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P54265 (DMPK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myotonin-protein kinase

Short name=MT-PK
EC=2.7.11.1
Alternative name(s):
DM-kinase
Short name=DMK
DMPK
Myotonic dystrophy protein kinase
Short name=MDPK
Gene names
Name:Dmpk
Synonyms:Dm15, Mdpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. Ref.5 Ref.8 Ref.9 Ref.11 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Coiled-coil-mediated oligomerization enhances the catalytic activity. Proteolytic processing of the C-terminus may release the protein from membranes and constitute a mean to regulate the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second messengers By similarity.

Subunit structure

Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability By similarity.

Subcellular location

Sarcoplasmic reticulum membrane. Cell membrane. Note: Localizes to sarcoplasmic reticulum membranes of cardiomyocytes. Ref.9 Ref.10 Ref.11 Ref.12

Isoform 1: Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Ref.9 Ref.10 Ref.11 Ref.12.

Isoform 8: Mitochondrion outer membrane; Single-pass type IV membrane protein Ref.9 Ref.10 Ref.11 Ref.12.

Isoform 5: Cytoplasmcytosol Ref.9 Ref.10 Ref.11 Ref.12.

Tissue specificity

Expressed in all tissues tested, with a predominance in brain, skeletal muscle, heart, and other tissues containing smooth muscle. In the heart, expression is restricted to the cardiomyocytes in the ventricle and atrium. Ref.9

Developmental stage

Primarily detected in striated muscle structures of the 14.5 day embryo, including all major muscles in the skeletal structures, cardiac muscle, diaphragm, and the smooth muscle of the lung and gut. Ref.9

Domain

The coiled coil domain is required for homodimerization and regulates the enzymatic activity By similarity.

Post-translational modification

Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK By similarity. Ref.10

Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity By similarity.

Disruption phenotype

Mice are fertile and no negative selection against the absence of the protein is apparent. Newborn do not display hypotonia, respiratory distress or gross anatomical abnormalities. However, a progressive muscle weakness a hall mark of myopathies is observed. Muscles from mature mice show variation in fiber size, increase fiber degeneration and fibrosis. They also display age-related progression in atrioventricular conduction defects that are reminiscent of congenital myotonic dystrophy. Ref.4 Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. DMPK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular calcium ion homeostasis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

muscle cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear envelope organization

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of catalytic activity

Inferred from sequence or structural similarity. Source: GOC

regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction

Inferred from mutant phenotype PubMed 11526199. Source: MGI

regulation of heart contraction

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of myotube differentiation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of skeletal muscle contraction by calcium ion signaling

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of sodium ion transport

Inferred from mutant phenotype PubMed 11526199. Source: MGI

regulation of synapse structural plasticity

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.10. Source: UniProtKB

integral component of mitochondrial outer membrane

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P54265-1)

Also known as: DMPK A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54265-2)

The sequence of this isoform differs from the canonical sequence as follows:
     328-356: Missing.
Isoform 3 (identifier: P54265-3)

Also known as: DMPK B;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
Isoform 4 (identifier: P54265-4)

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     412-416: DNQVP → LKRPT
     417-631: Missing.
Isoform 5 (identifier: P54265-5)

Also known as: DMPK E;

The sequence of this isoform differs from the canonical sequence as follows:
     536-537: AI → DP
     538-631: Missing.
Isoform 6 (identifier: P54265-6)

Also known as: DMPK F;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     536-537: AI → DP
     538-631: Missing.
Isoform 7 (identifier: P54265-7)

The sequence of this isoform differs from the canonical sequence as follows:
     536-557: AITGVPSPRATDPPSHLDGPPA → GESLTCFQPRGHWVEMGGMLGV
     558-631: Missing.
Isoform 8 (identifier: P54265-8)

Also known as: DMPK C;

The sequence of this isoform differs from the canonical sequence as follows:
     552-631: LDGPPAVAVG...WCFPGATFAP → MAPRPWLWAS...SREPPSPPEP
Isoform 9 (identifier: P54265-9)

Also known as: DMPK D;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     552-631: LDGPPAVAVG...WCFPGATFAP → MAPRPWLWAS...SREPPSPPEP
Isoform 10 (identifier: P54265-10)

The sequence of this isoform differs from the canonical sequence as follows:
     552-562: LDGPPAVAVGQ → ASRQILPKGTP
     563-631: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Myotonin-protein kinase
PRO_0000085925

Regions

Topological domain1 – 592592Cytoplasmic Potential
Transmembrane593 – 61321Helical; Anchor for type IV membrane protein; Potential
Topological domain614 – 63118Lumenal Potential
Domain71 – 339269Protein kinase
Domain340 – 41576AGC-kinase C-terminal
Nucleotide binding77 – 859ATP By similarity
Coiled coil464 – 53269 Potential

