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P05114

- HMGN1_HUMAN

UniProt

P05114 - HMGN1_HUMAN

Protein

Non-histone chromosomal protein HMG-14

Gene

HMGN1

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

    Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: ProtInc

    GO - Biological processi

    1. chromatin organization Source: Ensembl
    2. positive regulation of DNA-templated transcription, elongation Source: ProtInc
    3. post-embryonic camera-type eye morphogenesis Source: Ensembl
    4. pyrimidine dimer repair by nucleotide-excision repair Source: Ensembl
    5. regulation of development, heterochronic Source: Ensembl
    6. regulation of epithelial cell proliferation Source: Ensembl
    7. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. response to UV-B Source: Ensembl
    9. response to UV-C Source: Ensembl
    10. transcription-coupled nucleotide-excision repair Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-histone chromosomal protein HMG-14
    Alternative name(s):
    High mobility group nucleosome-binding domain-containing protein 1
    Gene namesi
    Name:HMGN1
    Synonyms:HMG14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:4984. HMGN1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus.

    GO - Cellular componenti

    1. chromatin Source: ProtInc
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35088.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10099Non-histone chromosomal protein HMG-14PRO_0000206691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine1 Publication
    Modified residuei14 – 141N6-acetyllysine1 Publication
    Modified residuei21 – 211Phosphoserine; by RPS6KA51 Publication
    Modified residuei25 – 251Phosphoserine; by RPS6KA51 Publication
    Modified residuei27 – 271N6-acetyllysineBy similarity
    Modified residuei82 – 821N6-acetyllysine1 Publication
    Modified residuei86 – 861Phosphoserine5 Publications
    Modified residuei89 – 891Phosphoserine5 Publications
    Modified residuei99 – 991Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation on Ser-21 and Ser-25 weakens binding to nucleosomes and increases the rate of H3 phosphorylation By similarity. Phosphorylation favors cytoplasmic localization.By similarity6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05114.
    PaxDbiP05114.
    PRIDEiP05114.

    PTM databases

    PhosphoSiteiP05114.

    Expressioni

    Gene expression databases

    BgeeiP05114.
    CleanExiHS_HMGN1.
    GenevestigatoriP05114.

    Organism-specific databases

    HPAiCAB012260.
    HPA048694.

    Interactioni

    Protein-protein interaction databases

    BioGridi109393. 20 interactions.
    IntActiP05114. 1 interaction.
    MINTiMINT-5008059.
    STRINGi9606.ENSP00000370125.

    Structurei

    3D structure databases

    ProteinModelPortaliP05114.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HMGN family.Curated

    Phylogenomic databases

    eggNOGiNOG29368.
    HOGENOMiHOG000116394.
    HOVERGENiHBG073479.
    KOiK11299.
    PhylomeDBiP05114.
    TreeFamiTF105374.

    Family and domain databases

    InterProiIPR000079. HMGN_fam.
    [Graphical view]
    PANTHERiPTHR23087. PTHR23087. 1 hit.
    PfamiPF01101. HMG14_17. 1 hit.
    [Graphical view]
    PRINTSiPR00925. NONHISHMG17.
    SMARTiSM00527. HMG17. 1 hit.
    [Graphical view]
    PROSITEiPS00355. HMG14_17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05114-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV    50
    QTKGKRGAKG KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD 100
    Length:100
    Mass (Da):10,659
    Last modified:January 23, 2007 - v3
    Checksum:i8F4CB5374D51FBF3
    GO

    RNA editingi

    Partially edited. A new initiator methionine may be created by a single uridine insertion in the 5'-UTR, causing an N-terminal extension of 45 amino acids. The existence of the RNA edited version is supported by direct protein sequencing by MS/MS of the following peptides specific to that version: 23-31 and 40-48. The RNA edited version is called ET-HMGN1.1 Publication

    Mass spectrometryi

    Molecular mass is 10527.8±0.7 Da from positions 2 - 100. Determined by ESI. 1 Publication
    Molecular mass is 10608 Da from positions 2 - 100. Determined by ESI. 1 Publication
    Molecular mass is 10688±1.3 Da from positions 2 - 100. Determined by ESI. 1 Publication
    Molecular mass is 10768 Da from positions 2 - 100. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 11M → MLGRREEWQRQGSPVSRRLS ARRGPQAPGTRLPRRHPARA FPAATM in RNA edited version.
    VAR_054790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02621 mRNA. Translation: AAA52676.1.
    M21339 Genomic DNA. Translation: AAA52677.1.
    BT007337 mRNA. Translation: AAP36001.1.
    AF064861 Genomic DNA. No translation available.
    AL163279 Genomic DNA. Translation: CAB90453.1.
    BC000075 mRNA. Translation: AAH00075.1.
    BC023984 mRNA. Translation: AAH23984.1.
    BC070153 mRNA. Translation: AAH70153.1.
    BC106080 mRNA. Translation: AAI06081.1.
    CCDSiCCDS33559.1.
    PIRiA33310.
    RefSeqiNP_004956.5. NM_004965.6.
    UniGeneiHs.356285.

