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Q61937

- NPM_MOUSE

UniProt

Q61937 - NPM_MOUSE

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Protein

Nucleophosmin

Gene

Npm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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. 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 (By similarity). Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. 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).By similarity

Sites

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. NF-kappaB binding Source: UniProtKB
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
  4. protein kinase inhibitor activity Source: UniProtKB
  5. ribosomal large subunit binding Source: MGI
  6. ribosomal small subunit binding Source: MGI
  7. RNA binding Source: MGI
  8. rRNA binding Source: MGI
  9. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. cell aging Source: UniProtKB
  2. cell growth Source: MGI
  3. cell volume homeostasis Source: MGI
  4. centrosome cycle Source: UniProtKB
  5. DNA repair Source: UniProtKB
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cell proliferation Source: UniProtKB
  8. negative regulation of mRNA splicing, via spliceosome Source: MGI
  9. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  10. nucleocytoplasmic transport Source: MGI
  11. positive regulation of cell proliferation Source: MGI
  12. positive regulation of cellular biosynthetic process Source: MGI
  13. positive regulation of centrosome duplication Source: MGI
  14. positive regulation of DNA replication Source: Ensembl
  15. positive regulation of protein kinase activity Source: MGI
  16. positive regulation of translation Source: UniProtKB
  17. protein homooligomerization Source: Ensembl
  18. protein localization Source: MGI
  19. protein oligomerization Source: MGI
  20. regulation of cell cycle Source: MGI
  21. regulation of centriole replication Source: UniProtKB
  22. regulation of centrosome duplication Source: MGI
  23. regulation of DNA damage response, signal transduction by p53 class mediator Source: MGI
  24. regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
  25. regulation of endodeoxyribonuclease activity Source: UniProtKB
  26. regulation of endoribonuclease activity Source: UniProtKB
  27. regulation of neuron apoptotic process Source: Ensembl
  28. ribosomal large subunit biogenesis Source: MGI
  29. ribosomal large subunit export from nucleus Source: MGI
  30. ribosomal small subunit biogenesis Source: MGI
  31. ribosomal small subunit export from nucleus Source: MGI
  32. rRNA export from nucleus Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
Gene namesi
Name:Npm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:106184. Npm1.

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 (By similarity).By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. granular component Source: MGI
  5. large ribosomal subunit Source: MGI
  6. nuclear speck Source: MGI
  7. nucleolus Source: MGI
  8. nucleoplasm Source: MGI
  9. nucleus Source: UniProtKB
  10. ribonucleoprotein complex Source: MGI
  11. small ribosomal subunit Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292NucleophosminPRO_0000219482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei4 – 41Phosphoserine; by PLK1 and PLK2By similarity
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei32 – 321N6-acetyllysineBy similarity
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei95 – 951PhosphothreonineBy similarity
Modified residuei125 – 1251Phosphoserine5 Publications
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei150 – 1501N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei198 – 1981Phosphothreonine; by CDK1 and CDK2By similarity
Modified residuei211 – 2111N6-acetyllysineBy similarity
Modified residuei217 – 2171Phosphothreonine; by CDK1By similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei227 – 2271N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
Cross-linki228 – 228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei232 – 2321Phosphothreonine; by CDK1By similarity
Modified residuei235 – 2351Phosphothreonine; by CDK1By similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei248 – 2481N6-acetyllysineBy similarity
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei255 – 2551N6-acetyllysineBy similarity
Modified residuei258 – 2581PhosphoserineBy similarity
Cross-linki261 – 261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei271 – 2711N6-acetyllysineBy similarity
Modified residuei277 – 2771PhosphothreonineBy similarity
Modified residuei290 – 2901N6-acetyllysineBy 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-198. Phosphorylation at Thr-198 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-198, Thr-217, Thr-232 and Thr-235 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-198 phosphorylated form has higher affinity for ROCK2 (By similarity).By similarity
Sumoylated by ARF.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiQ61937.
PaxDbiQ61937.
PRIDEiQ61937.

PTM databases

PhosphoSiteiQ61937.

Expressioni

Tissue specificityi

Expressed in B-cells that have been induced to switch to various Ig isotypes.1 Publication

Gene expression databases

BgeeiQ61937.
CleanExiMM_NPM1.
ExpressionAtlasiQ61937. baseline.
GenevestigatoriQ61937.

