HMGN3_MOUSE
ID HMGN3_MOUSE Reviewed; 99 AA.
AC Q9DCB1; Q7M737; Q99JU1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=High mobility group nucleosome-binding domain-containing protein 3;
GN Name=Hmgn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11356838; DOI=10.1074/jbc.m101692200;
RA West K.L., Ito Y., Birger Y., Postnikov Y., Shirakawa H., Bustin M.;
RT "HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression
RT pattern, expand the cellular repertoire of nucleosome-binding proteins.";
RL J. Biol. Chem. 276:25959-25969(2001).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12185205; DOI=10.1177/002215540205000914;
RA Ito Y., Bustin M.;
RT "Immunohistochemical localization of the nucleosome-binding protein HMGN3
RT in mouse brain.";
RL J. Histochem. Cytochem. 50:1273-1275(2002).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15082770; DOI=10.1128/mcb.24.9.3747-3756.2004;
RA West K.L., Castellini M.A., Duncan M.K., Bustin M.;
RT "Chromosomal proteins HMGN3a and HMGN3b regulate the expression of glycine
RT transporter 1.";
RL Mol. Cell. Biol. 24:3747-3756(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18502697; DOI=10.1016/j.gep.2008.04.002;
RA Lucey M.M., Wang Y., Bustin M., Duncan M.K.;
RT "Differential expression of the HMGN family of chromatin proteins during
RT ocular development.";
RL Gene Expr. Patterns 8:433-437(2008).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19651901; DOI=10.1128/mcb.00526-09;
RA Ueda T., Furusawa T., Kurahashi T., Tessarollo L., Bustin M.;
RT "The nucleosome binding protein HMGN3 modulates the transcription profile
RT of pancreatic beta cells and affects insulin secretion.";
RL Mol. Cell. Biol. 29:5264-5276(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19885867; DOI=10.1002/jcb.22377;
RA Kurahashi T., Furusawa T., Ueda T., Bustin M.;
RT "The nucleosome binding protein HMGN3 is expressed in pancreatic alpha-
RT cells and affects plasma glucagon levels in mice.";
RL J. Cell. Biochem. 109:49-57(2010).
CC -!- FUNCTION: Binds to nucleosomes, regulating chromatin structure and
CC consequently, chromatin-dependent processes such as transcription, DNA
CC replication and DNA repair. Affects both insulin and glucagon levels
CC and modulates the expression of pancreatic genes involved in insulin
CC secretion. Regulates the expression of the glucose transporter SLC2A2
CC by binding specifically to its promoter region and recruiting PDX1 and
CC additional transcription factors. Regulates the expression of SLC6A9, a
CC glycine transporter which regulates the glycine concentration in
CC synaptic junctions in the central nervous system, by binding to its
CC transcription start site. May play a role in ocular development and
CC astrocyte function. {ECO:0000269|PubMed:12185205,
CC ECO:0000269|PubMed:15082770, ECO:0000269|PubMed:18502697,
CC ECO:0000269|PubMed:19651901, ECO:0000269|PubMed:19885867}.
CC -!- SUBUNIT: Interacts with the ligand binding domain of the thyroid
CC receptor (TR) (in vitro). Requires the presence of thyroid hormone for
CC its interaction. Interacts with transcriptional regulator SEHBP.
CC Interacts with nucleosomes. {ECO:0000250|UniProtKB:Q15651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HMGN3a;
CC IsoId=Q9DCB1-1; Sequence=Displayed;
CC Name=2; Synonyms=HMGN3b;
CC IsoId=Q9DCB1-2; Sequence=VSP_017909, VSP_017910;
CC Name=3;
CC IsoId=Q9DCB1-3; Sequence=VSP_017911, VSP_017912;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, eye, prostate, thyroid,
CC kidney, testis, glial cells and insulin-producing cells of the
CC Langerhans pancreatic islets. In the brain, expressed in the lateral
CC olfactory tract, anterior commissure, corpus callosum, internal
CC capsule, fornix, stria medullans, optic tract, axon bundles, Purkinje
CC cell layer and granular layer of the cerebellum. In retina, expressed
CC in the nuclei of cells in the inner nuclear layer including amacrine,
CC bipolar and horizontal neurons and in the nuclei of ganglion neurons.
CC Detected at low levels in the liver. {ECO:0000269|PubMed:11356838,
CC ECO:0000269|PubMed:12185205, ECO:0000269|PubMed:15082770,
CC ECO:0000269|PubMed:18502697, ECO:0000269|PubMed:19651901,
CC ECO:0000269|PubMed:19885867}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed in the stroma and
CC endothelium of the cornea at birth. Subsequently expressed in the
CC corneal epithelium and the inner nuclear and ganglion cell layers of
CC the retina. The predominant form in developing ocular tissues is
CC isoform 2, although isoform 1 is also detectable.
