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O54949 (NLK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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 NLK

EC=2.7.11.24
Alternative name(s):
Nemo-like kinase
Gene names
Name:Nlk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.9 Ref.13

Cofactor

Magnesium. Ref.1 Ref.8

Enzyme regulation

Activated by the non-canonical Wnt signaling pathway, in which WNT5A leads to activation of MAP3K7/TAK1 and HIPK2, which subsequently phosphorylates and activates this protein. Activated by dimerization and subsequent intermolecular autophosphorylation on Thr-298. Other cytokines such as IL6 may also activate this regulatory circuit. Ref.1 Ref.4 Ref.6 Ref.12 Ref.19

Subunit structure

Interacts with RNF138/NARF By similarity. Forms a complex with CHD7, PPARG and SETDB1 in response to WNT5A signaling By similarity. Interacts with DAPK3/ZIPK, and this interaction may disrupt interaction with transcription factors such as TCF7L2/TCF4 By similarity. Interacts with FOXO1 and FOXO3 By similarity. Homodimer. Homodimerization is required for intermolecular autophosphorylation, kinase activation and nuclear localization. Interacts with the upstream activating kinases HIPK2 and MAP3K7/TAK1. Interaction with MAP3K7/TAK1 seems to be indirect, and may be mediated by other proteins such as STAT3, TAB1 and TAB2. Interacts with and phosphorylates a number of transcription factors including FOXO4, LEF1, MYB, MYBL1, MYBL2, NOTCH1 and TCF7L2/TCF4. May interact with components of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts with MEF2A. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly nuclear. A smaller fraction is cytoplasmic. Ref.1 Ref.19

Tissue specificity

Expressed at high levels in the brain, and at lower levels in heart, kidney, lung and liver. Ref.1

Domain

Contains a TQE activation loop motif in which autophosphorylation of the threonine residue (Thr-298) is sufficient for kinase activation. This mode of activation contrasts with that of classical MAP kinases, which contain a TXY activation loop motif in which phosphorylation of both the threonine and tyrosine residues is required for kinase activation.

Post-translational modification

Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. Ref.1 Ref.4 Ref.16 Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAC24499.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.1. Source: GOC

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of Wnt signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: MGI

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.8. Source: UniProtKB

serine phosphorylation of STAT3 protein

Inferred from direct assay Ref.9. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

MAP kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

SH2 domain binding

Inferred from physical interaction Ref.9. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.1. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay Ref.9. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hipk2Q9QZR52EBI-366894,EBI-366905

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Serine/threonine-protein kinase NLK
PRO_0000186337

Regions

Domain138 – 427290Protein kinase
Nucleotide binding144 – 1529ATP By similarity
Region1 – 304304Required for interaction with TAB2
Region1 – 125125Sufficient for interaction with DAPK3 By similarity
Region124 – 416293Sufficient for interaction with DAPK3 By similarity
Region428 – 527100Required for homodimerization and kinase activation and localization to the nucleus
Region434 – 52794Required for interaction with TAB2
Motif298 – 3003TQE
Compositional bias22 – 254Poly-Ala
Compositional bias27 – 348Poly-His
Compositional bias42 – 487Poly-His
Compositional bias71 – 8313Poly-Ala
Compositional bias106 – 1116Poly-Ala
Compositional bias115 – 1195Poly-Ala

Sites

Active site2641Proton acceptor By similarity
Binding site1671ATP Probable

Amino acid modifications

Modified residue2981Phosphothreonine; by autocatalysis Ref.19
Modified residue5221Phosphoserine By similarity

Experimental info

Mutagenesis1671K → M: Abrogates kinase activity and autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce ubiquitination and degradation of LEF1 and repress canonical Wnt/beta-catenin signaling. Abrogates ability to induce MYB degradation, and reduces ability to repress MYBL1 and MYBL2. Ref.1 Ref.4 Ref.7 Ref.10 Ref.12 Ref.16 Ref.17 Ref.19
Mutagenesis2981T → D or E: Abrogates autophosphorylation. Ref.1 Ref.10 Ref.19
Mutagenesis2981T → V: Abrogates autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce MYB degradation. Ref.1 Ref.10 Ref.19
Mutagenesis4371C → S: Retains kinase activity. Ref.4 Ref.19
Mutagenesis4371C → Y: Abrogates homodimerization and intermolecular autophosphorylation, with consequent loss of kinase activity. Loss of nuclear localization. Ref.4 Ref.19
Sequence conflict691S → P in AAC24499. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54949 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: CE6D5DCCB9133989

