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Q969S8

- HDA10_HUMAN

UniProt

Q969S8 - HDA10_HUMAN

Protein

Histone deacetylase 10

Gene

HDAC10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351By similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. histone deacetylase activity Source: UniProtKB
    3. histone deacetylase binding Source: UniProtKB
    4. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    7. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    8. protein binding Source: UniProtKB
    9. protein deacetylase activity Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB
    2. histone deacetylation Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. Notch signaling pathway Source: Reactome
    6. oligodendrocyte development Source: Ensembl
    7. protein deacetylation Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BRENDAi3.5.1.98. 2681.
    ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    SABIO-RKQ969S8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 10 (EC:3.5.1.98)
    Short name:
    HD10
    Gene namesi
    Name:HDAC10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18128. HDAC10.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Excluded from the nucleoli.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone deacetylase complex Source: UniProtKB
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351H → A: Abolishes deacetylase activity. Does not affect interaction with HDAC3. 2 Publications

    Organism-specific databases

    PharmGKBiPA38297.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 669669Histone deacetylase 10PRO_0000114712Add
    BLAST

    Proteomic databases

    MaxQBiQ969S8.
    PaxDbiQ969S8.
    PRIDEiQ969S8.

    PTM databases

    PhosphoSiteiQ969S8.

    Expressioni

    Tissue specificityi

    Ubiquitous. High expression in liver, spleen, pancreas and kidney.

    Gene expression databases

    ArrayExpressiQ969S8.
    BgeeiQ969S8.
    CleanExiHS_HDAC10.
    GenevestigatoriQ969S8.

    Organism-specific databases

    HPAiCAB045977.

    Interactioni

    Subunit structurei

    Interacts with HDAC2, HDAC3 and NCOR2.2 Publications

    Protein-protein interaction databases

    BioGridi123818. 22 interactions.
    IntActiQ969S8. 10 interactions.
    STRINGi9606.ENSP00000216271.

    Structurei

    3D structure databases

    ProteinModelPortaliQ969S8.
    SMRiQ969S8. Positions 30-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 323323Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOVERGENiHBG051892.
    InParanoidiQ969S8.
    KOiK11407.
    OMAiGLEQRCL.
    OrthoDBiEOG7992PT.
    PhylomeDBiQ969S8.
    TreeFamiTF106173.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PRINTSiPR01270. HDASUPER.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q969S8-1) [UniParc]FASTAAdd to Basket

    Also known as: B, Alpha

    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.

    « Hide

    MGTALVYHED MTATRLLWDD PECEIERPER LTAALDRLRQ RGLEQRCLRL    50
    SAREASEEEL GLVHSPEYVS LVRETQVLGK EELQALSGQF DAIYFHPSTF 100
    HCARLAAGAG LQLVDAVLTG AVQNGLALVR PPGHHGQRAA ANGFCVFNNV 150
    AIAAAHAKQK HGLHRILVVD WDVHHGQGIQ YLFEDDPSVL YFSWHRYEHG 200
    RFWPFLRESD ADAVGRGQGL GFTVNLPWNQ VGMGNADYVA AFLHLLLPLA 250
    FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRVCAV 300
    LEGGYHLESL AESVCMTVQT LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ 350
    APHWKSLQQQ DVTAVPMSPS SHSPEGRPPP LLPGGPVCKA AASAPSSLLD 400
    QPCLCPAPSV RTAVALTTPD ITLVLPPDVI QQEASALREE TEAWARPHES 450
    LAREEALTAL GKLLYLLDGM LDGQVNSGIA ATPASAAAAT LDVAVRRGLS 500
    HGAQRLLCVA LGQLDRPPDL AHDGRSLWLN IRGKEAAALS MFHVSTPLPV 550
    MTGGFLSCIL GLVLPLAYGF QPDLVLVALG PGHGLQGPHA ALLAAMLRGL 600
    AGGRVLALLE ENSTPQLAGI LARVLNGEAP PSLGPSSVAS PEDVQALMYL 650
    RGQLEPQWKM LQCHPHLVA 669
    Length:669
    Mass (Da):71,445
    Last modified:December 1, 2001 - v1
    Checksum:i872D9427E6893A18
    GO
    Isoform 2 (identifier: Q969S8-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         252-271: Missing.