    Genome annotation databases

    EnsembliENST00000380749; ENSP00000370125; ENSG00000205581.
    GeneIDi3150.
    KEGGihsa:3150.
    UCSCiuc002yxo.3. human.

    Polymorphism databases

    DMDMi123101.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02621 mRNA. Translation: AAA52676.1 .
    M21339 Genomic DNA. Translation: AAA52677.1 .
    BT007337 mRNA. Translation: AAP36001.1 .
    AF064861 Genomic DNA. No translation available.
    AL163279 Genomic DNA. Translation: CAB90453.1 .
    BC000075 mRNA. Translation: AAH00075.1 .
    BC023984 mRNA. Translation: AAH23984.1 .
    BC070153 mRNA. Translation: AAH70153.1 .
    BC106080 mRNA. Translation: AAI06081.1 .
    CCDSi CCDS33559.1.
    PIRi A33310.
    RefSeqi NP_004956.5. NM_004965.6.
    UniGenei Hs.356285.

    3D structure databases

    ProteinModelPortali P05114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109393. 20 interactions.
    IntActi P05114. 1 interaction.
    MINTi MINT-5008059.
    STRINGi 9606.ENSP00000370125.

    PTM databases

    PhosphoSitei P05114.

    Polymorphism databases

    DMDMi 123101.

    Proteomic databases

    MaxQBi P05114.
    PaxDbi P05114.
    PRIDEi P05114.

    Protocols and materials databases

    DNASUi 3150.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380749 ; ENSP00000370125 ; ENSG00000205581 .
    GeneIDi 3150.
    KEGGi hsa:3150.
    UCSCi uc002yxo.3. human.

    Organism-specific databases

    CTDi 3150.
    GeneCardsi GC21M040714.
    H-InvDB HIX0038161.
    HIX0203332.
    HGNCi HGNC:4984. HMGN1.
    HPAi CAB012260.
    HPA048694.
    MIMi 163920. gene.
    neXtProti NX_P05114.
    PharmGKBi PA35088.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29368.
    HOGENOMi HOG000116394.
    HOVERGENi HBG073479.
    KOi K11299.
    PhylomeDBi P05114.
    TreeFami TF105374.

    Miscellaneous databases

    ChiTaRSi HMGN1. human.
    GeneWikii HMGN1.
    GenomeRNAii 3150.
    NextBioi 12484.
    PROi P05114.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05114.
    CleanExi HS_HMGN1.
    Genevestigatori P05114.

    Family and domain databases

    InterProi IPR000079. HMGN_fam.
    [Graphical view ]
    PANTHERi PTHR23087. PTHR23087. 1 hit.
    Pfami PF01101. HMG14_17. 1 hit.
    [Graphical view ]
    PRINTSi PR00925. NONHISHMG17.
    SMARTi SM00527. HMG17. 1 hit.
    [Graphical view ]
    PROSITEi PS00355. HMG14_17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Chromosomal protein HMG-14. Complete human cDNA sequence and evidence for a multigene family."
      Landsman D., Srikantha T., Westermann R., Bustin M.
      J. Biol. Chem. 261:16082-16086(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Chromosomal protein HMG-14. Identification, characterization, and chromosome localization of a functional gene from the large human multigene family."
      Landsman D., McBride O.W., Soares N., Crippa M.P., Srikantha T., Bustin M.
      J. Biol. Chem. 264:3421-3427(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Bone marrow, Brain and Ovary.
    6. "Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry."
      Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G.
      Protein Sci. 9:170-179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-31, PHOSPHORYLATION AT SER-21 AND SER-25, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    7. Cited for: PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), RNA EDITING, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "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].
    13. "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-86 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-14 AND LYS-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-86 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-8; SER-86 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHMGN1_HUMAN
    AccessioniPrimary (citable) accession number: P05114
    Secondary accession number(s): Q3KQR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 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 21
      Human chromosome 21: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3