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P05114 (HMGN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-histone chromosomal protein HMG-14
Alternative name(s):
High mobility group nucleosome-binding domain-containing protein 1
Gene names
Name:HMGN1
Synonyms:HMG14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus. Ref.6 Ref.7

Post-translational modification

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

Sequence similarities

Belongs to the HMGN family.

Mass spectrometry

Molecular mass is 10527.8±0.7 Da from positions 2 - 100. Determined by ESI. Ref.6

Molecular mass is 10608 Da from positions 2 - 100. Determined by ESI. Ref.6

Molecular mass is 10688±1.3 Da from positions 2 - 100. Determined by ESI. Ref.6

Molecular mass is 10768 Da from positions 2 - 100. Determined by ESI. Ref.6

RNA editing

Modified position: not applicable.
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. Ref.7

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityRNA editing
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA-templated transcription, elongation

Traceable author statement PubMed 8047885. Source: ProtInc

post-embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

pyrimidine dimer repair by nucleotide-excision repair

Inferred from electronic annotation. Source: Ensembl

regulation of development, heterochronic

Inferred from electronic annotation. Source: Ensembl

regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to UV-B

Inferred from electronic annotation. Source: Ensembl

response to UV-C

Inferred from electronic annotation. Source: Ensembl

transcription-coupled nucleotide-excision repair

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

Traceable author statement PubMed 8047885. Source: ProtInc

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 16780588. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 8047885. Source: ProtInc

chromatin binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10099Non-histone chromosomal protein HMG-14
PRO_0000206691

Amino acid modifications

Modified residue81Phosphoserine Ref.17
Modified residue141N6-acetyllysine Ref.14
Modified residue211Phosphoserine; by RPS6KA5 Ref.6
Modified residue251Phosphoserine; by RPS6KA5 Ref.6
Modified residue271N6-acetyllysine By similarity
Modified residue821N6-acetyllysine Ref.14
Modified residue861Phosphoserine Ref.10 Ref.11 Ref.13 Ref.15 Ref.17
Modified residue891Phosphoserine Ref.10 Ref.11 Ref.13 Ref.15 Ref.17
Modified residue991Phosphoserine Ref.10

Natural variations

Natural variant11M → MLGRREEWQRQGSPVSRRLS ARRGPQAPGTRLPRRHPARA FPAATM in RNA edited version.
VAR_054790

Sequences

Sequence LengthMass (Da)Tools
P05114 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8F4CB5374D51FBF3

FASTA10010,659
        10         20         30         40         50         60 
MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG 

        70         80         90        100 
KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Evidence for insertional RNA editing in humans."
Zougman A., Ziolkowski P., Mann M., Wisniewski J.R.
Curr. Biol. 18:1760-1765(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA33310.
RefSeqNP_004956.5. NM_004965.6.
UniGeneHs.356285.

3D structure databases

ProteinModelPortalP05114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109393. 20 interactions.
IntActP05114. 1 interaction.
MINTMINT-5008059.
STRING9606.ENSP00000370125.

PTM databases

PhosphoSiteP05114.

Polymorphism databases

DMDM123101.

Proteomic databases

PaxDbP05114.
PRIDEP05114.

Protocols and materials databases

DNASU3150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380749; ENSP00000370125; ENSG00000205581.
GeneID3150.
KEGGhsa:3150.
UCSCuc002yxo.3. human.

Organism-specific databases

CTD3150.
GeneCardsGC21M040714.
H-InvDBHIX0038161.
HIX0203332.
HGNCHGNC:4984. HMGN1.
HPACAB012260.
HPA048694.
MIM163920. gene.
neXtProtNX_P05114.
PharmGKBPA35088.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29368.
HOGENOMHOG000116394.
HOVERGENHBG073479.
KOK11299.
PhylomeDBP05114.
TreeFamTF105374.

Gene expression databases

BgeeP05114.
CleanExHS_HMGN1.
GenevestigatorP05114.

Family and domain databases

InterProIPR000079. HMGN_fam.
[Graphical view]
PANTHERPTHR23087. PTHR23087. 1 hit.
PfamPF01101. HMG14_17. 1 hit.
[Graphical view]
PRINTSPR00925. NONHISHMG17.
SMARTSM00527. HMG17. 1 hit.
[Graphical view]
PROSITEPS00355. HMG14_17. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHMGN1. human.
GeneWikiHMGN1.
GenomeRNAi3150.
NextBio12484.
PROP05114.
SOURCESearch...

Entry information

Entry nameHMGN1_HUMAN
AccessionPrimary (citable) accession number: P05114
Secondary accession number(s): Q3KQR8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM