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Q9Y4C1

- KDM3A_HUMAN

UniProt

Q9Y4C1 - KDM3A_HUMAN

Protein

Lysine-specific demethylase 3A

Gene

KDM3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TMP1 which are required for packaging and condensation of sperm chromatin. Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1120 – 11201Iron; catalyticCurated
    Metal bindingi1122 – 11221Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi1249 – 12491Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri662 – 68726C6-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. core promoter binding Source: Ensembl
    3. dioxygenase activity Source: UniProtKB-KW
    4. iron ion binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. transcription regulatory region sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. formaldehyde biosynthetic process Source: UniProtKB
    3. histone H3-K9 demethylation Source: UniProtKB
    4. histone H3-K9 dimethylation Source: Ensembl
    5. hormone-mediated signaling pathway Source: UniProtKB
    6. negative regulation of histone H3-K9 methylation Source: Ensembl
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. spermatid nucleus elongation Source: Ensembl
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Differentiation, Spermatogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 3A (EC:1.14.11.-)
    Alternative name(s):
    JmjC domain-containing histone demethylation protein 2A
    Jumonji domain-containing protein 1A
    Gene namesi
    Name:KDM3A
    Synonyms:JHDM2A, JMJD1, JMJD1A, KIAA0742, TSGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20815. KDM3A.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Nuclear in round spermatids. When spermatids start to elongate, localizes to the cytoplasm where it forms distinct foci which disappear in mature spermatozoa By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1120 – 11201H → Y: Abolishes histone demethylase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA164721293.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13211321Lysine-specific demethylase 3APRO_0000084285Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei264 – 2641Phosphoserine1 Publication
    Modified residuei445 – 4451Phosphoserine1 Publication
    Modified residuei895 – 8951N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4C1.
    PaxDbiQ9Y4C1.
    PRIDEiQ9Y4C1.

    PTM databases

    PhosphoSiteiQ9Y4C1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y4C1.
    BgeeiQ9Y4C1.
    CleanExiHS_JMJD1A.
    GenevestigatoriQ9Y4C1.

    Interactioni

    Protein-protein interaction databases

    BioGridi120927. 15 interactions.
    IntActiQ9Y4C1. 3 interactions.
    MINTiMINT-6946055.
    STRINGi9606.ENSP00000323659.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4C1.
    SMRiQ9Y4C1. Positions 941-1280.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1058 – 1281224JmjCPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi885 – 8895LXXLL motif

    Domaini

    The JmjC domain and the C6-type zinc-finger are required for the demethylation activity.1 Publication
    Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the association with nuclear receptors.By similarity

