expressioni

Gene expression databases

BgeeiP47756.
CleanExiHS_CAPZB.
ExpressionAtlasiP47756. baseline and differential.
GenevisibleiP47756. HS.

Organism-specific databases

HPAiHPA031531.
HPA056066.

Interactioni

Subunit structurei

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 CCDC53.3 Publications

Protein-protein interaction databases

BioGridi107282. 55 interactions.
IntActiP47756. 19 interactions.
MINTiMINT-254051.
STRINGi9606.ENSP00000264202.

Structurei

3D structure databases

ProteinModelPortaliP47756.
SMRiP47756. Positions 2-251.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiP47756.
KOiK10365.
PhylomeDBiP47756.
TreeFamiTF105732.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47756-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA
60 70 80 90 100
RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA
110 120 130 140 150
NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS
160 170 180 190 200
IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KSGSGTMNLG GSLTRQMEKD
210 220 230 240 250
ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSIDAIP
260 270
DNQKFKQLQR ELSQVLTQRQ IYIQPDN
Length:277
Mass (Da):31,350
Last modified:January 23, 2007 - v4
Checksum:iABA1621F9E0152A6
GO
Isoform 2 (identifier: P47756-2) [UniParc]FASTAAdd to basket

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

Show »
Length:272
Mass (Da):30,629
Checksum:iE6466A68B1254FD0
GO
Isoform 3 (identifier: P47756-3)

Sequence is not available
Length:
Mass (Da):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei246 – 27732IDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2. 3 PublicationsVSP_000767Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41277.1. [P47756-2]
CCDS55579.1. [P47756-1]
RefSeqiNP_001193469.1. NM_001206540.2. [P47756-1]
NP_001269091.1. NM_001282162.1.
NP_004921.1. NM_004930.4. [P47756-2]
UniGeneiHs.432760.

Genome annotation databases

EnsembliENST00000264202; ENSP00000264202; ENSG00000077549. [P47756-2]
ENST00000375142; ENSP00000364284; ENSG00000077549. [P47756-1]
GeneIDi832.
KEGGihsa:832.
UCSCiuc001bce.3. human. [P47756-2]
uc021ohr.1. human. [P47756-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41277.1. [P47756-2]
CCDS55579.1. [P47756-1]
RefSeqiNP_001193469.1. NM_001206540.2. [P47756-1]
NP_001269091.1. NM_001282162.1.
NP_004921.1. NM_004930.4. [P47756-2]
UniGeneiHs.432760.

3D structure databases

ProteinModelPortaliP47756.
SMRiP47756. Positions 2-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107282. 55 interactions.
IntActiP47756. 19 interactions.
MINTiMINT-254051.
STRINGi9606.ENSP00000264202.

PTM databases

PhosphoSiteiP47756.

Polymorphism and mutation databases

DMDMi13124696.

2D gel databases

DOSAC-COBS-2DPAGEP47756.
OGPiP47756.
REPRODUCTION-2DPAGEIPI00026185.
SWISS-2DPAGEP47756.

Proteomic databases

MaxQBiP47756.
PaxDbiP47756.
PRIDEiP47756.

Protocols and materials databases

DNASUi832.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264202; ENSP00000264202; ENSG00000077549. [P47756-2]
ENST00000375142; ENSP00000364284; ENSG00000077549. [P47756-1]
GeneIDi832.
KEGGihsa:832.
UCSCiuc001bce.3. human. [P47756-2]
uc021ohr.1. human. [P47756-1]

Organism-specific databases

CTDi832.
GeneCardsiGC01M019665.
HGNCiHGNC:1491. CAPZB.
HPAiHPA031531.
HPA056066.
MIMi601572. gene.
neXtProtiNX_P47756.
PharmGKBiPA26072.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiP47756.
KOiK10365.
PhylomeDBiP47756.
TreeFamiTF105732.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiCAPZB. human.
GeneWikiiCAPZB.
GenomeRNAii832.
NextBioi3446.
PROiP47756.
SOURCEiSearch...

Gene expression databases

BgeeiP47756.
CleanExiHS_CAPZB.
ExpressionAtlasiP47756. baseline and differential.
GenevisibleiP47756. HS.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "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.

Entry informationi

Entry nameiCAPZB_HUMAN
AccessioniPrimary (citable) accession number: P47756
Secondary accession number(s): Q32Q68
, Q5U0L4, Q8TB49, Q9NUC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 150 of the entry and version 4 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

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. 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.