Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9WVS8 (MK07_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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:
Mitogen-activated protein kinase 7

Short name=MAP kinase 7
Short name=MAPK 7
EC=2.7.11.24
Alternative name(s):
Big MAP kinase 1
Short name=BMK-1
Extracellular signal-regulated kinase 5
Short name=ERK-5
Gene names
Name:Mapk7
Synonyms:Bmk1, Erk5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression By similarity. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction By similarity. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF) By similarity.

Subunit structure

Interacts with MAP2K5 By similarity. Forms oligomers. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D By similarity. Interacts with SGK1 By similarity. Interacts with PML By similarity. Ref.2

Subcellular location

Cytoplasm. Nucleus. NucleusPML body By similarity. Note: Translocates to the nucleus upon activation By similarity. Ref.2

Isoform 1: Cytoplasm By similarity. Nucleus By similarity. Note: Isoform 1 is detected in cytoplasm and nucleus By similarity. Ref.2

Isoform 2: Nucleus By similarity. Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity. Ref.2

Isoform 3: Nucleus By similarity. Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity. Ref.2

Tissue specificity

Detected in testis, brain, kidney, lung and heart. Detected in total embryo (at protein level). Ref.2

Domain

The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell.

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Differentiation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of NFAT protein import into nucleus

Inferred from mutant phenotype PubMed 18347059. Source: MGI

negative regulation of apoptotic process

Inferred from direct assay PubMed 14675480. Source: MGI

negative regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of heterotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of response to cytokine stimulus

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18347059. Source: MGI

positive regulation of protein metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 14515274. Source: UniProtKB

regulation of angiogenesis

Inferred from mutant phenotype PubMed 12221099. Source: MGI

   Cellular_componentPML body

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 18347059. Source: MGI

nucleus

Inferred from direct assay PubMed 18347059. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase activity

Inferred from direct assay PubMed 14515274. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 18347059. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WVS8-1)

Also known as: Big MAP kinase 1a; mERK5a;

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: Q9WVS8-2)

Also known as: Big MAP kinase 1b; mERK5b;

The sequence of this isoform differs from the canonical sequence as follows:
     2-77: AEPLKEEDGE...VVSSARRRLT → MCGLLSRG
Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.
Isoform 3 (identifier: Q9WVS8-3)

Also known as: Big MAP kinase 1c; mERK5c;

The sequence of this isoform differs from the canonical sequence as follows:
     2-139: Missing.
Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.
Isoform 4 (identifier: Q9WVS8-4)

Also known as: Big MAP kinase 1d; mERK5-T;

The sequence of this isoform differs from the canonical sequence as follows:
     493-806: DGPSAPLEAP...LSDLPDLQEP → GGVWAQQLSG
Note: Unable to translocate from the cytoplasm to the nucleus.
Isoform 5 (identifier: Q9WVS8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     757-806: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 806805Mitogen-activated protein kinase 7
PRO_0000186261

Regions

Domain55 – 347293Protein kinase
Nucleotide binding61 – 699ATP By similarity
Region2 – 7776Required for cytoplasmic targeting
Region78 – 13962Required for binding to MAP2K5
Region140 – 406267Necessary for oligomerization
Region407 – 806400May not be required for kinase activity; required to stimulate MEF2C activity
Region505 – 53935Nuclear localization signal
Motif219 – 2213TXY
Compositional bias434 – 46532Pro-rich
Compositional bias521 – 5244Poly-Arg
Compositional bias578 – 700123Pro-rich

Sites

Active site1821Proton acceptor By similarity
Binding site841ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue7101Phosphoserine By similarity
Modified residue7231Phosphothreonine By similarity

Natural variations

Alternative sequence2 – 139138Missing in isoform 3.
VSP_035201
Alternative sequence2 – 7776AEPLK…RRRLT → MCGLLSRG in isoform 2.
VSP_035202
Alternative sequence493 – 806314DGPSA…DLQEP → GGVWAQQLSG in isoform 4.
VSP_035203
Alternative sequence757 – 80650Missing in isoform 5.
VSP_035204

Experimental info

Sequence conflict1911N → D in BAE28357. Ref.4
Sequence conflict3081P → H in BAE28357. Ref.4
Sequence conflict3311E → K in AAI00399. Ref.5
Sequence conflict4091A → V in AAD39394. Ref.2
Sequence conflict4091A → V in AAD39395. Ref.2
Sequence conflict4091A → V in AAD39396. Ref.2
Sequence conflict4241A → R in AAD39394. Ref.2
Sequence conflict4241A → R in AAD39395. Ref.2
Sequence conflict4241A → R in AAD39396. Ref.2
Sequence conflict5781P → PPAPA in BAE28357. Ref.4
Sequence conflict5781P → PPAPA in BAE33103. Ref.4
Sequence conflict5881A → R in AAD39394. Ref.2
Sequence conflict5881A → R in AAD39395. Ref.2
Sequence conflict5881A → R in AAD39396. Ref.2
Sequence conflict5921A → Q in AAD39394. Ref.2
Sequence conflict5921A → Q in AAD39395. Ref.2
Sequence conflict5921A → Q in AAD39396. Ref.2
Sequence conflict6181S → C in AAD39394. Ref.2
Sequence conflict6181S → C in AAD39395. Ref.2
Sequence conflict6181S → C in AAD39396. Ref.2
Sequence conflict6421P → A in AAD39394. Ref.2
Sequence conflict6421P → A in AAD39395. Ref.2
Sequence conflict6421P → A in AAD39396. Ref.2
Sequence conflict8031L → V in BAE28357. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Big MAP kinase 1a) (mERK5a) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E7CC41C4BBDE0633