CC {ECO:0000269|PubMed:18502697}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. Mice have a mild
CC diabetic phenotype and lower plasma glucagon levels. The overall shape
CC of the islets, the location of the alpha cells in the mantle of the
CC pancreatic islets or proliferation of pancreatic alpha cells are not
CC affected. {ECO:0000269|PubMed:19651901, ECO:0000269|PubMed:19885867}.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR EMBL; AK002970; BAB22485.1; -; mRNA.
DR EMBL; AK153223; BAE31816.1; -; mRNA.
DR EMBL; BC005693; AAH05693.1; -; mRNA.
DR EMBL; BK000004; DAA00393.1; -; mRNA.
DR EMBL; BK000005; DAA00394.1; -; mRNA.
DR CCDS; CCDS52872.1; -. [Q9DCB1-1]
DR CCDS; CCDS52873.1; -. [Q9DCB1-2]
DR RefSeq; NP_080398.1; NM_026122.4. [Q9DCB1-1]
DR RefSeq; NP_778249.1; NM_175074.2. [Q9DCB1-2]
DR AlphaFoldDB; Q9DCB1; -.
DR BioGRID; 220508; 6.
DR STRING; 10090.ENSMUSP00000124278; -.
DR iPTMnet; Q9DCB1; -.
DR PhosphoSitePlus; Q9DCB1; -.
DR MaxQB; Q9DCB1; -.
DR PaxDb; Q9DCB1; -.
DR PeptideAtlas; Q9DCB1; -.
DR PRIDE; Q9DCB1; -.
DR ProteomicsDB; 273150; -. [Q9DCB1-1]
DR ProteomicsDB; 273151; -. [Q9DCB1-2]
DR ProteomicsDB; 273152; -. [Q9DCB1-3]
DR TopDownProteomics; Q9DCB1-1; -. [Q9DCB1-1]
DR TopDownProteomics; Q9DCB1-2; -. [Q9DCB1-2]
DR Antibodypedia; 3656; 172 antibodies from 24 providers.
DR DNASU; 94353; -.
DR Ensembl; ENSMUST00000161796; ENSMUSP00000125616; ENSMUSG00000066456. [Q9DCB1-2]
DR Ensembl; ENSMUST00000162246; ENSMUSP00000124278; ENSMUSG00000066456. [Q9DCB1-1]
DR Ensembl; ENSMUST00000185315; ENSMUSP00000140356; ENSMUSG00000066456. [Q9DCB1-3]
DR Ensembl; ENSMUST00000190154; ENSMUSP00000140247; ENSMUSG00000066456. [Q9DCB1-3]
DR GeneID; 94353; -.
DR KEGG; mmu:94353; -.
DR UCSC; uc009qwc.3; mouse. [Q9DCB1-3]
DR UCSC; uc009qwd.2; mouse. [Q9DCB1-2]
DR UCSC; uc009qwe.2; mouse. [Q9DCB1-1]
DR CTD; 9324; -.
DR MGI; MGI:2138069; Hmgn3.
DR VEuPathDB; HostDB:ENSMUSG00000066456; -.
DR eggNOG; ENOG502S1R1; Eukaryota.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_2_0_1; -.
DR InParanoid; Q9DCB1; -.
DR OMA; TKAEGIC; -.
DR OrthoDB; 1617797at2759; -.
DR PhylomeDB; Q9DCB1; -.
DR BioGRID-ORCS; 94353; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Hmgn3; mouse.
DR PRO; PR:Q9DCB1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCB1; protein.
DR Bgee; ENSMUSG00000066456; Expressed in lens of camera-type eye and 243 other tissues.
DR ExpressionAtlas; Q9DCB1; baseline and differential.
DR Genevisible; Q9DCB1; MM.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR InterPro; IPR031073; HMGN3.
DR InterPro; IPR000079; HMGN_fam.
DR PANTHER; PTHR23087:SF2; PTHR23087:SF2; 1.
DR Pfam; PF01101; HMG14_17; 1.
DR PRINTS; PR00925; NONHISHMG17.
DR SMART; SM00527; HMG17; 1.
DR PROSITE; PS00355; HMG14_17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..99
FT /note="High mobility group nucleosome-binding domain-
FT containing protein 3"
FT /id="PRO_0000232575"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15651"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15651"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15651"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 76..77
FT /note="AP -> EN (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017909"
FT VAR_SEQ 78..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017910"
FT VAR_SEQ 88..95
FT /note="AQRTESIE -> VLSTNTSH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017911"
FT VAR_SEQ 96..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017912"
SQ SEQUENCE 99 AA; 10769 MW; DE0277EFBE8232CF CRC64;
MPKRKSPENT EGKDGTKLTK QEPTRRSARL SAKPVPPKPE SKPRKTSAKK EPGTKISRGA
KGKKEEKQEA GEEGTAPSAN GDTKVEEAQR TESIEKEGE
