ID   HMGN1_BOVIN             Reviewed;         101 AA.
AC   P02316; Q3T0D1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Non-histone chromosomal protein HMG-14;
DE   AltName: Full=High mobility group nucleosome-binding domain-containing protein 1;
GN   Name=HMGN1; Synonyms=HMG14;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-101.
RX   PubMed=456580; DOI=10.1016/0014-5793(79)80378-6;
RA   Walker J.M., Goodwin G.H., Johns E.W.;
RT   "The primary structure of the nucleosome-associated chromosomal protein HMG
RT   14.";
RL   FEBS Lett. 100:394-398(1979).
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. Inhibits the phosphorylation of nucleosomal
CC       histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with transcriptional regulator SEHBP.
CC       {ECO:0000250|UniProtKB:P05114}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylation on Ser-21 and Ser-25 weakens binding to
CC       nucleosomes and increases the rate of H3 phosphorylation.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR   EMBL; BC102449; AAI02450.1; -; mRNA.
DR   PIR; A02654; NSBOH4.
DR   RefSeq; NP_001029944.1; NM_001034772.1.
DR   AlphaFoldDB; P02316; -.
DR   STRING; 9913.ENSBTAP00000008696; -.
DR   iPTMnet; P02316; -.
DR   PaxDb; P02316; -.
DR   PeptideAtlas; P02316; -.
DR   PRIDE; P02316; -.
DR   GeneID; 614915; -.
DR   KEGG; bta:614915; -.
DR   CTD; 3150; -.
DR   eggNOG; ENOG502S7UM; Eukaryota.
DR   HOGENOM; CLU_141985_1_0_1; -.
DR   InParanoid; P02316; -.
DR   OrthoDB; 1636546at2759; -.
DR   TreeFam; TF105374; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
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; Direct protein sequencing; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:456580"
FT   CHAIN           2..101
FT                   /note="Non-histone chromosomal protein HMG-14"
FT                   /id="PRO_0000206690"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18608"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         25
FT                   /note="ADP-ribosylserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         25
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18608"
FT   MOD_RES         82
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18608"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05114"
SQ   SEQUENCE   101 AA;  10831 MW;  CAE905527B3B618D CRC64;
     MPKRKVSSAE GAAKEEPKRR SARLSAKPAP AKVETKPKKA AGKDKSSDKK VQTKGKRGAK
     GKQAEVANQE TKEDLPAENG ETKNEESPAS DEAEEKEAKS D