HMGN2_MOUSE
ID HMGN2_MOUSE Reviewed; 90 AA.
AC P09602;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Non-histone chromosomal protein HMG-17;
DE AltName: Full=High mobility group nucleosome-binding domain-containing protein 2;
GN Name=Hmgn2; Synonyms=Hmg-17, Hmg17;
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].
RX PubMed=3194220; DOI=10.1093/nar/16.21.10386;
RA Landsman D., Zavou S., Soares N., Goodwin G.H., Bustin M.;
RT "Mouse non-histone chromosomal protein HMG-17 cDNA sequence.";
RL Nucleic Acids Res. 16:10386-10386(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=3342876; DOI=10.1016/0014-5793(88)80581-7;
RA Vartiainen E., Palvimo J., Mahonen A., Linnala-Kankkunen A.,
RA Maeenpaeae P.H.;
RT "Selective decrease in low-Mr HMG proteins HMG I and HMG Y during
RT differentiation of mouse teratocarcinoma cells.";
RL FEBS Lett. 228:45-48(1988).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering
CC the interaction between the DNA and the histone octamer. May be
CC involved in the process which maintains transcribable genes in a unique
CC chromatin conformation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}.
CC -!- PTM: Phosphorylation favors cytoplasmic localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR EMBL; X12944; CAA31404.1; -; mRNA.
DR EMBL; AK002374; BAB22051.1; -; mRNA.
DR EMBL; AK078413; BAC37262.1; -; mRNA.
DR EMBL; BC084680; AAH84680.1; -; mRNA.
DR CCDS; CCDS18759.1; -.
DR PIR; S01946; S01946.
DR RefSeq; NP_058653.1; NM_016957.3.
DR AlphaFoldDB; P09602; -.
DR BioGRID; 200333; 1.
DR STRING; 10090.ENSMUSP00000075031; -.
DR iPTMnet; P09602; -.
DR PhosphoSitePlus; P09602; -.
DR EPD; P09602; -.
DR PaxDb; P09602; -.
DR PRIDE; P09602; -.
DR ProteomicsDB; 273368; -.
DR DNASU; 15331; -.
DR Ensembl; ENSMUST00000075602; ENSMUSP00000075031; ENSMUSG00000070713.
DR Ensembl; ENSMUST00000102552; ENSMUSP00000099612; ENSMUSG00000003038.
DR Ensembl; ENSMUST00000102553; ENSMUSP00000099613; ENSMUSG00000003038.
DR GeneID; 15331; -.
DR KEGG; mmu:15331; -.
DR UCSC; uc008vdq.1; mouse.
DR CTD; 3151; -.
DR MGI; MGI:96136; Hmgn2.
DR VEuPathDB; HostDB:ENSMUSG00000003038; -.
DR VEuPathDB; HostDB:ENSMUSG00000070713; -.
DR eggNOG; ENOG502S5FK; Eukaryota.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_0_2_1; -.
DR InParanoid; P09602; -.
DR OMA; SARLSAX; -.
DR PhylomeDB; P09602; -.
DR BioGRID-ORCS; 15331; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hmgn2; mouse.
DR PRO; PR:P09602; -.
DR Proteomes; UP000000589; Chromosome 4.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P09602; protein.
DR Bgee; ENSMUSG00000003038; Expressed in embryonic facial prominence and 115 other tissues.
DR ExpressionAtlas; P09602; baseline and differential.
DR Genevisible; P09602; MM.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0040034; P:regulation of development, heterochronic; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR InterPro; IPR000079; HMGN_fam.
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 Acetylation; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3342876"
FT CHAIN 2..90
FT /note="Non-histone chromosomal protein HMG-17"
FT /id="PRO_0000206698"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05204"
FT MOD_RES 29
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05204"
FT MOD_RES 29
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05204"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05204"
SQ SEQUENCE 90 AA; 9423 MW; B614F853310532D9 CRC64;
MPKRKAEGDA KGDKTKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE KVPKGKKGKA
DAGKDANNPA ENGDAKTDQA QKAEGAGDAK