    Sequence similaritiesi

    Belongs to the JHDM2 histone demethylase family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri662 – 68726C6-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG305537.
    InParanoidiQ9Y4C1.
    KOiK15601.
    OMAiRRLQFNK.
    OrthoDBiEOG7B5WVG.
    PhylomeDBiQ9Y4C1.
    TreeFamiTF324723.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y4C1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLTLGESWP VLVGRRFLSL SAADGSDGSH DSWDVERVAE WPWLSGTIRA     50
    VSHTDVTKKD LKVCVEFDGE SWRKRRWIEV YSLLRRAFLV EHNLVLAERK 100
    SPEISERIVQ WPAITYKPLL DKAGLGSITS VRFLGDQQRV FLSKDLLKPI 150
    QDVNSLRLSL TDNQIVSKEF QALIVKHLDE SHLLKGDKNL VGSEVKIYSL 200
    DPSTQWFSAT VINGNPASKT LQVNCEEIPA LKIVDPSLIH VEVVHDNLVT 250
    CGNSARIGAV KRKSSENNGT LVSKQAKSCS EASPSMCPVQ SVPTTVFKEI 300
    LLGCTAATPP SKDPRQQSTP QAANSPPNLG AKIPQGCHKQ SLPEEISSCL 350
    NTKSEALRTK PDVCKAGLLS KSSQIGTGDL KILTEPKGSC TQPKTNTDQE 400
    NRLESVPQAL TGLPKECLPT KASSKAELEI ANPPELQKHL EHAPSPSDVS 450
    NAPEVKAGVN SDSPNNCSGK KVEPSALACR SQNLKESSVK VDNESCCSRS 500
    NNKIQNAPSR KSVLTDPAKL KKLQQSGEAF VQDDSCVNIV AQLPKCRECR 550
    LDSLRKDKEQ QKDSPVFCRF FHFRRLQFNK HGVLRVEGFL TPNKYDNEAI 600
    GLWLPLTKNV VGIDLDTAKY ILANIGDHFC QMVISEKEAM STIEPHRQVA 650
    WKRAVKGVRE MCDVCDTTIF NLHWVCPRCG FGVCVDCYRM KRKNCQQGAA 700
    YKTFSWLKCV KSQIHEPENL MPTQIIPGKA LYDVGDIVHS VRAKWGIKAN 750
    CPCSNRQFKL FSKPASKEDL KQTSLAGEKP TLGAVLQQNP SVLEPAAVGG 800
    EAASKPAGSM KPACPASTSP LNWLADLTSG NVNKENKEKQ PTMPILKNEI 850
    KCLPPLPPLS KSSTVLHTFN STILTPVSNN NSGFLRNLLN SSTGKTENGL 900
    KNTPKILDDI FASLVQNKTT SDLSKRPQGL TIKPSILGFD TPHYWLCDNR 950
    LLCLQDPNNK SNWNVFRECW KQGQPVMVSG VHHKLNSELW KPESFRKEFG 1000
    EQEVDLVNCR TNEIITGATV GDFWDGFEDV PNRLKNEKEP MVLKLKDWPP 1050
    GEDFRDMMPS RFDDLMANIP LPEYTRRDGK LNLASRLPNY FVRPDLGPKM 1100
    YNAYGLITPE DRKYGTTNLH LDVSDAANVM VYVGIPKGQC EQEEEVLKTI 1150
    QDGDSDELTI KRFIEGKEKP GALWHIYAAK DTEKIREFLK KVSEEQGQEN 1200
    PADHDPIHDQ SWYLDRSLRK RLHQEYGVQG WAIVQFLGDV VFIPAGAPHQ 1250
    VHNLYSCIKV AEDFVSPEHV KHCFWLTQEF RYLSQTHTNH EDKLQVKNVI 1300
    YHAVKDAVAM LKASESSFGK P 1321
    Length:1,321
    Mass (Da):147,341
    Last modified:October 5, 2010 - v4
    Checksum:i9689B3279F450C8A
    GO

    Sequence cautioni

    The sequence BAA34462.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241D → G in CAH18459. (PubMed:17974005)Curated
    Sequence conflicti24 – 241D → G in CAH18373. (PubMed:17974005)Curated
    Sequence conflicti51 – 511V → A in CAE45820. (PubMed:17974005)Curated
    Sequence conflicti500 – 5001S → G in CAH18373. (PubMed:17974005)Curated
    Sequence conflicti698 – 6981G → GG in CAH18459. (PubMed:17974005)Curated
    Sequence conflicti729 – 7291K → KG in CAH18459. (PubMed:17974005)Curated
    Sequence conflicti767 – 7671K → R in CAH18459. (PubMed:17974005)Curated
    Sequence conflicti773 – 7731T → TQT in CAH18459. (PubMed:17974005)Curated
    Sequence conflicti980 – 9801G → R in CAE45820. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035940
    Natural varianti194 – 1941E → K.
    Corresponds to variant rs13424350 [ dbSNP | Ensembl ].
    VAR_030623
    Natural varianti212 – 2121I → V.3 Publications
    Corresponds to variant rs2030259 [ dbSNP | Ensembl ].
    VAR_026220
    Natural varianti447 – 4471S → P.1 Publication
    Corresponds to variant rs34605051 [ dbSNP | Ensembl ].
    VAR_055977
    Natural varianti710 – 7101V → E.
    Corresponds to variant rs11677451 [ dbSNP | Ensembl ].
    VAR_030624

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018285 mRNA. Translation: BAA34462.2. Different initiation.
    AL832150 Transcribed RNA. Translation: CAH18459.3.
    BX640698 mRNA. Translation: CAE45820.1.
    CR749581 mRNA. Translation: CAH18373.1.
    AC068288 Genomic DNA. Translation: AAY24210.1.
    CH471053 Genomic DNA. Translation: EAW99453.1.
    CH471053 Genomic DNA. Translation: EAW99456.1.
    CCDSiCCDS1990.1.
    RefSeqiNP_001140160.1. NM_001146688.1.
    NP_060903.2. NM_018433.5.
    UniGeneiHs.557425.

    Genome annotation databases

    EnsembliENST00000312912; ENSP00000323659; ENSG00000115548.
    ENST00000409064; ENSP00000386516; ENSG00000115548.
    ENST00000409556; ENSP00000386660; ENSG00000115548.
    GeneIDi55818.
    KEGGihsa:55818.
    UCSCiuc002sri.4. human.

    Polymorphism databases

    DMDMi308153659.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018285 mRNA. Translation: BAA34462.2 . Different initiation.
    AL832150 Transcribed RNA. Translation: CAH18459.3 .
    BX640698 mRNA. Translation: CAE45820.1 .
    CR749581 mRNA. Translation: CAH18373.1 .
    AC068288 Genomic DNA. Translation: AAY24210.1 .
    CH471053 Genomic DNA. Translation: EAW99453.1 .
    CH471053 Genomic DNA. Translation: EAW99456.1 .
    CCDSi CCDS1990.1.
    RefSeqi NP_001140160.1. NM_001146688.1.
    NP_060903.2. NM_018433.5.
    UniGenei Hs.557425.

    3D structure databases

    ProteinModelPortali Q9Y4C1.
    SMRi Q9Y4C1. Positions 941-1280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120927. 15 interactions.
    IntActi Q9Y4C1. 3 interactions.
    MINTi MINT-6946055.
    STRINGi 9606.ENSP00000323659.

    Chemistry

    BindingDBi Q9Y4C1.
    ChEMBLi CHEMBL1938209.

    PTM databases

    PhosphoSitei Q9Y4C1.

    Polymorphism databases

    DMDMi 308153659.

    Proteomic databases

    MaxQBi Q9Y4C1.
    PaxDbi Q9Y4C1.
    PRIDEi Q9Y4C1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312912 ; ENSP00000323659 ; ENSG00000115548 .
    ENST00000409064 ; ENSP00000386516 ; ENSG00000115548 .
    ENST00000409556 ; ENSP00000386660 ; ENSG00000115548 .
    GeneIDi 55818.
    KEGGi hsa:55818.
    UCSCi uc002sri.4. human.

    Organism-specific databases

    CTDi 55818.
    GeneCardsi GC02P086667.
    H-InvDB HIX0002238.
    HGNCi HGNC:20815. KDM3A.
    MIMi 611512. gene.
    neXtProti NX_Q9Y4C1.
    PharmGKBi PA164721293.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305537.
    InParanoidi Q9Y4C1.
    KOi K15601.
    OMAi RRLQFNK.
    OrthoDBi EOG7B5WVG.
    PhylomeDBi Q9Y4C1.
    TreeFami TF324723.

    Miscellaneous databases

    ChiTaRSi KDM3A. human.
    GenomeRNAii 55818.
    NextBioi 61002.
    PROi Q9Y4C1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4C1.
    Bgeei Q9Y4C1.
    CleanExi HS_JMJD1A.
    Genevestigatori Q9Y4C1.

    Family and domain databases

    InterProi IPR003347. JmjC_dom.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-212.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-212 AND PRO-447.
      Tissue: Fetal kidney, Salivary gland and Testis.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-212.
    5. "JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor."
      Yamane K., Toumazou C., Tsukada Y.I., Erdjument-Bromage H., Tempst P., Wong J., Zhang Y.
      Cell 125:483-495(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-1120.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-187.

    Entry informationi

    Entry nameiKDM3A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4C1
    Secondary accession number(s): D6W5M3
    , Q53S72, Q68D47, Q68UT9, Q6N050, Q8IY08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 111 of the entry and version 4 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 2
      Human chromosome 2: 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