HMGN5_MOUSE
ID HMGN5_MOUSE Reviewed; 406 AA.
AC Q9JL35; O88832; Q3V272; Q8VC71; Q9CUW1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=High mobility group nucleosome-binding domain-containing protein 5;
DE AltName: Full=Nucleosome-binding protein 1;
DE AltName: Full=Nucleosome-binding protein 45;
DE Short=NBP-45;
DE AltName: Full=Protein GARP45;
GN Name=Hmgn5; Synonyms=Garp45, Nsbp1;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10692437; DOI=10.1074/jbc.275.9.6368;
RA Shirakawa H., Landsman D., Postnikov Y.V., Bustin M.;
RT "NBP-45, a novel nucleosomal binding protein with a tissue-specific and
RT developmentally regulated expression.";
RL J. Biol. Chem. 275:6368-6374(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Onoda G., Suzuki N., Saito H., Honda T., Sato H., Kuwano R.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Limb;
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=19160411; DOI=10.1002/jcb.22046;
RA Shirakawa H., Rochman M., Furusawa T., Kuehn M.R., Horigome S., Haketa K.,
RA Sugita Y., Inada T., Komai M., Bustin M.;
RT "The nucleosomal binding protein NSBP1 is highly expressed in the placenta
RT and modulates the expression of differentiation markers in placental Rcho-1
RT cells.";
RL J. Cell. Biochem. 106:651-658(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS
RP OF SER-18 AND SER-22.
RX PubMed=19748358; DOI=10.1016/j.molcel.2009.07.002;
RA Rochman M., Postnikov Y., Correll S., Malicet C., Wincovitch S.,
RA Karpova T.S., McNally J.G., Wu X., Bubunenko N.A., Grigoryev S., Bustin M.;
RT "The interaction of NSBP1/HMGN5 with nucleosomes in euchromatin counteracts
RT linker histone-mediated chromatin compaction and modulates transcription.";
RL Mol. Cell 35:642-656(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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).
CC -!- FUNCTION: Preferentially binds to euchromatin and modulates cellular
CC transcription by counteracting linker histone-mediated chromatin
CC compaction. {ECO:0000269|PubMed:10692437, ECO:0000269|PubMed:19748358}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10692437,
CC ECO:0000269|PubMed:19748358}. Note=Associates with nucleosomes in
CC euchromatin and is largely excluded from constitutive heterochromatin.
CC -!- TISSUE SPECIFICITY: Expressed in liver, spleen, lung, heart, kidney,
CC muscle and brain (at protein level). Widely expressed with highest
CC levels in submaxillary gland, thymus, kidney and liver and lowest
CC levels in brain, lung, pancreas and eye. {ECO:0000269|PubMed:10692437,
CC ECO:0000269|PubMed:19748358}.
CC -!- DEVELOPMENTAL STAGE: At 7.5 dpc, expression is detected in the
CC ectoplacental cone but not in embryonic tissues. By 9.5 dpc and 12.5
CC dpc, strongly expressed in the giant trophoblast, spongiotrophoblast
CC and decidual cells of the placenta (at protein level). At 9.5 dpc and
CC 11.5 dpc, weakly expressed in the developing embryo.
CC {ECO:0000269|PubMed:19160411}.
CC -!- DOMAIN: Specifically targeted by its C-terminus to nucleosomes in
CC euchromatin. {ECO:0000269|PubMed:19748358}.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF213454; AAF30179.1; -; mRNA.
DR EMBL; AB018374; BAA33783.2; -; mRNA.
DR EMBL; AK013748; BAB28982.2; -; mRNA.
DR EMBL; AK131996; BAE20926.1; -; mRNA.
DR EMBL; AL954348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021626; AAH21626.1; -; mRNA.
DR EMBL; BC083087; AAH83087.1; -; mRNA.
DR CCDS; CCDS41101.1; -.
DR RefSeq; NP_057919.2; NM_016710.2.
DR AlphaFoldDB; Q9JL35; -.
DR BioGRID; 206145; 3.
DR STRING; 10090.ENSMUSP00000033597; -.
DR iPTMnet; Q9JL35; -.
DR PhosphoSitePlus; Q9JL35; -.
DR CPTAC; non-CPTAC-4040; -.
DR EPD; Q9JL35; -.
DR jPOST; Q9JL35; -.
DR MaxQB; Q9JL35; -.
DR PaxDb; Q9JL35; -.
DR PeptideAtlas; Q9JL35; -.
DR PRIDE; Q9JL35; -.
DR ProteomicsDB; 269577; -.
DR Antibodypedia; 391; 144 antibodies from 25 providers.
DR DNASU; 50887; -.
DR Ensembl; ENSMUST00000033597; ENSMUSP00000033597; ENSMUSG00000031245.
DR GeneID; 50887; -.
DR KEGG; mmu:50887; -.
DR UCSC; uc009ucs.1; mouse.
DR CTD; 79366; -.
DR MGI; MGI:1355295; Hmgn5.
DR VEuPathDB; HostDB:ENSMUSG00000031245; -.
DR eggNOG; ENOG502QQGX; Eukaryota.
DR GeneTree; ENSGT00730000111570; -.
DR HOGENOM; CLU_685059_0_0_1; -.
DR InParanoid; Q9JL35; -.
DR OMA; QDQGATQ; -.
DR OrthoDB; 1581874at2759; -.
DR PhylomeDB; Q9JL35; -.
DR TreeFam; TF105374; -.
DR BioGRID-ORCS; 50887; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Hmgn5; mouse.
DR PRO; PR:Q9JL35; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JL35; protein.
DR Bgee; ENSMUSG00000031245; Expressed in gastrula and 258 other tissues.
DR Genevisible; Q9JL35; MM.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA: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; IMP:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR040164; HMGN5.
DR InterPro; IPR000079; HMGN_fam.
DR PANTHER; PTHR23145; PTHR23145; 2.
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 Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..406
FT /note="High mobility group nucleosome-binding domain-
FT containing protein 5"
FT /id="PRO_0000206718"
FT REGION 1..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT MUTAGEN 18
FT /note="S->E: May abolish association with nucleosomes; when
FT associated with E-22."
FT /evidence="ECO:0000269|PubMed:19748358"
FT MUTAGEN 22
FT /note="S->E: May abolish association with nucleosomes; when
FT associated with E-18."
FT /evidence="ECO:0000269|PubMed:19748358"
FT CONFLICT 74
FT /note="M -> V (in Ref. 1; AAF30179)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="N -> H (in Ref. 2; BAA33783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 45344 MW; 59A4305613EC9679 CRC64;
MPKRKAAGDV SQEPKRRSAR LSAMPVPFTP ELKPKRASTS RKTKTTNVVE ENKDASTIPI
PETKPEDVKD ECNMENAENG EAKIMEAPIP KMEAEEVKEQ INEDTEEDGG EKKEAVAAEA
KDDELKANIQ DVEKDEDGKE HKDTGEEVED GKIEEEGLNE KPGTAKSEDA EVSKDEEEKG
DNEKGEDGKE EGDEKEEEKD DKEGDTGTEK EVKEQNKEAE EDDGKCKEEE NKEVGKEGQP
EEDGKEDLHE EVGKEDLHEE DGKEGQPEED GKEIHHEEDG KEGQPEEDGK EYLHEEDGEE
GQPKEDQKEG QPEEDGKEDQ PEEDGKEGQC KEDGKEGHHE EGGKEDLHEE DGKEKDGGKE
DRKEEGEQEV AVDEGSDENK VEAEEEGAEN KDFKQDGEKE EPLSIV
