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Q9DCB1 (HMGN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High mobility group nucleosome-binding domain-containing protein 3
Gene names
Name:Hmgn3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with the ligand binding domain of the thyroid receptor (TR) (in vitro). Requires the presence of thyroid hormone for its interaction. Interacts with nucleosomes By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in the brain, eye, prostate, thyroid, kidney, testis, glial cells and insulin-producing cells of the Langerhans pancreatic islets. In the brain, expressed in the lateral olfactory tract, anterior commissure, corpus callosum, internal capsule, fornix, stria medullans, optic tract, axon bundles, Purkinje cell layer and granular layer of the cerebellum. In retina, expressed in the nuclei of cells in the inner nuclear layer including amacrine, bipolar and horizontal neurons and in the nuclei of ganglion neurons. Detected at low levels in the liver. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Developmental stage

Transiently expressed in the stroma and endothelium of the cornea at birth. Subsequently expressed in the corneal epithelium and the inner nuclear and ganglion cell layers of the retina. The predominant form in developing ocular tissues is isoform 2, although isoform 1 is also detectable. Ref.6

Disruption phenotype

Mice are viable and fertile. Mice have a mild diabetic phenotype and lower plasma glucagon levels. The overall shape of the islets, the location of the alpha cells in the mantle of the pancreatic islets or proliferation of pancreatic alpha cells are not affected. Ref.7 Ref.8

Sequence similarities

Belongs to the HMGN family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9DCB1-1)

Also known as: HMGN3a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9DCB1-2)

Also known as: HMGN3b;

The sequence of this isoform differs from the canonical sequence as follows:
     76-77: AP → EN
     78-99: Missing.
Isoform 3 (identifier: Q9DCB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     88-95: AQRTESIE → VLSTNTSH
     96-99: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9999High mobility group nucleosome-binding domain-containing protein 3
PRO_0000232575

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue101Phosphothreonine By similarity
Modified residue781Phosphoserine By similarity
Modified residue931Phosphoserine By similarity

Natural variations

Alternative sequence76 – 772AP → EN in isoform 2.
VSP_017909
Alternative sequence78 – 9922Missing in isoform 2.
VSP_017910
Alternative sequence88 – 958AQRTESIE → VLSTNTSH in isoform 3.
VSP_017911
Alternative sequence96 – 994Missing in isoform 3.
VSP_017912

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HMGN3a) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: DE0277EFBE8232CF

FASTA9910,769
        10         20         30         40         50         60 
MPKRKSPENT EGKDGTKLTK QEPTRRSARL SAKPVPPKPE SKPRKTSAKK EPGTKISRGA 

        70         80         90 
KGKKEEKQEA GEEGTAPSAN GDTKVEEAQR TESIEKEGE 

« Hide

Isoform 2 (HMGN3b) [UniParc].

Checksum: B7340DA18071905B
Show »

FASTA778,455
Isoform 3 [UniParc].

Checksum: 5F67D6D091D77319
Show »

FASTA9510,250

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow and Brain.
[2]"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] (ISOFORM 3).
Strain: FVB/N.
Tissue: Mammary gland.
[3]"HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression pattern, expand the cellular repertoire of nucleosome-binding proteins."
West K.L., Ito Y., Birger Y., Postnikov Y., Shirakawa H., Bustin M.
J. Biol. Chem. 276:25959-25969(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[4]"Immunohistochemical localization of the nucleosome-binding protein HMGN3 in mouse brain."
Ito Y., Bustin M.
J. Histochem. Cytochem. 50:1273-1275(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]"Chromosomal proteins HMGN3a and HMGN3b regulate the expression of glycine transporter 1."
West K.L., Castellini M.A., Duncan M.K., Bustin M.
Mol. Cell. Biol. 24:3747-3756(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"Differential expression of the HMGN family of chromatin proteins during ocular development."
Lucey M.M., Wang Y., Bustin M., Duncan M.K.
Gene Expr. Patterns 8:433-437(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"The nucleosome binding protein HMGN3 modulates the transcription profile of pancreatic beta cells and affects insulin secretion."
Ueda T., Furusawa T., Kurahashi T., Tessarollo L., Bustin M.
Mol. Cell. Biol. 29:5264-5276(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[8]"The nucleosome binding protein HMGN3 is expressed in pancreatic alpha-cells and affects plasma glucagon levels in mice."
Kurahashi T., Furusawa T., Ueda T., Bustin M.
J. Cell. Biochem. 109:49-57(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002970 mRNA. Translation: BAB22485.1.
AK153223 mRNA. Translation: BAE31816.1.
BC005693 mRNA. Translation: AAH05693.1.
BK000004 mRNA. Translation: DAA00393.1.
BK000005 mRNA. Translation: DAA00394.1.
CCDSCCDS52872.1. [Q9DCB1-1]
CCDS52873.1. [Q9DCB1-2]
RefSeqNP_080398.1. NM_026122.4. [Q9DCB1-1]
NP_778249.1. NM_175074.2. [Q9DCB1-2]
UniGeneMm.244426.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCB1. 1 interaction.
MINTMINT-4128604.

PTM databases

PhosphoSiteQ9DCB1.

Proteomic databases

MaxQBQ9DCB1.
PaxDbQ9DCB1.
PRIDEQ9DCB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000161796; ENSMUSP00000125616; ENSMUSG00000066456. [Q9DCB1-2]
ENSMUST00000162246; ENSMUSP00000124278; ENSMUSG00000066456. [Q9DCB1-1]
GeneID94353.
KEGGmmu:94353.
UCSCuc009qwc.3. mouse. [Q9DCB1-3]
uc009qwd.2. mouse. [Q9DCB1-2]
uc009qwe.2. mouse. [Q9DCB1-1]

Organism-specific databases

CTD9324.
MGIMGI:2138069. Hmgn3.

Phylogenomic databases

eggNOGNOG70460.
GeneTreeENSGT00730000111287.
HOGENOMHOG000116395.
HOVERGENHBG073479.
InParanoidQ9DCB1.
KOK11301.
OMALTKQEPT.
OrthoDBEOG7HXCTV.
PhylomeDBQ9DCB1.

Gene expression databases

BgeeQ9DCB1.
CleanExMM_HMGN3.
GenevestigatorQ9DCB1.

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

NextBio352321.
PROQ9DCB1.
SOURCESearch...

Entry information

Entry nameHMGN3_MOUSE
AccessionPrimary (citable) accession number: Q9DCB1
Secondary accession number(s): Q7M737, Q99JU1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot