Reviewed,
UniProtKB/Swiss-Prot Q92769 (HDAC2_HUMAN)
Last modified
February 9, 2010.
Version 112.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone deacetylase 2 Short name=HD2 EC=3.5.1.98 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| 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 By similarity. 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. |
| Catalytic activity | Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. |
| Subunit structure | Interacts with the non-histone region of H2AFY 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/BRAF35, AOF2/LSD1, RCOR1/CoREST and PHF21A/BHC80. 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, DNMT1, MINT, HDAC7, HDAC10, HCFC1, NRIP1, MJD2A/JHDM3A, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the non-histone region of H2AFY. Interacts with PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with CBFA2T3. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.20 Ref.29 |
| Subcellular location | |
| Tissue specificity | Widely expressed; lower levels in brain and lung. |
| Sequence similarities | Belongs to the histone deacetylase family. Type 1 subfamily. |
| Sequence caution | The sequence CAI14206.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BRMS1 | Q9HCU9 | 2 | EBI-301821,EBI-714781 | |
| DAXX | Q9UER7 | 1 | EBI-301821,EBI-77321 | |
| HCFC1 | P51610 | 1 | EBI-301821,EBI-396176 | |
| HDAC1 | Q13547 | 2 | EBI-301821,EBI-301834 | |
| HDAC10 | Q969S8 | 1 | EBI-301821,EBI-301762 | |
| MBD1 | Q9UIS9 | 2 | EBI-301821,EBI-867196 | |
| RFX5 | P48382 | 1 | EBI-301821,EBI-923266 | |
| SIN3A | Q96ST3 | 2 | EBI-301821,EBI-347218 | |
| SUV39H1 | O43463 | 2 | EBI-301821,EBI-349968 |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q92769-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q92769-2) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MRSPPCGLLR...PVAAVAGEPM | ||||||
| Note: No experimental confirmation available. |
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.31 | ||||||
| Modified residue | 90 | 1 | N6-acetyllysine Ref.31 | ||||||
| Modified residue | 394 | 1 | Phosphoserine Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.27 Ref.30 | ||||||
| Modified residue | 407 | 1 | Phosphoserine Ref.25 Ref.22 | ||||||
| Modified residue | 422 | 1 | Phosphoserine Ref.19 Ref.25 Ref.27 Ref.30 Ref.22 | ||||||
| Modified residue | 424 | 1 | Phosphoserine Ref.19 Ref.25 Ref.27 Ref.30 Ref.22 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → MRSPPCGLLRWFGGPLLASW CRCHLRFRAFGTSAGWYRAF PAPPPLLPPACPSPRDYRPH VSLSPFLSRPSRGGSSSSSS SRRRSPVAAVAGEPM in isoform 2. | VSP_037162 | |||||
| Natural variant | 230 | 1 | R → C: dbSNP rs1042903. Ref.1 | VAR_025311 | |||||
| Natural variant | 315 | 1 | Y → H: dbSNP rs17852888. Ref.4 | 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 | ||||||
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] (ISOFORM 1), 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] (ISOFORM 2). 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] | "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] (ISOFORM 1), VARIANT HIS-315. Tissue: Testis. |
| [5] | "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. |
| [6] | "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. |
| [7] | "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. |
| [8] | "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. |
| [9] | "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. |
| [10] | "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. |
| [11] | "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. |
| [12] | "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. |
| [13] | "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. |
| [14] | "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; AOF2; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I. |
| [15] | "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. |
| [16] | "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. |
| [17] | "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. |
| [18] | "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. |
| [19] | "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: Epithelium. |
| [20] | "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. |
| [21] | "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: Epithelium. |
| [22] | "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. |
| [23] | "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. |
| [24] | "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. |
| [25] | "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. |
| [26] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [27] | "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. |
| [28] | "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. |
| [29] | "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. |
| [30] | "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: T-cell. |
| [31] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U31814 mRNA. Translation: AAC50814.1. AK296856 mRNA. Translation: BAG59420.1. AL590398 Genomic DNA. Translation: CAI14206.1. AL590398, AL671967 Genomic DNA. Translation: CAI14207.1. AL671967, AL590398 Genomic DNA. Translation: CAI15363.1. BC031055 mRNA. Translation: AAH31055.2. |
| IPI | IPI00289601. IPI00929375. |
| RefSeq | NP_001518.2. |
| UniGene | Hs.3352 |
3D structure databases | |
| SMR | Q92769. Positions 13-374. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-24220N. |
| IntAct | Q92769. 28 interactions. |
| STRING | Q92769. |
PTM databases | |
| PhosphoSite | Q92769. |
Proteomic databases | |
| PRIDE | Q92769. |
Genome annotation databases | |
| Ensembl | ENST00000368632; ENSP00000357621; ENSG00000196591; Homo sapiens. [Genome view] ENST00000398283; ENSP00000381331; ENSG00000196591; Homo sapiens. [Genome view] |
| GeneID | 3066. |
| KEGG | hsa:3066. |
| UCSC | uc003pwc.1. human. |
Organism-specific databases | |
| CTD | 3066. |
| GeneCards | GC06M114368. |
| HGNC | HGNC:4853. HDAC2. |
| HPA | CAB005054. HPA011727. |
| MIM | 605164. gene. |
| PharmGKB | PA29227. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG15575. |
| HOGENOM | HBG396919. |
| HOVERGEN | Q92769. |
| InParanoid | Q92769. |
| OMA | XYHQRVL. |
| OrthoDB | EOG94XN2W. |
| 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_11061. Signalling by NGF. |
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. [Graphical view] |
| Gene3D | G3DSA:3.40.800.20. His_deacetylse. 1 hit. |
| PANTHER | PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 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 Resources | |
| 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 project | HPI (Human Proteome Initiative) | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


