NPM_BOVIN
ID NPM_BOVIN Reviewed; 294 AA.
AC Q3T160;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nucleophosmin;
DE Short=NPM;
GN Name=NPM1;
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.
CC -!- FUNCTION: Involved in diverse cellular processes such as ribosome
CC biogenesis, centrosome duplication, protein chaperoning, histone
CC assembly, cell proliferation, and regulation of tumor suppressors
CC p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear
CC export. Associated with nucleolar ribonucleoprotein structures and bind
CC single-stranded nucleic acids. Acts as a chaperonin for the core
CC histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on
CC apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1
CC endonuclease activity on AP single-stranded RNA. May exert a control of
CC APEX1 endonuclease activity within nucleoli devoted to repair AP on
CC rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2,
CC regulates centrosome duplication. Regulates centriole duplication:
CC phosphorylation by PLK2 is able to trigger centriole replication.
CC Negatively regulates the activation of EIF2AK2/PKR and suppresses
CC apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
CC Antagonizes the inhibitory effect of ATF5 on cell proliferation and
CC relieves ATF5-induced G2/M blockade. In complex with MYC enhances the
CC transcription of MYC target genes (By similarity). May act as
CC chaperonin or cotransporter in the nucleolar localization of
CC transcription termination factor TTF1 (By similarity).
CC {ECO:0000250|UniProtKB:P06748, ECO:0000250|UniProtKB:Q61937}.
CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC to-head fashion (By similarity). Disulfide-linked dimers under certain
CC conditions (By similarity). The SWAP complex consists of NPM1, NCL,
CC PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3.
CC Interacts with the methylated form of RPS10. Interacts (via N-terminal
CC domain) with APEX1; the interaction is RNA-dependent and decreases in
CC hydrogen peroxide-damaged cells. Interacts with NEK2. Interacts with
CC ROCK2 and BRCA2. Interacts with RPGR. Interacts with CENPW. Interacts
CC with EIF2AK2/PKR. Interacts with CEBPA. Interacts with DDX31; this
CC interaction prevents interaction between NPM1 and HDM2. Interacts with
CC MYC; competitive with NOP53. Interacts with NOP53; the interaction is
CC direct and competitive with MYC (By similarity). Interacts with LRRC34
CC (By similarity). Interacts with RRP1B. Interacts with NPM3. Interacts
CC with ALKBH2 (By similarity). Interacts with TTF1 (via C-terminal
CC region) (By similarity). {ECO:0000250|UniProtKB:P06748,
CC ECO:0000250|UniProtKB:Q61937}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P06748}.
CC Note=Generally nucleolar, but is translocated to the nucleoplasm in
CC case of serum starvation or treatment with anticancer drugs. Can
CC shuttle between cytoplasm and nucleus. Co-localizes with the methylated
CC form of RPS10 in the granular component (GC) region of the nucleolus.
CC Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for
CC its localization to the centrosome during mitosis.
CC {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
CC affinity to histones. {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: ADP-ribosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4
CC by PLK2 in S phase is required for centriole duplication and is
CC sufficient to trigger centriole replication. Phosphorylation at Ser-4
CC by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125
CC and Thr-200. Phosphorylation at Thr-200 may trigger initiation of
CC centrosome duplication. Phosphorylated by CDK1 at Thr-200, Thr-219,
CC Thr-234 and Thr-237 during cell mitosis. When these four sites are
CC phosphorated, RNA-binding activity seem to be abolished. May be
CC phosphorylated at Ser-70 by NEK2. The Thr-200 phosphorylated form has
CC higher affinity for ROCK2 (By similarity).
CC {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}.
CC -!- PTM: May be ubiquitinated. Ubiquitination leads to proteasomal
CC degradation. Deubiquitinated by USP36 (By similarity).
CC {ECO:0000250|UniProtKB:P06748}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; BC102099; AAI02100.1; -; mRNA.
DR RefSeq; NP_001030518.1; NM_001035441.2.
DR AlphaFoldDB; Q3T160; -.
DR BMRB; Q3T160; -.
DR SMR; Q3T160; -.
DR PaxDb; Q3T160; -.
DR PeptideAtlas; Q3T160; -.
DR PRIDE; Q3T160; -.
DR GeneID; 614028; -.
DR KEGG; bta:614028; -.
DR CTD; 4869; -.
DR eggNOG; KOG0488; Eukaryota.
DR InParanoid; Q3T160; -.
DR OrthoDB; 1485080at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IBA:GO_Central.
DR GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB.
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 Acetylation; ADP-ribosylation; Chaperone; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..294
FT /note="Nucleophosmin"
FT /id="PRO_0000253598"
FT REGION 1..187
FT /note="Required for interaction with SENP3"
FT /evidence="ECO:0000250"
FT REGION 1..117
FT /note="Necessary for interaction with APEX1"
FT /evidence="ECO:0000250"
FT REGION 121..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..294
FT /note="Required for nucleolar localization"
FT /evidence="ECO:0000250"
FT MOTIF 152..157
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 192..198
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 162..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 55
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT SITE 80
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 4
FT /note="Phosphoserine; by PLK1 and PLK2"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61937"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 125
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 150
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 200
FT /note="Phosphothreonine; by CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 208
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 219
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 257
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 267
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 267
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61937"
FT MOD_RES 273
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06748"
SQ SEQUENCE 294 AA; 32703 MW; 644EBD839DDF160A CRC64;
MEDSMDMDMS PLRPQNYLFG CELKADRDYH FKVDNDENEH QLSLRTVSLG AGAKDELHVV
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
EDAESEEEEE EEVKLLSISG KRSAPGSGSK VPQKKVKLAA DEDEDDDDDD DDDDDEDDDD
DDFDEEVEEK APVKKSVRDT PAKNAQKSNQ NGKDSKPSTP RSKGQESFKK QEKTPKTPRG
PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL
