HMGN2_HUMAN
ID HMGN2_HUMAN Reviewed; 90 AA.
AC P05204; Q0VGD5; Q6FGI5; Q96C64;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
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=HMG17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754870; DOI=10.1016/s0021-9258(17)38417-x;
RA Landsman D., Soares N., Gonzalez F.J., Bustin M.;
RT "Chromosomal protein HMG-17. Complete human cDNA sequence and evidence for
RT a multigene family.";
RL J. Biol. Chem. 261:7479-7484(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2565024; DOI=10.1093/nar/17.6.2301;
RA Landsman D., McBride O.W., Bustin M.;
RT "Human non-histone chromosomal protein HMG-17: identification,
RT characterization, chromosome localization and RFLPs of a functional gene
RT from the large multigene family.";
RL Nucleic Acids Res. 17:2301-2314(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Eye, Lung, Lymph, Mammary gland, Muscle,
RC Salivary gland, and Skin;
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 PROTEIN SEQUENCE OF 2-28, AND VARIANT LYS-7.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=2040281; DOI=10.1111/j.1432-1033.1991.tb16003.x;
RA Giancotti V., Bandiera A., Buratti E., Fusco A., Marzari R., Coles B.,
RA Goodwin G.H.;
RT "Comparison of multiple forms of the high mobility group I proteins in
RT rodent and human cells. Identification of the human high mobility group I-C
RT protein.";
RL Eur. J. Biochem. 198:211-216(1991).
RN [7]
RP PROTEIN SEQUENCE OF 19-31, PHOSPHORYLATION AT SER-25 AND SER-29,
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=10739259; DOI=10.1110/ps.9.1.170;
RA Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G.;
RT "Phosphorylation and subcellular redistribution of high mobility group
RT proteins 14 and 17, analyzed by mass spectrometry.";
RL Protein Sci. 9:170-179(2000).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP ADP-RIBOSYLATION AT SER-29.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
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 -!- INTERACTION:
CC P05204; Q15554: TERF2; NbExp=2; IntAct=EBI-1758689, EBI-706637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10739259}. Cytoplasm
CC {ECO:0000269|PubMed:10739259}. Note=Cytoplasmic enrichment upon
CC phosphorylation.
CC -!- PTM: Phosphorylation favors cytoplasmic localization.
CC {ECO:0000269|PubMed:10739259}.
CC -!- MASS SPECTROMETRY: Mass=9261.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- MASS SPECTROMETRY: Mass=9341.3; Mass_error=1.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- MASS SPECTROMETRY: Mass=9421.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR EMBL; M12623; AAA52678.1; -; mRNA.
DR EMBL; X13546; CAA31898.1; -; Genomic_DNA.
DR EMBL; CR542122; CAG46919.1; -; mRNA.
DR EMBL; AL513365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000378; AAH00378.1; -; mRNA.
DR EMBL; BC003050; AAH03050.1; -; mRNA.
DR EMBL; BC014644; AAH14644.2; -; mRNA.
DR EMBL; BC032140; AAH32140.2; -; mRNA.
DR EMBL; BC070297; AAH70297.1; -; mRNA.
DR EMBL; BC071707; AAH71707.1; -; mRNA.
DR EMBL; BC072010; AAH72010.1; -; mRNA.
DR EMBL; BC072011; AAH72011.1; -; mRNA.
DR EMBL; BC075837; AAH75837.1; -; mRNA.
DR EMBL; BC081567; AAH81567.1; -; mRNA.
DR EMBL; BC110390; AAI10391.1; -; mRNA.
DR CCDS; CCDS283.1; -.
DR PIR; S03700; S03700.
DR RefSeq; NP_005508.1; NM_005517.3.
DR AlphaFoldDB; P05204; -.
DR BioGRID; 109394; 141.
DR IntAct; P05204; 97.
DR MINT; P05204; -.
DR STRING; 9606.ENSP00000355228; -.
DR GlyGen; P05204; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05204; -.
DR PhosphoSitePlus; P05204; -.
DR SwissPalm; P05204; -.
DR BioMuta; HMGN2; -.
DR DMDM; 123106; -.
DR EPD; P05204; -.
DR jPOST; P05204; -.
DR MassIVE; P05204; -.
DR MaxQB; P05204; -.
DR PaxDb; P05204; -.
DR PeptideAtlas; P05204; -.
DR PRIDE; P05204; -.
DR ProteomicsDB; 51825; -.
DR TopDownProteomics; P05204; -.
DR Antibodypedia; 30645; 299 antibodies from 34 providers.
DR DNASU; 3151; -.
DR Ensembl; ENST00000361427.6; ENSP00000355228.5; ENSG00000198830.11.
DR Ensembl; ENST00000619352.4; ENSP00000481160.1; ENSG00000198830.11.
DR GeneID; 3151; -.
DR KEGG; hsa:3151; -.
DR MANE-Select; ENST00000361427.6; ENSP00000355228.5; NM_005517.4; NP_005508.1.
DR UCSC; uc001bmp.5; human.
DR CTD; 3151; -.
DR DisGeNET; 3151; -.
DR GeneCards; HMGN2; -.
DR HGNC; HGNC:4986; HMGN2.
DR HPA; ENSG00000198830; Low tissue specificity.
DR MIM; 163910; gene.
DR neXtProt; NX_P05204; -.
DR OpenTargets; ENSG00000198830; -.
DR PharmGKB; PA35089; -.
DR VEuPathDB; HostDB:ENSG00000198830; -.
DR eggNOG; ENOG502S5FK; Eukaryota.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_0_2_1; -.
DR InParanoid; P05204; -.
DR OMA; SARLSAX; -.
DR PhylomeDB; P05204; -.
DR PathwayCommons; P05204; -.
DR SignaLink; P05204; -.
DR SIGNOR; P05204; -.
DR BioGRID-ORCS; 3151; 375 hits in 1087 CRISPR screens.
DR ChiTaRS; HMGN2; human.
DR GeneWiki; HMGN2; -.
DR GenomeRNAi; 3151; -.
DR Pharos; P05204; Tbio.
DR PRO; PR:P05204; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P05204; protein.
DR Bgee; ENSG00000198830; Expressed in ventricular zone and 102 other tissues.
DR Genevisible; P05204; HS.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IMP:UniProtKB.
DR DisProt; DP00039; -.
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:2040281"
FT CHAIN 2..90
FT /note="Non-histone chromosomal protein HMG-17"
FT /id="PRO_0000206697"
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:0000269|PubMed:10739259"
FT MOD_RES 29
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 29
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000269|PubMed:10739259"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VARIANT 7
FT /note="E -> K (in variant H17)"
FT /evidence="ECO:0000269|PubMed:2040281"
FT /id="VAR_003716"
FT CONFLICT 5
FT /note="K -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="AR -> SA (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9393 MW; B1C58E52200422C8 CRC64;
MPKRKAEGDA KGDKAKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE KVPKGKKGKA
DAGKEGNNPA ENGDAKTDQA QKAEGAGDAK
