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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

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

Functioni

Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].3 Publications

Kineticsi

kcat is 4.14 (sec-1) for acetyl-CoA.1 Publication

  1. KM=6.68 µM for acetyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei199 – 1991Interaction with histone H4 N-terminus1 Publication
    Active sitei276 – 2761Proton donor/acceptor1 Publication

    GO - Molecular functioni

    • H4 histone acetyltransferase activity Source: UniProtKB
    • histone acetyltransferase activity Source: ProtInc

    GO - Biological processi

    • chromatin organization Source: Reactome
    • chromatin silencing at telomere Source: InterPro
    • DNA packaging Source: ProtInc
    • DNA replication-dependent nucleosome assembly Source: UniProtKB
    • DNA replication-independent nucleosome assembly Source: UniProtKB
    • histone H4 acetylation Source: UniProtKB
    • internal protein amino acid acetylation Source: ProtInc
    • response to nutrient Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 2681.
    ReactomeiREACT_264245. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase type B catalytic subunit (EC:2.3.1.483 Publications)
    Alternative name(s):
    Histone acetyltransferase 1
    Gene namesi
    Name:HAT1
    Synonyms:KAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4821. HAT1.

    Subcellular locationi

    Isoform B :
    • Cytoplasm
    • Nucleus
    • Nucleus matrix
    • Nucleusnucleoplasm

    • Note: Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein.

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • intracellular membrane-bounded organelle Source: HPA
    • nuclear chromatin Source: UniProtKB
    • nuclear matrix Source: UniProtKB-SubCell
    • nucleoplasm Source: HPA
    • nucleus Source: ProtInc
    • protein complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi62 – 621D → A: Strongly reduces HAT activity. 1 Publication
    Mutagenesisi64 – 641E → A: Strongly reduces HAT activity. 1 Publication
    Mutagenesisi187 – 1871E → Q: Strongly reduces HAT activity. 1 Publication
    Mutagenesisi199 – 1991W → A: Strongly reduces HAT activity. 1 Publication
    Mutagenesisi276 – 2761E → Q: Strongly reduces HAT activity. 1 Publication
    Mutagenesisi277 – 2771D → N: Strongly reduces HAT activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29197.

    Polymorphism and mutation databases

    BioMutaiHAT1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 419418Histone acetyltransferase type B catalytic subunitPRO_0000083902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei15 – 151N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO14929.
    PaxDbiO14929.
    PeptideAtlasiO14929.
    PRIDEiO14929.

    PTM databases

    PhosphoSiteiO14929.

    Expressioni

    Developmental stagei

    Highly expressed in mitotic cells (at protein level).1 Publication

    Inductioni

    Up-regulated by estrogen.1 Publication

    Gene expression databases

    BgeeiO14929.
    CleanExiHS_HAT1.
    ExpressionAtlasiO14929. baseline and differential.
    GenevisibleiO14929. HS.

    Organism-specific databases

    HPAiCAB037191.
    HPA036788.

    Interactioni

    Subunit structurei

    Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628054EBI-2339359,EBI-302023
    MEOX2A4D1273EBI-10181798,EBI-10172134
    RBBP4Q090283EBI-2339359,EBI-620823
    RELQ048643EBI-2339359,EBI-307352
    TCF4P158843EBI-2339359,EBI-533224
    TNFAIP1Q138293EBI-2339359,EBI-2505861
    vprP125203EBI-2339359,EBI-6164519From a different organism.

