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Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)

 MP2K5_MOUSE             Reviewed;         448 AA.
Q9WVS7; Q8CFM3; Q8K360; Q9D222;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-MAR-2018, entry version 149.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 5;
Short=MAP kinase kinase 5;
Short=MAPKK 5;
EC=2.7.12.2;
AltName: Full=MAPK/ERK kinase 5;
Short=MEK 5;
Name=Map2k5; Synonyms=Mek5, Mkk5, Prkmk5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
SER-311 AND THR-315.
TISSUE=Brain;
PubMed=10473620; DOI=10.1074/jbc.274.37.26563;
Kamakura S., Moriguchi T., Nishida E.;
"Activation of the protein kinase ERK5/BMK1 by receptor tyrosine
kinases. Identification and characterization of a signaling pathway to
the nucleus.";
J. Biol. Chem. 274:26563-26571(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Head, and Hypothalamus;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH SQSTM1; PRKCZ; PRKCI; PARD6A AND MAP3K3, AND DOMAIN.
PubMed=12813044; DOI=10.1074/jbc.M303221200;
Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
Michaelsen E., Bjoerkoey G., Johansen T.;
"Interaction codes within the family of mammalian Phox and Bem1p
domain-containing proteins.";
J. Biol. Chem. 278:34568-34581(2003).
[5]
FUNCTION, DOMAIN, INTERACTION WITH MAP3K2 AND MAPK7, AND MUTAGENESIS
OF ARG-20; ILE-21; ASP-64; GLU-65; GLY-67 AND ASP-68.
PubMed=16507987; DOI=10.1128/MCB.26.6.2065-2079.2006;
Nakamura K., Uhlik M.T., Johnson N.L., Hahn K.M., Johnson G.L.;
"PB1 domain-dependent signaling complex is required for extracellular
signal-regulated kinase 5 activation.";
Mol. Cell. Biol. 26:2065-2079(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
STRUCTURE BY NMR OF 7-107.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PB1 domain of mouse mitogen activated
protein kinase kinase 5 (MAP2K5).";
Submitted (JAN-2006) to the PDB data bank.
-!- FUNCTION: Acts as a scaffold for the formation of a ternary
MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this
pathway appears to play a critical role in protecting cells from
stress-induced apoptosis, neuronal survival and cardiac
development and angiogenesis. {ECO:0000269|PubMed:10473620,
ECO:0000269|PubMed:16507987}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex
with SQSTM1 and PRKCZ or PRKCI. {ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:16507987}.
-!- INTERACTION:
Q61083:Map3k2; NbExp=4; IntAct=EBI-446144, EBI-446134;
Q61084:Map3k3; NbExp=15; IntAct=EBI-446144, EBI-446250;
P28656:Nap1l1; NbExp=20; IntAct=EBI-446144, EBI-645055;
Q64337:Sqstm1; NbExp=3; IntAct=EBI-446144, EBI-645025;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9WVS7-1; Sequence=Displayed;
Name=2;
IsoId=Q9WVS7-2; Sequence=VSP_015840;
Name=3;
IsoId=Q9WVS7-3; Sequence=VSP_015838, VSP_015839;
Name=4;
IsoId=Q9WVS7-4; Sequence=VSP_015836, VSP_015837;
-!- DOMAIN: Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues
of the PB1 domain. This domain also mediates interactions with
SQSTM1 and PARD6A. {ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:16507987}.
-!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
kinases. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB019374; BAA82040.1; -; mRNA.
EMBL; AK020716; BAB32187.1; -; mRNA.
EMBL; BC013697; AAH13697.1; -; mRNA.
EMBL; BC028260; AAH28260.1; -; mRNA.
CCDS; CCDS23269.1; -. [Q9WVS7-1]
RefSeq; NP_035970.1; NM_011840.2. [Q9WVS7-1]
RefSeq; XP_006511208.1; XM_006511145.2. [Q9WVS7-2]
UniGene; Mm.325746; -.
PDB; 1WI0; NMR; -; A=8-107.
PDBsum; 1WI0; -.
ProteinModelPortal; Q9WVS7; -.
SMR; Q9WVS7; -.
CORUM; Q9WVS7; -.
IntAct; Q9WVS7; 11.
STRING; 10090.ENSMUSP00000034920; -.
iPTMnet; Q9WVS7; -.
PhosphoSitePlus; Q9WVS7; -.
PaxDb; Q9WVS7; -.
PRIDE; Q9WVS7; -.
Ensembl; ENSMUST00000034920; ENSMUSP00000034920; ENSMUSG00000058444. [Q9WVS7-1]
GeneID; 23938; -.
