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Protein

Non-histone chromosomal protein HMG-17

Gene

HMGN2

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 (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-histone chromosomal protein HMG-17
Alternative name(s):
High mobility group nucleosome-binding domain-containing protein 2
Gene namesi
Name:HMGN2
Synonyms:HMG17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4986. HMGN2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Cytoplasmic enrichment upon phosphorylation.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35089.

Polymorphism and mutation databases

BioMutaiHMGN2.
DMDMi123106.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 9089Non-histone chromosomal protein HMG-17PRO_0000206697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei82 – 821N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylation favors cytoplasmic localization.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05204.
PaxDbiP05204.
PRIDEiP05204.

PTM databases

PhosphoSiteiP05204.

Expressioni

Gene expression databases

BgeeiP05204.
CleanExiHS_HMGN2.
GenevisibleiP05204. HS.

Organism-specific databases

HPAiCAB018371.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629931EBI-1758689,EBI-401755

Protein-protein interaction databases

BioGridi109394. 9 interactions.
IntActiP05204. 6 interactions.
MINTiMINT-8201765.
STRINGi9606.ENSP00000355228.

Structurei

3D structure databases

DisProtiDP00039.
ProteinModelPortaliP05204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HMGN family.Curated

Phylogenomic databases

eggNOGiNOG44189.
GeneTreeiENSGT00730000110660.
HOGENOMiHOG000116395.
HOVERGENiHBG073479.
InParanoidiP05204.
KOiK11300.
OMAiDVKASHE.
OrthoDBiEOG7FNCBN.
PhylomeDBiP05204.

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.

P05204-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRKAEGDA KGDKAKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE
60 70 80 90
KVPKGKKGKA DAGKEGNNPA ENGDAKTDQA QKAEGAGDAK
Length:90
Mass (Da):9,393
Last modified:January 23, 2007 - v3
Checksum:iB1C58E52200422C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → N (PubMed:3754870).Curated
Sequence conflicti26 – 272AR → SA AA sequence (PubMed:2040281).Curated

Mass spectrometryi

Molecular mass is 9261.5 Da from positions 2 - 90. Determined by ESI. 1 Publication
Molecular mass is 9341.3±1.9 Da from positions 2 - 90. Determined by ESI. 1 Publication
Molecular mass is 9421.5 Da from positions 2 - 90. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71E → K in variant H17. 1 Publication
VAR_003716

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12623 mRNA. Translation: AAA52678.1.
X13546 Genomic DNA. Translation: CAA31898.1.
CR542122 mRNA. Translation: CAG46919.1.
AL513365 Genomic DNA. Translation: CAI21489.1.
BC000378 mRNA. Translation: AAH00378.1.
BC003050 mRNA. Translation: AAH03050.1.
BC014644 mRNA. Translation: AAH14644.2.
BC032140 mRNA. Translation: AAH32140.2.
BC070297 mRNA. Translation: AAH70297.1.
BC071707 mRNA. Translation: AAH71707.1.
BC072010 mRNA. Translation: AAH72010.1.
BC072011 mRNA. Translation: AAH72011.1.
BC075837 mRNA. Translation: AAH75837.1.
BC081567 mRNA. Translation: AAH81567.1.
BC110390 mRNA. Translation: AAI10391.1.
CCDSiCCDS283.1.
PIRiS03700.
RefSeqiNP_005508.1. NM_005517.3.
UniGeneiHs.181163.

Genome annotation databases

EnsembliENST00000361427; ENSP00000355228; ENSG00000198830.
ENST00000619352; ENSP00000481160; ENSG00000198830.
GeneIDi3151.
KEGGihsa:3151.
UCSCiuc001bmp.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12623 mRNA. Translation: AAA52678.1.
X13546 Genomic DNA. Translation: CAA31898.1.
CR542122 mRNA. Translation: CAG46919.1.
AL513365 Genomic DNA. Translation: CAI21489.1.
BC000378 mRNA. Translation: AAH00378.1.
BC003050 mRNA. Translation: AAH03050.1.
BC014644 mRNA. Translation: AAH14644.2.
BC032140 mRNA. Translation: AAH32140.2.
BC070297 mRNA. Translation: AAH70297.1.
BC071707 mRNA. Translation: AAH71707.1.
BC072010 mRNA. Translation: AAH72010.1.
BC072011 mRNA. Translation: AAH72011.1.
BC075837 mRNA. Translation: AAH75837.1.
BC081567 mRNA. Translation: AAH81567.1.
BC110390 mRNA. Translation: AAI10391.1.
CCDSiCCDS283.1.
PIRiS03700.
RefSeqiNP_005508.1. NM_005517.3.
UniGeneiHs.181163.

3D structure databases

DisProtiDP00039.
ProteinModelPortaliP05204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109394. 9 interactions.
IntActiP05204. 6 interactions.
MINTiMINT-8201765.
STRINGi9606.ENSP00000355228.

PTM databases

PhosphoSiteiP05204.

Polymorphism and mutation databases

BioMutaiHMGN2.
DMDMi123106.

Proteomic databases

MaxQBiP05204.
PaxDbiP05204.
PRIDEiP05204.

Protocols and materials databases

DNASUi3151.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361427; ENSP00000355228; ENSG00000198830.
ENST00000619352; ENSP00000481160; ENSG00000198830.
GeneIDi3151.
KEGGihsa:3151.
UCSCiuc001bmp.4. human.

Organism-specific databases

CTDi3151.
GeneCardsiGC01P026800.
HGNCiHGNC:4986. HMGN2.
HPAiCAB018371.
MIMi163910. gene.
neXtProtiNX_P05204.
PharmGKBiPA35089.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44189.
GeneTreeiENSGT00730000110660.
HOGENOMiHOG000116395.
HOVERGENiHBG073479.
InParanoidiP05204.
KOiK11300.
OMAiDVKASHE.
OrthoDBiEOG7FNCBN.
PhylomeDBiP05204.

Miscellaneous databases

ChiTaRSiHMGN2. human.
GeneWikiiHMGN2.
GenomeRNAii3151.
NextBioi12488.
PROiP05204.
SOURCEiSearch...

Gene expression databases

BgeeiP05204.
CleanExiHS_HMGN2.
GenevisibleiP05204. HS.

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-17. Complete human cDNA sequence and evidence for a multigene family."
    Landsman D., Soares N., Gonzalez F.J., Bustin M.
    J. Biol. Chem. 261:7479-7484(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human non-histone chromosomal protein HMG-17: identification, characterization, chromosome localization and RFLPs of a functional gene from the large multigene family."
    Landsman D., McBride O.W., Bustin M.
    Nucleic Acids Res. 17:2301-2314(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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: Brain, Colon, Eye, Lung, Lymph, Mammary gland, Muscle, Salivary gland and Skin.
  6. "Comparison of multiple forms of the high mobility group I proteins in rodent and human cells. Identification of the human high mobility group I-C protein."
    Giancotti V., Bandiera A., Buratti E., Fusco A., Marzari R., Coles B., Goodwin G.H.
    Eur. J. Biochem. 198:211-216(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-28, VARIANT LYS-7.
    Tissue: Peripheral blood lymphocyte.
  7. "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-25 AND SER-29, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
  8. "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-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHMGN2_HUMAN
AccessioniPrimary (citable) accession number: P05204
Secondary accession number(s): Q0VGD5, Q6FGI5, Q96C64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 148 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 1
    Human chromosome 1: 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.