Reviewed, UniProtKB/Swiss-Prot Q13164 (MK07_HUMAN)

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase 7
      Short name=MAP kinase 7
      Short name=MAPK 7
    EC=2.7.11.24
Alternative name(s):
    Extracellular signal-regulated kinase 5
      Short name=ERK-5
    Big MAP kinase 1
      Short name=BMK-1

Gene names

Name:	MAPK7
Synonyms:	BMK1, ERK5, PRKM7

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	816 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.8 Ref.9 Ref.10
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by tyrosine and threonine phosphorylation By similarity. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF). Ref.8 Ref.9
Subunit structure	Interacts with MAP2K5. Forms oligomers By similarity. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D By similarity. Ref.2
Subcellular location	Cytoplasm. Nucleus. Note: Translocates to the nucleus upon activation. Ref.8
Tissue specificity	Expressed in many adult tissues. Abundant in heart, placenta, lung, kidney and skeletal muscle. Not detectable in liver. 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. Autophosphorylated in vitro on threonine and tyrosine residues when the C-terminal part of the kinase, which could have a regulatory role, is absent. Ref.11 Ref.12
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 AAA81381.1 differs from that shown. Reason: Frameshift at positions 19 and 32.

Ontologies

Keywords
Biological process	Cell cycle Differentiation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.2 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAP2K5	Q13163	1	EBI-1213983,EBI-307294

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13164-1)

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: Q13164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q13164-3)

The sequence of this isoform differs from the canonical sequence as follows:
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

