HMGN1_MOUSE
ID HMGN1_MOUSE Reviewed; 96 AA.
AC P18608; Q5HZY9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Non-histone chromosomal protein HMG-14;
DE AltName: Full=High mobility group nucleosome-binding domain-containing protein 1;
GN Name=Hmgn1; Synonyms=Hmg-14, Hmg14;
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].
RC TISSUE=Liver;
RX PubMed=2402471; DOI=10.1093/nar/18.17.5311;
RA Landsman D., Bustin M.;
RT "Mouse non-histone chromosomal protein HMG-14 cDNA sequence.";
RL Nucleic Acids Res. 18:5311-5311(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, 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 [3]
RP PROTEIN SEQUENCE OF 2-19.
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 [4]
RP PHOSPHORYLATION AT SER-7.
RX PubMed=7925294; DOI=10.1002/j.1460-2075.1994.tb06774.x;
RA Barratt M.J., Hazzalin C.A., Zhelev N., Mahadevan L.C.;
RT "A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its
RT basic amino-terminal domain in vivo and on isolated mononucleosomes.";
RL EMBO J. 13:4524-4535(1994).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION AT SER-7; SER-20 AND SER-24.
RX PubMed=15327773; DOI=10.1016/j.molcel.2004.08.006;
RA Lim J.-H., Catez F., Birger Y., West K.L., Prymakowska-Bosak M.,
RA Postnikov Y.V., Bustin M.;
RT "Chromosomal protein HMGN1 modulates histone H3 phosphorylation.";
RL Mol. Cell 15:573-584(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-87 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-80; SER-84; SER-87 AND
RP SER-95, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-26, AND IDENTIFICATION
RP BY MASS 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. Inhibits the phosphorylation of nucleosomal
CC histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.
CC {ECO:0000269|PubMed:15327773}.
CC -!- SUBUNIT: Interacts with transcriptional regulator SEHBP.
CC {ECO:0000250|UniProtKB:P05114}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}.
CC -!- PTM: Phosphorylation favors cytoplasmic localization (By similarity).
CC Phosphorylation on Ser-20 and Ser-24 weakens binding to nucleosomes and
CC increases the rate of H3 phosphorylation. {ECO:0000250,
CC ECO:0000269|PubMed:15327773, ECO:0000269|PubMed:7925294}.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR EMBL; X53476; CAA37569.1; -; mRNA.
DR EMBL; BC083138; AAH83138.1; -; mRNA.
DR EMBL; BC088834; AAH88834.1; -; mRNA.
DR CCDS; CCDS28353.1; -.
DR PIR; S11219; S11219.
DR RefSeq; NP_032277.3; NM_008251.3.
DR AlphaFoldDB; P18608; -.
DR BioGRID; 200332; 2.
DR STRING; 10090.ENSMUSP00000061012; -.
DR iPTMnet; P18608; -.
DR PhosphoSitePlus; P18608; -.
DR EPD; P18608; -.
DR jPOST; P18608; -.
DR MaxQB; P18608; -.
DR PaxDb; P18608; -.
DR PeptideAtlas; P18608; -.
DR PRIDE; P18608; -.
DR ProteomicsDB; 273367; -.
DR TopDownProteomics; P18608; -.
DR Antibodypedia; 23386; 406 antibodies from 36 providers.
DR DNASU; 15312; -.
DR Ensembl; ENSMUST00000050884; ENSMUSP00000061012; ENSMUSG00000040681.
DR GeneID; 15312; -.
DR KEGG; mmu:15312; -.
DR UCSC; uc008aco.1; mouse.
DR CTD; 3150; -.
DR MGI; MGI:96120; Hmgn1.
DR VEuPathDB; HostDB:ENSMUSG00000040681; -.
DR eggNOG; ENOG502S7UM; Eukaryota.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_1_0_1; -.
DR InParanoid; P18608; -.
DR OMA; CHWPEGA; -.
DR OrthoDB; 1636546at2759; -.
DR PhylomeDB; P18608; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR BioGRID-ORCS; 15312; 4 hits in 110 CRISPR screens.
DR ChiTaRS; Hmgn1; mouse.
DR PRO; PR:P18608; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P18608; protein.
DR Bgee; ENSMUSG00000040681; Expressed in retinal neural layer and 142 other tissues.
DR ExpressionAtlas; P18608; baseline and differential.
DR Genevisible; P18608; MM.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001674; C:female germ cell nucleus; IDA: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; IMP:MGI.
DR GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; IMP:MGI.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP:MGI.
DR GO; GO:0040034; P:regulation of development, heterochronic; IGI:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR GO; GO:0010225; P:response to UV-C; IDA:MGI.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; 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; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3342876"
FT CHAIN 2..96
FT /note="Non-histone chromosomal protein HMG-14"
FT /id="PRO_0000206692"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:15327773,
FT ECO:0000269|PubMed:7925294"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 20
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:15327773"
FT MOD_RES 24
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05114"
FT MOD_RES 24
FT /note="Phosphoserine; alternate; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:15327773"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 80
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 96 AA; 10152 MW; 65C4C09DE0973786 CRC64;
MPKRKVSADG AAKAEPKRRS ARLSAKPAPA KVDAKPKKAA GKDKASDKKV QIKGKRGAKG
KQADVADQQT TELPAENGET ENQSPASEEE KEAKSD
