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P54198

- HIRA_HUMAN

UniProt

P54198 - HIRA_HUMAN

Protein

Protein HIRA

Gene

HIRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. chromatin modification Source: UniProtKB-KW
    3. DNA replication-independent nucleosome assembly Source: UniProt
    4. gastrulation Source: Ensembl
    5. muscle cell differentiation Source: Ensembl
    6. osteoblast differentiation Source: Ensembl
    7. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    SignaLinkiP54198.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein HIRA
    Alternative name(s):
    TUP1-like enhancer of split protein 1
    Gene namesi
    Name:HIRA
    Synonyms:DGCR1, HIR, TUPLE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4916. HIRA.

    Subcellular locationi

    Nucleus. NucleusPML body
    Note: Primarily, though not exclusively, localized to the nucleus. Localizes to PML bodies immediately prior to onset of senescence.

    GO - Cellular componenti

    1. nuclear chromatin Source: UniProt
    2. nucleoplasm Source: Reactome
    3. nucleus Source: ProtInc
    4. PML body Source: UniProtKB-SubCell
    5. protein complex Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi449 – 45810Missing: Impairs binding to ASF1A.
    Mutagenesisi458 – 4603RRR → AKK: Abrogates binding to ASF1A.
    Mutagenesisi458 – 4603RRR → KKK: Impairs binding to ASF1A.
    Mutagenesisi458 – 4592RR → AK: Impairs binding to ASF1A.
    Mutagenesisi458 – 4581R → A: Impairs binding to ASF1A.
    Mutagenesisi458 – 4581R → K: Impairs binding to ASF1A; when associated with K-460.
    Mutagenesisi459 – 46810Missing: Abrogates binding to ASF1A. 1 Publication
    Mutagenesisi459 – 4591R → A: Abrogates binding to ASF1A. 1 Publication
    Mutagenesisi460 – 4601R → A: Abrogates binding to ASF1A. 1 Publication
    Mutagenesisi460 – 4601R → K: Impairs binding to ASF1A; when associated with K-458. 1 Publication
    Mutagenesisi461 – 4611I → D: Abrogates binding to ASF1A. 1 Publication
    Mutagenesisi464 – 4641L → D: Impairs binding to ASF1A. 1 Publication
    Mutagenesisi466 – 4661I → D: Impairs binding to ASF1A. 1 Publication
    Mutagenesisi555 – 5551T → A: Impairs phosphorylation by CDK2. 1 Publication
    Mutagenesisi628 – 6314KRKL → AAAA: Impairs binding to CCNA1 and phosphorylation by CDK2.

    Organism-specific databases

    Orphaneti567. 22q11.2 deletion syndrome.
    PharmGKBiPA29293.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10171017Protein HIRAPRO_0000051019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei549 – 5491Phosphoserine1 Publication
    Modified residuei555 – 5551Phosphothreonine; by CDK21 Publication
    Modified residuei557 – 5571Phosphoserine1 Publication
    Modified residuei576 – 5761Phosphothreonine1 Publication
    Modified residuei584 – 5841Phosphoserine1 Publication
    Modified residuei586 – 5861Phosphothreonine3 Publications
    Modified residuei610 – 6101Phosphoserine1 Publication
    Modified residuei611 – 6111Phosphoserine1 Publication
    Modified residuei612 – 6121Phosphoserine1 Publication
    Modified residuei614 – 6141Phosphoserine1 Publication
    Modified residuei661 – 6611Phosphoserine2 Publications
    Modified residuei687 – 6871Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated.1 Publication
    Phosphorylated by CDK2/CCNA1 and CDK2/CCNE1 on Thr-555 in vitro. Also phosphorylated on Thr-555 and Ser-687 in vivo.5 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP54198.
    PaxDbiP54198.
    PeptideAtlasiP54198.
    PRIDEiP54198.

    PTM databases

    PhosphoSiteiP54198.

    Expressioni

    Tissue specificityi

    Expressed at high levels in kidney, pancreas and skeletal muscle and at lower levels in brain, heart, liver, lung, and placenta.1 Publication

    Developmental stagei

    Expressed during embryogenesis.

    Gene expression databases

    ArrayExpressiP54198.
    BgeeiP54198.
    CleanExiHS_HIRA.
    GenevestigatoriP54198.

    Organism-specific databases

    HPAiCAB039243.
    CAB039244.