Isoform 4 (identifier: Q13164-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: MAEPLKEEDG...TVPYGEFKSV → MLFFHTMPSA...HASLLPSPSS
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 816	815	Mitogen-activated protein kinase 7		PRO_0000186260
Regions
	Domain	55 – 347	293	Protein kinase
	Nucleotide binding	61 – 69	9	ATP By similarity
	Region	2 – 77	76	Required for cytoplasmic targeting By similarity
	Region	78 – 139	62	Required for binding to MAP2K5 By similarity
	Region	140 – 406	267	Necessary for oligomerization By similarity
	Region	407 – 806	400	May not be required for kinase activity; required to stimulate MEF2C activity By similarity
	Region	505 – 539	35	Nuclear localization signal By similarity
	Motif	219 – 221	3	TXY
	Compositional bias	338 – 341	4	Poly-Ala
	Compositional bias	403 – 694	292	Pro-rich
	Compositional bias	513 – 543	31	Arg-rich
Sites
	Active site	182	1	Proton acceptor By similarity
	Binding site	84	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	219	1	Phosphothreonine By similarity
	Modified residue	221	1	Phosphotyrosine Ref.11
	Modified residue	720	1	Phosphoserine Ref.12
	Modified residue	731	1	Phosphoserine
	Modified residue	733	1	Phosphothreonine Ref.12
Natural variations
	Alternative sequence	1 – 139	139	Missing in isoform 2.		VSP_035198
	Alternative sequence	1 – 133	133	MAEPL…EFKSV → MLFFHTMPSAPMGSQGKAVT CLESEGCGEDGACPWSVIRP THASLLPSPSS in isoform 4.		VSP_035199
	Alternative sequence	493 – 816	324	DGPSA…DLQDP → GALWAGRVGRGETWTWTRLQ AFTFSPAQLPRKWPQRTPGG S in isoform 3 and isoform 4.		VSP_035200
	Natural variant	535	1	R → H		VAR_046225
	Natural variant	550	1	G → A: dbSNP rs56388327. Ref.14		VAR_042257
Experimental info
	Mutagenesis	219 – 221	3	TEY → AEF: Loss activation by MAP2K5. Ref.8
	Sequence conflict	610	1	V → L in AAA81381. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 27729FE31658CE3B	FASTA	816	88,386
	10 20 30 40 50 60 MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD VGDEYEIIET 70 80 90 100 110 120 IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 130 140 150 160 170 180 LRPTVPYGEF KSVYVVLDLM 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 EPGCPDVEMP 430 440 450 460 470 480 SPWAPSGDCA MESPPPAPPP CPGPAPDTID LTLQPPPPVS EPAPPKKDGA ISDNTKAALK 490 500 510 520 530 540 AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 550 560 570 580 590 600 KERGAGASGG PSTDPLAGLV LSDNDRSLLE RWTRMARPAA PALTSVPAPA PAPTPTPTPV 610 620 630 640 650 660 QPTSPPPGPV AQPTGPQPQS AGSTSGPVPQ PACPPPGPAP HPTGPPGPIP VPAPPQIATS 670 680 690 700 710 720 TSLLAAQSLV PPPGLPGSST PGVLPYFPPG LPPPDAGGAP QSSMSESPDV NLVTQQLSKS 730 740 750 760 770 780 QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD 790 800 810 WLEGHGMNPA DIESLQREIQ MDSPMLLADL PDLQDP
	Isoform 2. Checksum: EC01D3784EB8AAB0	FASTA	677	73,218
	10 20 30 40 50 60 MESDLHQIIH SSQPLTLEHV RYFLYQLLRG LKYMHSAQVI HRDLKPSNLL VNENCELKIG 70 80 90 100 110 120 DFGMARGLCT SPAEHQYFMT EYVATRWYRA PELMLSLHEY TQAIDLWSVG CIFGEMLARR 130 140 150 160 170 180 QLFPGKNYVH QLQLIMMVLG TPSPAVIQAV GAERVRAYIQ SLPPRQPVPW ETVYPGADRQ 190 200 210 220 230 240 ALSLLGRMLR FEPSARISAA AALRHPFLAK YHDPDDEPDC APPFDFAFDR EALTRERIKE 250 260 270 280 290 300 AIVAEIEDFH ARREGIRQQI RFQPSLQPVA SEPGCPDVEM PSPWAPSGDC AMESPPPAPP 310 320 330 340 350 360 PCPGPAPDTI DLTLQPPPPV SEPAPPKKDG AISDNTKAAL KAALLKSLRS RLRDGPSAPL 370 380 390 400 410 420 EAPEPRKPVT AQERQREREE KRRRRQERAK EREKRRQERE RKERGAGASG GPSTDPLAGL 430 440 450 460 470 480 VLSDNDRSLL ERWTRMARPA APALTSVPAP APAPTPTPTP VQPTSPPPGP VAQPTGPQPQ 490 500 510 520 530 540 SAGSTSGPVP QPACPPPGPA PHPTGPPGPI PVPAPPQIAT STSLLAAQSL VPPPGLPGSS 550 560 570 580 590 600 TPGVLPYFPP GLPPPDAGGA PQSSMSESPD VNLVTQQLSK SQVEDPLPPV FSGTPKGSGA 610 620 630 640 650 660 GYGVGFDLEE FLNQSFDMGV ADGPQDGQAD SASLSASLLA DWLEGHGMNP ADIESLQREI 670 QMDSPMLLAD LPDLQDP
	Isoform 3. Checksum: 6E654D7CA1287E32	FASTA	533	59,328
	10 20 30 40 50 60 MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD VGDEYEIIET 70 80 90 100 110 120 IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 130 140 150 160 170 180 LRPTVPYGEF KSVYVVLDLM 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 EPGCPDVEMP 430 440 450 460 470 480 SPWAPSGDCA MESPPPAPPP CPGPAPDTID LTLQPPPPVS EPAPPKKDGA ISDNTKAALK 490 500 510 520 530 AALLKSLRSR LRGALWAGRV GRGETWTWTR LQAFTFSPAQ LPRKWPQRTP GGS
	Isoform 4. Checksum: E0FAC412C3DE60F9	FASTA	451	50,152
