Q92769 (HDAC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 133.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone deacetylase 2 Short name=HD2 EC=3.5.1.98 | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Ref.30 |
| Catalytic activity | Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. |
| Subunit structure | Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region) By similarity. Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A. and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22 Ref.30 Ref.31 |
| Subcellular location | |
| Tissue specificity | Widely expressed; lower levels in brain and lung. |
| Post-translational modification | S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching By similarity. |
| Sequence similarities | Belongs to the histone deacetylase family. HD type 1 subfamily. |
| Sequence caution | The sequence AAH31055.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAG59420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI14206.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BRMS1 | Q9HCU9 | 3 | EBI-301821,EBI-714781 | |
| DAXX | Q9UER7 | 2 | EBI-301821,EBI-77321 | |
| HCFC1 | P51610 | 2 | EBI-301821,EBI-396176 | |
| HDAC1 | Q13547 | 5 | EBI-301821,EBI-301834 | |
| MBD1 | Q9UIS9 | 2 | EBI-301821,EBI-867196 | |
| MYC | P01106 | 2 | EBI-301821,EBI-447544 | |
| RFX5 | P48382 | 4 | EBI-301821,EBI-923266 | |
| SIN3A | Q96ST3 | 3 | EBI-301821,EBI-347218 | |
| SUV39H1 | O43463 | 3 | EBI-301821,EBI-349968 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 488 | 488 | Histone deacetylase 2 | PRO_0000114693 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 9 – 322 | 314 | Histone deacetylase | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 300 – 303 | 4 | Poly-Gly | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 142 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 75 | 1 | N6-acetyllysine Ref.33 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 90 | 1 | N6-acetyllysine Ref.33 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 262 | 1 | S-nitrosocysteine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 274 | 1 | S-nitrosocysteine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 394 | 1 | Phosphoserine Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 407 | 1 | Phosphoserine Ref.24 Ref.27 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 422 | 1 | Phosphoserine Ref.21 Ref.24 Ref.27 Ref.28 Ref.32 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 424 | 1 | Phosphoserine Ref.21 Ref.24 Ref.27 Ref.28 Ref.32 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 230 | 1 | R → C. Ref.1 Corresponds to variant rs1042903 [ dbSNP | Ensembl ]. | VAR_025311 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 315 | 1 | Y → H. Ref.5 Corresponds to variant rs17852888 [ dbSNP | Ensembl ]. | VAR_025312 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 93 – 94 | 2 | QR → HI in AAC50814. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 103 | 1 | V → A in AAC50814. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 146 | 1 | S → Y in AAC50814. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 248 | 1 | K → M in BAG59420. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 281 | 1 | G → D in BAG59420. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 12 – 15 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 34 – 45 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 49 – 51 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 52 – 55 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 65 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 66 – 68 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 71 – 79 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 82 – 87 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 94 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 108 – 114 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 123 – 126 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 134 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 156 – 164 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 165 – 167 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 171 – 175 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 185 – 190 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 192 – 201 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 224 – 229 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 235 – 238 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 242 – 253 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 256 – 261 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 283 – 290 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 296 – 299 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 306 – 320 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 335 – 337 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 343 – 345 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 357 – 371 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3." Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E. Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996) [PubMed: 8917507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-230. Tissue: Mammary gland. |
| [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue. |
| [3] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | 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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-315. Tissue: Testis. |
| [6] | "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4." Schmidt D.R., Schreiber S.L. Biochemistry 38:14711-14717(1999) [PubMed: 10545197] [Abstract] Cited for: INTERACTION WITH ATR, IDENTIFICATION IN A COMPLEX CONTAINING ATR AND CHD4. |
| [7] | "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci." Rountree M.R., Bachman K.E., Baylin S.B. Nat. Genet. 25:269-277(2000) [PubMed: 10888872] [Abstract] Cited for: INTERACTION WITH DNMT1 AND DMAP1. |
| [8] | "NuRD and SIN3 histone deacetylase complexes in development." Ahringer J. Trends Genet. 16:351-356(2000) [PubMed: 10904264] [Abstract] Cited for: REVIEW ON DEACETYLASE COMPLEXES. |
| [9] | "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation." Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M. Genes Dev. 15:1140-1151(2001) [PubMed: 11331609] [Abstract] Cited for: INTERACTION WITH MINT. |
| [10] | "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain." Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W. Mol. Cell. Biol. 21:6470-6483(2001) [PubMed: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3. |
| [11] | "Isolation and characterization of a novel class II histone deacetylase, HDAC10." Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., Trogani N., Widmer R., Atadja P., Cohen D. J. Biol. Chem. 277:6656-6666(2002) [PubMed: 11739383] [Abstract] Cited for: INTERACTION WITH HDAC10. |
| [12] | "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2." Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R. J. Biol. Chem. 277:35783-35786(2002) [PubMed: 12176973] [Abstract] Cited for: INTERACTION WITH SP3. |
| [13] | "Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek." Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G. J. Cell Sci. 115:3319-3330(2002) [PubMed: 12140263] [Abstract] Cited for: INTERACTION WITH DAXX AND DEK. |
| [14] | "Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene." Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S. EMBO J. 22:6299-6309(2003) [PubMed: 14633989] [Abstract] Cited for: INTERACTION WITH APEX1. |
| [15] | "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed: 12670868] [Abstract] Cited for: INTERACTION WITH HCFC1. |
| [16] | "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed: 12493763] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC1; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I. |
| [17] | "Identification and characterization of three new components of the mSin3A corepressor complex." Fleischer T.C., Yun U.J., Ayer D.E. Mol. Cell. Biol. 23:3456-3467(2003) [PubMed: 12724404] [Abstract] Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2. |
| [18] | "The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains." Choi Y.B., Ko J.K., Shin J. J. Biol. Chem. 279:50930-50941(2004) [PubMed: 15456770] [Abstract] Cited for: INTERACTION WITH PELP1. |
| [19] | "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition." Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V. Nucleic Acids Res. 32:1957-1966(2004) [PubMed: 15060175] [Abstract] Cited for: INTERACTION WITH NRIP1. |
| [20] | "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein." Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F. J. Biol. Chem. 280:28507-28518(2005) [PubMed: 15927959] [Abstract] Cited for: INTERACTION WITH JMJD2A. |
| [21] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [22] | "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus." Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O. Nucleic Acids Res. 34:3288-3298(2006) [PubMed: 16820529] [Abstract] Cited for: INTERACTION WITH SAP30L. |
| [23] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma. |
| [24] | "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: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [25] | "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: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [26] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [27] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-407; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [28] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [29] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. |
| [30] | "FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4." Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D. PLoS ONE 4:E5071-E5071(2009) [PubMed: 19343227] [Abstract] Cited for: FUNCTION, INTERACTION WITH TSHZ3. |
| [31] | "Chfr is linked to tumour metastasis through the downregulation of HDAC1." Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H. Nat. Cell Biol. 11:295-302(2009) [PubMed: 19182791] [Abstract] Cited for: INTERACTION WITH CHFR. |
| [32] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [33] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75 AND LYS-90, MASS SPECTROMETRY. |
| [34] | "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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [35] | "Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides." Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R., O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R. Bioorg. Med. Chem. Lett. 20:3142-3145(2010) [PubMed: 20392638] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U31814 mRNA. Translation: AAC50814.1. AK296856 mRNA. Translation: BAG59420.1. Different initiation. AL590398 Genomic DNA. Translation: CAI14206.1. Sequence problems. AL590398, AL671967 Genomic DNA. Translation: CAI14207.1. AL671967, AL590398 Genomic DNA. Translation: CAI15363.1. CH471051 Genomic DNA. Translation: EAW48254.1. CH471051 Genomic DNA. Translation: EAW48255.1. BC031055 mRNA. Translation: AAH31055.2. Different initiation. | ||||||||||||
| IPI | IPI00289601. | ||||||||||||
| RefSeq | NP_001518.3. NM_001527.3. | ||||||||||||
| UniGene | Hs.3352. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q92769. | ||||||||||||
| SMR | Q92769. Positions 9-374. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-24220N. | ||||||||||||
| IntAct | Q92769. 68 interactions. | ||||||||||||
| MINT | MINT-90593. | ||||||||||||
| STRING | Q92769. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q92769. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 68068066. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q92769. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000368632; ENSP00000357621; ENSG00000196591. ENST00000398283; ENSP00000381331; ENSG00000196591. | ||||||||||||
| GeneID | 3066. | ||||||||||||
| KEGG | hsa:3066. | ||||||||||||
| UCSC | uc003pwc.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 3066. | ||||||||||||
| GeneCards | GC06M114307. | ||||||||||||
| H-InvDB | HIX0006155. | ||||||||||||
| HGNC | HGNC:4853. HDAC2. | ||||||||||||
| HPA | CAB005054. HPA011727. | ||||||||||||
| MIM | 605164. gene. | ||||||||||||
| neXtProt | NX_Q92769. | ||||||||||||
| PharmGKB | PA29227. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG15575. | ||||||||||||
| GeneTree | ENSGT00530000062889. | ||||||||||||
| HOGENOM | HBG396919. | ||||||||||||
| HOVERGEN | HBG057112. | ||||||||||||
| InParanoid | Q92769. | ||||||||||||
| OrthoDB | EOG4868CH. | ||||||||||||
| PhylomeDB | Q92769. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Pathway_Interaction_DB | hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins. smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling. telomerasepathway. Regulation of Telomerase. hdac_classi_pathway. Signaling events mediated by HDAC Class I. | ||||||||||||
| Reactome | REACT_111102. Signal Transduction. REACT_604. Hemostasis. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q92769. | ||||||||||||
| Bgee | Q92769. | ||||||||||||
| CleanEx | HS_HDAC2. | ||||||||||||
| Genevestigator | Q92769. | ||||||||||||
| GermOnline | ENSG00000196591. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.800.20. His_deacetylse. 1 hit. | ||||||||||||
| KO | K06067. | ||||||||||||
| PANTHER | PTHR10625. His_deacetylse. 1 hit. | ||||||||||||
| Pfam | PF00850. Hist_deacetyl. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF037913. His_deacetylse_1. 1 hit. | ||||||||||||
| PRINTS | PR01270. HDASUPER. PR01271. HISDACETLASE. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| DrugBank | DB02546. Vorinostat. | ||||||||||||
| NextBio | 12129. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | HDAC2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q92769 Secondary accession number(s): B4DL58 Q8NEH4 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with