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Protein

Zinc finger protein unc-98

Gene

unc-98

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable transcription factor required for muscle structure. Its dual subcellular localization suggests that it may function both as a muscle adhesion complex protein and as a transcription factor, or work together with transcription factors, to influence gene expression. Thought to act as a molecular bridge between unc-97 and myo-3 at the M-line of muscles, possibly in a signaling role.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 13523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri141 – 16323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri169 – 18820C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri246 – 26823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • cytoskeletal protein binding Source: WormBase
  • DNA binding Source: UniProtKB-KW
  • myosin binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • locomotion Source: UniProtKB
  • locomotory behavior Source: UniProtKB
  • muscle organ development Source: UniProtKB-KW
  • myeloid cell differentiation Source: GO_Central
  • myofibril assembly Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • post-embryonic body morphogenesis Source: UniProtKB
  • regulation of neurogenesis Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Muscle protein

Keywords - Biological processi

Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein unc-98
Alternative name(s):
Uncoordinated protein 98
Gene namesi
Name:unc-98
ORF Names:F08C6.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF08C6.7; CE31900; WBGene00006827; unc-98.

Subcellular locationi

GO - Cellular componenti

  • M band Source: UniProtKB
  • myosin filament Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Thick filament

Pathology & Biotechi

Disruption phenotypei

Worms exhibit disorganised A and I bands in body-wall muscle structure.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Zinc finger protein unc-98PRO_0000046896Add
BLAST

Proteomic databases

EPDiQ19203.
PaxDbiQ19203.
PRIDEiQ19203.

Expressioni

Tissue specificityi

Expressed in embryos from 1.5- to 2-fold stage in myofibrils. In larvae and adults, it is expressed in body wall muscle, and in addition, anal depressor muscle and vulval muscles. More specifically it is found in the thick filaments of muscle fibers.2 Publications

Interactioni

Subunit structurei

Interacts with hum-6, mep-1, myo-3, unc-96 and unc-97/PINCH.3 Publications

GO - Molecular functioni

  • cytoskeletal protein binding Source: WormBase
  • myosin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi45944. 2 interactions.
DIPiDIP-25572N.
IntActiQ19203. 50 interactions.
MINTiMINT-115012.
STRINGi6239.F08C6.7.

Structurei

3D structure databases

ProteinModelPortaliQ19203.
SMRiQ19203. Positions 48-87, 97-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 310113Interacts with myo-3Add
BLAST

Domaini

The N-terminal part (1-106) mediates the nuclear localization, while the fourth zinc finger is required for the localization to M-lines and dense bodies.1 Publication

Sequence similaritiesi

Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 13523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri141 – 16323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri169 – 18820C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri246 – 26823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000130978.
HOGENOMiHOG000154785.
InParanoidiQ19203.
OMAiAHERIHD.
OrthoDBiEOG77T18B.
PhylomeDBiQ19203.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q19203-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIFKEAR KERDDFEELM NACDLAKMSV KNNEMVHGLE TFGINGESSE
60 70 80 90 100
NGNKEKPKEI MKVVAPTVEA YVGSSSAQTP TKSSGGALDG SDQQEVRQDG
110 120 130 140 150
TSVQKDDNGF VFYKCRFCGL TFNFMNTLRA HERIHDVSQP YVCGKCGDSF
160 170 180 190 200
EFACQLEYHA AQHSEIDGYK CECGRTFFSY TEMLYHKHTD DPLELIGAPE
210 220 230 240 250
TTTIKVSKKR VLPVSEQDLP QPAFVTEGYE PKHPLRVYND VRSKPYICEY
260 270 280 290 300
CSKSYSDSRG LAYHMYSHRG EKYFNPRASR YMMGREGVGY TDSRSYYLFP
310
RTSGYVTPRF
Length:310
Mass (Da):35,353
Last modified:March 1, 2003 - v2
Checksum:iF052E8CD0BA3AAB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF515600 mRNA. Translation: AAM76039.1.
FO080866 Genomic DNA. Translation: CCD67350.1.
PIRiT15974.
RefSeqiNP_509284.2. NM_076883.6.
UniGeneiCel.9298.

Genome annotation databases

EnsemblMetazoaiF08C6.7; F08C6.7; WBGene00006827.
GeneIDi181020.
KEGGicel:CELE_F08C6.7.
UCSCiF08C6.7. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF515600 mRNA. Translation: AAM76039.1.
FO080866 Genomic DNA. Translation: CCD67350.1.
PIRiT15974.
RefSeqiNP_509284.2. NM_076883.6.
UniGeneiCel.9298.

3D structure databases

ProteinModelPortaliQ19203.
SMRiQ19203. Positions 48-87, 97-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45944. 2 interactions.
DIPiDIP-25572N.
IntActiQ19203. 50 interactions.
MINTiMINT-115012.
STRINGi6239.F08C6.7.

Proteomic databases

EPDiQ19203.
PaxDbiQ19203.
PRIDEiQ19203.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF08C6.7; F08C6.7; WBGene00006827.
GeneIDi181020.
KEGGicel:CELE_F08C6.7.
UCSCiF08C6.7. c. elegans.

Organism-specific databases

CTDi181020.
WormBaseiF08C6.7; CE31900; WBGene00006827; unc-98.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000130978.
HOGENOMiHOG000154785.
InParanoidiQ19203.
OMAiAHERIHD.
OrthoDBiEOG77T18B.
PhylomeDBiQ19203.

Miscellaneous databases

PROiQ19203.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes."
    Mercer K.B., Flaherty D.B., Miller R.K., Qadota H., Tinley T.L., Moerman D.G., Benian G.M.
    Mol. Biol. Cell 14:2492-2507(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HUM-6; MEP-1 AND UNC-97, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Identification of genetic elements associated with muscle structure in the nematode Caenorhabditis elegans."
    Zengel J.M., Epstein H.F.
    Cell Motil. 1:73-97(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  4. "UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle."
    Miller R.K., Qadota H., Landsverk M.L., Mercer K.B., Epstein H.F., Benian G.M.
    J. Cell Biol. 175:853-859(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO-3, TISSUE SPECIFICITY.
  5. "Caenorhabditis elegans UNC-96 is a new component of M-lines that interacts with UNC-98 and paramyosin and is required in adult muscle for assembly and/or maintenance of thick filaments."
    Mercer K.B., Miller R.K., Tinley T.L., Sheth S., Qadota H., Benian G.M.
    Mol. Biol. Cell 17:3832-3847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC-96.

Entry informationi

Entry nameiUNC98_CAEEL
AccessioniPrimary (citable) accession number: Q19203
Secondary accession number(s): Q8MUP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.