    Protein-protein interaction databases

    BioGridi114092. 30 interactions.
    DIPiDIP-52811N.
    IntActiO14929. 19 interactions.
    MINTiMINT-2795393.
    STRINGi9606.ENSP00000264108.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 283Combined sources
    Helixi29 – 324Combined sources
    Beta strandi33 – 408Combined sources
    Helixi41 – 444Combined sources
    Helixi47 – 493Combined sources
    Helixi57 – 604Combined sources
    Turni61 – 644Combined sources
    Beta strandi65 – 717Combined sources
    Beta strandi73 – 797Combined sources
    Turni80 – 823Combined sources
    Beta strandi85 – 906Combined sources
    Beta strandi92 – 943Combined sources
    Turni97 – 993Combined sources
    Beta strandi100 – 1023Combined sources
    Helixi107 – 1126Combined sources
    Helixi123 – 1319Combined sources
    Helixi132 – 1354Combined sources
    Beta strandi140 – 1489Combined sources
    Beta strandi157 – 1648Combined sources
    Helixi171 – 18515Combined sources
    Beta strandi199 – 21012Combined sources
    Beta strandi213 – 22917Combined sources
    Turni230 – 2323Combined sources
    Beta strandi233 – 24311Combined sources
    Helixi245 – 2473Combined sources
    Helixi252 – 26514Combined sources
    Beta strandi273 – 2775Combined sources
    Helixi280 – 29415Combined sources
    Helixi298 – 3003Combined sources
    Helixi302 – 3054Combined sources
    Helixi311 – 32111Combined sources
    Helixi325 – 33915Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P0WX-ray1.90A/B20-341[»]
    ProteinModelPortaliO14929.
    SMRiO14929. Positions 23-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14929.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 643Interaction with histone H4 N-terminus1 Publication
    Regioni225 – 2273Interaction with histone H4 N-terminusCurated
    Regioni241 – 2433Acetyl-CoA binding1 Publication
    Regioni248 – 2547Acetyl-CoA binding1 Publication

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    eggNOGiNOG326277.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    InParanoidiO14929.
    KOiK11303.
    PhylomeDBiO14929.
    TreeFamiTF314995.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    [Graphical view]
    PANTHERiPTHR12046. PTHR12046. 1 hit.
    PfamiPF10394. Hat1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform A (identifier: O14929-1) [UniParc]FASTAAdd to basket

    Also known as: a, Nuclear

    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

            10         20         30         40         50
    MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT
    60 70 80 90 100
    FFPEYTHQLF GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD
    110 120 130 140 150
    CVEADDVEGK IRQIIPPGFC TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS
    160 170 180 190 200
    PTGGENFTFQ IYKADMTCRG FREYHERLQT FLMWFIETAS FIDVDDERWH
    210 220 230 240 250
    YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ MLILTPFQGQ
    260 270 280 290 300
    GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF
    310 320 330 340 350
    SREKLMQGFN EDMAIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS
    360 370 380 390 400
    YRLDIKRRLI SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE
    410
    SFQELVEDYR RVIERLAQE
    Length:419
    Mass (Da):49,513
    Last modified:January 1, 1998 - v1
    Checksum:i509DF06E0E4E2647
    GO
    Isoform B (identifier: O14929-2) [UniParc]FASTAAdd to basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Show »
    Length:334
    Mass (Da):39,786
    Checksum:i40E4B9925CD5DF81
    GO

    Sequence cautioni

    The sequence AAH18682.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171A → P in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8585Missing in isoform B. 1 PublicationVSP_041129Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030424 mRNA. Translation: AAC02425.1.
    AC015976 Genomic DNA. Translation: AAY14731.1.
    AC114745 Genomic DNA. Translation: AAX93247.1.
    CH471058 Genomic DNA. Translation: EAX11195.1.
    BC018682 mRNA. Translation: AAH18682.1. Different initiation.
    BC045673 mRNA. No translation available.
    BC063003 mRNA. Translation: AAH63003.1.
    CCDSiCCDS2245.1. [O14929-1]
    RefSeqiNP_003633.1. NM_003642.3. [O14929-1]
    UniGeneiHs.632532.

    Genome annotation databases

    EnsembliENST00000264108; ENSP00000264108; ENSG00000128708.
    GeneIDi8520.
    KEGGihsa:8520.
    UCSCiuc002uhi.3. human. [O14929-1]
    uc010fqi.2. human. [O14929-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Histone acetyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030424 mRNA. Translation: AAC02425.1.
    AC015976 Genomic DNA. Translation: AAY14731.1.
    AC114745 Genomic DNA. Translation: AAX93247.1.
    CH471058 Genomic DNA. Translation: EAX11195.1.
    BC018682 mRNA. Translation: AAH18682.1. Different initiation.
    BC045673 mRNA. No translation available.
    BC063003 mRNA. Translation: AAH63003.1.
    CCDSiCCDS2245.1. [O14929-1]
    RefSeqiNP_003633.1. NM_003642.3. [O14929-1]
    UniGeneiHs.632532.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P0WX-ray1.90A/B20-341[»]
    ProteinModelPortaliO14929.
    SMRiO14929. Positions 23-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114092. 30 interactions.
    DIPiDIP-52811N.
    IntActiO14929. 19 interactions.
    MINTiMINT-2795393.
    STRINGi9606.ENSP00000264108.

    PTM databases

    PhosphoSiteiO14929.

    Polymorphism and mutation databases

    BioMutaiHAT1.

    Proteomic databases

    MaxQBiO14929.
    PaxDbiO14929.
    PeptideAtlasiO14929.
    PRIDEiO14929.

    Protocols and materials databases

    DNASUi8520.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264108; ENSP00000264108; ENSG00000128708.
    GeneIDi8520.
    KEGGihsa:8520.
    UCSCiuc002uhi.3. human. [O14929-1]
    uc010fqi.2. human. [O14929-2]

    Organism-specific databases

    CTDi8520.
    GeneCardsiGC02P172779.
    HGNCiHGNC:4821. HAT1.
    HPAiCAB037191.
    HPA036788.
    MIMi603053. gene.
    neXtProtiNX_O14929.
    PharmGKBiPA29197.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG326277.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    InParanoidiO14929.
    KOiK11303.
    PhylomeDBiO14929.
    TreeFamiTF314995.

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 2681.
    ReactomeiREACT_264245. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSiHAT1. human.
    EvolutionaryTraceiO14929.
    GeneWikiiHAT1.
    GenomeRNAii8520.
    NextBioi31898.
    PROiO14929.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO14929.
    CleanExiHS_HAT1.
    ExpressionAtlasiO14929. baseline and differential.
    GenevisibleiO14929. HS.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    [Graphical view]
    PANTHERiPTHR12046. PTHR12046. 1 hit.
    PfamiPF10394. Hat1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase."
      Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
      Curr. Biol. 8:96-108(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ENZYME ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION.
      Tissue: Teratocarcinoma.
    2. "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].
    3. 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] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-419 (ISOFORM A).
      Tissue: Brain, Lung and Testis.
    5. "Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase."
      Makowski A.M., Dutnall R.N., Annunziato A.T.
      J. Biol. Chem. 276:43499-43502(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    6. "Quantitative real-time RT-PCR analysis of eight novel estrogen-regulated genes in breast cancer."
      Sorbello V., Fuso L., Sfiligoi C., Scafoglio C., Ponzone R., Biglia N., Weisz A., Sismondi P., De Bortoli M.
      Int. J. Biol. Markers 18:123-129(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ESTROGEN.
    7. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. "Irradiation with heavy-ion particles changes the cellular distribution of human histone acetyltransferase HAT1."
      Lebel E.A., Boukamp P., Tafrov S.T.
      Mol. Cell. Biochem. 339:271-284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    9. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1."
      Wu H., Moshkina N., Min J., Zeng H., Joshua J., Zhou M.M., Plotnikov A.N.
      Proc. Natl. Acad. Sci. U.S.A. 109:8925-8930(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-341 IN COMPLEX WITH ACETYL-COA AND HISTONE H4 PEPTIDE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-62; GLU-64; GLU-187; TRP-199; GLU-276 AND ASP-277, ACTIVE SITE, INTERACTION WITH HISTONE H4.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-317.

    Entry informationi

    Entry nameiHAT1_HUMAN
    AccessioniPrimary (citable) accession number: O14929
    Secondary accession number(s): Q49A44
    , Q53QF0, Q53SU4, Q6P594, Q8WWB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: July 22, 2015
    This is version 135 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.