	10 20 30 40 50 60 MLFFHTMPSA PMGSQGKAVT CLESEGCGED GACPWSVIRP THASLLPSPS SYVVLDLMES 70 80 90 100 110 120 DLHQIIHSSQ PLTLEHVRYF LYQLLRGLKY MHSAQVIHRD LKPSNLLVNE NCELKIGDFG 130 140 150 160 170 180 MARGLCTSPA EHQYFMTEYV ATRWYRAPEL MLSLHEYTQA IDLWSVGCIF GEMLARRQLF 190 200 210 220 230 240 PGKNYVHQLQ LIMMVLGTPS PAVIQAVGAE RVRAYIQSLP PRQPVPWETV YPGADRQALS 250 260 270 280 290 300 LLGRMLRFEP SARISAAAAL RHPFLAKYHD PDDEPDCAPP FDFAFDREAL TRERIKEAIV 310 320 330 340 350 360 AEIEDFHARR EGIRQQIRFQ PSLQPVASEP GCPDVEMPSP WAPSGDCAME SPPPAPPPCP 370 380 390 400 410 420 GPAPDTIDLT LQPPPPVSEP APPKKDGAIS DNTKAALKAA LLKSLRSRLR GALWAGRVGR 430 440 450 GETWTWTRLQ AFTFSPAQLP RKWPQRTPGG S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of BMK1: a new mammalian map kinase." Lee J.-D., Ulevitch R.J., Han J. Biochem. Biophys. Res. Commun. 213:715-724(1995) [PubMed: 7646528] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Placenta.
[2]	"Components of a new human protein kinase signal transduction pathway." Zhou G., Bao Z.Q., Dixon J.E. J. Biol. Chem. 270:12665-12669(1995) [PubMed: 7759517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAP2K5, TISSUE SPECIFICITY. Tissue: Fetal brain.
[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: 15716121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Placenta.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Spleen.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Muscle and Pancreas.
[7]	Bienvenut W.V., Fleming J., Leug H.Y. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-35; 75-98; 119-131; 198-205; 296-343; 377-392; 468-485; 489-505; 544-571; 720-735 AND 798-816, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[8]	"BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C." Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D. EMBO J. 16:7054-7066(1997) [PubMed: 9384584] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 219-THR--TYR-221.
[9]	"Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor." Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., Lee J.-D. Nature 395:713-716(1998) [PubMed: 9790194] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[10]	"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: 11278431] [Abstract] Cited for: FUNCTION.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, MASS SPECTROMETRY. Tissue: Lung.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, MASS SPECTROMETRY.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221; SER-731 AND THR-733, MASS SPECTROMETRY.
[14]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-535 AND ALA-550.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U29725 mRNA. Translation: AAA82931.1. U29726 mRNA. Translation: AAA82932.1. U29727 Genomic DNA. Translation: AAA82933.1. U25278 mRNA. Translation: AAA81381.1. Frameshift. AY534741 mRNA. Translation: AAS38577.1. AB209611 mRNA. Translation: BAD92848.1. Different initiation. CH471212 Genomic DNA. Translation: EAW50883.1. CH471212 Genomic DNA. Translation: EAW50886.1. BC007404 mRNA. Translation: AAH07404.1. BC007992 mRNA. Translation: AAH07992.1. BC009963 mRNA. Translation: AAH09963.1. BC030134 mRNA. Translation: AAH30134.1.
IPI	IPI00149048. IPI00219601. IPI00426283. IPI00555640.
PIR	B56708.
RefSeq	NP_002740.2. NP_620601.1. NP_620602.2. NP_620603.2.
UniGene	Hs.150136
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13164. 1 interaction.
STRING	Q13164.
PTM databases
PhosphoSite	Q13164.
Proteomic databases
PRIDE	Q13164.
Genome annotation databases
Ensembl	ENST00000308406; ENSP00000311005; ENSG00000166484; Homo sapiens. [Genome view] ENST00000395602; ENSP00000378966; ENSG00000166484; Homo sapiens. [Genome view] ENST00000395604; ENSP00000378968; ENSG00000166484; Homo sapiens. [Genome view]
GeneID	5598.
KEGG	hsa:5598.
Organism-specific databases
CTD	5598.
GeneCards	GC17P019221.
HGNC	HGNC:6880. MAPK7.
HPA	CAB018561.
MIM	602521. gene.
PharmGKB	PA30625.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04009.
HOVERGEN	Q13164.
InParanoid	Q13164.
OMA	VADGPQD.
PhylomeDB	Q13164.
Enzyme and pathway databases
BRENDA	2.7.11.24. 247.
Pathway_Interaction_DB	mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.
Reactome	REACT_11061. Signalling by NGF.
Gene expression databases
ArrayExpress	Q13164.
Bgee	Q13164.
CleanEx	HS_MAPK7.
Genevestigator	Q13164.
GermOnline	ENSG00000166484. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	21728.
SOURCE	Search...

Entry information

Entry name

MK07_HUMAN

Accession

Primary (citable) accession number: Q13164
Secondary accession number(s): Q16634 , Q59F50, Q6QLU7, Q7L4P4, Q969G1, Q96G51

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 2, 2008
Last modified:	February 9, 2010
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.