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Q61937 (NPM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleophosmin

Short name=NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
Gene names
Name:Npm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.6

Subcellular location

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.

Tissue specificity

Expressed in B-cells that have been induced to switch to various Ig isotypes. Ref.5

Post-translational modification

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.

Sumoylated by ARF By similarity.

Sequence similarities

Belongs to the nucleoplasmin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandDNA-binding
RNA-binding
   Molecular functionChaperone
   PTMAcetylation
ADP-ribosylation
Disulfide bond
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cell growth

Inferred from direct assay PubMed 18809582. Source: MGI

cell volume homeostasis

Inferred from direct assay PubMed 18809582. Source: MGI

centrosome cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay PubMed 16376875. Source: MGI

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

nucleocytoplasmic transport

Inferred from direct assay PubMed 15485902. Source: MGI

positive regulation of cell proliferation

Inferred from direct assay PubMed 18809582. Source: MGI

positive regulation of cellular biosynthetic process

Inferred from direct assay PubMed 18809582. Source: MGI

positive regulation of centrosome duplication

Inferred from genetic interaction PubMed 17015463. Source: MGI

positive regulation of protein kinase activity

Inferred from direct assay PubMed 17015463. Source: MGI

positive regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization

Inferred from mutant phenotype PubMed 16199867. Source: MGI

protein oligomerization

Inferred from sequence orthology PubMed 18809582. Source: MGI

rRNA export from nucleus

Inferred from direct assay PubMed 18809582. Source: MGI

regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from genetic interaction PubMed 16199867. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype PubMed 15485902. Source: MGI

regulation of centriole replication

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centrosome duplication

Inferred from mutant phenotype PubMed 16007073. Source: MGI

regulation of eIF2 alpha phosphorylation by dsRNA

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endodeoxyribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endoribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred from direct assay PubMed 18809582. Source: MGI

ribosomal large subunit export from nucleus

Inferred from mutant phenotype PubMed 18809582. Source: MGI

ribosomal small subunit biogenesis

Inferred from direct assay PubMed 18809582. Source: MGI

ribosomal small subunit export from nucleus

Inferred from direct assay PubMed 18809582. Source: MGI

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 18809582. Source: MGI

granular component

Inferred from direct assay PubMed 15485902. Source: MGI

large ribosomal subunit

Inferred from direct assay PubMed 18809582. Source: MGI

nuclear speck

Inferred from direct assay PubMed 16376875. Source: MGI

nucleolus

Inferred from direct assay PubMed 10716735PubMed 12374805PubMed 15485902PubMed 15596447PubMed 15615785PubMed 15989966PubMed 16027046PubMed 16297385PubMed 16648475PubMed 16855206PubMed 18023416PubMed 18809582PubMed 2100262. Source: MGI

nucleoplasm

Inferred from direct assay PubMed 12374805PubMed 16297385PubMed 18809582. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence orthology PubMed 18809582. Source: MGI

small ribosomal subunit

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NF-kappaB binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Inferred from direct assay PubMed 16376875. Source: MGI

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

rRNA binding

Inferred from direct assay PubMed 15596447PubMed 18809582. Source: MGI

ribosomal large subunit binding

Inferred from sequence orthology PubMed 18809582. Source: MGI

ribosomal small subunit binding

Inferred from sequence orthology PubMed 18809582. Source: MGI

unfolded protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q009872EBI-626362,EBI-389668From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Nucleophosmin
PRO_0000219482

Regions

Region1 – 185185Required for interaction with SENP3 By similarity
Region1 – 117117Necessary for interaction with APEX1 By similarity
Region241 – 29252Required for nucleolar localization By similarity
Motif152 – 1576Nuclear localization signal Potential
Motif190 – 1967Nuclear localization signal Potential
Compositional bias1 – 99Met-rich
Compositional bias120 – 13213Asp/Glu-rich (acidic)
Compositional bias158 – 18730Asp/Glu-rich (highly acidic)

Sites

Site551Interaction between pentamers By similarity
Site801Interaction between pentamers By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue41Phosphoserine; by PLK1 and PLK2 By similarity
Modified residue101Phosphoserine By similarity
Modified residue321N6-acetyllysine By similarity
Modified residue701Phosphoserine Ref.10
Modified residue751Phosphothreonine By similarity
Modified residue951Phosphothreonine By similarity
Modified residue1251Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Modified residue1391Phosphoserine By similarity
Modified residue1501N6-acetyllysine By similarity
Modified residue1541N6-acetyllysine By similarity
Modified residue1981Phosphothreonine; by CDK1 and CDK2 By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue2171Phosphothreonine; by CDK1 By similarity
Modified residue2251Phosphoserine By similarity
Modified residue2271N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine; alternate By similarity
Modified residue2321Phosphothreonine; by CDK1 By similarity
Modified residue2351Phosphothreonine; by CDK1 By similarity
Modified residue2401Phosphoserine By similarity
Modified residue2411Phosphoserine By similarity
Modified residue2481N6-acetyllysine By similarity
Modified residue2521Phosphoserine By similarity
Modified residue2551N6-acetyllysine By similarity
Modified residue2581Phosphoserine By similarity
Modified residue2651N6-acetyllysine By similarity
Modified residue2711N6-acetyllysine By similarity
Modified residue2771Phosphothreonine By similarity
Modified residue2901N6-acetyllysine By similarity
Cross-link228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Secondary structure

.................. 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61937 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E68750C549ED25E6

FASTA29232,560
        10         20         30         40         50         60 
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 

        70         80         90        100        110        120 
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 

       130        140        150        160        170        180 
EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF 

       190        200        210        220        230        240 
DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS 

       250        260        270        280        290 
SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A B-cell-specific DNA recombination complex."
Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.
J. Biol. Chem. 273:17025-17035(1998) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33212 mRNA. Translation: AAA39801.1.
AK028253 mRNA. Translation: BAC25844.1.
BC054755 mRNA. Translation: AAH54755.1.
CCDSCCDS24532.1.
PIRI52858.
RefSeqNP_032748.1. NM_008722.3.
UniGeneMm.485384.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4N8MX-ray1.80A/B/C/D/E1-130[»]
ProteinModelPortalQ61937.
SMRQ61937. Positions 13-120, 223-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201823. 47 interactions.
IntActQ61937. 10 interactions.
MINTMINT-270928.

Chemistry

ChEMBLCHEMBL5386.

PTM databases

PhosphoSiteQ61937.

Proteomic databases

MaxQBQ61937.
PaxDbQ61937.
PRIDEQ61937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
GeneID18148.
KEGGmmu:18148.
UCSCuc007ikd.2. mouse.

Organism-specific databases

CTD4869.
MGIMGI:106184. Npm1.

Phylogenomic databases

eggNOGNOG79897.
GeneTreeENSGT00440000034554.
HOGENOMHOG000013061.
HOVERGENHBG001860.
InParanoidQ61937.
KOK11276.
OMANCFRTED.
OrthoDBEOG79W97G.
PhylomeDBQ61937.
TreeFamTF327704.

Gene expression databases

ArrayExpressQ61937.
BgeeQ61937.
CleanExMM_NPM1.
GenevestigatorQ61937.

Family and domain databases

Gene3D2.60.120.340. 1 hit.
InterProIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERPTHR22747. PTHR22747. 1 hit.
SUPFAMSSF69203. SSF69203. 1 hit.
ProtoNetSearch...

Other

NextBio293410.
PROQ61937.
SOURCESearch...

Entry information

Entry nameNPM_MOUSE
AccessionPrimary (citable) accession number: Q61937
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot