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Q3T160

- NPM_BOVIN

UniProt

Q3T160 - NPM_BOVIN

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Protein
Nucleophosmin
Gene
NPM1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication By similarity. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei55 – 551Interaction between pentamers By similarity
Sitei80 – 801Interaction between pentamers By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. protein kinase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
  3. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  4. positive regulation of translation Source: UniProtKB
  5. regulation of centriole replication Source: UniProtKB
  6. regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
  7. regulation of endodeoxyribonuclease activity Source: UniProtKB
  8. regulation of endoribonuclease activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Gene namesi
Name:NPM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Nucleusnucleolus. Nucleusnucleoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
Note: Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Colocalizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for its localization to the centrosome during mitosis. Interacts with CENPW By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Nucleophosmin
PRO_0000253598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei4 – 41Phosphoserine; by PLK1 and PLK2 By similarity
Modified residuei10 – 101Phosphoserine By similarity
Modified residuei32 – 321N6-acetyllysine By similarity
Modified residuei70 – 701Phosphoserine By similarity
Modified residuei75 – 751Phosphothreonine By similarity
Modified residuei95 – 951Phosphothreonine By similarity
Modified residuei125 – 1251Phosphoserine; by CDK2 By similarity
Modified residuei137 – 1371Phosphoserine By similarity
Modified residuei139 – 1391Phosphoserine By similarity
Modified residuei150 – 1501N6-acetyllysine By similarity
Modified residuei154 – 1541N6-acetyllysine By similarity
Modified residuei200 – 2001Phosphothreonine; by CDK1 and CDK2 By similarity
Modified residuei213 – 2131N6-acetyllysine By similarity
Modified residuei219 – 2191Phosphothreonine; by CDK1 By similarity
Modified residuei227 – 2271Phosphoserine By similarity
Modified residuei229 – 2291N6-acetyllysine By similarity
Modified residuei230 – 2301N6-acetyllysine; alternate By similarity
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei234 – 2341Phosphothreonine By similarity
Modified residuei237 – 2371Phosphothreonine By similarity
Modified residuei242 – 2421Phosphoserine By similarity
Modified residuei243 – 2431Phosphoserine By similarity
Modified residuei250 – 2501N6-acetyllysine By similarity
Modified residuei254 – 2541Phosphoserine By similarity
Modified residuei257 – 2571N6-acetyllysine By similarity
Modified residuei260 – 2601Phosphoserine By similarity
Cross-linki263 – 263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei267 – 2671N6-acetyllysine By similarity
Modified residuei273 – 2731N6-acetyllysine By similarity
Modified residuei279 – 2791Phosphothreonine By similarity
Modified residuei292 – 2921N6-acetyllysine By similarity

Post-translational modificationi

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones By similarity.
ADP-ribosylated By similarity.
Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-200. Phosphorylation at Thr-200 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-200, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-200 phosphorylated form has higher affinity for ROCK2 By similarity.
Sumoylated by ARF By similarity.

Keywords - PTMi

Acetylation, ADP-ribosylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3T160.
PRIDEiQ3T160.

Interactioni

Subunit structurei

Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with NSUN2 and SENP3. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2 and BRCA2 By similarity. Interacts with RPGR By similarity. Interacts with EIF2AK2/PKR By similarity.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020363.

Structurei

3D structure databases

ProteinModelPortaliQ3T160.
SMRiQ3T160. Positions 15-118, 243-294.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 187187Required for interaction with SENP3 By similarity
Add
BLAST
Regioni1 – 117117Necessary for interaction with APEX1 By similarity
Add
BLAST
Regioni243 – 29452Required for nucleolar localization By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi152 – 1576Nuclear localization signal Reviewed prediction
Motifi192 – 1987Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 99Met-rich
Compositional biasi120 – 13213Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi163 – 18927Asp/Glu-rich (highly acidic)
Add
BLAST

Sequence similaritiesi

Belongs to the nucleoplasmin family.

Phylogenomic databases

eggNOGiNOG79897.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiQ3T160.
KOiK11276.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
SUPFAMiSSF69203. SSF69203. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3T160-1 [UniParc]FASTAAdd to Basket

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MEDSMDMDMS PLRPQNYLFG CELKADRDYH FKVDNDENEH QLSLRTVSLG    50
AGAKDELHVV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL 100
RLKCGSGPVH ISGQHLVAVE EDAESEEEEE EEVKLLSISG KRSAPGSGSK 150
VPQKKVKLAA DEDEDDDDDD DDDDDEDDDD DDFDEEVEEK APVKKSVRDT 200
PAKNAQKSNQ NGKDSKPSTP RSKGQESFKK QEKTPKTPRG PSSVEDIKAK 250
MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL 294
Length:294
Mass (Da):32,703
Last modified:October 11, 2005 - v1
Checksum:i644EBD839DDF160A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102099 mRNA. Translation: AAI02100.1.
RefSeqiNP_001030518.1. NM_001035441.2.
UniGeneiBt.61659.

Genome annotation databases

GeneIDi614028.
KEGGibta:614028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102099 mRNA. Translation: AAI02100.1 .
RefSeqi NP_001030518.1. NM_001035441.2.
UniGenei Bt.61659.

3D structure databases

ProteinModelPortali Q3T160.
SMRi Q3T160. Positions 15-118, 243-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000020363.

Proteomic databases

PaxDbi Q3T160.
PRIDEi Q3T160.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 614028.
KEGGi bta:614028.

Organism-specific databases

CTDi 4869.

Phylogenomic databases

eggNOGi NOG79897.
HOGENOMi HOG000013061.
HOVERGENi HBG001860.
InParanoidi Q3T160.
KOi K11276.

Miscellaneous databases

NextBioi 20898902.

Family and domain databases

Gene3Di 2.60.120.340. 1 hit.
InterProi IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view ]
PANTHERi PTHR22747. PTHR22747. 1 hit.
SUPFAMi SSF69203. SSF69203. 1 hit.
ProtoNeti Search...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiNPM_BOVIN
AccessioniPrimary (citable) accession number: Q3T160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 11, 2005
Last modified: January 22, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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