Sites

Active site1951Proton acceptor By similarity
Binding site1001ATP By similarity

Amino acid modifications

Modified residue2161Phosphoserine; by autocatalysis By similarity
Modified residue2281Phosphoserine; by autocatalysis By similarity
Modified residue2341Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence328 – 35629Missing in isoform 2.
VSP_004819
Alternative sequence378 – 3825Missing in isoform 3, isoform 4, isoform 6 and isoform 9.
VSP_004820
Alternative sequence412 – 4165DNQVP → LKRPT in isoform 4.
VSP_004821
Alternative sequence417 – 631215Missing in isoform 4.
VSP_004822
Alternative sequence536 – 55722AITGV…DGPPA → GESLTCFQPRGHWVEMGGML GV in isoform 7.
VSP_004825
Alternative sequence536 – 5372AI → DP in isoform 5 and isoform 6.
VSP_004823
Alternative sequence538 – 63194Missing in isoform 5 and isoform 6.
VSP_004824
Alternative sequence552 – 63180LDGPP…ATFAP → MAPRPWLWASARWWGQAPCT AVTCCSLPGSLGLAYPRRVA CSCSPLLWLLPPHWAALGWW PIPAVSPQSGVSREPPSPPE P in isoform 8 and isoform 9.
VSP_004827
Alternative sequence552 – 56211LDGPPAVAVGQ → ASRQILPKGTP in isoform 10.
VSP_004828
Alternative sequence558 – 63174Missing in isoform 7.
VSP_004826
Alternative sequence563 – 63169Missing in isoform 10.
VSP_004829

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DMPK A) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5EE800A37EA81DF4

FASTA63169,602
        10         20         30         40         50         60 
MSAEVRLRQL QQLVLDPGFL GLEPLLDLLL GVHQELGASH LAQDKYVADF LQWVEPIAAR 

        70         80         90        100        110        120 
LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 

       130        140        150        160        170        180 
DVLVKGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 

       190        200        210        220        230        240 
MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL QPDGMVRSLV AVGTPDYLSP 

       250        260        270        280        290        300 
EILQAVGGGP GAGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYAKI VHYREHLSLP 

       310        320        330        340        350        360 
LADTVVPEEA QDLIRGLLCP AEIRLGRGGA GDFQKHPFFF GLDWEGLRDS VPPFTPDFEG 

       370        380        390        400        410        420 
ATDTCNFDVV EDRLTAMVSG GGETLSDMQE DMPLGVRLPF VGYSYCCMAF RDNQVPDPTP 

       430        440        450        460        470        480 
MELEALQLPV SDLQGLDLQP PVSPPDQVAE EADLVAVPAP VAEAETTVTL QQLQEALEEE 

       490        500        510        520        530        540 
VLTRQSLSRE LEAIRTANQN FSSQLQEAEV RNRDLEAHVR QLQERMEMLQ APGAAAITGV 

       550        560        570        580        590        600 
PSPRATDPPS HLDGPPAVAV GQCPLVGPGP MHRRHLLLPA RIPRPGLSEA RCLLLFAAAL 

       610        620        630 
AAAATLGCTG LVAYTGGLTP VWCFPGATFA P 

« Hide

Isoform 2 [UniParc].

Checksum: 8A9EBB4E930E5EB0
Show »

FASTA60266,397
Isoform 3 (DMPK B) [UniParc].

Checksum: 84F11B047BB340EF
Show »

FASTA62669,244
Isoform 4 [UniParc].

Checksum: 24F3F18634D0131C
Show »

FASTA41146,532
Isoform 5 (DMPK E) [UniParc].

Checksum: 21F148D98B3657BB
Show »

FASTA53760,161
Isoform 6 (DMPK F) [UniParc].

Checksum: A79E9629B958241E
Show »

FASTA53259,803
Isoform 7 [UniParc].

Checksum: D0247256B70FD18C
Show »

FASTA55762,322
Isoform 8 (DMPK C) [UniParc].

Checksum: D1576187FFBB8824
Show »

FASTA63270,329
Isoform 9 (DMPK D) [UniParc].

Checksum: C5DD789C58BE9379
Show »

FASTA62769,972
Isoform 10 [UniParc].

Checksum: C8D00A5C40223DBD
Show »

