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P45973 (CBX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromobox protein homolog 5
Alternative name(s):
Antigen p25
Heterochromatin protein 1 homolog alpha
Short name=HP1 alpha
Gene names
Name:CBX5
Synonyms:HP1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Ref.18

Subunit structure

Interacts with SUV420H1 and SUV420H2 By similarity. Interacts with HP1BP3 By similarity. Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100, STAM2 and TRIM28 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-9'. Interacts with BAHD1, MIS12 and DSN1. Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28 compete for interaction with CBX5. Interacts with INCENP and TRIM24. Interacts with JC virus agnoprotein; this interaction induces the dissociation of CBX5 from LBR, resulting in destabilization of the nuclear envelope. Interacts with CHAMP1. Interacts with ASXL1. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 Ref.23 Ref.29

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Note: Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase. Ref.8

Post-translational modification

Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle By similarity. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis. Ref.8

Ubiquitinated. Ref.24

Sequence similarities

Contains 2 chromo domains.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCentromere
Chromosome
Nucleus
   DomainRepeat
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9636147. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromocenter

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

histone deacetylase complex

Inferred from sequence or structural similarity. Source: BHF-UCL

histone methyltransferase complex

Inferred from sequence or structural similarity. Source: BHF-UCL

kinetochore

Inferred from electronic annotation. Source: Ensembl

nuclear centromeric heterochromatin

Non-traceable author statement PubMed 16177824. Source: BHF-UCL

nuclear envelope

Traceable author statement Ref.5. Source: ProtInc

nucleolus

Inferred from direct assay PubMed 9636146. Source: BHF-UCL

transcriptional repressor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

methylated histone residue binding

Inferred from direct assay Ref.18PubMed 21029866. Source: UniProtKB

protein binding, bridging

Inferred from sequence or structural similarity. Source: BHF-UCL

repressing transcription factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191Chromobox protein homolog 5
PRO_0000080208

Regions

Domain20 – 7859Chromo 1
Domain121 – 17959Chromo 2; shadow subtype
Region116 – 19176Interaction with ASXL1
Compositional bias11 – 144Poly-Ser

Amino acid modifications

Modified residue111Phosphoserine Ref.17 Ref.20 Ref.25
Modified residue121Phosphoserine Ref.17 Ref.25
Modified residue131Phosphoserine Ref.17 Ref.20 Ref.25 Ref.27
Modified residue141Phosphoserine Ref.17 Ref.20 Ref.25 Ref.27
Modified residue921Phosphoserine Ref.16 Ref.17 Ref.20 Ref.25
Modified residue951Phosphoserine Ref.27
Modified residue971Phosphoserine Ref.20 Ref.25 Ref.27

Experimental info

Mutagenesis1651I → E: No effect on interaction with POGZ. Abolishes interaction with TRIM28, CHAF1A and NIPBL. Ref.23
Mutagenesis1741W → A: Abolishes interaction with TRIM28, CHAF1A and NIPBL. Ref.23

Secondary structure

....................... 191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45973 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 16FFC476367093B1

FASTA19122,225
        10         20         30         40         50         60 
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP 

        70         80         90        100        110        120 
ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD IKSKKKREQS NDIARGFERG 

       130        140        150        160        170        180 
LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED 

       190 
AENKEKETAK S 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a human homologue of Drosophila heterochromatin protein HP1 using anti-centromere autoantibodies with anti-chromo specificity."
Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A., Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C.
J. Cell Sci. 104:573-582(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Placenta.
[5]"Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1."
Ye Q., Worman H.J.
J. Biol. Chem. 271:14653-14656(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-191.
[6]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[7]"Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR."
Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.
J. Biol. Chem. 272:14983-14989(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LBR AND CBX3.
[8]"Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells."
Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B.
Chromosoma 108:220-234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[9]"Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification."
Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A.
Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM24.
[10]"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 LYS-9.
[11]"A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1."
Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.
Nat. Cell Biol. 6:1135-1141(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIS12 AND DSN1.
[12]"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28.
[13]"Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: role in nuclear egress of viral particles."
Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N., Takahashi H., Tanaka S., Hall W.W., Nagashima K., Sawa H.
EMBO Rep. 6:452-457(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JC VIRUS AGNOPROTEIN.
[14]"In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation."
Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R.
Mol. Cell. Biol. 25:4552-4564(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SETDB1.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.
Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HISTONE-BINDING.
[19]"Human BAHD1 promotes heterochromatic gene silencing."
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P.
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAHD1.
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-14; SER-92 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHAMP1 AND POGZ.
[22]"ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1."
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.
J. Biol. Chem. 285:18-29(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASXL1.
[23]"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POGZ; TRIM28; CHAF1A; NIPBL AND INCENP, MUTAGENESIS OF ILE-165 AND TRP-174.
[24]"Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10."
Chaturvedi P., Parnaik V.K.
PLoS ONE 5:E10620-E10620(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14; SER-92 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-95 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Recognition and specificity determinants of the human cbx chromodomains."
Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S., Wasney G.A., Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H.
J. Biol. Chem. 286:521-529(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-75 IN COMPLEX WITH TRIMETHYLATED HISTONE H3 PEPTIDE, SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 110-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S62077 mRNA. Translation: AAB26994.1.
L07515 mRNA. Translation: AAA72327.1.
AK313506 mRNA. Translation: BAG36286.1.
CH471054 Genomic DNA. Translation: EAW96759.1.
BC006821 mRNA. Translation: AAH06821.1.
U26311 mRNA. Translation: AAC50553.1.
PIRG01808.
RefSeqNP_001120793.1. NM_001127321.1.
NP_001120794.1. NM_001127322.1.
NP_036249.1. NM_012117.2.
UniGeneHs.349283.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FDTX-ray2.00A18-75[»]
3I3CX-ray2.48A/B/C/D110-173[»]
ProteinModelPortalP45973.
SMRP45973. Positions 18-68, 112-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117030. 144 interactions.
DIPDIP-5986N.
IntActP45973. 123 interactions.
MINTMINT-1178082.
STRING9606.ENSP00000209875.

PTM databases

PhosphoSiteP45973.

Polymorphism databases

DMDM1170338.

Proteomic databases

PaxDbP45973.
PeptideAtlasP45973.
PRIDEP45973.

Protocols and materials databases

DNASU23468.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000209875; ENSP00000209875; ENSG00000094916.
ENST00000439541; ENSP00000401009; ENSG00000094916.
ENST00000550411; ENSP00000449207; ENSG00000094916.
GeneID23468.
KEGGhsa:23468.
UCSCuc001sfh.4. human.

Organism-specific databases

CTD23468.
GeneCardsGC12M054624.
HGNCHGNC:1555. CBX5.
HPACAB017548.
HPA016699.
MIM604478. gene.
neXtProtNX_P45973.
PharmGKBPA26130.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG132879.
HOGENOMHOG000220852.
HOVERGENHBG000400.
InParanoidP45973.
KOK11587.
OMASEFMKTY.
OrthoDBEOG7QRQWW.
PhylomeDBP45973.
TreeFamTF350503.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP45973.
BgeeP45973.
CleanExHS_CBX5.
GenevestigatorP45973.

Family and domain databases

InterProIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSPR00504. CHROMODOMAIN.
SMARTSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 2 hits.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCBX5. human.
EvolutionaryTraceP45973.
GeneWikiCBX5_(gene).
GenomeRNAi23468.
NextBio45793.
PROP45973.
SOURCESearch...

Entry information

Entry nameCBX5_HUMAN
AccessionPrimary (citable) accession number: P45973
Secondary accession number(s): B2R8T9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM