P45973 (CBX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Protein existence	Evidence 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.21
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.22 Ref.24 Ref.25 Ref.26 Ref.29
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. 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.27
Sequence similarities	Contains 2 chromo domains.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Centromere Chromosome Nucleus
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 9636147. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromocenter Inferred from electronic annotation. Source: Compara 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: Compara 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_function	chromatin binding Inferred from electronic annotation. Source: Compara methylated histone residue binding Inferred from direct assay Ref.21PubMed 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADNP	Q9H2P0	2	EBI-78219,EBI-1764854
ASXL1	Q8IXJ9	2	EBI-78219,EBI-1646500
Asxl1	P59598	5	EBI-78219,EBI-5743705	From a different organism.
CHAF1A	Q13111	3	EBI-78219,EBI-1020839
INCENP	Q9NQS7	6	EBI-78219,EBI-307907
LBR	Q14739	4	EBI-78219,EBI-1055147
MBD1	Q9UIS9	5	EBI-78219,EBI-867196
POGZ	Q7Z3K3	5	EBI-78219,EBI-1389308
SUV39H1	O43463	3	EBI-78219,EBI-349968
TRIM28	Q13263	7	EBI-78219,EBI-78139

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

Chromobox protein homolog 5

PRO_0000080208

Regions

Domain

20 – 78

59

Chromo 1

Domain

121 – 179

59

Chromo 2; shadow subtype

Region

116 – 191

76

Interaction with ASXL1

Compositional bias

11 – 14

4

Poly-Ser

Amino acid modifications

Modified residue

8

1

Phosphothreonine Ref.17

Modified residue

11

1

Phosphoserine Ref.15 Ref.17 Ref.20 Ref.23

Modified residue

12

1

Phosphoserine Ref.15 Ref.20 Ref.23

Modified residue

13

1

Phosphoserine Ref.15 Ref.17 Ref.20

Modified residue

14

1

Phosphoserine Ref.15 Ref.17 Ref.20 Ref.23

Modified residue

92

1

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23

Modified residue

97

1

Phosphoserine Ref.18 Ref.23

Modified residue

110

1

Phosphoserine Ref.17

Experimental info

Mutagenesis

165

1

I → E: No effect on interaction with POGZ. Abolishes interaction with TRIM28, CHAF1A and NIPBL. Ref.26

Mutagenesis

174

1

W → A: Abolishes interaction with TRIM28, CHAF1A and NIPBL. Ref.26

Secondary structure

1

.

.

.

.

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191

Helix Strand Turn

Details...

Beta strand

19 – 31

13

Beta strand

34 – 41

8

Helix

46 – 48

3

Beta strand

50 – 53

4

Helix

54 – 56

3

Helix

60 – 67

8

Helix

116 – 119

4

Beta strand

123 – 130

8

Beta strand

137 – 142

6

Beta strand

148 – 152

5

Helix

153 – 159

7

Helix

161 – 168

8

Sequences

	Sequence		Length	Mass (Da)
	P45973 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 16FFC476367093B1	FASTA	191	22,225
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND SER-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-11; SER-13; SER-14; SER-92 AND SER-110, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-97, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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.
[23]	"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-12; SER-14; SER-92 AND SER-97, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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].
[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.

IPI

IPI00024662.

PIR

G01808.

RefSeq

NP_001120793.1. NM_001127321.1.
NP_001120794.1. NM_001127322.1.
NP_036249.1. NM_012117.2.

UniGene

Hs.349283.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FDT	X-ray	2.00	A	18-75	[»]
3I3C	X-ray	2.48	A/B/C/D	110-173	[»]

ProteinModelPortal

P45973.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5986N.

IntAct

P45973. 104 interactions.

MINT

MINT-1178082.

STRING

9606.ENSP00000209875.

PTM databases

PhosphoSite

P45973.

Polymorphism databases

DMDM

1170338.

Proteomic databases

PaxDb

P45973.

PeptideAtlas

P45973.

PRIDE

P45973.

Protocols and materials databases

DNASU

23468.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000209875; ENSP00000209875; ENSG00000094916.
ENST00000439541; ENSP00000401009; ENSG00000094916.
ENST00000550411; ENSP00000449207; ENSG00000094916.

GeneID

23468.

KEGG

hsa:23468.

UCSC

uc001sfh.4. human.

Organism-specific databases

CTD

23468.

GeneCards

GC12M054624.

HGNC

HGNC:1555. CBX5.

HPA

CAB017548.
HPA016699.

MIM

604478. gene.

neXtProt

NX_P45973.

PharmGKB

PA26130.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG132879.

HOGENOM

HOG000220852.

HOVERGEN

HBG000400.

InParanoid

P45973.

KO

K11587.

OMA

DKHNTWE.

OrthoDB

EOG4NVZMP.

PhylomeDB

P45973.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P45973.

Bgee

P45973.

CleanEx

HS_CBX5.

Genevestigator

P45973.

GermOnline

ENSG00000094916. Homo sapiens.

Family and domain databases

InterPro

IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]

Pfam

PF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]

PRINTS

PR00504. CHROMODOMAIN.

SMART

SM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 2 hits.

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CBX5. human.

EvolutionaryTrace

P45973.

GenomeRNAi

23468.

NextBio

45793.

SOURCE

Search...

Entry information

Entry name

CBX5_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.