NPM_CHICK
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 03-AUG-2022, entry version 113.
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.ENSGALP00000003431; -.
DR PaxDb; P16039; -.
DR GeneID; 396203; -.
DR KEGG; gga:396203; -.
DR CTD; 4869; -.
DR VEuPathDB; HostDB:geneid_396203; -.
DR eggNOG; KOG0488; Eukaryota.
DR InParanoid; P16039; -.
DR OrthoDB; 1485080at2759; -.
DR PhylomeDB; P16039; -.
DR PRO; PR:P16039; -.
DR Proteomes; UP000000539; Unplaced.
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 InterPro; IPR032569; NPM1_C.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF16276; NPM1-C; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 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