KEGG; mmu:23938; -.
UCSC; uc009qaw.1; mouse. [Q9WVS7-1]
UCSC; uc009qaz.1; mouse. [Q9WVS7-4]
UCSC; uc012guv.1; mouse. [Q9WVS7-2]
CTD; 5607; -.
MGI; MGI:1346345; Map2k5.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; Q9WVS7; -.
KO; K04463; -.
OMA; EDLMGHP; -.
OrthoDB; EOG091G06I7; -.
PhylomeDB; Q9WVS7; -.
TreeFam; TF106468; -.
ChiTaRS; Map2k5; mouse.
EvolutionaryTrace; Q9WVS7; -.
PRO; PR:Q9WVS7; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000058444; -.
CleanEx; MM_MAP2K5; -.
Genevisible; Q9WVS7; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005819; C:spindle; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0070375; P:ERK5 cascade; IEA:Ensembl.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0000165; P:MAPK cascade; IMP:MGI.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0060761; P:negative regulation of response to cytokine stimulus; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
CDD; cd06395; PB1_Map2k5; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000270; PB1_dom.
InterPro; IPR034851; PB1_MAP2K5.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00666; PB1; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Tyrosine-protein kinase.
CHAIN 1 448 Dual specificity mitogen-activated
protein kinase kinase 5.
/FTId=PRO_0000086384.
DOMAIN 18 109 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 166 419 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 172 180 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 18 25 Interaction with MAPK7.
{ECO:0000269|PubMed:16507987}.
REGION 64 68 Interaction with MAP3K2/MAP3K3.
{ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:16507987}.
REGION 117 131 Interaction with MAPK7.
{ECO:0000269|PubMed:16507987}.
ACT_SITE 283 283 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 195 195 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:Q13163}.
MOD_RES 315 315 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13163}.
VAR_SEQ 108 118 ACKPPGERNIH -> GYRRGSRLREY (in isoform
4). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_015836.
VAR_SEQ 119 448 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_015837.
VAR_SEQ 183 186 AHHV -> LLHI (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015838.
VAR_SEQ 187 448 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015839.
VAR_SEQ 359 367 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015840.
MUTAGEN 20 20 R->A: Loss of MAPK7 binding; when
associated with A-21.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 21 21 I->A: Loss of MAPK7 binding; when
associated with A-20.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 64 64 D->A: Loss of MAP3K2/MAP3K3 binding; when
associated with A-65.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 65 65 E->A: Loss of MAP3K2/MAP3K3 binding; when
associated with A-64.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 67 67 G->A: Loss of MAP3K2/MAP3K3 binding; when
associated with A-68.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 68 68 D->A: Loss of MAP3K2/MAP3K3 binding; when
associated with A-67.
{ECO:0000269|PubMed:16507987}.
MUTAGEN 311 311 S->A: Dominant negative form; when
associated with V-315.
{ECO:0000269|PubMed:10473620}.
MUTAGEN 311 311 S->D: Dominant active form; when
associated with D-315.
{ECO:0000269|PubMed:10473620}.
MUTAGEN 315 315 T->D: Dominant active form; when
associated with D-311.
{ECO:0000269|PubMed:10473620}.
MUTAGEN 315 315 T->V: Dominant negative form; when
associated with A-311.
{ECO:0000269|PubMed:10473620}.
STRAND 17 22 {ECO:0000244|PDB:1WI0}.
STRAND 28 34 {ECO:0000244|PDB:1WI0}.
STRAND 36 38 {ECO:0000244|PDB:1WI0}.
HELIX 41 51 {ECO:0000244|PDB:1WI0}.
STRAND 60 62 {ECO:0000244|PDB:1WI0}.
STRAND 70 74 {ECO:0000244|PDB:1WI0}.
HELIX 75 95 {ECO:0000244|PDB:1WI0}.
STRAND 102 106 {ECO:0000244|PDB:1WI0}.
SEQUENCE 448 AA; 50105 MW; 50C50E8F0F712BE7 CRC64;
MLWLALGPFC AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ VLPEATTTAF
EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE PLQIFPRACK PPGERNIHGL
KVNTRAGPSQ HTSPVVSDSL PSNSLKKSSA ELRKILANGQ MNEQDIRYRD TLGHGNGGTV
YKAHHVPSGK ILAVKVILLD ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC
TEFMDGGSLD VYRKIPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTGGQVKLC
DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA LGRFPYPQIQ
KNQGSLMPLQ LLQCIVDEDS PVLPLGEFSE PFVHFITQCM RKQPKERPAP EELMGHPFIV
QFNDGNSTVV SMWVCRALEE RRSQQGPP


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