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   24-JAN-2024, entry version 202.
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, Salivary
RC   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; 177.
DR   IntAct; P05204; 99.
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; 9606-ENSP00000355228; -.
DR   PeptideAtlas; P05204; -.
DR   ProteomicsDB; 51825; -.
DR   Pumba; P05204; -.
DR   TopDownProteomics; P05204; -.
DR   Antibodypedia; 30645; 331 antibodies from 34 providers.
DR   DNASU; 3151; -.
DR   Ensembl; ENST00000361427.6; ENSP00000355228.5; ENSG00000198830.12.
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   AGR; HGNC:4986; -.
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; 381 hits in 1164 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 104 other cell types or tissues.
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   InterPro; IPR000079; HMGN_fam.
DR   PANTHER; PTHR23087:SF13; NON-HISTONE CHROMOSOMAL PROTEIN HMG-17; 1.
DR   PANTHER; PTHR23087; NONHISTONE CHROMOSOMAL PROTEIN HMG; 1.
DR   Pfam; PF01101; HMG14_17; 1.
DR   PRINTS; PR00925; NONHISHMG17.
DR   SMART; SM00527; HMG17; 1.
DR   PROSITE; PS00355; HMG14_17; 1.
DR   Genevisible; P05204; HS.
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
//