    Interactioni

    Subunit structurei

    Interacts with histone H3F3B, PAX3 and PAX7 By similarity. Interacts with CCNA1, HIRIP3, NFU1/HIRIP5 and histone H2B. Part of a complex which includes ASF1A, CABIN1, histone H3.3, histone H4 and UBN1.By similarity7 Publications

    Protein-protein interaction databases

    BioGridi113141. 20 interactions.
    DIPiDIP-29240N.
    IntActiP54198. 7 interactions.
    MINTiMINT-3020150.
    STRINGi9606.ENSP00000263208.

    Structurei

    Secondary structure

    1
    1017
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi450 – 4534
    Beta strandi459 – 4624

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I32X-ray2.70E/F425-472[»]
    ProteinModelPortaliP54198.
    SMRiP54198. Positions 16-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54198.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati11 – 5343WD 1Add
    BLAST
    Repeati68 – 10740WD 2Add
    BLAST
    Repeati129 – 16840WD 3Add
    BLAST
    Repeati172 – 21140WD 4Add
    BLAST
    Repeati220 – 26344WD 5Add
    BLAST
    Repeati266 – 32257WD 6Add
    BLAST
    Repeati326 – 36742WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni421 – 729309Interaction with CCNA1Add
    BLAST
    Regioni421 – 47959Interaction with ASF1AAdd
    BLAST
    Regioni439 – 47537Required for repression of histone gene transcriptionAdd
    BLAST
    Regioni593 – 826234Interaction with histone H2BAdd
    BLAST
    Regioni594 – 739146Interaction with PAX3By similarityAdd
    BLAST
    Regioni738 – 1017280Interaction with histone H4Add
    BLAST
    Regioni740 – 82889Interaction with PAX3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi408 – 4125Poly-Gln
    Compositional biasi640 – 6434Poly-Lys
    Compositional biasi805 – 8084Poly-Val

    Sequence similaritiesi

    Belongs to the WD repeat HIR1 family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000007670.
    HOVERGENiHBG005969.
    InParanoidiP54198.
    KOiK11293.
    OMAiLEDIRKX.
    PhylomeDBiP54198.
    TreeFamiTF323161.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR011494. Hira.
    IPR019015. HIRA_B_motif.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF07569. Hira. 1 hit.
    PF09453. HIRA_B. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P54198-1) [UniParc]FASTAAdd to Basket

    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

    MKLLKPTWVN HNGKPIFSVD IHPDGTKFAT GGQGQDSGKV VIWNMSPVLQ     50
    EDDEKDENIP KMLCQMDNHL ACVNCVRWSN SGMYLASGGD DKLIMVWKRA 100
    TYIGPSTVFG SSGKLANVEQ WRCVSILRNH SGDVMDVAWS PHDAWLASCS 150
    VDNTVVIWNA VKFPEILATL RGHSGLVKGL TWDPVGKYIA SQADDRSLKV 200
    WRTLDWQLET SITKPFDECG GTTHVLRLSW SPDGHYLVSA HAMNNSGPTA 250
    QIIEREGWKT NMDFVGHRKA VTVVKFNPKI FKKKQKNGSS AKPSCPYCCC 300
    AVGSKDRSLS VWLTCLKRPL VVIHELFDKS IMDISWTLNG LGILVCSMDG 350
    SVAFLDFSQD ELGDPLSEEE KSRIHQSTYG KSLAIMTEAQ LSTAVIENPE 400
    MLKYQRRQQQ QQLDQKSAAT REMGSATSVA GVVNGESLED IRKNLLKKQV 450
    ETRTADGRRR ITPLCIAQLD TGDFSTAFFN SIPLSGSLAG TMLSSHSSPQ 500
    LLPLDSSTPN SFGASKPCTE PVVAASARPA GDSVNKDSMN ATSTPAALSP 550
    SVLTTPSKIE PMKAFDSRFT ERSKATPGAP ALTSMTPTAV ERLKEQNLVK 600
    ELRPRDLLES SSDSDEKVPL AKASSLSKRK LELEVETVEK KKKGRPRKDS 650
    RLMPVSLSVQ SPAALTAEKE AMCLSAPALA LKLPIPSPQR AFTLQVSSDP 700
    SMYIEVENEV TVVGGVKLSR LKCNREGKEW ETVLTSRILT AAGSCDVVCV 750
    ACEKRMLSVF STCGRRLLSP ILLPSPISTL HCTGSYVMAL TAAATLSVWD 800
    VHRQVVVVKE ESLHSILAGS DMTVSQILLT QHGIPVMNLS DGKAYCFNPS 850
    LSTWNLVSDK QDSLAQCADF RSSLPSQDAM LCSGPLAIIQ GRTSNSGRQA 900
    ARLFSVPHVV QQETTLAYLE NQVAAALTLQ SSHEYRHWLL VYARYLVNEG 950
    FEYRLREICK DLLGPVHYST GSQWESTVVG LRKRELLKEL LPVIGQNLRF 1000
    QRLFTECQEQ LDILRDK 1017
    Length:1,017
    Mass (Da):111,835
    Last modified:February 21, 2006 - v2
    Checksum:i475784B2FF9D16D6
    GO
    Isoform Short (identifier: P54198-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         593-799: Missing.

