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Protein

Chromo domain-containing protein cec-4

Gene

cec-4

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Chromatin anchor protein which binds to methylated lysine residues on histone H3, thereby recruiting heterochromatin to the nuclear periphery. May be required for the correct positioning of chromatin and nucleoli in embryos.1 Publication

GO - Molecular functioni

  • methylated histone binding Source: WormBase

GO - Biological processi

  • chromosome attachment to the nuclear envelope Source: WormBase
  • regulation of cell differentiation Source: WormBase
  • regulation of gene expression Source: WormBase
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Chromo domain-containing protein cec-4Curated
Gene namesi
Name:cec-4Imported
ORF Names:F32E10.2Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiF32E10.2; CE04475; WBGene00017990; cec-4.

Subcellular locationi

GO - Cellular componenti

  • nuclear inner membrane Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Reduced anchoring of heterochromatin to the nuclear periphery. Altered nucleolar localization with nucleoli positioned away from the nuclear periphery. When exposed to hlh-1, a transcription factor that induces muscle differentiation, 25% of embryos continue to develop and the embryonic cells do not transdifferentiate into muscle-like cells like their wild-type counterparts.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87Y → A: Abolishes binding to the tri-methylated 'Lys-9' residues on histone H3; when associated with A-111. 1 Publication1
Mutagenesisi111Y → A: Abolishes binding to the tri-methylated 'Lys-9' residues on histone H3; when associated with A-87. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004356811 – 270Chromo domain-containing protein cec-4CuratedAdd BLAST270

Proteomic databases

EPDiQ19972.
PaxDbiQ19972.
PeptideAtlasiQ19972.

Expressioni

Developmental stagei

Expressed at all developmental stages from embryogenesis to adulthood. Evenly expressed in most tissues during the L1 stage of larval development, however, expression is weak in the intestine and high in muscle.1 Publication

Gene expression databases

BgeeiWBGene00017990.

Interactioni

Subunit structurei

Interacts with mono-, di- and tri-methylated 'Lys-9' residues on histone H3. Weakly interacts with methylated 'Lys-37' residues on histone H3.1 Publication

GO - Molecular functioni

  • methylated histone binding Source: WormBase

Protein-protein interaction databases

STRINGi6239.F32E10.2.

Structurei

3D structure databases

ProteinModelPortaliQ19972.
SMRiQ19972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 147ChromoPROSITE-ProRule annotationAdd BLAST61

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
GeneTreeiENSGT00730000112558.
HOGENOMiHOG000018021.
InParanoidiQ19972.
OrthoDBiEOG091G10UM.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q19972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKTVEGEH GTPKTNFTKK ETSKNHDDFK KIIGHKVVEE HYVEYEVELT
60 70 80 90 100
SGKTITATEF DFKGDDSLLS TYKKKVTKQS DDSSGEYAVE RVLAHRKVKG
110 120 130 140 150
SPLYLVQWKG YPHPVWNSEM WEEDLDNCKD LLAAYKKHQE DLKIAQTPKK
160 170 180 190 200
TPSKTPKKTP KSLKRRALTP SDDEEEAGPI APEPKKTPKQ STKKLKRTTS
210 220 230 240 250
PETNLVEKSK KKAIPDLENH TLDQEKNDVI ERVEEIQEDE DDDDEQREEV
260 270
VTTAPVETKS RWGFGSWKWF
Length:270
Mass (Da):31,072
Last modified:November 1, 1996 - v1
Checksum:i3FC640C358424844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284604 Genomic DNA. Translation: CCD70433.1.
PIRiB88734.
RefSeqiNP_501231.1. NM_068830.6.
UniGeneiCel.6591.

Genome annotation databases

EnsemblMetazoaiF32E10.2.1; F32E10.2.1; WBGene00017990.
F32E10.2.2; F32E10.2.2; WBGene00017990.
GeneIDi177536.
KEGGicel:CELE_F32E10.2.
UCSCiF32E10.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284604 Genomic DNA. Translation: CCD70433.1.
PIRiB88734.
RefSeqiNP_501231.1. NM_068830.6.
UniGeneiCel.6591.

3D structure databases

ProteinModelPortaliQ19972.
SMRiQ19972.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F32E10.2.

Proteomic databases

EPDiQ19972.
PaxDbiQ19972.
PeptideAtlasiQ19972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF32E10.2.1; F32E10.2.1; WBGene00017990.
F32E10.2.2; F32E10.2.2; WBGene00017990.
GeneIDi177536.
KEGGicel:CELE_F32E10.2.
UCSCiF32E10.2. c. elegans.

Organism-specific databases

CTDi177536.
WormBaseiF32E10.2; CE04475; WBGene00017990; cec-4.

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
GeneTreeiENSGT00730000112558.
HOGENOMiHOG000018021.
InParanoidiQ19972.
OrthoDBiEOG091G10UM.

Miscellaneous databases

PROiQ19972.

Gene expression databases

BgeeiWBGene00017990.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEC4_CAEEL
AccessioniPrimary (citable) accession number: Q19972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 16, 2016
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 116 of the entry and version 1 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.