ID   HMGN2_RAT               Reviewed;          90 AA.
AC   P18437;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 106.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-90.
RX   PubMed=2169420; DOI=10.1111/j.1432-1033.1990.tb19198.x;
RA   Nielsen E., Welinder B., Madsen O.D.;
RT   "Protein HMG-17 is hyper-expressed in rat glucagonoma. Single-step
RT   isolation and sequencing.";
RL   Eur. J. Biochem. 192:81-86(1990).
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   PIR; S11349; S11349.
DR   AlphaFoldDB; P18437; -.
DR   STRING; 10116.ENSRNOP00000064333; -.
DR   iPTMnet; P18437; -.
DR   PhosphoSitePlus; P18437; -.
DR   PaxDb; P18437; -.
DR   PRIDE; P18437; -.
DR   UCSC; RGD:620649; rat.
DR   RGD; 620649; Hmgn2.
DR   eggNOG; ENOG502S5FK; Eukaryota.
DR   InParanoid; P18437; -.
DR   PRO; PR:P18437; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005694; C:chromosome; TAS:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
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:RGD.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0031640; P:killing of cells of another organism; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0040034; P:regulation of development, heterochronic; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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:2169420"
FT   CHAIN           2..90
FT                   /note="Non-histone chromosomal protein HMG-17"
FT                   /id="PRO_0000206701"
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   COMPBIAS        54..90
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:0000250|UniProtKB:P05204"
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;  9366 MW;  47F1F07B4002937E CRC64;
     MPKRNAEGDA KGDKAKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE KVPKGKKGKA
     DAGKDANNPA EDGDAKTDQA QKADGAGDAK