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Reviewed, UniProtKB/Swiss-Prot Q9V6Q2 (CID_DROME)

Last modified January 19, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Histone H3-like centromeric protein cid
Alternative name(s):
    Centromere identifier protein
    CENP-A homolog
Gene names
Name: cid
ORF Names: CG13329
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Ref.6 Ref.9

Subunit structure

Forms a nucleosome-like histone octamer containing two molecules each of H2A, H2B, cid and H4 assembled in one cid-H4 heterotetramer and two H2A-H2B heterodimers. The cid-H4 heterotetramer is more compact and structurally more rigid than corresponding H3-H4 heterotetramers By similarity. Interacts with the condensin subunit Cap-G. Ref.8

Subcellular location

Nucleus. Centromere. Kinetochore. Note: Localizes exclusively in the kinetochore domain of centromeres. Ref.1 Ref.7

Sequence similarities

Belongs to the histone H3 family.

Sequence caution

The sequence AAM75058.1 differs from that shown. Reason: Frameshift at position 86.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Histone H3-like centromeric protein cid
PRO_0000249474

Regions

Region133 – 22593H3-like

Amino acid modifications

Modified residue741Phosphoserine Ref.10
Modified residue751Phosphoserine Ref.10
Modified residue761Phosphothreonine Ref.10
Modified residue771Phosphoserine Ref.10

Natural variations

Natural variant113 – 1142AA → TS in strain: Tai 255.1.

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Sequences

Sequence LengthMass (Da)Tools
Q9V6Q2-1 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: E125327C4EDD12D2

FASTA22525,968
        10         20         30         40         50         60 
MPRHSRAKRA PRPSANNSKS PNDDDTAFRS PEPEDGTDYG LEFTTSQLTL QDNNRRSSTL 

        70         80         90        100        110        120 
RRDAGRRQPA ARDSSTSGEE EDQENRYPTT RSPQTRRMTV QQESKTRAAG PVAAQNQTRR 

       130        140        150        160        170        180 
RKAANPMSRA KRMDREIRRL QHHPGTLIPK LPFSRLVREF IVKYSDDEPL RVTEGALLAM 

       190        200        210        220 
QESCEMYLTQ RLADSYMLTK HRNRVTLEVR DMALMAYICD RGRQF

« Hide

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References

« Hide 'large scale' references
[1]"Heterochromatic deposition of centromeric histone H3-like proteins."
Henikoff S., Ahmad K., Platero J.S., van Steensel B.
Proc. Natl. Acad. Sci. U.S.A. 97:716-721(2000) [PubMed: 10639145] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]"Drosophila melanogaster and D. simulans rescue strains produce fit offspring, despite divergent centromere-specific histone alleles."
Sainz A., Wilder J.A., Wolf M., Hollocher H.
Heredity 91:28-35(2003) [PubMed: 12815450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Antigua, In, Melbourne, Oregon-R and Tai 255.1.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[6]"The role of Drosophila CID in kinetochore formation, cell-cycle progression and heterochromatin interactions."
Blower M.D., Karpen G.H.
Nat. Cell Biol. 3:730-739(2001) [PubMed: 11483958] [Abstract]
Cited for: FUNCTION.
[7]"Centromeric chromatin exhibits a histone modification pattern that is distinct from both euchromatin and heterochromatin."
Sullivan B.A., Karpen G.H.
Nat. Struct. Mol. Biol. 11:1076-1083(2004) [PubMed: 15475964] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The Drosophila melanogaster condensin subunit Cap-G interacts with the centromere-specific histone H3 variant CID."
Jaeger H., Rauch M., Heidmann S.
Chromosoma 113:350-361(2005) [PubMed: 15592865] [Abstract]
Cited for: INTERACTION WITH CAP-G.
[9]"Drosophila CENP-A mutations cause a BubR1-dependent early mitotic delay without normal localization of kinetochore components."
Blower M.D., Daigle T., Kaufman T., Karpen G.H.
PLoS Genet. 2:1025-1032(2006) [PubMed: 16839185] [Abstract]
Cited for: FUNCTION.
[10]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-75; THR-76 AND SER-77, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF259371 Genomic DNA. Translation: AAF72652.1.
AY126929 Genomic DNA. Translation: AAM80987.1.
AY126930 Genomic DNA. Translation: AAM80988.1.
AY126931 Genomic DNA. Translation: AAM80989.1.
AY126932 Genomic DNA. Translation: AAM80990.1.
AY126933 Genomic DNA. Translation: AAM80991.1.
AE013599 Genomic DNA. Translation: AAF58371.2.
AY128465 mRNA. Translation: AAM75058.1. Frameshift.
RefSeqNP_523730.2.
UniGeneDm.5691

3D structure databases

SMRQ9V6Q2. Positions 134-219.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29506N.
IntActQ9V6Q2. 1 interaction.
STRINGQ9V6Q2.

Genome annotation databases

EnsemblFBtr0087667; FBpp0086787; FBgn0040477; Drosophila melanogaster. [Genome view]
GeneID36495.
KEGGdme:Dmel_CG13329.
NMPDRfig|7227.3.peg.5063.

Organism-specific databases

CTD36495.
FlyBaseFBgn0040477. cid.

Phylogenomic databases

eggNOGinNOG11670.
InParanoidQ9V6Q2.
OMAGLEFTTS.
OrthoDBEOG9BVS11.
PhylomeDBQ9V6Q2.

Gene expression databases

GermOnlineCG13329. Drosophila melanogaster.

Family and domain databases

InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
Gene3DG3DSA:1.10.20.10. Histone-fold. 1 hit.
PANTHERPTHR11426. Histone_H3. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
PROSITEPS00959. HISTONE_H3_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio798852.

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Entry information

Entry nameCID_DROME
AccessionPrimary (citable) accession number: Q9V6Q2
Secondary accession number(s): Q7YUD4 expand/collapse secondary AC list , Q7YUD5, Q8MQP5, Q9NG62
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 1, 2002
Last modified: January 19, 2010
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents