ID   NPM_CHICK               Reviewed;         294 AA.
AC   P16039;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Nucleophosmin;
DE            Short=NPM;
DE   AltName: Full=Nucleolar phosphoprotein B23;
DE   AltName: Full=Nucleolar protein NO38;
DE   AltName: Full=Numatrin;
GN   Name=NPM1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2320420; DOI=10.1093/nar/18.5.1286;
RA   Maridor G., Nigg E.A.;
RT   "cDNA sequences of chicken nucleolin/C23 and NO38/B23, two major nucleolar
RT   proteins.";
RL   Nucleic Acids Res. 18:1286-1286(1990).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=2114180; DOI=10.1016/0167-4781(90)90032-w;
RA   Maridor G., Krek W., Nigg E.A.;
RT   "Structure and developmental expression of chicken nucleolin and NO38:
RT   coordinate expression of two abundant non-ribosomal nucleolar proteins.";
RL   Biochim. Biophys. Acta 1049:126-133(1990).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2914325; DOI=10.1016/0092-8674(89)90241-9;
RA   Borer R.A., Lehner C.F., Eppenberger H.M., Nigg E.A.;
RT   "Major nucleolar proteins shuttle between nucleus and cytoplasm.";
RL   Cell 56:379-390(1989).
CC   -!- FUNCTION: Acts as a chaperonin for the core histones H3, H2B and H4.
CC       Associated with nucleolar ribonucleoprotein structures and bind single-
CC       stranded nucleic acids. It may function in the assembly and/or
CC       transport of ribosome. May stimulate endonuclease activity on
CC       apurinic/apyrimidinic (AP) double-stranded DNA. May inhibit
CC       endonuclease activity on AP single-stranded RNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC       to-head fashion. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC       {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Generally
CC       nucleolar, but is translocated to the nucleoplasm in case of serum
CC       starvation or treatment with anticancer drugs. {ECO:0000250}.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR   EMBL; X17200; CAA35061.1; -; mRNA.
DR   PIR; S08415; DNCHFM.
DR   RefSeq; NP_990598.1; NM_205267.1.
DR   AlphaFoldDB; P16039; -.
DR   SMR; P16039; -.
DR   BioGRID; 676463; 2.
DR   STRING; 9031.ENSGALP00000058806; -.
DR   PaxDb; 9031-ENSGALP00000003431; -.
DR   GeneID; 396203; -.
DR   KEGG; gga:396203; -.
DR   CTD; 4869; -.
DR   VEuPathDB; HostDB:geneid_396203; -.
DR   eggNOG; KOG0488; Eukaryota.
DR   InParanoid; P16039; -.
DR   PhylomeDB; P16039; -.
DR   PRO; PR:P16039; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IBA:GO_Central.
DR   GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0006407; P:rRNA export from nucleus; IBA:GO_Central.
DR   Gene3D; 1.10.10.2100; -; 1.
DR   Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1.
DR   InterPro; IPR032569; NPM1_C.
DR   InterPro; IPR004301; Nucleoplasmin.
DR   InterPro; IPR024057; Nucleoplasmin_core_dom.
DR   InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR   PANTHER; PTHR22747:SF28; NUCLEOPHOSMIN; 1.
DR   PANTHER; PTHR22747; NUCLEOPLASMIN; 1.
DR   Pfam; PF16276; NPM1-C; 1.
DR   Pfam; PF03066; Nucleoplasmin; 1.
DR   SUPFAM; SSF69203; Nucleoplasmin-like core domain; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..294
FT                   /note="Nucleophosmin"
FT                   /id="PRO_0000219484"
FT   REGION          121..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           153..158
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           190..196
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        162..185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57
FT                   /note="Interaction between pentamers"
FT                   /evidence="ECO:0000250"
FT   SITE            82
FT                   /note="Interaction between pentamers"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  32632 MW;  B1FF89B5F2322DED CRC64;
     MEDSAMDMES MGPLRPQTFL FGCELKAEKE YQFKVDDEEN EHQLSLRTVT LGAGAKDELH
     VVEAEALDYE GNPTKVVLAS LKMSVQPTVS LGGFEITPPF VLRLKCGSGP VYVSGQHLVA
     LEEEPESEDE EEDTKIGNAS TKRPASGGGA KTPQKKPKLS EDDEDDDEDE DDDEDDEDDL
     DDDEEEIKTP MKKPAREPAG KNMQKAKQNG KDSKPSTPAS KTKTPDSKKD KSLTPKTPKV
     PLSLEEIKAK MQASVDKGCS LPKLEPKFAN YVKNCFRTED QKVIQALWQW RQTL
//