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Q62101 (KPCD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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:
Serine/threonine-protein kinase D1

EC=2.7.11.13
Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu
Gene names
Name:Prkd1
Synonyms:Pkcm, Pkd, Prkcm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-469 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-748 and phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress By similarity. Ref.7

Subunit structure

Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13 and SRC By similarity. Interacts with DAPK1 in an oxidative stress-regulated manner By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Golgi apparatustrans-Golgi network. Note: Translocation to the cell membrane is required for kinase activation By similarity. Ref.4

Post-translational modification

Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD By similarity. Ref.3 Ref.5 Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.

Contains 1 PH domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Differentiation
Immunity
Inflammatory response
Innate immunity
Neurogenesis
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
   DomainRepeat
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi vesicle transport

Inferred from mutant phenotype Ref.4. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of CREB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone deacetylase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of keratinocyte proliferation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from direct assay PubMed 10882525. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 10882525. Source: MGI

cytoplasm

Inferred from direct assay PubMed 10882525. Source: MGI

cytosol

Inferred from direct assay Ref.4. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 10882525. Source: MGI

plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB3P051062EBI-6903636,EBI-702847From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Serine/threonine-protein kinase D1
PRO_0000055715

Regions

Domain428 – 547120PH
Domain589 – 845257Protein kinase
Zinc finger144 – 19451Phorbol-ester/DAG-type 1
Zinc finger276 – 32651Phorbol-ester/DAG-type 2
Nucleotide binding595 – 6039ATP By similarity
Compositional bias16 – 2611Poly-Ala
Compositional bias198 – 2014Poly-Arg

Sites

Active site7121Proton acceptor By similarity
Binding site6181ATP By similarity

Amino acid modifications

Modified residue931Phosphotyrosine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2061Phosphoserine By similarity
Modified residue3511Phosphoserine By similarity
Modified residue4031Phosphoserine; by MAPK13 By similarity
Modified residue4071Phosphoserine; by MAPK13 By similarity
Modified residue4381Phosphotyrosine By similarity
Modified residue4541Phosphoserine By similarity
Modified residue4691Phosphotyrosine; by ABL By similarity
Modified residue5081Phosphotyrosine By similarity
Modified residue7441Phosphoserine; by PKC/PRKCD Ref.5 Ref.7
Modified residue7481Phosphoserine; by autocatalysis and PKC/PRKCD Ref.5 Ref.7
Modified residue9161Phosphoserine; by autocatalysis Ref.3

Experimental info

Mutagenesis7441S → A: Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-748. Ref.7
Mutagenesis7441S → D: High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-748. Ref.7
Mutagenesis7481S → A: Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-744. Ref.7
Mutagenesis7481S → D: High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-744. Ref.7
Sequence conflict6831R → W in CAA84283. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62101 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A59FEBAFCE0D0F13

FASTA918102,037
        10         20         30         40         50         60 
MSVPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH LQIGLSREPV 

        70         80         90        100        110        120 
LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL LFRHDPASDN ILQLVKIASD 

       130        140        150        160        170        180 
IQEGDLIEVV LSASATFEDF QIRPHALFVH SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL 

       190        200        210        220        230        240 
NYHKRCAFKI PNNCSGVRRR RLSNVSLTGL GTVRTASAEF STSVPDEPLL SPVSPGFEQK 

       250        260        270        280        290        300 
SPSESFIGRE KRSNSQSYIG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL 

       310        320        330        340        350        360 
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG SDDNDSERNS 

       370        380        390        400        410        420 
GLMDDMDEAM VQDTEMALAE GQSGGAEMQD PDADQEDSNR TISPSTSNNI PLMRVVQSVK 

       430        440        450        460        470        480 
HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW RLDSKCITLF QNDTGSRYYK EIPLSEILCL 

       490        500        510        520        530        540 
EPAKPSALTP VGATPHCFEI TTANVVYYVG ENVVNPSSSP PNNSVLPSGI GPDVARMWEV 

       550        560        570        580        590        600 
AIQHALMPVI PKGSSVGSGS NSHKDISVSI SVSNCQIQEN VDISTVYQIF PDEVLGSGQF 

       610        620        630        640        650        660 
GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN LECMFETPER 

       670        680        690        700        710        720 
VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL RHLHFKNIVH CDLKPENVLL 

       730        740        750        760        770        780 
ASADPFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY 

       790        800        810        820        830        840 
VSLSGTFPFN EDEDIHDQIQ NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL 

       850        860        870        880        890        900 
SHPWLQDYQT WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL ISLSASHSDS 

       910 
PEAEEREMKA LSERVSIL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain."
Valverde A.M., Sinnet-Smith J., Van Lint J., Rozengurt E.
Proc. Natl. Acad. Sci. U.S.A. 91:8572-8576(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Lung.
[2]"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.
[3]"Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/protein kinase Cmu."
Matthews S.A., Rozengurt E., Cantrell D.
J. Biol. Chem. 274:26543-26549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-916.
[4]"Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network."
Liljedahl M., Maeda Y., Colanzi A., Ayala I., Van Lint J., Malhotra V.
Cell 104:409-420(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF TRANS-GOLGI NETWORK, SUBCELLULAR LOCATION.
[5]"Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo."
Waldron R.T., Rey O., Iglesias T., Tugal T., Cantrell D., Rozengurt E.
J. Biol. Chem. 276:32606-32615(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-744 AND SER-748.
[6]"The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins."
Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E., Colicelli J.
Mol. Cell. Biol. 22:916-926(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RIN1 PHOSPHORYLATION.
[7]"Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain."
Waldron R.T., Rozengurt E.
J. Biol. Chem. 278:154-163(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-744 AND SER-748, PHOSPHORYLATION AT SER-744 AND SER-748.
[8]"PKD1/PKCmu promotes alphavbeta3 integrin recycling and delivery to nascent focal adhesions."
Woods A.J., White D.P., Caswell P.T., Norman J.C.
EMBO J. 23:2531-2543(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[9]"Protein kinase D potentiates DNA synthesis induced by Gq-coupled receptors by increasing the duration of ERK signaling in swiss 3T3 cells."
Sinnett-Smith J., Zhukova E., Hsieh N., Jiang X., Rozengurt E.
J. Biol. Chem. 279:16883-16893(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION.
[10]"Bone morphogenic protein 2 activates protein kinase D to regulate histone deacetylase 7 localization and repression of Runx2."
Jensen E.D., Gopalakrishnan R., Westendorf J.J.
J. Biol. Chem. 284:2225-2234(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
[11]"Protein kinase D is implicated in the reversible commitment to differentiation in primary cultures of mouse keratinocytes."
Jadali A., Ghazizadeh S.
J. Biol. Chem. 285:23387-23397(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34524 mRNA. Translation: CAA84283.1.
AC099603 Genomic DNA. No translation available.
AC154543 Genomic DNA. No translation available.
CT009740 Genomic DNA. No translation available.
CT010578 Genomic DNA. No translation available.
PIRI48719.
RefSeqNP_032884.2. NM_008858.3.
UniGeneMm.133719.

3D structure databases

ProteinModelPortalQ62101.
SMRQ62101. Positions 145-194, 277-326, 426-547, 556-847.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62101. 2 interactions.
STRING10090.ENSMUSP00000002765.

PTM databases

PhosphoSiteQ62101.

Proteomic databases

PaxDbQ62101.
PRIDEQ62101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002765; ENSMUSP00000002765; ENSMUSG00000002688.
GeneID18760.
KEGGmmu:18760.
UCSCuc007nmj.1. mouse.

Organism-specific databases

CTD5587.
MGIMGI:99879. Prkd1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117523.
HOGENOMHOG000015135.
HOVERGENHBG003564.
InParanoidQ62101.
KOK06070.
OMAMAECQND.
OrthoDBEOG75B84N.
TreeFamTF314320.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

BgeeQ62101.
CleanExMM_PRKD1.
GenevestigatorQ62101.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22968. PTHR22968. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio294945.
PROQ62101.
SOURCESearch...

Entry information

Entry nameKPCD1_MOUSE
AccessionPrimary (citable) accession number: Q62101
Secondary accession number(s): E9QNA3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 137 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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