    Show »
    Length:649
    Mass (Da):69,385
    Checksum:i7756351E6BC838FB
    GO
    Isoform 4 (identifier: Q969S8-4) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         612-669: NSTPQLAGIL...MLQCHPHLVA → VSWAGWRCCG...GPGAEWRGTS

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:658
    Mass (Da):70,033
    Checksum:i0EABDDA886585928
    GO
    Isoform 5 (identifier: Q969S8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         252-301: Missing.
         447-669: Missing.

    Show »
    Length:396
    Mass (Da):43,016
    Checksum:i22DE1D205E5856A0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921A → T in AAS48345. 1 PublicationCurated
    Sequence conflicti177 – 1771Q → R in AAS48345. 1 PublicationCurated
    Sequence conflicti337 – 3371Q → QRC in CAC21653. (PubMed:17974005)Curated
    Sequence conflicti594 – 5941A → T in AAK92205. (PubMed:11677242)Curated
    Sequence conflicti594 – 5941A → T in AAK92206. (PubMed:11677242)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti429 – 4291V → I.
    Corresponds to variant rs34402301 [ dbSNP | Ensembl ].
    VAR_049356
    Natural varianti584 – 5841G → C.1 Publication
    VAR_015067

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei252 – 30150Missing in isoform 5. 1 PublicationVSP_014698Add
    BLAST
    Alternative sequencei252 – 27120Missing in isoform 2. 1 PublicationVSP_002089Add
    BLAST
    Alternative sequencei447 – 669223Missing in isoform 5. 1 PublicationVSP_014699Add
    BLAST
    Alternative sequencei612 – 66958NSTPQ…PHLVA → VSWAGWRCCGVGRGKGPVTA SVFAPGPELHTPASRDPGPG AEWRGTS in isoform 4. 2 PublicationsVSP_002090Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426160 mRNA. Translation: AAL30513.1.
    AF393962 mRNA. Translation: AAK84023.1.
    AF407272 mRNA. Translation: AAK92205.1.
    AF407273 mRNA. Translation: AAK92206.1.
    CR456465 mRNA. Translation: CAG30351.1.
    AY450395 mRNA. Translation: AAS48345.1.
    AL022328 Genomic DNA. No translation available.
    BC125083 mRNA. Translation: AAI25084.1.
    AL512711 mRNA. Translation: CAC21653.2.
    CCDSiCCDS14088.1. [Q969S8-1]
    CCDS54545.1. [Q969S8-2]
    RefSeqiNP_001152758.1. NM_001159286.1. [Q969S8-2]
    NP_114408.3. NM_032019.5. [Q969S8-1]
    UniGeneiHs.26593.

    Genome annotation databases

    EnsembliENST00000216271; ENSP00000216271; ENSG00000100429. [Q969S8-1]
    ENST00000349505; ENSP00000343540; ENSG00000100429. [Q969S8-2]
    ENST00000454936; ENSP00000406150; ENSG00000100429. [Q969S8-5]
    GeneIDi83933.
    KEGGihsa:83933.
    UCSCiuc003bkg.3. human. [Q969S8-1]
    uc010hav.3. human. [Q969S8-2]

    Polymorphism databases

    DMDMi27734403.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426160 mRNA. Translation: AAL30513.1 .
    AF393962 mRNA. Translation: AAK84023.1 .
    AF407272 mRNA. Translation: AAK92205.1 .
    AF407273 mRNA. Translation: AAK92206.1 .
    CR456465 mRNA. Translation: CAG30351.1 .
    AY450395 mRNA. Translation: AAS48345.1 .
    AL022328 Genomic DNA. No translation available.
    BC125083 mRNA. Translation: AAI25084.1 .
    AL512711 mRNA. Translation: CAC21653.2 .
    CCDSi CCDS14088.1. [Q969S8-1 ]
    CCDS54545.1. [Q969S8-2 ]
    RefSeqi NP_001152758.1. NM_001159286.1. [Q969S8-2 ]
    NP_114408.3. NM_032019.5. [Q969S8-1 ]
    UniGenei Hs.26593.