FASTA80687,733
        10         20         30         40         50         60 
MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD VGDEYEIIET 

        70         80         90        100        110        120 
IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 

       130        140        150        160        170        180 
LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH 

       190        200        210        220        230        240 
RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT 

       250        260        270        280        290        300 
QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 

       310        320        330        340        350        360 
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA 

       370        380        390        400        410        420 
PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPVCPDVEMP 

       430        440        450        460        470        480 
SPWAPSGDCA MESPPPALPP CSDPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK 

       490        500        510        520        530        540 
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 

       550        560        570        580        590        600 
KERGAGTLGG PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS 

       610        620        630        640        650        660 
TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS TSLLASQSLV 

       670        680        690        700        710        720 
PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV NLVTQQLSKS QVEDPLPPVF 

       730        740        750        760        770        780 
SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD WLEGHGMNPA 

       790        800 
DIESLQREIQ MDSPMLLSDL PDLQEP 

« Hide

Isoform 2 (Big MAP kinase 1b) (mERK5b) [UniParc].

Checksum: 7909E06820499AF5
Show »

FASTA73880,511
Isoform 3 (Big MAP kinase 1c) (mERK5c) [UniParc].

Checksum: 8B0E505EA2545FFA
Show »

FASTA66872,594
Isoform 4 (Big MAP kinase 1d) (mERK5-T) [UniParc].

Checksum: 905BD56BC58913D8
Show »

FASTA50255,914
Isoform 5 [UniParc].

Checksum: C0CCFA5D2F8C84F5
Show »

FASTA75682,314

References

« Hide 'large scale' references
[1]"Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus."
Kamakura S., Moriguchi T., Nishida E.
J. Biol. Chem. 274:26563-26571(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains."
Yan C., Luo H., Lee J.-D., Abe J.-I., Berk B.C.
J. Biol. Chem. 276:10870-10878(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6.
[3]"Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant."
McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.
Gene 345:183-190(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION.
Strain: C57BL/6.
Tissue: Bone marrow.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: NOD.
[5]"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] (ISOFORM 5).
Strain: C57BL/6J.
Tissue: Kidney.
[6]"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.
[7]"Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells."
Dinev D., Jordan B.W.M., Neufeld B., Lee J.-D., Lindemann D., Rapp U.R., Ludwig S.
EMBO Rep. 2:829-834(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival."
Dong F., Gutkind J.S., Larner A.C.
J. Biol. Chem. 276:10811-10816(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure."
Hayashi M., Kim S.W., Imanaka-Yoshida K., Yoshida T., Abel E.D., Eliceiri B., Yang Y., Ulevitch R.J., Lee J.D.
J. Clin. Invest. 113:1138-1148(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB019373 mRNA. Translation: BAA82039.1.
AF126159 mRNA. Translation: AAD39394.1.
AF126160 mRNA. Translation: AAD39395.1.
AF126161 mRNA. Translation: AAD39396.1.
AK148119 mRNA. Translation: BAE28357.1.
AK155187 mRNA. Translation: BAE33103.1.
AY534740 mRNA. Translation: AAS38576.1.
BC100398 mRNA. Translation: AAI00399.1.
AL604029 Genomic DNA. Translation: CAI24182.1.
AL604029 Genomic DNA. Translation: CAI24184.1.
AL604029 Genomic DNA. Translation: CAI24185.1.
RefSeqNP_035971.1. NM_011841.1.
XP_006533340.1. XM_006533277.1.
XP_006533341.1. XM_006533278.1.
UniGeneMm.38172.

3D structure databases

ProteinModelPortalQ9WVS8.
SMRQ9WVS8. Positions 11-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204806. 3 interactions.

PTM databases

PhosphoSiteQ9WVS8.

Proteomic databases

PRIDEQ9WVS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079080; ENSMUSP00000078087; ENSMUSG00000001034. [Q9WVS8-1]
GeneID23939.
KEGGmmu:23939.
UCSCuc007jho.1. mouse. [Q9WVS8-2]
uc007jhp.1. mouse. [Q9WVS8-1]
uc007jht.1. mouse. [Q9WVS8-4]

Organism-specific databases

CTD5598.
MGIMGI:1346347. Mapk7.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOVERGENHBG108137.
InParanoidQ9WVS8.
KOK04464.
OMAIIETIGT.
PhylomeDBQ9WVS8.
TreeFamTF105099.

Gene expression databases

BgeeQ9WVS8.
CleanExMM_MAPK7.
GenevestigatorQ9WVS8.

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

NextBio303745.
PROQ9WVS8.
SOURCESearch...

Entry information

Entry nameMK07_MOUSE
AccessionPrimary (citable) accession number: Q9WVS8
Secondary accession number(s): Q3U2N7 expand/collapse secondary AC list , Q3UG52, Q497T0, Q5NCN6, Q5NCN7, Q5NCN9, Q6QLU8, Q9R1D9, Q9WVF3, Q9WVF4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 121 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