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Q99879

- H2B1M_HUMAN

UniProt

Q99879 - H2B1M_HUMAN

Protein

Histone H2B type 1-M

Gene

HIST1H2BM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. nucleosome assembly Source: UniProtKB

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_27271. Meiotic recombination.
    REACT_75792. Meiotic synapsis.
    REACT_75925. Amyloids.
    REACT_7963. Packaging Of Telomere Ends.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2B type 1-M
    Alternative name(s):
    Histone H2B.e
    Short name:
    H2B/e
    Gene namesi
    Name:HIST1H2BM
    Synonyms:H2BFE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4750. HIST1H2BM.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleoplasm Source: Reactome
    3. nucleosome Source: UniProtKB
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29125.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 126125Histone H2B type 1-MPRO_0000071831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei6 – 61N6-acetyllysine; alternate2 Publications
    Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
    Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
    Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
    Modified residuei13 – 131N6-acetyllysine; alternate2 Publications
    Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
    Modified residuei15 – 151Phosphoserine; by STK4/MST11 Publication
    Modified residuei16 – 161N6-acetyllysine; alternate2 Publications
    Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
    Modified residuei21 – 211N6-acetyllysine; alternate2 Publications
    Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
    Modified residuei24 – 241N6-acetyllysine; alternate1 Publication
    Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
    Modified residuei35 – 351N6-crotonyllysine; alternate1 Publication
    Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
    Modified residuei37 – 371Phosphoserine; by AMPKBy similarity
    Modified residuei47 – 471N6-methyllysineBy similarity
    Modified residuei58 – 581N6,N6-dimethyllysineBy similarity
    Modified residuei80 – 801Dimethylated arginineBy similarity
    Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
    Modified residuei87 – 871Omega-N-methylarginineBy similarity
    Modified residuei93 – 931Omega-N-methylarginineBy similarity
    Modified residuei109 – 1091N6-methyllysineBy similarity
    Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
    Modified residuei116 – 1161PhosphothreonineBy similarity
    Modified residuei117 – 1171N6-methylated lysineBy similarity
    Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications

    Post-translational modificationi

    Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
    Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription By similarity. Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.By similarity1 Publication
    GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes By similarity.By similarity
    Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ99879.
    PRIDEiQ99879.

    PTM databases

    PhosphoSiteiQ99879.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99879.
    BgeeiQ99879.
    CleanExiHS_HIST1H2BM.
    GenevestigatoriQ99879.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

    Protein-protein interaction databases

    BioGridi113938. 12 interactions.
    IntActiQ99879. 7 interactions.
    MINTiMINT-3060064.
    STRINGi9606.ENSP00000352442.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99879.
    SMRiQ99879. Positions 6-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG317029.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiQ99879.
    KOiK11252.
    OMAiKESYAID.
    OrthoDBiEOG72VH8J.
    PhylomeDBiQ99879.
    TreeFamiTF300212.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000558. Histone_H2B.
    [Graphical view]
    PANTHERiPTHR23428. PTHR23428. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00621. HISTONEH2B.
    SMARTiSM00427. H2B. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00357. HISTONE_H2B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEPVKSAPV PKKGSKKAIN KAQKKDGKKR KRSRKESYSV YVYKVLKQVH    50
    PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR 100
    LLLPGELAKH AVSEGTKAVT KYTSSK 126
    Length:126
    Mass (Da):13,989
    Last modified:January 23, 2007 - v3
    Checksum:iEB394C60B42C202A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761G → R in AAH67487. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101H → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036205

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z83738 Genomic DNA. Translation: CAB06033.1.
    AF531296 Genomic DNA. Translation: AAN06696.1.
    AL049822 Genomic DNA. Translation: CAB81655.1.
    BC066244 mRNA. Translation: AAH66244.1.
    BC067486 mRNA. Translation: AAH67486.1.
    BC067487 mRNA. Translation: AAH67487.1.
    BC067488 mRNA. Translation: AAH67488.1.
    BC067489 mRNA. Translation: AAH67489.1.
    CCDSiCCDS4629.1.
    RefSeqiNP_003512.1. NM_003521.2.
    UniGeneiHs.182432.

    Genome annotation databases

    GeneIDi8342.
    KEGGihsa:8342.
    UCSCiuc003njo.3. human.

    Polymorphism databases

    DMDMi7387742.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z83738 Genomic DNA. Translation: CAB06033.1 .
    AF531296 Genomic DNA. Translation: AAN06696.1 .
    AL049822 Genomic DNA. Translation: CAB81655.1 .
    BC066244 mRNA. Translation: AAH66244.1 .
    BC067486 mRNA. Translation: AAH67486.1 .
    BC067487 mRNA. Translation: AAH67487.1 .
    BC067488 mRNA. Translation: AAH67488.1 .
    BC067489 mRNA. Translation: AAH67489.1 .
    CCDSi CCDS4629.1.
    RefSeqi NP_003512.1. NM_003521.2.
    UniGenei Hs.182432.

    3D structure databases

    ProteinModelPortali Q99879.
    SMRi Q99879. Positions 6-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113938. 12 interactions.
    IntActi Q99879. 7 interactions.
    MINTi MINT-3060064.
    STRINGi 9606.ENSP00000352442.

    PTM databases

    PhosphoSitei Q99879.

    Polymorphism databases

    DMDMi 7387742.

    Proteomic databases

    PaxDbi Q99879.
    PRIDEi Q99879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8342.
    KEGGi hsa:8342.
    UCSCi uc003njo.3. human.

    Organism-specific databases

    CTDi 8342.
    GeneCardsi GC06P027782.
    HGNCi HGNC:4750. HIST1H2BM.
    MIMi 602802. gene.
    neXtProti NX_Q99879.
    PharmGKBi PA29125.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317029.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi Q99879.
    KOi K11252.
    OMAi KESYAID.
    OrthoDBi EOG72VH8J.
    PhylomeDBi Q99879.
    TreeFami TF300212.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_27271. Meiotic recombination.
    REACT_75792. Meiotic synapsis.
    REACT_75925. Amyloids.
    REACT_7963. Packaging Of Telomere Ends.

    Miscellaneous databases

    GeneWikii HIST1H2BM.
    GenomeRNAii 8342.
    NextBioi 31240.
    PROi Q99879.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99879.
    Bgeei Q99879.
    CleanExi HS_HIST1H2BM.
    Genevestigatori Q99879.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000558. Histone_H2B.
    [Graphical view ]
    PANTHERi PTHR23428. PTHR23428. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00621. HISTONEH2B.
    SMARTi SM00427. H2B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00357. HISTONE_H2B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human histone gene cluster at the D6S105 locus."
      Albig W., Doenecke D.
      Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The human and mouse replication-dependent histone genes."
      Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
      Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 59-73, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    6. "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase."
      Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.
      Cell 113:507-517(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    7. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
      Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-121.
    8. "Inhibition of core histones acetylation by carcinogenic nickel(II)."
      Golebiowski F., Kasprzak K.S.
      Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
    9. "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II."
      Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.
      Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-121.
    10. "Gene-specific characterization of human histone H2B by electron capture dissociation."
      Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.
      J. Proteome Res. 5:233-239(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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-6; LYS-13; LYS-16; LYS-17; LYS-21 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
      Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
      Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.
    13. "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation."
      Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.
      Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-35.
    14. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
      Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
      Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP49.
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-110.

    Entry informationi

    Entry nameiH2B1M_HUMAN
    AccessioniPrimary (citable) accession number: Q99879
    Secondary accession number(s): Q6NWQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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