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Q9ULG1

- INO80_HUMAN

UniProt

Q9ULG1 - INO80_HUMAN

Protein

DNA helicase INO80

Gene

INO80

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    DNA helicase and probable main scaffold component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; according to PubMed:20687897 the contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Recruited by YY1 to YY1-activated genes, where it acts as an essential coactivator. Binds DNA. In vitro, has double-stranded DNA-dependent ATPase activity. Involved in UV-damage excision repair, DNA replication and chromosome segregation during normal cell division cycle.7 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi543 – 5508ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. alpha-tubulin binding Source: UniProtKB
    2. ATPase activity Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. DNA binding Source: UniProtKB
    5. DNA helicase activity Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to ionizing radiation Source: UniProtKB
    3. cellular response to UV Source: UniProtKB
    4. chromatin remodeling Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. double-strand break repair Source: UniProtKB
    7. double-strand break repair via homologous recombination Source: UniProtKB
    8. mitotic sister chromatid segregation Source: UniProtKB
    9. positive regulation of cell growth Source: UniProtKB
    10. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    13. spindle assembly Source: UniProtKB
    14. UV-damage excision repair Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Mitosis

    Keywords - Ligandi

    Actin-binding, ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA helicase INO80 (EC:3.6.4.12)
    Short name:
    hINO80
    Alternative name(s):
    INO80 complex subunit A
    Putative DNA helicase INO80 complex homolog 1
    Gene namesi
    Name:INO80
    Synonyms:INO80A, INOC1, KIAA1259
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:26956. INO80.

    Subcellular locationi

    Nucleus 3 PublicationsPROSITE-ProRule annotation
    Note: Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner.

    GO - Cellular componenti

    1. Ino80 complex Source: UniProtKB
    2. microtubule Source: UniProtKB-KW
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi653 – 6531E → Q: Abolishes DNA-dependent ATPase and nucleosome remodeling activities. 1 Publication

    Organism-specific databases

    PharmGKBiPA162392040.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15561556DNA helicase INO80PRO_0000248829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei1512 – 15121Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULG1.
    PaxDbiQ9ULG1.
    PRIDEiQ9ULG1.

    PTM databases

    PhosphoSiteiQ9ULG1.

    Expressioni

    Tissue specificityi

    According to PubMed:10574462, widely expressed. According to PubMed:16298340, specifically expressed in brain, liver and pancreas.2 Publications

    Gene expression databases

    ArrayExpressiQ9ULG1.
    BgeeiQ9ULG1.
    CleanExiHS_INO80.
    GenevestigatoriQ9ULG1.

    Organism-specific databases

    HPAiHPA055495.

    Interactioni

    Subunit structurei

    Component of the chromatin-remodeling INO80 complex; three different complex modules assemble on different domains of INO80. Interacts with DDB1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTR5Q9H9F96EBI-769345,EBI-769418
    DDB1Q165314EBI-769345,EBI-350322
    YY1P254905EBI-769345,EBI-765538

    Protein-protein interaction databases

    BioGridi120076. 24 interactions.
    DIPiDIP-34296N.
    IntActiQ9ULG1. 14 interactions.
    STRINGi9606.ENSP00000355205.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULG1.
    SMRiQ9ULG1. Positions 518-821, 1096-1241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini280 – 405126DBINOPROSITE-ProRule annotationAdd
    BLAST
    Domaini530 – 701172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1105 – 1260156Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 266266Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80DAdd
    BLAST
    Regioni212 – 526315Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1Add
    BLAST
    Regioni521 – 15561036Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2Add
    BLAST

    Domaini

    The DBINO region is involved in binding to DNA.

