HMGN2_BOVIN
ID HMGN2_BOVIN Reviewed; 90 AA.
AC P02313; A5PJU3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, 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=HMG17;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-40.
RX PubMed=793593; DOI=10.1016/0006-291x(76)90498-8;
RA Walker J.M., Hastings J.R.B., Johns E.W., Gaastra W.;
RT "The partial amino acid sequence of a non-histone chromosomal protein.";
RL Biochem. Biophys. Res. Commun. 73:72-78(1976).
RN [3]
RP PROTEIN SEQUENCE OF 29-90.
RX PubMed=330164; DOI=10.1111/j.1432-1033.1977.tb11616.x;
RA Walker J.M., Hastings J.R.B., Johns E.W.;
RT "The primary structure of a non-histone chromosomal protein.";
RL Eur. J. Biochem. 76:461-468(1977).
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 EMBL; BC142241; AAI42242.1; -; mRNA.
DR PIR; A90200; NSBOH7.
DR RefSeq; NP_001092415.1; NM_001098945.1.
DR AlphaFoldDB; P02313; -.
DR STRING; 9913.ENSBTAP00000048748; -.
DR iPTMnet; P02313; -.
DR PaxDb; P02313; -.
DR PeptideAtlas; P02313; -.
DR PRIDE; P02313; -.
DR GeneID; 512161; -.
DR KEGG; bta:512161; -.
DR CTD; 3151; -.
DR eggNOG; ENOG502S5FK; Eukaryota.
DR InParanoid; P02313; -.
DR Proteomes; UP000009136; Unplaced.
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:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR DisProt; DP00195; -.
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:793593"
FT CHAIN 2..90
FT /note="Non-histone chromosomal protein HMG-17"
FT /id="PRO_0000206695"
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"
FT VARIANT 4
FT /note="R -> A"
FT VARIANT 4
FT /note="R -> V"
FT CONFLICT 11
FT /note="E -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9380 MW; 4B64344980A422C5 CRC64;
MPKRKAEGDA EGDKAKVKDE PQRRSARLSA KPAPPKPEPK PKKAPAKKGE KVPKGKKGKA
DAGKDGNNPA ENGDAKTDQA QKAEGAGDAK
