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Q64430 (ATP7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase 1

EC=3.6.3.54
Alternative name(s):
Copper pump 1
Menkes disease-associated protein homolog
Gene names
Name:Atp7a
Synonyms:Mnk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells By similarity.

Catalytic activity

ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

Subunit structure

Monomer. Interacts with PDZD11 By similarity.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein By similarity. Note: Constitutively cycles between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels By similarity.

Tissue specificity

Found in most tissues except liver. In the kidney, it is detected in the proximal and distal tubules.

Developmental stage

Widespread expressed throughout development.

Domain

The C-terminal di-leucine, 1478-Leu-Leu-1479, is an endocytic targeting signal which functions in retrieving recycling from the plasma membrane to the TGN. Mutation of the di-leucine signal results in the accumulation of the protein in the plasma membrane By similarity.

Involvement in disease

Defects in Atp7a are associated with mottled, an X-linked recessive condition characterized by mottled pigmentation of the coat, defects in connective tissue and neonatal or fetal death. It is due to a defect in absorption and transport of copper. The mottled mutants exhibit a diversity of phenotypes. Two of these mutants are called brindled and blotchy and their phenotypes resemble classical Menkes disease (MD) and occipital horn syndrome (OHS) in humans, respectively. Other mutants are called dappled, mosaic, tortoiseshell, pewter, etc.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 6 HMA domains.

Ontologies

Keywords
   Biological processCopper transport
Ion transport
Transport
   Cellular componentCell membrane
Golgi apparatus
Membrane
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP metabolic process

Inferred from mutant phenotype PubMed 11311799. Source: MGI

T-helper cell differentiation

Inferred from mutant phenotype PubMed 8434133. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 10632785PubMed 1115218PubMed 3385878. Source: MGI

blood vessel remodeling

Inferred from mutant phenotype PubMed 16338116. Source: MGI

cartilage development

Inferred from mutant phenotype PubMed 8895222. Source: MGI

catecholamine metabolic process

Inferred from mutant phenotype PubMed 17511. Source: MGI

cellular copper ion homeostasis

Inferred from mutant phenotype PubMed 10332039PubMed 11311799PubMed 16338116PubMed 1779648PubMed 187892PubMed 27591PubMed 3674914PubMed 4858102PubMed 564942PubMed 571898PubMed 573617PubMed 573619PubMed 6685755PubMed 7197928PubMed 7688531PubMed 7873696PubMed 8025644PubMed 8096378PubMed 9321757PubMed 9686356. Source: MGI

central nervous system neuron development

Inferred from mutant phenotype PubMed 8174230. Source: MGI

cerebellar Purkinje cell differentiation

Inferred from mutant phenotype PubMed 2473662. Source: MGI

collagen fibril organization

Inferred from mutant phenotype PubMed 16338116PubMed 20889PubMed 4808708PubMed 8096378PubMed 8895222. Source: MGI

copper ion export

Inferred from mutant phenotype PubMed 6542992. Source: MGI

copper ion import

Inferred from mutant phenotype PubMed 573617PubMed 573619PubMed 7197928. Source: MGI

copper ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite morphogenesis

Inferred from mutant phenotype PubMed 2473662. Source: MGI

detoxification of copper ion

Inferred from mutant phenotype PubMed 7509170. Source: MGI

dopamine metabolic process

Inferred from mutant phenotype PubMed 1752214PubMed 8174230. Source: MGI

elastic fiber assembly

Inferred from mutant phenotype PubMed 16338116PubMed 20889PubMed 3385878PubMed 937819. Source: MGI

elastin biosynthetic process

Inferred from mutant phenotype PubMed 8096378. Source: MGI

epinephrine metabolic process

Inferred from mutant phenotype PubMed 1752214. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 1115218. Source: MGI

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 2473662. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 16338116PubMed 1752214PubMed 2473662. Source: MGI

lung alveolus development

Inferred from mutant phenotype PubMed 937819. Source: MGI

mitochondrion organization

Inferred from mutant phenotype PubMed 2288383PubMed 8009964. Source: MGI

negative regulation of metalloenzyme activity

Inferred from mutant phenotype PubMed 17511. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17003121. Source: MGI