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 DBINO domain.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000231795.
    HOVERGENiHBG057875.
    InParanoidiQ9ULG1.
    KOiK11665.
    OMAiSLHMTSS.
    OrthoDBiEOG7B05C6.
    PhylomeDBiQ9ULG1.
    TreeFamiTF324408.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR020838. DBINO.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF13892. DBINO. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51413. DBINO. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ULG1-1 [UniParc]FASTAAdd to Basket

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    MASELGARDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD     50
    SEDGLDDSNP LLPQSGDPLI QVKEEPPNSL LGETSGAGSS GMLNTYSLNG 100
    VLQSESKCDK GNLYNFSKLK KSRKWLKSIL LSDESSEADS QSEDDDEEEL 150
    NLSREELHNM LRLHKYKKLH QNKYSKDKEL QQYQYYSAGL LSTYDPFYEQ 200
    QRHLLGPKKK KFKEEKKLKA KLKKVKKKRR RDEELSSEES PRRHHHQTKV 250
    FAKFSHDAPP PGTKKKHLSI EQLNARRRKV WLSIVKKELP KANKQKASAR 300
    NLFLTNSRKL AHQCMKEVRR AALQAQKNCK ETLPRARRLT KEMLLYWKKY 350
    EKVEKEHRKR AEKEALEQRK LDEEMREAKR QQRKLNFLIT QTELYAHFMS 400
    RKRDMGHDGI QEEILRKLED SSTQRQIDIG GGVVVNITQE DYDSNHFKAQ 450
    ALKNAENAYH IHQARTRSFD EDAKESRAAA LRAANKSGTG FGESYSLANP 500
    SIRAGEDIPQ PTIFNGKLKG YQLKGMNWLA NLYEQGINGI LADEMGLGKT 550
    VQSIALLAHL AERENIWGPF LIISPASTLN NWHQEFTRFV PKFKVLPYWG 600
    NPHDRKVIRR FWSQKTLYTQ DAPFHVVITS YQLVVQDVKY FQRVKWQYMV 650
    LDEAQALKSS SSVRWKILLQ FQCRNRLLLT GTPIQNTMAE LWALLHFIMP 700
    TLFDSHEEFN EWFSKDIESH AENKSAIDEN QLSRLHMILK PFMLRRIKKD 750
    VENELSDKIE ILMYCQLTSR QKLLYQALKN KISIEDLLQS SMGSTQQAQN 800
    TTSSLMNLVM QFRKVCNHPE LFERQETWSP FHISLKPYHI SKFIYRHGQI 850
    RVFNHSRDRW LRVLSPFAPD YIQRSLFHRK GINEESCFSF LRFIDISPAE 900
    MANLMLQGLL ARWLALFLSL KASYRLHQLR SWGAPEGESH QRYLRNKDFL 950
    LGVNFPLSFP NLCSCPLLKS LVFSSHCKAV SGYSDQVVHQ RRSATSSLRR 1000
    CLLTELPSFL CVASPRVTAV PLDSYCNDRS AEYERRVLKE GGSLAAKQCL 1050
    LNGAPELAAD WLNRRSQFFP EPAGGLWSIR PQNGWSFIRI PGKESLITDS 1100
    GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYR KHTYMRLDGS 1150
    SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP 1200
    TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS 1250
    GGNFKPDTLK PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK 1300
    REKYAEKKKK EDELDGKRRK EGVNLVIPFV PSADNSNLSA DGDDSFISVD 1350
    SAMPSPFSEI SISSELHTGS IPLDESSSDM LVIVDDPASS APQSRATNSP 1400
    ASITGSVSDT VNGISIQEMP AAGRGHSARS RGRPKGSGST AKGAGKGRSR 1450
    KSTAGSAAAM AGAKAGAAAA SAAAYAAYGY NVSKGISASS PLQTSLVRPA 1500
    GLADFGPSSA SSPLSSPLSK GNNVPGNPKN LHMTSSLAPD SLVRKQGKGT 1550
    NPSGGR 1556
    Length:1,556
    Mass (Da):176,753
    Last modified:September 5, 2006 - v2
    Checksum:i712A1EEA26D6A720
    GO

    Sequence cautioni

    The sequence BAA86573.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti882 – 8821I → V.
    Corresponds to variant rs34153025 [ dbSNP | Ensembl ].
    VAR_049500
    Natural varianti1108 – 11081V → G.
    Corresponds to variant rs34178030 [ dbSNP | Ensembl ].
    VAR_061233

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033085 mRNA. Translation: BAA86573.1. Different initiation.
    CH471125 Genomic DNA. Translation: EAW92469.1.
    BC146785 mRNA. Translation: AAI46786.1.
    AL137280 mRNA. Translation: CAB70675.1.
    CCDSiCCDS10071.1.
    PIRiT46350.
    RefSeqiNP_060023.1. NM_017553.2.
    UniGeneiHs.292949.

    Genome annotation databases

    EnsembliENST00000361937; ENSP00000355205; ENSG00000128908.
    ENST00000401393; ENSP00000384686; ENSG00000128908.
    GeneIDi54617.
    KEGGihsa:54617.
    UCSCiuc001zni.3. human.

    Polymorphism databases

    DMDMi114149322.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033085 mRNA. Translation: BAA86573.1 . Different initiation.
    CH471125 Genomic DNA. Translation: EAW92469.1 .
    BC146785 mRNA. Translation: AAI46786.1 .
    AL137280 mRNA. Translation: CAB70675.1 .
    CCDSi CCDS10071.1.
    PIRi T46350.
    RefSeqi NP_060023.1. NM_017553.2.
    UniGenei Hs.292949.

    3D structure databases

    ProteinModelPortali Q9ULG1.
    SMRi Q9ULG1. Positions 518-821, 1096-1241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120076. 24 interactions.
    DIPi DIP-34296N.
    IntActi Q9ULG1. 14 interactions.
    STRINGi 9606.ENSP00000355205.

    PTM databases

    PhosphoSitei Q9ULG1.

    Polymorphism databases

    DMDMi 114149322.

    Proteomic databases

    MaxQBi Q9ULG1.
    PaxDbi Q9ULG1.
    PRIDEi Q9ULG1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361937 ; ENSP00000355205 ; ENSG00000128908 .
    ENST00000401393 ; ENSP00000384686 ; ENSG00000128908 .
    GeneIDi 54617.
    KEGGi hsa:54617.
    UCSCi uc001zni.3. human.

    Organism-specific databases

    CTDi 54617.
    GeneCardsi GC15M041271.
    HGNCi HGNC:26956. INO80.
    HPAi HPA055495.
    MIMi 610169. gene.
    neXtProti NX_Q9ULG1.
    PharmGKBi PA162392040.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000231795.
    HOVERGENi HBG057875.
    InParanoidi Q9ULG1.
    KOi K11665.
    OMAi SLHMTSS.
    OrthoDBi EOG7B05C6.
    PhylomeDBi Q9ULG1.
    TreeFami TF324408.

    Miscellaneous databases

    ChiTaRSi INO80. human.
    GenomeRNAii 54617.
    NextBioi 57137.
    PROi Q9ULG1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULG1.
    Bgeei Q9ULG1.
    CleanExi HS_INO80.
    Genevestigatori Q9ULG1.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR020838. DBINO.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF13892. DBINO. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51413. DBINO. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1302-1556.
      Tissue: Testis.
    5. Cited for: FUNCTION, IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity."
      Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.
      Biochem. Biophys. Res. Commun. 339:313-320(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. Cited for: FUNCTION, INTERACTION WITH YY1.
    8. "A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
      Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
      Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80 COMPLEX.
    9. "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
      Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
      Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The mammalian INO80 complex is recruited to DNA damage sites in an ARP8 dependent manner."
      Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.
      Biochem. Biophys. Res. Commun. 402:619-625(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Human INO80 chromatin-remodelling complex contributes to DNA double-strand break repair via the expression of Rad54B and XRCC3 genes."
      Park E.J., Hur S.K., Kwon J.
      Biochem. J. 431:179-187(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR.
    15. "Roles of human INO80 chromatin remodeling enzyme in DNA replication and chromosome segregation suppress genome instability."
      Hur S.K., Park E.J., Han J.E., Kim Y.A., Kim J.D., Kang D., Kwon J.
      Cell. Mol. Life Sci. 67:2283-2296(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway."
      Jiang Y., Wang X., Bao S., Guo R., Johnson D.G., Shen X., Li L.
      Proc. Natl. Acad. Sci. U.S.A. 107:17274-17279(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, FUNCTION OF THE INO80 COMPLEX.
    17. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
      Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX, MUTAGENESIS OF GLU-653.

    Entry informationi

    Entry nameiINO80_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULG1
    Secondary accession number(s): A6H8X4, Q9NTG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 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 15
      Human chromosome 15: 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