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Q07832 (PLK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PLK1

EC=2.7.11.21
Alternative name(s):
Polo-like kinase 1
Short name=PLK-1
Serine/threonine-protein kinase 13
Short name=STPK13
Gene names
Name:Plk1
Synonyms:Plk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, PLK1S1/KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating PLK1S1/KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis.Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning By similarity. Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation of Thr-210 by AURKA; phosphorylation by AURKA is enhanced by BORA. Once activated, activity is stimulated by binding target proteins. Binding of target proteins has no effect on the non-activated kinase. Several inhibitors targeting PLKs are currently in development and are under investigation in a growing number of clinical trials, such as BI 2536, an ATP-competitive PLK1 inhibitor or BI 6727, a dihydropteridinone that specifically inhibits the catalytic activity of PLK1 By similarity.

Subunit structure

Interacts with CEP170 and EVI5. Interacts and phosphorylates ERCC6L. Interacts with FAM29A. Interacts with SLX4/BTBD12 and TTDN1. Interacts with BUB1B. Interacts (via POLO-box domain) with the phosphorylated form of BUB1, CENPU and CDC25C. Interacts with isoform 3of SGOL1. Interacts with BORA, KIF2A and AURKA. Interacts with TOPORS and CYLD. Interacts with ECT2; the interaction is stimulated upon phosphorylation of ECT2 on 'Thr-444'. Interacts with PRC1. Interacts with KIF20A/MKLP2 (when phosphorylated), leading to the recruitment at the central spindle. Interacts (via POLO box domains) with PPP1R12A/MYPT1 (when previously phosphorylated by CDK1) By similarity. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2 By similarity. Interacts with BIRC6/bruce By similarity. Interacts with CDK1-phosphorylated DCTN6 during mitotic prometaphase; the interaction facilitates recruitment to kinetochores By similarity. Interacts with CDK1-phosphorylated FRY; this interaction occurs in mitotic cells, but not in interphase cells. FRY interaction facilitates AURKA-mediated PLK1 phosphorylation. Ref.7

Subcellular location

Nucleus By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Midbody By similarity. Note: During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGOL1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1 By similarity. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle By similarity.

Tissue specificity

Newborn and adult spleen, fetal and newborn kidney, liver, brain, thymus and adult bone marrow, thymus, ovary and testes.

Developmental stage

In the thymus, levels increased during fetal development, were highest in newborn animals and decreased in the adult. In the testes, the PLK levels were higher in the adult than in prepubescent mice while in the ovary, the levels were higher in the prepubescent mice. Accumulates to a maximum during the G2 and M phases, declines to a nearly undetectable level following mitosis and throughout G1 phase, and then begins to accumulate again during S phase.

Domain

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains By similarity.

Post-translational modification

Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase. Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1. Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint. Phosphorylated in vitro by STK10 By similarity.

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in anaphase and following DNA damage, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry into mitosis and is essential to maintain an efficient G2 DNA damage checkpoint. Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not lead to degradation: it promotes PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation By similarity.

Disruption phenotype

Lethality: homozygous embryos do not develop beyond the eight cell stage. Heterozygous mice are healthy and fertile but frequently develop tumors, most frequently lung-invading and liver-invading lymphomas. Analysis of chromosome spreads of spleen-derived cells from 6-month-old mice show aneuploidy. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Contains 2 POLO box domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

activation of mitotic anaphase-promoting complex activity

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic sister chromatid segregation

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic spindle assembly checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

polar body extrusion after meiotic divisions

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from electronic annotation. Source: Ensembl

protein localization to chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

condensed nuclear chromosome outer kinetochore

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from sequence or structural similarity. Source: UniProtKB

spindle microtubule

Inferred from electronic annotation. Source: Ensembl

spindle midzone

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 603602Serine/threonine-protein kinase PLK1
PRO_0000086557

Regions

Domain53 – 305253Protein kinase
Domain417 – 48064POLO box 1
Domain515 – 58470POLO box 2
Nucleotide binding59 – 679ATP By similarity
Nucleotide binding178 – 1814ATP By similarity
Region194 – 22128Activation loop By similarity
Region493 – 50715Linker By similarity
Region538 – 5403Important for interaction with phosphorylated proteins By similarity
Motif337 – 3404D-box that targets the protein for proteasomal degradation in anaphase By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site821ATP By similarity
Binding site1311ATP; via carbonyl oxygen By similarity
Binding site1941ATP By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity
Modified residue2101Phosphothreonine; by AURKA By similarity
Modified residue2141Phosphothreonine By similarity
Modified residue2691Phosphoserine; by autocatalysis By similarity
Modified residue3351Phosphoserine; by autocatalysis By similarity
Modified residue3751Phosphoserine By similarity
Modified residue4501Phosphoserine By similarity
Modified residue4981Phosphothreonine By similarity
Cross-link19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis821K → M: Abolishes activity. Ref.5
Mutagenesis1941D → N or R: Abolishes activity. Ref.5
Mutagenesis2061E → D: No change in activity. Ref.5
Mutagenesis2061E → V: Decreases activity three-fold. Ref.5
Mutagenesis2101T → E: Increases activity four-fold. Ref.5
Mutagenesis2101T → V: Decreases activity three-fold. Ref.5
Sequence conflict41A → V in AAA39948. Ref.1
Sequence conflict151A → T in AAA39948. Ref.1
Sequence conflict231P → L in AAA39948. Ref.1
Sequence conflict271V → A in AAA39948. Ref.1
Sequence conflict291G → S in AAA39948. Ref.1
Sequence conflict411P → L in AAA39948. Ref.1
Sequence conflict541V → I in AAA39948. Ref.1
Sequence conflict4951A → R in AAA39948. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07832 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 1B980646366EFA10

FASTA60368,301
        10         20         30         40         50         60 
MNAAAKAGKL ARAPADLGKG GVPGDAVPGA PVAAPLAKEI PEVLVDPRSR RQYVRGRFLG 

        70         80         90        100        110        120 
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQKEKMSM EISIHRSLAH QHVVGFHDFF 

       130        140        150        160        170        180 
EDSDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN QVIHRDLKLG 

       190        200        210        220        230        240 
NLFLNEDLEV KIGDFGLATK VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 

       250        260        270        280        290        300 
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL 

       310        320        330        340        350        360 
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSSRKPL KVLNKGVENP LPDRPREKEE 

       370        380        390        400        410        420 
PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 

       430        440        450        460        470        480 
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLN 

       490        500        510        520        530        540 
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK 

       550        560        570        580        590        600 
LILCPLMAAV TYINEKRDFQ TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 


KAS 

« Hide

References

« Hide 'large scale' references
[1]"Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila."
Clay F.J., McEwen S.J., Bertoncello I., Wilks A.F., Dunn A.R.
Proc. Natl. Acad. Sci. U.S.A. 90:4882-4886(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Bone marrow.
[2]"Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase."
Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L., Ferris D.K.
Cell Growth Differ. 5:249-257(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Thymus.
[3]"Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase."
Lake R.J., Jelinek W.R.
Mol. Cell. Biol. 13:7793-7801(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[4]"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: FVB/N.
Tissue: Mammary gland.
[5]"Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures."
Lee K.S., Erikson R.L.
Mol. Cell. Biol. 17:3408-3417(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-82; ASP-194; GLU-206 AND THR-210.
[6]"Polo-like kinase 1 is essential for early embryonic development and tumor suppression."
Lu L.Y., Wood J.L., Minter-Dykhouse K., Ye L., Saunders T.L., Yu X., Chen J.
Mol. Cell. Biol. 28:6870-6876(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
Ikeda M., Chiba S., Ohashi K., Mizuno K.
J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRY.
[8]"Tex14, a plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint."
Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.
Mol. Cell 45:680-695(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TEX14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06144 mRNA. Translation: AAA39948.1.
U01063 mRNA. Translation: AAA56635.1.
L19558 mRNA. Translation: AAA16071.1.
BC006880 mRNA. Translation: AAH06880.1.
PIRA47545.
A54596.
RefSeqNP_035251.3. NM_011121.3.
UniGeneMm.16525.

3D structure databases

ProteinModelPortalQ07832.
SMRQ07832. Positions 39-328, 372-594.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202250. 30 interactions.
IntActQ07832. 27 interactions.
MINTMINT-4596676.

PTM databases

PhosphoSiteQ07832.

Proteomic databases

PaxDbQ07832.
PRIDEQ07832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033154; ENSMUSP00000033154; ENSMUSG00000030867.
GeneID18817.
KEGGmmu:18817.
UCSCuc009joo.2. mouse.

Organism-specific databases

CTD5347.
MGIMGI:97621. Plk1.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000248546.
HOVERGENHBG001843.
InParanoidQ07832.
KOK06631.
OMALCKKGHS.
OrthoDBEOG78M01K.
PhylomeDBQ07832.
TreeFamTF101089.

Gene expression databases

ArrayExpressQ07832.
BgeeQ07832.
CleanExMM_PLK1.
GenevestigatorQ07832.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
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.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295174.
PROQ07832.
SOURCESearch...

Entry information

Entry namePLK1_MOUSE
AccessionPrimary (citable) accession number: Q07832
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 141 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