    3D structure databases

    ProteinModelPortali Q969S8.
    SMRi Q969S8. Positions 30-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123818. 22 interactions.
    IntActi Q969S8. 10 interactions.
    STRINGi 9606.ENSP00000216271.

    Chemistry

    BindingDBi Q969S8.
    ChEMBLi CHEMBL2093865.
    GuidetoPHARMACOLOGYi 2614.

    PTM databases

    PhosphoSitei Q969S8.

    Polymorphism databases

    DMDMi 27734403.

    Proteomic databases

    MaxQBi Q969S8.
    PaxDbi Q969S8.
    PRIDEi Q969S8.

    Protocols and materials databases

    DNASUi 83933.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216271 ; ENSP00000216271 ; ENSG00000100429 . [Q969S8-1 ]
    ENST00000349505 ; ENSP00000343540 ; ENSG00000100429 . [Q969S8-2 ]
    ENST00000454936 ; ENSP00000406150 ; ENSG00000100429 . [Q969S8-5 ]
    GeneIDi 83933.
    KEGGi hsa:83933.
    UCSCi uc003bkg.3. human. [Q969S8-1 ]
    uc010hav.3. human. [Q969S8-2 ]

    Organism-specific databases

    CTDi 83933.
    GeneCardsi GC22M050683.
    H-InvDB HIX0080289.
    HGNCi HGNC:18128. HDAC10.
    HPAi CAB045977.
    MIMi 608544. gene.
    neXtProti NX_Q969S8.
    PharmGKBi PA38297.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOVERGENi HBG051892.
    InParanoidi Q969S8.
    KOi K11407.
    OMAi GLEQRCL.
    OrthoDBi EOG7992PT.
    PhylomeDBi Q969S8.
    TreeFami TF106173.

    Enzyme and pathway databases

    BRENDAi 3.5.1.98. 2681.
    Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    SABIO-RK Q969S8.

    Miscellaneous databases

    ChiTaRSi HDAC10. human.
    GeneWikii HDAC10.
    GenomeRNAii 83933.
    NextBioi 73053.
    PROi Q969S8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q969S8.
    Bgeei Q969S8.
    CleanExi HS_HDAC10.
    Genevestigatori Q969S8.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain."
      Tong J.J., Liu J., Bertos N.R., Yang X.-J.
      Nucleic Acids Res. 30:1114-1123(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HDAC3, MUTAGENESIS OF HIS-135.
      Tissue: Fetal brain.
    2. "Molecular cloning and characterization of a novel histone deacetylase HDAC10."
      Guardiola A.R., Yao T.-P.
      J. Biol. Chem. 277:3350-3356(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), MUTAGENESIS OF HIS-135.
      Tissue: Leukemia.
    3. "Isolation and characterization of mammalian HDAC10, a novel histone deacetylase."
      Kao H.-Y., Lee C.-H., Komarov A., Han C.C., Evans R.M.
      J. Biol. Chem. 277:187-193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), CHARACTERIZATION.
      Tissue: Hepatoma.
    4. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH HDAC2 AND NCOR2, VARIANT CYS-584.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Lin L., Li H., Zhou G., Shen C., Xiao W., Li M., Ke R., Yang S.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-446.
      Tissue: Amygdala.
    10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).

    Entry informationi

    Entry nameiHDA10_HUMAN
    AccessioniPrimary (citable) accession number: Q969S8
    Secondary accession number(s): Q08AP4
    , Q6STF9, Q96P77, Q96P78, Q9H028, Q9UGX1, Q9UGX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 119 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3