ID   HMGN2_CANLF             Reviewed;          90 AA.
AC   Q711A6;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
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; ORFNames=V2.22;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Thyroid;
RX   PubMed=10964405; DOI=10.1006/abio.2000.4674;
RA   Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D.;
RT   "A method for the large-scale cloning of nuclear proteins and nuclear
RT   targeting sequences on a functional basis.";
RL   Anal. Biochem. 284:231-239(2000).
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:0000269|PubMed:10964405}. Cytoplasm
CC       {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation.
CC       {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; AJ388518; CAB46820.1; -; mRNA.
DR   RefSeq; NP_001003101.1; NM_001003101.2.
DR   AlphaFoldDB; Q711A6; -.
DR   STRING; 9612.ENSCAFP00000030733; -.
DR   PaxDb; Q711A6; -.
DR   Ensembl; ENSCAFT00030026301; ENSCAFP00030022963; ENSCAFG00030014201.
DR   Ensembl; ENSCAFT00040007618; ENSCAFP00040006647; ENSCAFG00040003963.
DR   GeneID; 403686; -.
DR   KEGG; cfa:403686; -.
DR   CTD; 3151; -.
DR   eggNOG; ENOG502S5FK; Eukaryota.
DR   HOGENOM; CLU_141985_0_2_1; -.
DR   InParanoid; Q711A6; -.
DR   OMA; SARLSAX; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Bgee; ENSCAFG00000028705; Expressed in thymus and 46 other tissues.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acetylation; ADP-ribosylation; Cytoplasm; DNA-binding; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..90
FT                   /note="Non-histone chromosomal protein HMG-17"
FT                   /id="PRO_0000206696"
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: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;  9379 MW;  B1C49E43200422C8 CRC64;
     MPKRKAEGDA KGDKAKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE KVPKGKKGKA
     DAGKDGNNPA ENGDAKTDQA QKAEGAGDAK