FASTA56262,682

References

[1]"Structure and genomic sequence of the myotonic dystrophy (DM kinase) gene."
Mahadevan M.S., Amemiya C., Jansen G., Sabourin L., Baird S., Neville C.E., Wormskamp N., Segers B., Batzer M., Lamerdin J., de Jong P.J., Wieringa B., Korneluk R.G.
Hum. Mol. Genet. 2:299-304(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"No imprinting involved in the expression of DM-kinase mRNAs in mouse and human tissues."
Jansen G., Bartolomei M., Kalscheuer V., Merkx G., Wormskamp N., Mariman E., Smeets D., Ropers H.-H., Wieringa B.
Hum. Mol. Genet. 2:1221-1227(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"Characterization of the myotonic dystrophy region predicts multiple protein isoform-encoding mRNAs."
Jansen G., Mahadevan M.S., Amemiya C., Wormskamp N., Segers B., Hendriks W., O'Hoy K., Baird S., Sabourin L., Lennon G., Jap P.L., Iles D., Coerwinkel M., Hofker M., Carrano A.V., de Jong P.J., Korneluk R.G., Wieringa B.
Nat. Genet. 1:261-266(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-631 (ISOFORMS 2; 4; 5 AND 8).
Tissue: Brain.
[4]"Mice lacking the myotonic dystrophy protein kinase develop a late onset progressive myopathy."
Reddy S., Smith D.B., Rich M.M., Leferovich J.M., Reilly P., Davis B.M., Tran K., Rayburn H., Bronson R., Cros D., Balice-Gordon R.J., Housman D.
Nat. Genet. 13:325-335(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Myotonic dystrophy protein kinase is involved in the modulation of the Ca2+ homeostasis in skeletal muscle cells."
Benders A.A., Groenen P.J., Oerlemans F.T., Veerkamp J.H., Wieringa B.
J. Clin. Invest. 100:1440-1447(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS.
[6]"Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties."
Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G., Wieringa B.
Hum. Mol. Genet. 9:605-616(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 3; 5; 6; 8 AND 9).
[7]"Progressive atrioventricular conduction block in a mouse myotonic dystrophy model."
Berul C.I., Maguire C.T., Gehrmann J., Reddy S.
J. Interv. Card. Electrophysiol. 4:351-358(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"A role for myotonic dystrophy protein kinase in synaptic plasticity."
Schulz P.E., McIntosh A.D., Kasten M.R., Wieringa B., Epstein H.F.
J. Neurophysiol. 89:1177-1186(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYNAPTIC PLASTICITY.
[9]"Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum."
Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.
J. Biol. Chem. 280:8016-8021(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CALCIUM UPTAKE BY CARDIAC SARCOPLASMIC RETICULUM, FUNCTION IN PHOSPHORYLATION OF PLN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[10]"Divergent mitochondrial and endoplasmic reticulum association of DMPK splice isoforms depends on unique sequence arrangements in tail anchors."
van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B., van de Loo F.A., Fransen J., Wieringa B., Wansink D.G.
Mol. Cell. Biol. 25:1402-1414(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TOPOLOGY, AUTOPHOSPHORYLATION.
[11]"Myotonic dystrophy protein kinase is expressed in embryonic myocytes and is required for myotube formation."
Harmon E.B., Harmon M.L., Larsen T.D., Paulson A.F., Perryman M.B.
Dev. Dyn. 237:2353-2366(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MYOGENESIS, SUBCELLULAR LOCATION.
[12]"Myotonic dystrophy protein kinase is critical for nuclear envelope integrity."
Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B.
J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR ENVELOPE STABILITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21503 expand/collapse EMBL AC list , Z21504, Z21505, Z21506 Genomic DNA. Translation: CAA79715.1.
Z38015 Genomic DNA. Translation: CAA86113.1.
S60313 mRNA. Translation: AAC60667.1.
S60314 mRNA. Translation: AAC60666.1.
S60315 mRNA. Translation: AAC60665.1.
S60316 mRNA. Translation: AAC60664.1.
PIRI78393.
I78394.
I78395.
I78396.
S71829.
RefSeqNP_001177420.1. NM_001190491.1.
NP_115794.1. NM_032418.2.
XP_006539581.1. XM_006539518.1.
XP_006539582.1. XM_006539519.1.
UniGeneMm.6529.

3D structure databases

ProteinModelPortalP54265.
SMRP54265. Positions 11-416, 468-531.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000032568.

PTM databases

PhosphoSiteP54265.

Proteomic databases

PaxDbP54265.
PRIDEP54265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032568; ENSMUSP00000032568; ENSMUSG00000030409. [P54265-1]
ENSMUST00000108473; ENSMUSP00000104113; ENSMUSG00000030409. [P54265-5]
GeneID13400.
KEGGmmu:13400.
UCSCuc009fkn.2. mouse. [P54265-1]
uc009fkp.2. mouse. [P54265-5]
uc009fkq.2. mouse. [P54265-8]

Organism-specific databases

CTD1760.
MGIMGI:94906. Dmpk.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117511.
HOGENOMHOG000233033.
HOVERGENHBG107817.
InParanoidP54265.
KOK08788.
OMATLSDMQE.
OrthoDBEOG7F511X.
PhylomeDBP54265.
TreeFamTF105337.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressP54265.
BgeeP54265.
CleanExMM_DMPK.
GenevestigatorP54265.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283791.
PROP54265.
SOURCESearch...

Entry information

Entry nameDMPK_MOUSE
AccessionPrimary (citable) accession number: P54265
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 125 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

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