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Protein

Nucleoplasmin-3

Gene

NPM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May act as a chaperone.

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoplasmin-3
Gene namesi
Name:NPM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:7931. NPM3.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31733.

Polymorphism and mutation databases

BioMutaiNPM3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 178177Nucleoplasmin-3PRO_0000219489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine6 Publications
Modified residuei13 – 131Phosphoserine2 Publications
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei158 – 1581Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated.Curated

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75607.
PaxDbiO75607.
PeptideAtlasiO75607.
PRIDEiO75607.

PTM databases

PhosphoSiteiO75607.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO75607.
CleanExiHS_NPM3.
GenevisibleiO75607. HS.

Organism-specific databases

HPAiHPA036295.
HPA036296.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NPM2Q86SE83EBI-721544,EBI-6658150
tatP046082EBI-721544,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi115640. 12 interactions.
IntActiO75607. 4 interactions.
MINTiMINT-1426791.
STRINGi9606.ENSP00000359128.

Structurei

3D structure databases

ProteinModelPortaliO75607.
SMRiO75607. Positions 37-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 109Ala-rich
Compositional biasi145 – 16420Asp/Glu-rich (highly acidic)Add
BLAST
Compositional biasi148 – 1569Poly-Glu

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiNOG87795.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000030911.
HOVERGENiHBG045601.
InParanoidiO75607.
KOiK11278.
OMAiKVPFYTF.
OrthoDBiEOG79W97G.
PhylomeDBiO75607.
TreeFamiTF327704.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGTAAALA FLSQESRTRA GGVGGLRVPA PVTMDSFFFG CELSGHTRSF
60 70 80 90 100
TFKVEEEDDA EHVLALTMLC LTEGAKDECN VVEVVARNHD HQEIAVPVAN
110 120 130 140 150
LKLSCQPMLS LDDFQLQPPV TFRLKSGSGP VRITGRHQIV TMSNDVSEEE
160 170
SEEEEEDSDE EEVELCPILP AKKQGGRP
Length:178
Mass (Da):19,344
Last modified:January 23, 2007 - v3
Checksum:i8C899DE8C3CD61FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 622EH → DD in AAD51496 (Ref. 3) Curated
Sequence conflicti83 – 831E → K in AAD51496 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161S → N.
Corresponds to variant rs34376117 [ dbSNP | Ensembl ].
VAR_050410
Natural varianti80 – 801N → I.1 Publication
Corresponds to variant rs2735420 [ dbSNP | Ensembl ].
VAR_050411

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY049737 mRNA. Translation: AAL12172.1.
AF081280 mRNA. Translation: AAC31609.1.
AF079325 Genomic DNA. Translation: AAD51496.1.
BC041067 mRNA. Translation: AAH41067.1.
BC054868 mRNA. Translation: AAH54868.1.
CCDSiCCDS7519.1.
RefSeqiNP_008924.1. NM_006993.2.
UniGeneiHs.90691.

Genome annotation databases

EnsembliENST00000370110; ENSP00000359128; ENSG00000107833.
GeneIDi10360.
KEGGihsa:10360.
UCSCiuc001ktt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY049737 mRNA. Translation: AAL12172.1.
AF081280 mRNA. Translation: AAC31609.1.
AF079325 Genomic DNA. Translation: AAD51496.1.
BC041067 mRNA. Translation: AAH41067.1.
BC054868 mRNA. Translation: AAH54868.1.
CCDSiCCDS7519.1.
RefSeqiNP_008924.1. NM_006993.2.
UniGeneiHs.90691.

3D structure databases

ProteinModelPortaliO75607.
SMRiO75607. Positions 37-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115640. 12 interactions.
IntActiO75607. 4 interactions.
MINTiMINT-1426791.
STRINGi9606.ENSP00000359128.

PTM databases

PhosphoSiteiO75607.

Polymorphism and mutation databases

BioMutaiNPM3.

Proteomic databases

MaxQBiO75607.
PaxDbiO75607.
PeptideAtlasiO75607.
PRIDEiO75607.

Protocols and materials databases

DNASUi10360.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370110; ENSP00000359128; ENSG00000107833.
GeneIDi10360.
KEGGihsa:10360.
UCSCiuc001ktt.3. human.

Organism-specific databases

CTDi10360.
GeneCardsiGC10M103532.
HGNCiHGNC:7931. NPM3.
HPAiHPA036295.
HPA036296.
MIMi606456. gene.
neXtProtiNX_O75607.
PharmGKBiPA31733.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG87795.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000030911.
HOVERGENiHBG045601.
InParanoidiO75607.
KOiK11278.
OMAiKVPFYTF.
OrthoDBiEOG79W97G.
PhylomeDBiO75607.
TreeFamiTF327704.

Miscellaneous databases

GeneWikiiNPM3.
GenomeRNAii10360.
NextBioi39273.
PROiO75607.
SOURCEiSearch...

Gene expression databases

BgeeiO75607.
CleanExiHS_NPM3.
GenevisibleiO75607. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and nuclear localization of human NPM3, a member of the nucleophosmin/nucleoplasmin family of nuclear chaperones."
    Shackleford G.M., Ganguly A., MacArthur C.A.
    BMC Genomics 2:8-8(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Hu G.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Retinoic acid induces differential expression of FGF8 isoforms in LNCaP cells."
    Brondani V., Albrecht G., Hamy F.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-80.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  5. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-151 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNPM3_HUMAN
AccessioniPrimary (citable) accession number: O75607
Secondary accession number(s): Q9UNY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.