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 8174230. Source: MGI

norepinephrine biosynthetic process

Inferred from mutant phenotype PubMed 4405722PubMed 4858102. Source: MGI

norepinephrine metabolic process

Inferred from mutant phenotype PubMed 4147174. Source: MGI

peptidyl-lysine modification

Inferred from mutant phenotype PubMed 4808708. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 16338116PubMed 1752214PubMed 2473662PubMed 4561716PubMed 4670054PubMed 4858102. Source: MGI

positive regulation of catalytic activity

Inferred from mutant phenotype PubMed 10098864PubMed 11311799. Source: MGI

positive regulation of metalloenzyme activity

Inferred from mutant phenotype PubMed 10098864PubMed 12488345PubMed 14140PubMed 16371425PubMed 17511PubMed 20889PubMed 7769737PubMed 8096378. Source: MGI

pyramidal neuron development

Inferred from mutant phenotype PubMed 2473662. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 11311799. Source: MGI

regulation of oxidative phosphorylation

Inferred from mutant phenotype PubMed 8550574. Source: MGI

release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 11311799. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 16371425. Source: MGI

serotonin metabolic process

Inferred from mutant phenotype PubMed 8174230. Source: MGI

skin development

Inferred from mutant phenotype PubMed 4808708. Source: MGI

tryptophan metabolic process

Inferred from mutant phenotype PubMed 4147174. Source: MGI

tyrosine metabolic process

Inferred from mutant phenotype PubMed 4147174. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15634787. Source: MGI

cytoplasmic vesicle

Inferred from direct assay PubMed 15634787PubMed 17003121. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 15634671Ref.4. Source: MGI

neuron projection

Inferred from direct assay PubMed 15634787. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15634671. Source: MGI

plasma membrane

Inferred from direct assay PubMed 10332039. Source: MGI

trans-Golgi network

Inferred from direct assay PubMed 10332039PubMed 12488345PubMed 16371425PubMed 17003121. Source: MGI

trans-Golgi network transport vesicle

Inferred from sequence or structural similarity. Source: HGNC

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 10332039. Source: MGI

copper-exporting ATPase activity

Inferred from direct assay PubMed 15634671. Source: MGI

superoxide dismutase copper chaperone activity

Inferred from direct assay PubMed 16371425. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14911491Copper-transporting ATPase 1
PRO_0000046312

Regions

Topological domain1 – 644644Cytoplasmic Potential
Transmembrane645 – 66622Helical; Potential
Topological domain667 – 70539Extracellular Potential
Transmembrane706 – 72520Helical; Potential
Topological domain726 – 7327Cytoplasmic Potential
Transmembrane733 – 75321Helical; Potential
Topological domain754 – 77219Extracellular Potential
Transmembrane773 – 79321Helical; Potential
Topological domain794 – 926133Cytoplasmic Potential
Transmembrane927 – 95024Helical; Potential
Topological domain951 – 98030Extracellular Potential
Transmembrane981 – 100222Helical; Potential
Topological domain1003 – 1347345Cytoplasmic Potential
Transmembrane1348 – 136518Helical; Potential
Topological domain1366 – 137611Extracellular Potential
Transmembrane1377 – 139620Helical; Potential
Topological domain1397 – 149195Cytoplasmic Potential
Domain9 – 7567HMA 1
Domain172 – 23867HMA 2
Domain278 – 34467HMA 3
Domain378 – 44467HMA 4
Domain480 – 54667HMA 5
Domain556 – 62267HMA 6
Region1477 – 149115PDZD11-binding By similarity
Motif1478 – 14792Endocytosis signal By similarity
Compositional bias356 – 3627Poly-Ser

Sites

Active site103514-aspartylphosphate intermediate Probable
Metal binding12921Magnesium By similarity
Metal binding12961Magnesium By similarity

Amino acid modifications

Modified residue3391Phosphoserine By similarity
Modified residue3571Phosphoserine Ref.6
Modified residue12031Phosphothreonine By similarity
Modified residue14571Phosphoserine Ref.6
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation9661N-linked (GlcNAc...) Potential

Natural variations

Natural variant6741H → R in MD. Ref.3
Natural variant13811S → P in MD. Ref.3

Experimental info

Sequence conflict441E → D in AAA57445. Ref.1
Sequence conflict441E → D in AAB37301. Ref.4
Sequence conflict1031I → V in AAA57445. Ref.1
Sequence conflict1031I → V in AAB37301. Ref.4
Sequence conflict1721M → R in AAA57445. Ref.1
Sequence conflict1721M → R in AAB37301. Ref.4
Sequence conflict245 – 2462LK → PI in AAB08487. Ref.2
Sequence conflict4451P → PA in AAB08487. Ref.2
Sequence conflict4451P → PA in AAB37301. Ref.4
Sequence conflict4701L → P in AAB08487. Ref.2
Sequence conflict4701L → P in BAA22369. Ref.3
Sequence conflict4701L → P in AAB37301. Ref.4
Sequence conflict5151M → T in AAA57445. Ref.1
Sequence conflict5151M → T in AAB37301. Ref.4
Sequence conflict7171C → F in AAB08487. Ref.2
Sequence conflict7701T → A in AAB08487. Ref.2
Sequence conflict7751P → S in AAB08487. Ref.2
Sequence conflict8851I → T in AAB08487. Ref.2
Sequence conflict11691Y → H in AAB08487. Ref.2
Sequence conflict12041A → P in AAB08487. Ref.2
Sequence conflict12041A → P in AAB37301. Ref.4
Sequence conflict12171I → M in AAA57445. Ref.1
Sequence conflict12531R → Q in AAA57445. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64430 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2FADCC6806994CA5

FASTA1,491161,959
        10         20         30         40         50         60 
MEPSVDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATI IYDPKLQTPK 

        70         80         90        100        110        120 
TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLTLPW DHIQSTLLKT KGVTGVKISP 

       130        140        150        160        170        180 
QQRSAVVTII PSVVSASQIV ELVPDLSLDM GTQEKKSGAC EEHSTPQAGE VMLKMKVEGM 

       190        200        210        220        230        240 
TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVFQPHLI TAEEIKKQIE AVGFPAFIKK 

       250        260        270        280        290        300 
QPKYLKLGAI DVERLKNTPV KSSEGSQQKS PSYPSDSTTM FTIEGMHCKS CVSNIESALS 

       310        320        330        340        350        360 
TLQYVSSIVV SLENRSAIVK YNASLVTPEM LRKAIEAISP GQYRVSIASE VESTASSPSS 

       370        380        390        400        410        420 
SSLQKMPLNI VSQPLTQEAV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLANSTGTIE 

       430        440        450        460        470        480 
FDPLLTSPET LREAIEDMGF DAALPDMKEP LVVIAQPSLE TPLLPSSNEL ENVMTSVQNK 

       490        500        510        520        530        540 
CYIQVSGMTC ASCVANIERN LRREEGIYSV LVALMAGKAE VRYNPAVIQP RVIAEFIREL 

       550        560        570        580        590        600 
GFGAMVMENA GEGNGILELV VRGMTCASCV HKIESTLTKH KGIFYCSVAL ATNKAHIKYD 

       610        620        630        640        650        660 
PEIIGPRDII HTIGSLGFEA SLVKKDRSAN HLDHKREIKQ WRGSFLVSLF FCIPVMGLMV 

       670        680        690        700        710        720 
YMMVMDHHLA TLHHNQNMSN EEMINMHSAM FLERQILPGL SIMNLLSLLL CLPVQFCGGW 

       730        740        750        760        770        780 
YFYIQAYKAL KHKTANMDVL IVLATTIAFA YSLVILLVAM FERAKVNPIT FFDTPPMLFV 

       790        800        810        820        830        840 
FIALGRWLEH IAKGKTSEAL AKLISLQATE ATIVTLNSEN LLLSEEQVDV ELVQRGDIIK 

       850        860        870        880        890        900 
VVPGGKFPVD GRVIEGHSMV DESLITGEAM PVAKKPGSTV IAGSINQNGS LLIRATHVGA 

       910        920        930        940        950        960 
DTTLSQIVKL VEEAQTSKAP IQQFADKLSG YFVPFIVLVS IVTLLVWIII GFQNFEIVET 

       970        980        990       1000       1010       1020 
YFPGYNRSIS RTETIIRFAF QASITVLCIA CPCSLGLATP TAVMVGTGVG AQNGILIKGG 

      1030       1040       1050       1060       1070       1080 
EPLEMAHKVK VVVFDKTGTI THGTPVVNQV KVLVESNKIS RNKILAIVGT AESNSEHPLG 