FASTA52758,313
        10         20         30         40         50         60 
MSLCGTRANA KMMAAYNGGT SAAAAGHHHH HHHHLPHLPP PHLHHHHHPQ HHLHPGSAAA 

        70         80         90        100        110        120 
VHPVQQHTSS AAAAAAAAAA AAAMLNPGQQ QPYFPSPAPG QAPGPAAAAP AQVQAAAAAT 

       130        140        150        160        170        180 
VKAHHHQHSH HPQQQLDIEP DRPIGYGAFG VVWSVTDPRD GKRVALKKMP NVFQNLVSCK 

       190        200        210        220        230        240 
RVFRELKMLC FFKHDNVLSA LDILQPPHID YFEEIYVVTE LMQSDLHKII VSPQPLSSDH 

       250        260        270        280        290        300 
VKVFLYQILR GLKYLHSAGI LHRDIKPGNL LVNSNCVLKI CDFGLARVEE LDESRHMTQE 

       310        320        330        340        350        360 
VVTQYYRAPE ILMGSRHYSN AIDIWSVGCI FAELLGRRIL FQAQSPIQQL DLITDLLGTP 

       370        380        390        400        410        420 
SLEAMRTACE GAKAHILRGP HKQPSLPVLY TLSSQATHEA VHLLCRMLVF DPSKRISAKD 

       430        440        450        460        470        480 
ALAHPYLDEG RLRYHTCMCK CCFSTSTGRV YTSDFEPVTN PKFDDTFEKN LSSVRQVKEI 