    Show »
    Length:810
    Mass (Da):89,299
    Checksum:iA169BFDCE4C8D4D7
    GO

    Sequence cautioni

    The sequence CAA53044.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA54721.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA57436.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91V → G in CAA54721. (PubMed:7633437)Curated
    Sequence conflicti889 – 8891I → N in CAA54721. (PubMed:7633437)Curated
    Sequence conflicti889 – 8891I → N in CAA57436. (PubMed:7633437)Curated
    Sequence conflicti889 – 8891I → N in CAA61979. (PubMed:8681138)Curated
    Sequence conflicti990 – 9901L → M in CAA53044. (PubMed:8111380)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei593 – 799207Missing in isoform Short. 1 PublicationVSP_006772Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81844 mRNA. Translation: CAA57436.1. Different initiation.
    X77633 mRNA. Translation: CAA54721.1. Different initiation.
    X89887 mRNA. Translation: CAA61979.1.
    X91501 Genomic DNA. Translation: CAA62800.1.
    CR456503 mRNA. Translation: CAG30389.1.
    BC032721 mRNA. Translation: AAH32721.1.
    BC039835 mRNA. Translation: AAH39835.1.
    X75296 mRNA. Translation: CAA53044.1. Different initiation.
    CCDSiCCDS13759.1. [P54198-1]
    PIRiI37465.
    S45344.
    RefSeqiNP_003316.3. NM_003325.3. [P54198-1]
    UniGeneiHs.474206.

    Genome annotation databases

    EnsembliENST00000263208; ENSP00000263208; ENSG00000100084. [P54198-1]
    ENST00000340170; ENSP00000345350; ENSG00000100084. [P54198-2]
    GeneIDi7290.
    KEGGihsa:7290.
    UCSCiuc002zpf.1. human. [P54198-1]
    uc010grn.1. human. [P54198-2]

    Polymorphism databases

    DMDMi88984228.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81844 mRNA. Translation: CAA57436.1 . Different initiation.
    X77633 mRNA. Translation: CAA54721.1 . Different initiation.
    X89887 mRNA. Translation: CAA61979.1 .
    X91501 Genomic DNA. Translation: CAA62800.1 .
    CR456503 mRNA. Translation: CAG30389.1 .
    BC032721 mRNA. Translation: AAH32721.1 .
    BC039835 mRNA. Translation: AAH39835.1 .
    X75296 mRNA. Translation: CAA53044.1 . Different initiation.
    CCDSi CCDS13759.1. [P54198-1 ]
    PIRi I37465.
    S45344.
    RefSeqi NP_003316.3. NM_003325.3. [P54198-1 ]
    UniGenei Hs.474206.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I32 X-ray 2.70 E/F 425-472 [» ]
    ProteinModelPortali P54198.
    SMRi P54198. Positions 16-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113141. 20 interactions.
    DIPi DIP-29240N.
    IntActi P54198. 7 interactions.
    MINTi MINT-3020150.
    STRINGi 9606.ENSP00000263208.

    PTM databases

    PhosphoSitei P54198.

    Polymorphism databases

    DMDMi 88984228.

    Proteomic databases

    MaxQBi P54198.
    PaxDbi P54198.
    PeptideAtlasi P54198.
    PRIDEi P54198.

    Protocols and materials databases

    DNASUi 7290.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263208 ; ENSP00000263208 ; ENSG00000100084 . [P54198-1 ]
    ENST00000340170 ; ENSP00000345350 ; ENSG00000100084 . [P54198-2 ]
    GeneIDi 7290.
    KEGGi hsa:7290.
    UCSCi uc002zpf.1. human. [P54198-1 ]
    uc010grn.1. human. [P54198-2 ]

    Organism-specific databases

    CTDi 7290.
    GeneCardsi GC22M019318.
    HGNCi HGNC:4916. HIRA.
    HPAi CAB039243.
    CAB039244.
    MIMi 600237. gene.
    neXtProti NX_P54198.
    Orphaneti 567. 22q11.2 deletion syndrome.
    PharmGKBi PA29293.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000007670.
    HOVERGENi HBG005969.
    InParanoidi P54198.
    KOi K11293.
    OMAi LEDIRKX.
    PhylomeDBi P54198.
    TreeFami TF323161.

    Enzyme and pathway databases

    Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    SignaLinki P54198.

    Miscellaneous databases

    ChiTaRSi HIRA. human.
    EvolutionaryTracei P54198.
    GeneWikii HIRA.
    GenomeRNAii 7290.
    NextBioi 28503.
    PROi P54198.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54198.
    Bgeei P54198.
    CleanExi HS_HIRA.
    Genevestigatori P54198.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR011494. Hira.
    IPR019015. HIRA_B_motif.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF07569. Hira. 1 hit.
    PF09453. HIRA_B. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region."
      Lamour V., Lecluse Y., Desmaze C., Spector M., Bodescot M., Aurias A., Osley M.A., Lipinski M.
      Hum. Mol. Genet. 4:791-799(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Brain.
    2. "Structural organization of the WD repeat protein-encoding gene HIRA in the DiGeorge syndrome critical region of human chromosome 22."
      Lorain S., Demczuk S., Lamour V., Toth S., Aurias A., Roe B.A., Lipinski M.
      Genome Res. 6:43-50(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    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 LONG).
      Tissue: Eye and Lymph.
    5. "Isolation of a putative transcriptional regulator from the region of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital heart disease."
      Halford S., Wadey R., Roberts C., Daw S.C.M., Whiting J.A., O'Donnell H., Dunham I., Bentley D., Lindsay E., Baldini A., Francis F., Lehrach H., Williamson R., Wilson D.I., Goodship J., Cross I., Burn J., Scambler P.J.
      Hum. Mol. Genet. 2:2099-2107(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-1017 (ISOFORM SHORT).
      Tissue: Fetal brain.
    6. "The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is expressed in embryonic structures affected in human CATCH22 patients."
      Wilming L.G., Snoeren C.A.S., van Rijswijk A., Grosveld F., Meijers C.
      Hum. Mol. Genet. 6:247-258(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA."
      Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y., Almouzni G., Lipinski M.
      Mol. Cell. Biol. 18:5546-5556(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIRIP3; HISTONE H2B; HISTONE H4 AND NFU1, SUBCELLULAR LOCATION.
    8. "HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression."
      Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S., Lipinski M., Adams P.D.
      Mol. Cell. Biol. 21:1854-1865(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNA1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-555 AND SER-687, MUTAGENESIS OF THR-555 AND 628-LYS--LEU-631.
    9. "Coupling of DNA synthesis and histone synthesis in S phase independent of cyclin/cdk2 activity."
      Nelson D.M., Ye X., Hall C., Santos H., Ma T., Kao G.D., Yen T.J., Harper J.W., Adams P.D.
      Mol. Cell. Biol. 22:7459-7472(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. Cited for: INTERACTION WITH ASF1A.
    11. "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis."
      Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.
      Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ASF1A; CABIN1; HISTONE H3.3 AND UBN1.
    12. "Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
      Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.
      Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASF1A, SUBCELLULAR LOCATION.
    13. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND THR-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the HIRA/ASF1a chromatin-remodeling pathway in senescent cells."
      Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M., Ceulemans H., Schultz D., Marmorstein R., Adams P.D.
      Mol. Cell. Biol. 29:758-770(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBN1.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-557; THR-576 AND THR-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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 THR-586 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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-610; SER-611; SER-612; SER-614 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly."
      Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A., Dunbrack R., Adams P.D., Marmorstein R.
      Nat. Struct. Mol. Biol. 13:921-929(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 425-472 IN COMPLEX WITH ASF1A, MUTAGENESIS OF 449-GLN--ARG-458; 459-ARG--GLN-468; ARG-459; ARG-460; ILE-461; LEU-464 AND ILE-466.

    Entry informationi

    Entry nameiHIRA_HUMAN
    AccessioniPrimary (citable) accession number: P54198
    Secondary accession number(s): Q05BU9, Q8IXN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 143 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3