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P45973

- CBX5_HUMAN

UniProt

P45973 - CBX5_HUMAN

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Protein
Chromobox protein homolog 5
Gene
CBX5, HP1A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. methylated histone binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein binding, bridging Source: BHF-UCL
  5. repressing transcription factor binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 5
Alternative name(s):
Antigen p25
Heterochromatin protein 1 homolog alpha
Short name:
HP1 alpha
Gene namesi
Name:CBX5
Synonyms:HP1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1555. CBX5.

Subcellular locationi

Nucleus. Chromosome. Chromosomecentromere
Note: Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase.1 Publication

GO - Cellular componenti

  1. chromocenter Source: Ensembl
  2. histone deacetylase complex Source: BHF-UCL
  3. histone methyltransferase complex Source: BHF-UCL
  4. kinetochore Source: Ensembl
  5. nuclear centromeric heterochromatin Source: BHF-UCL
  6. nuclear envelope Source: ProtInc
  7. nuclear heterochromatin Source: ProtInc
  8. nucleolus Source: BHF-UCL
  9. nucleoplasm Source: Reactome
  10. nucleus Source: UniProtKB
  11. transcriptional repressor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651I → E: No effect on interaction with POGZ. Abolishes interaction with TRIM28, CHAF1A and NIPBL. 1 Publication
Mutagenesisi174 – 1741W → A: Abolishes interaction with TRIM28, CHAF1A and NIPBL. 1 Publication

Organism-specific databases

PharmGKBiPA26130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Chromobox protein homolog 5
PRO_0000080208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine3 Publications
Modified residuei12 – 121Phosphoserine2 Publications
Modified residuei13 – 131Phosphoserine4 Publications
Modified residuei14 – 141Phosphoserine4 Publications
Modified residuei92 – 921Phosphoserine4 Publications
Modified residuei95 – 951Phosphoserine1 Publication
Modified residuei97 – 971Phosphoserine3 Publications

Post-translational modificationi

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.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP45973.
PaxDbiP45973.
PeptideAtlasiP45973.
PRIDEiP45973.

PTM databases

PhosphoSiteiP45973.

Expressioni

Gene expression databases

ArrayExpressiP45973.
BgeeiP45973.
CleanExiHS_CBX5.
GenevestigatoriP45973.

Organism-specific databases

HPAiCAB017548.
HPA016699.

Interactioni

Subunit structurei

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 ASXL1.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADNPQ9H2P02EBI-78219,EBI-1764854
ASXL1Q8IXJ92EBI-78219,EBI-1646500
Asxl1P595985EBI-78219,EBI-5743705From a different organism.
ATRXP461002EBI-78219,EBI-396461
CHAF1AQ131117EBI-78219,EBI-1020839
H3F3BP842432EBI-78219,EBI-120658
HIST1H3DP684319EBI-78219,EBI-79722
INCENPQ9NQS76EBI-78219,EBI-307907
LBRQ147394EBI-78219,EBI-1055147
legAS4Q5ZUS46EBI-78219,EBI-8871796From a different organism.
MBD1Q9UIS96EBI-78219,EBI-867196
POGZQ7Z3K36EBI-78219,EBI-1389308
SENP7Q9BQF62EBI-78219,EBI-766251
SUV39H1O434633EBI-78219,EBI-349968
TRIM28Q132639EBI-78219,EBI-78139

Protein-protein interaction databases

BioGridi117030. 145 interactions.
DIPiDIP-5986N.
IntActiP45973. 125 interactions.
MINTiMINT-1178082.
STRINGi9606.ENSP00000209875.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 3113
Beta strandi34 – 418
Helixi46 – 483
Beta strandi50 – 534
Helixi54 – 563
Helixi60 – 678
Helixi116 – 1194
Beta strandi123 – 1308
Beta strandi137 – 1426
Beta strandi148 – 1525
Helixi153 – 1597
Helixi161 – 1688

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FDTX-ray2.00A18-75[»]
3I3CX-ray2.48A/B/C/D110-173[»]
ProteinModelPortaliP45973.
SMRiP45973. Positions 18-68, 112-170.

Miscellaneous databases

EvolutionaryTraceiP45973.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 7859Chromo 1
Add
BLAST
Domaini121 – 17959Chromo 2; shadow subtype
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 19176Interaction with ASXL1
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 144Poly-Ser

Sequence similaritiesi

Contains 2 chromo domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG132879.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiP45973.
KOiK11587.
OMAiSEFMKTY.
OrthoDBiEOG7QRQWW.
PhylomeDBiP45973.
TreeFamiTF350503.

Family and domain databases

InterProiIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45973-1 [UniParc]FASTAAdd to Basket

« Hide

MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT    50
WEPEKNLDCP ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD 100
IKSKKKREQS NDIARGFERG LEPEKIIGAT DSCGDLMFLM KWKDTDEADL 150
VLAKEANVKC PQIVIAFYEE RLTWHAYPED AENKEKETAK S 191
Length:191
Mass (Da):22,225
Last modified:November 1, 1995 - v1
Checksum:i16FFC476367093B1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8875.1.
PIRiG01808.
RefSeqiNP_001120793.1. NM_001127321.1.
NP_001120794.1. NM_001127322.1.
NP_036249.1. NM_012117.2.
UniGeneiHs.349283.

Genome annotation databases

EnsembliENST00000209875; ENSP00000209875; ENSG00000094916.
ENST00000439541; ENSP00000401009; ENSG00000094916.
ENST00000550411; ENSP00000449207; ENSG00000094916.
GeneIDi23468.
KEGGihsa:23468.
UCSCiuc001sfh.4. human.

Polymorphism databases

DMDMi1170338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS8875.1.
PIRi G01808.
RefSeqi NP_001120793.1. NM_001127321.1.
NP_001120794.1. NM_001127322.1.
NP_036249.1. NM_012117.2.
UniGenei Hs.349283.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P45973.
SMRi P45973. Positions 18-68, 112-170.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117030. 145 interactions.
DIPi DIP-5986N.
IntActi P45973. 125 interactions.
MINTi MINT-1178082.
STRINGi 9606.ENSP00000209875.

PTM databases

PhosphoSitei P45973.

Polymorphism databases

DMDMi 1170338.

Proteomic databases

MaxQBi P45973.
PaxDbi P45973.
PeptideAtlasi P45973.
PRIDEi P45973.

Protocols and materials databases

DNASUi 23468.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000209875 ; ENSP00000209875 ; ENSG00000094916 .
ENST00000439541 ; ENSP00000401009 ; ENSG00000094916 .
ENST00000550411 ; ENSP00000449207 ; ENSG00000094916 .
GeneIDi 23468.
KEGGi hsa:23468.
UCSCi uc001sfh.4. human.

Organism-specific databases

CTDi 23468.
GeneCardsi GC12M054624.
HGNCi HGNC:1555. CBX5.
HPAi CAB017548.
HPA016699.
MIMi 604478. gene.
neXtProti NX_P45973.
PharmGKBi PA26130.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG132879.
HOGENOMi HOG000220852.
HOVERGENi HBG000400.
InParanoidi P45973.
KOi K11587.
OMAi SEFMKTY.
OrthoDBi EOG7QRQWW.
PhylomeDBi P45973.
TreeFami TF350503.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi CBX5. human.
EvolutionaryTracei P45973.
GeneWikii CBX5_(gene).
GenomeRNAii 23468.
NextBioi 45793.
PROi P45973.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45973.
Bgeei P45973.
CleanExi HS_CBX5.
Genevestigatori P45973.

Family and domain databases

InterProi IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view ]
PRINTSi PR00504. CHROMODOMAIN.
SMARTi SM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 2 hits.
PROSITEi PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. 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.

Entry informationi

Entry nameiCBX5_HUMAN
AccessioniPrimary (citable) accession number: P45973
Secondary accession number(s): B2R8T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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