      1090       1100       1110       1120       1130       1140 
AAVTKYCKKE LDTETLGTCT DFQVVPGCGI SCKVTNIEGL LHKSNLKIEE NNIKNASLVQ 

      1150       1160       1170       1180       1190       1200 
IDAINEQSST SSSMIIDAHL SNAVNTQQYK VLIGNREWMI RNGLVISNDV DESMIEHERR 

      1210       1220       1230       1240       1250       1260 
GRTAVLVTID DELCGLIAIA DTVKPEAELA VHILKSMGLE VVLMTGDNSK TARSIASQVG 

      1270       1280       1290       1300       1310       1320 
ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV GDGINDSPAL AMANVGIAIG TGTDVAIEAA 

      1330       1340       1350       1360       1370       1380 
DVVLIRNDLL DVVASIDLSR KTVKRIRINF VFALIYNLVG IPIAAGVFLP IGLVLQPWMG 

      1390       1400       1410       1420       1430       1440 
SAAMAASSVS VVLSSLFLKL YRKPTYDNYE LHPRSHTGQR SPSEISVHVG IDDTSRNSPR 

      1450       1460       1470       1480       1490 
LGLLDRIVNY SRASINSLLS DKRSLNSVVT SEPDKHSLLV GDFREDDDTT L 

« Hide

References

« Hide 'large scale' references
[1]"The mottled gene is the mouse homologue of the Menkes disease gene."
Levinson B., Vulpe C., Elder B., Martin C., Verley F., Packman S., Gitschier J.
Nat. Genet. 6:369-373(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"Mutations in the murine homologue of the Menkes gene in dappled and blotchy mice."
Mercer J.F.B., Grimes A., Ambrosini L., Lockhart P., Paynter J.A., Dierick H., Glover T.W.
Nat. Genet. 6:374-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c, DL and ICR X Swiss Webster.
Tissue: Embryo and Kidney.
[3]"Occurrence of two missense mutations in Cu-ATPase of the macular mouse, a Menkes disease model."
Ohta Y., Shiraishi N., Nishikimi M.
Biochem. Mol. Biol. Int. 43:913-918(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-674 AND PRO-1381.
Strain: C3H.
Tissue: Placenta.
[4]"Molecular basis of the brindled mouse mutant (Mo(br)): a murine model of Menkes disease."
Grimes A., Hearn C.J., Lockhart P., Newgreen D.F., Mercer J.F.B.
Hum. Mol. Genet. 6:1037-1042(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CBA X C3H.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"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-357 AND SER-1457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03434 mRNA. Translation: AAA57445.1.
U03736 mRNA. Translation: AAB08487.1.
AB007134 mRNA. Translation: BAA22369.1.
U71091 mRNA. Translation: AAB37301.1.
AL672288 Genomic DNA. Translation: CAM16891.1.
PIRS43793.
RefSeqNP_033856.3. NM_009726.5.
UniGeneMm.254297.

3D structure databases

ProteinModelPortalQ64430.
SMRQ64430. Positions 8-624, 637-1406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198268. 1 interaction.

PTM databases

PhosphoSiteQ64430.

Proteomic databases

PaxDbQ64430.
PRIDEQ64430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113557; ENSMUSP00000109186; ENSMUSG00000033792.
GeneID11977.
KEGGmmu:11977.
UCSCuc012hnn.1. mouse.

Organism-specific databases

CTD538.
MGIMGI:99400. Atp7a.

Phylogenomic databases

eggNOGCOG2217.
GeneTreeENSGT00530000063773.
HOGENOMHOG000250397.
HOVERGENHBG050616.
KOK17686.
OrthoDBEOG7C2R0G.

Enzyme and pathway databases

BRENDA3.6.3.4. 3474.

Gene expression databases

ArrayExpressQ64430.
BgeeQ64430.
CleanExMM_ATP7A.
GenevestigatorQ64430.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 6 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 6 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP7A. mouse.
NextBio280111.
PROQ64430.
SOURCESearch...

Entry information

Entry nameATP7A_MOUSE
AccessionPrimary (citable) accession number: Q64430
Secondary accession number(s): A2AG69 expand/collapse secondary AC list , O35101, P97422, Q64431
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 143 of the entry and version 3 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MGD cross-references

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