HMGN2_PIG
ID HMGN2_PIG Reviewed; 90 AA.
AC P80272;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 2-90.
RC TISSUE=Thymus;
RX PubMed=8512325; DOI=10.1006/abbi.1993.1306;
RA Boumba V.A., Tsolas O., Choli-Papadopoulou D., Seferiadis K.;
RT "Isolation by a new method and sequence analysis of chromosomal HMG-17
RT protein from porcine thymus.";
RL Arch. Biochem. Biophys. 303:436-442(1993).
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; S33866; S33866.
DR RefSeq; NP_001231041.1; NM_001244112.1.
DR RefSeq; NP_001231043.1; NM_001244114.1.
DR AlphaFoldDB; P80272; -.
DR STRING; 9823.ENSSSCP00000003858; -.
DR PaxDb; P80272; -.
DR PeptideAtlas; P80272; -.
DR PRIDE; P80272; -.
DR Ensembl; ENSSSCT00070050262; ENSSSCP00070042470; ENSSSCG00070025139.
DR GeneID; 100524500; -.
DR KEGG; ssc:100524500; -.
DR CTD; 3151; -.
DR eggNOG; ENOG502S5FK; Eukaryota.
DR HOGENOM; CLU_141985_0_2_1; -.
DR InParanoid; P80272; -.
DR OMA; SARLSAX; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; P80272; SS.
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 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:8512325"
FT CHAIN 2..90
FT /note="Non-histone chromosomal protein HMG-17"
FT /id="PRO_0000206699"
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
