P05114 (HMGN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 an 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 component	Cytoplasm Nucleus
Coding sequence diversity	RNA editing
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin organization Inferred from electronic annotation. Source: Compara positive regulation of DNA-dependent transcription, elongation Traceable author statement PubMed 8047885. Source: ProtInc post-embryonic camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara pyrimidine dimer repair by nucleotide-excision repair Inferred from electronic annotation. Source: Compara regulation of development, heterochronic Inferred from electronic annotation. Source: Compara regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara response to UV-B Inferred from electronic annotation. Source: Compara response to UV-C Inferred from electronic annotation. Source: Compara transcription-coupled nucleotide-excision repair Inferred from electronic annotation. Source: Compara
Cellular_component	chromatin 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_function	DNA binding Traceable author statement PubMed 8047885. Source: ProtInc nucleosomal DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 100	99	Non-histone chromosomal protein HMG-14		PRO_0000206691
Amino acid modifications
	Modified residue	8	1	Phosphoserine Ref.16
	Modified residue	14	1	N6-acetyllysine Ref.13
	Modified residue	21	1	Phosphoserine; by RPS6KA5 Ref.6
	Modified residue	25	1	Phosphoserine; by RPS6KA5 Ref.6
	Modified residue	81	1	Phosphothreonine By similarity
	Modified residue	82	1	N6-acetyllysine Ref.13
	Modified residue	86	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
	Modified residue	89	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
	Modified residue	99	1	Phosphoserine Ref.10
Natural variations
	Natural variant	1	1	M → MLGRREEWQRQGSPVSRRLS ARRGPQAPGTRLPRRHPARA FPAATM in RNA edited version.		VAR_054790

Sequences

	Sequence		Length	Mass (Da)
	P05114 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8F4CB5374D51FBF3	FASTA	100	10,659
	10 20 30 40 50 60 MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG 70 80 90 100 KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD

References

	« Hide 'large scale' referencesShow '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. , 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), MASS SPECTROMETRY, RNA EDITING, SUBCELLULAR LOCATION.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00554761.
PIR	A33310.
RefSeq	NP_004956.5. NM_004965.6.
UniGene	Hs.356285.
3D structure databases
ProteinModelPortal	P05114.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05114. 1 interaction.
MINT	MINT-5008059.
STRING	9606.ENSP00000370125.
PTM databases
PhosphoSite	P05114.
Polymorphism databases
DMDM	123101.
Proteomic databases
PaxDb	P05114.
PRIDE	P05114.
Protocols and materials databases
DNASU	3150.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380749; ENSP00000370125; ENSG00000205581.
GeneID	3150.
KEGG	hsa:3150.
UCSC	uc002yxo.3. human.
Organism-specific databases
CTD	3150.
GeneCards	GC21M040714.
H-InvDB	HIX0038161. HIX0203332.
HGNC	HGNC:4984. HMGN1.
HPA	CAB012260. HPA048694.
MIM	163920. gene.
neXtProt	NX_P05114.
PharmGKB	PA35088.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG29368.
HOGENOM	HOG000116394.
HOVERGEN	HBG073479.
KO	K11299.
OrthoDB	EOG4CZBHP.
Gene expression databases
ArrayExpress	P05114.
Bgee	P05114.
CleanEx	HS_HMGN1.
Genevestigator	P05114.
GermOnline	ENSG00000205581. Homo sapiens.
Family and domain databases
InterPro	IPR000079. HMGN_fam. [Graphical view]
PANTHER	PTHR23087. PTHR23087. 1 hit.
Pfam	PF01101. HMG14_17. 1 hit. [Graphical view]
PRINTS	PR00925. NONHISHMG17.
SMART	SM00527. HMG17. 1 hit. [Graphical view]
PROSITE	PS00355. HMG14_17. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HMGN1. human.
GenomeRNAi	3150.
NextBio	12484.
SOURCE	Search...

Entry information

Entry name

HMGN1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.