Interactioni

Subunit structurei

Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. Interacts with NSUN2 and SENP3 (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2 and BRCA2 (By similarity). Interacts with RPGR. Interacts with CENPW (By similarity). Interacts with EIF2AK2/PKR.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009872EBI-626362,EBI-389668From a different organism.

Protein-protein interaction databases

BioGridi201823. 47 interactions.
IntActiQ61937. 10 interactions.
MINTiMINT-270928.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 2410
Beta strandi29 – 313
Helixi37 – 393
Beta strandi40 – 4910
Beta strandi58 – 658
Beta strandi69 – 8012
Turni81 – 833
Beta strandi84 – 9411
Beta strandi96 – 1049
Beta strandi109 – 1179

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N8MX-ray1.80A/B/C/D/E1-130[»]
ProteinModelPortaliQ61937.
SMRiQ61937. Positions 13-120, 223-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 185185Required for interaction with SENP3By similarityAdd
BLAST
Regioni1 – 117117Necessary for interaction with APEX1By similarityAdd
BLAST
Regioni241 – 29252Required for nucleolar localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi152 – 1576Nuclear localization signalSequence Analysis
Motifi190 – 1967Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 99Met-rich
Compositional biasi120 – 13213Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi158 – 18730Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiNOG79897.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiQ61937.
KOiK11276.
OMAiNCFRTED.
OrthoDBiEOG79W97G.
PhylomeDBiQ61937.
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.

Q61937-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEDE EDVKLLGMSG KRSAPGGGNK
160 170 180 190 200
VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF DEEETEEKVP VKKSVRDTPA
210 220 230 240 250
KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS SVEDIKAKMQ
260 270 280 290
ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL
Length:292
Mass (Da):32,560
Last modified:November 1, 1996 - v1
Checksum:iE68750C549ED25E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33212 mRNA. Translation: AAA39801.1.
AK028253 mRNA. Translation: BAC25844.1.
BC054755 mRNA. Translation: AAH54755.1.
CCDSiCCDS24532.1.
PIRiI52858.
RefSeqiNP_032748.1. NM_008722.3.
UniGeneiMm.485384.

Genome annotation databases

EnsembliENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
GeneIDi18148.
KEGGimmu:18148.
UCSCiuc007ikd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33212 mRNA. Translation: AAA39801.1 .
AK028253 mRNA. Translation: BAC25844.1 .
BC054755 mRNA. Translation: AAH54755.1 .
CCDSi CCDS24532.1.
PIRi I52858.
RefSeqi NP_032748.1. NM_008722.3.
UniGenei Mm.485384.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4N8M X-ray 1.80 A/B/C/D/E 1-130 [» ]
ProteinModelPortali Q61937.
SMRi Q61937. Positions 13-120, 223-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201823. 47 interactions.
IntActi Q61937. 10 interactions.
MINTi MINT-270928.

Chemistry

ChEMBLi CHEMBL5386.

PTM databases

PhosphoSitei Q61937.

Proteomic databases

MaxQBi Q61937.
PaxDbi Q61937.
PRIDEi Q61937.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075641 ; ENSMUSP00000075067 ; ENSMUSG00000057113 .
GeneIDi 18148.
KEGGi mmu:18148.
UCSCi uc007ikd.2. mouse.

Organism-specific databases

CTDi 4869.
MGIi MGI:106184. Npm1.

Phylogenomic databases

eggNOGi NOG79897.
GeneTreei ENSGT00440000034554.
HOGENOMi HOG000013061.
HOVERGENi HBG001860.
InParanoidi Q61937.
KOi K11276.
OMAi NCFRTED.
OrthoDBi EOG79W97G.
PhylomeDBi Q61937.
TreeFami TF327704.

Enzyme and pathway databases

Reactomei REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

NextBioi 293410.
PROi Q61937.
SOURCEi Search...

Gene expression databases

Bgeei Q61937.
CleanExi MM_NPM1.
ExpressionAtlasi Q61937. baseline.
Genevestigatori Q61937.

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

« Hide 'large scale' publications
  1. "DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli. Correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23."
    Schmidt-Zachmann M.S., Franke W.W.
    Chromosoma 96:417-426(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-45.
    Tissue: Brain.
  5. Cited for: PROTEIN SEQUENCE OF 46-52 AND 266-271, SUBUNIT, TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Spleen.
  6. "Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR."
    Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.
    J. Biol. Chem. 278:41709-41717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF2AK2.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNPM_MOUSE
AccessioniPrimary (citable) accession number: Q61937
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 133 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3