Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Non-histone chromosomal protein HMG-14

Gene

HMGN1

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 861Phosphoserine6 Publications
Modified residuei89 – 891Phosphoserine6 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 similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05114.
PaxDbiP05114.
PRIDEiP05114.

PTM databases

PhosphoSiteiP05114.

Expressioni

Gene expression databases

BgeeiP05114.
CleanExiHS_HMGN1.
ExpressionAtlasiP05114. baseline.
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.
GeneTreeiENSGT00730000110877.
HOGENOMiHOG000116394.
HOVERGENiHBG073479.
InParanoidiP05114.
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

        10         20         30         40         50
MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV
60 70 80 90 100
QTKGKRGAKG KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP05114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP05114.

Polymorphism databases

DMDMi123101.

Proteomic databases

MaxQBiP05114.
PaxDbiP05114.
PRIDEiP05114.

Protocols and materials databases

DNASUi3150.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3150.
GeneCardsiGC21M040714.
H-InvDBHIX0038161.
HIX0203332.
HGNCiHGNC:4984. HMGN1.
HPAiCAB012260.
HPA048694.
MIMi163920. gene.
neXtProtiNX_P05114.
PharmGKBiPA35088.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG29368.
GeneTreeiENSGT00730000110877.
HOGENOMiHOG000116394.
HOVERGENiHBG073479.
InParanoidiP05114.
KOiK11299.
PhylomeDBiP05114.
TreeFamiTF105374.

Miscellaneous databases

ChiTaRSiHMGN1. human.
GeneWikiiHMGN1.
GenomeRNAii3150.
NextBioi12484.
PROiP05114.
SOURCEiSearch...

Gene expression databases

BgeeiP05114.
CleanExiHS_HMGN1.
ExpressionAtlasiP05114. baseline.
GenevestigatoriP05114.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [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.

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: March 4, 2015
This is version 153 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

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.