       490        500        510        520 
IHQFILEQQK GNRVPLCINP QSAAFKSFIS STVAQPSEMP PSPLVWE 

« Hide

References

« Hide 'large scale' references
[1]"Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus."
Brott B.K., Pinsky B.A., Erikson R.L.
Proc. Natl. Acad. Sci. U.S.A. 95:963-968(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-167 AND THR-298.
Strain: BALB/c.
Tissue: Brain.
[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]"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 and FVB/N.
Tissue: Brain and Kidney.
[4]"The TAK1-NLK-MAPK-related pathway antagonizes signalling between beta-catenin and transcription factor TCF."
Ishitani T., Ninomiya-Tsuji J., Nagai S., Nishita M., Meneghini M., Barker N., Waterman M., Bowerman B., Clevers H., Shibuya H., Matsumoto K.
Nature 399:798-802(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF LYS-167 AND CYS-437.
[5]"Abnormal bone marrow stroma in mice deficient for nemo-like kinase, Nlk."
Kortenjann M., Nehls M., Smith A.J., Carsetti R., Schuler J., Kohler G., Boehm T.
Eur. J. Immunol. 31:3580-3587(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The TAK1-NLK mitogen-activated protein kinase cascade functions in the Wnt-5a/Ca(2+) pathway to antagonize Wnt/beta-catenin signaling."
Ishitani T., Kishida S., Hyodo-Miura J., Ueno N., Yasuda J., Waterman M., Shibuya H., Moon R.T., Ninomiya-Tsuji J., Matsumoto K.
Mol. Cell. Biol. 23:131-139(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[7]"Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-activated protein kinase-related Nemo-like kinase-dependent phosphorylation in Wnt/beta-catenin signaling."
Ishitani T., Ninomiya-Tsuji J., Matsumoto K.
Mol. Cell. Biol. 23:1379-1389(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LEF1 AND TCF7L2, MUTAGENESIS OF LYS-167.
[8]"Nemo-like kinase suppresses a wide range of transcription factors, including nuclear factor-kappaB."
Yasuda J., Yokoo H., Yamada T., Kitabayashi I., Sekiya T., Ichikawa H.
Cancer Sci. 95:52-57(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm induction."
Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N., Matsumoto K., Shibuya H.
Genes Dev. 18:381-386(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH STAT3.
[10]"Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK."
Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S.
Genes Dev. 18:816-829(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYB AND HIPK2, MUTAGENESIS OF LYS-167 AND THR-298.
[11]"Differential sensitivity of v-Myb and c-Myb to Wnt-1-induced protein degradation."
Kanei-Ishii C., Nomura T., Tanikawa J., Ichikawa-Iwata E., Ishii S.
J. Biol. Chem. 279:44582-44589(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYB.
[12]"The Wnt-NLK signaling pathway inhibits A-Myb activity by inhibiting the association with coactivator CBP and methylating histone H3."
Kurahashi T., Nomura T., Kanei-Ishii C., Shinkai Y., Ishii S.
Mol. Biol. Cell 16:4705-4713(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MYBL1 AND MYBL2, MUTAGENESIS OF LYS-167.
[13]"Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior formation in Xenopus development."
Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T., Shibuya H.
Mol. Cell. Biol. 27:7623-7630(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MEF2A.
[14]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[15]"Fbxw7 acts as an E3 ubiquitin ligase that targets c-Myb for nemo-like kinase (NLK)-induced degradation."
Kanei-Ishii C., Nomura T., Takagi T., Watanabe N., Nakayama K.I., Ishii S.
J. Biol. Chem. 283:30540-30548(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E3 UBIQUITIN-PROTEIN LIGASE COMPLEXES.
[16]"TAB2 scaffolds TAK1 and NLK in repressing canonical Wnt signaling."
Li M., Wang H., Huang T., Wang J., Ding Y., Li Z., Zhang J., Li L.
J. Biol. Chem. 285:13397-13404(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH MAP3K7 AND TAB2, MUTAGENESIS OF LYS-167.
[17]"Nemo-like kinase suppresses Notch signalling by interfering with formation of the Notch active transcriptional complex."
Ishitani T., Hirao T., Suzuki M., Isoda M., Ishitani S., Harigaya K., Kitagawa M., Matsumoto K., Itoh M.
Nat. Cell Biol. 12:278-285(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NOTCH1, MUTAGENESIS OF LYS-167.
[18]"Oxidative stress-dependent regulation of Forkhead box O4 activity by nemo-like kinase."
Szypowska A.A., de Ruiter H., Meijer L.A.T., Smits L.M.M., Burgering B.M.T.
Antioxid. Redox Signal. 14:563-578(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FOXO4.
[19]"Homodimerization of Nemo-like kinase is essential for activation and nuclear localization."
Ishitani S., Inaba K., Matsumoto K., Ishitani T.
Mol. Biol. Cell 22:266-277(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-298, MUTAGENESIS OF LYS-167; THR-298 AND CYS-437.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036332 mRNA. Translation: AAC24499.1. Different initiation.
AL591177, AL591376 Genomic DNA. Translation: CAI25549.2.
AL591376, AL591177 Genomic DNA. Translation: CAI25603.2.
BC057667 mRNA. Translation: AAH57667.2.
BC058652 mRNA. Translation: AAH58652.2.
CCDSCCDS25113.2.
RefSeqNP_032728.3. NM_008702.3.
UniGeneMm.9001.

3D structure databases

ProteinModelPortalO54949.
SMRO54949. Positions 144-521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO54949. 2 interactions.

PTM databases

PhosphoSiteO54949.

Proteomic databases

PaxDbO54949.
PRIDEO54949.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000142739; ENSMUSP00000119345; ENSMUSG00000017376.
GeneID18099.
KEGGmmu:18099.
UCSCuc007kjw.1. mouse.

Organism-specific databases

CTD51701.
MGIMGI:1201387. Nlk.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110881.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidQ5SYE6.
KOK04468.
OMACKCCYTT.
OrthoDBEOG72RMZ3.
PhylomeDBO54949.
TreeFamTF315210.

Gene expression databases

ArrayExpressO54949.
BgeeO54949.
CleanExMM_NLK.
GenevestigatorO54949.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNLK. mouse.
NextBio293259.
PROO54949.
SOURCESearch...

Entry information

Entry nameNLK_MOUSE
AccessionPrimary (citable) accession number: O54949
Secondary accession number(s): Q5SYE6, Q6PF98
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 3, 2009
Last modified: July 9, 2014
This is version 122 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