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Protein

Dual specificity mitogen-activated protein kinase kinase 2

Gene

MAP2K2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei10 – 112Cleavage; by anthrax lethal factor
Binding sitei101 – 1011ATPPROSITE-ProRule annotation
Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 869ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase activity Source: UniProtKB
  • PDZ domain binding Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome
  • protein tyrosine kinase activity Source: UniProtKB-KW
  • scaffold protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiREACT_1183. ERK2 activation.
REACT_22272. Signal transduction by L1.
REACT_252852. Signaling by FGFR3.
REACT_264618. Uptake and function of anthrax toxins.
REACT_355200. Signaling by FGFR2.
REACT_355289. Signaling by FGFR1.
REACT_355408. Signaling by FGFR4.
REACT_614. RAF phosphorylates MEK.
REACT_962. MEK activation.
SignaLinkiP36507.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity mitogen-activated protein kinase kinase 2 (EC:2.7.12.2)
Short name:
MAP kinase kinase 2
Short name:
MAPKK 2
Alternative name(s):
ERK activator kinase 2
MAPK/ERK kinase 2
Short name:
MEK 2
Gene namesi
Name:MAP2K2
Synonyms:MEK2, MKK2, PRKMK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6842. MAP2K2.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell cortex Source: Ensembl
  • cytoplasm Source: HPA
  • cytoplasmic side of plasma membrane Source: UniProtKB
  • cytosol Source: UniProtKB
  • early endosome Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular region Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • intracellular Source: GO_Central
  • late endosome Source: UniProtKB
  • microtubule Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • peroxisomal membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cardiofaciocutaneous syndrome 4 (CFC4)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices.

See also OMIM:615280
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571F → C in CFC4. 1 Publication
VAR_035095
Natural varianti57 – 571F → V in CFC4. 1 Publication
VAR_069781
Natural varianti128 – 1281P → Q in CFC4; results in increased kinase activity. 1 Publication
VAR_069782
Natural varianti134 – 1341Y → H in CFC4. 1 Publication
VAR_069783

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Ectodermal dysplasia, Mental retardation

Organism-specific databases

MIMi615280. phenotype.
Orphaneti1340. Cardiofaciocutaneous syndrome.
638. Neurofibromatosis-Noonan syndrome.
PharmGKBiPA30587.

Chemistry

DrugBankiDB06616. Bosutinib.
DB08911. Trametinib.

Polymorphism and mutation databases

BioMutaiMAP2K2.
DMDMi547915.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Dual specificity mitogen-activated protein kinase kinase 2PRO_0000086372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei222 – 2221O-acetylserine; by Yersinia yopJ; alternate1 Publication
Modified residuei222 – 2221Phosphoserine; by RAF; alternate1 Publication
Modified residuei226 – 2261O-acetylserine; by Yersinia yopJ; alternate1 Publication
Modified residuei226 – 2261Phosphoserine; alternate1 Publication
Modified residuei293 – 2931Phosphoserine1 Publication
Modified residuei295 – 2951Phosphoserine2 Publications
Modified residuei394 – 3941Phosphothreonine4 Publications
Modified residuei396 – 3961Phosphothreonine3 Publications

Post-translational modificationi

MAPKK is itself dependent on Ser/Thr phosphorylation for activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1). Phosphorylated by MAP2K1/MEK1 (By similarity).By similarity
Acetylation of Ser-222 and Ser-226 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP36507.
PaxDbiP36507.
PeptideAtlasiP36507.
PRIDEiP36507.

2D gel databases

REPRODUCTION-2DPAGEIPI00003783.

PTM databases

PhosphoSiteiP36507.

Miscellaneous databases

PMAP-CutDBP36507.

Expressioni

Gene expression databases

BgeeiP36507.
CleanExiHS_MAP2K2.
ExpressionAtlasiP36507. baseline and differential.
GenevisibleiP36507. HS.

Organism-specific databases

HPAiCAB003835.
HPA051993.

Interactioni

Subunit structurei

Interacts with MORG1 (By similarity). Interacts with SGK1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103986EBI-1056930,EBI-365961
CCNDBP1O952733EBI-1056930,EBI-748961
DLG1Q1295910EBI-1056930,EBI-357481
RAF1P040493EBI-1056930,EBI-365996

Protein-protein interaction databases

BioGridi111591. 25 interactions.
DIPiDIP-29119N.
IntActiP36507. 15 interactions.
MINTiMINT-99667.
STRINGi9606.ENSP00000262948.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 713Combined sources
Beta strandi72 – 809Combined sources
Beta strandi85 – 917Combined sources
Turni92 – 943Combined sources
Beta strandi97 – 1037Combined sources
Helixi110 – 11910Combined sources
Helixi120 – 1223Combined sources
Beta strandi133 – 14816Combined sources
Helixi155 – 1617Combined sources
Beta strandi162 – 1643Combined sources
Helixi167 – 18620Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi208 – 2103Combined sources
Helixi217 – 2226Combined sources
Helixi236 – 2394Combined sources
Helixi246 – 26217Combined sources
Helixi272 – 2798Combined sources
Helixi318 – 32710Combined sources
Turni335 – 3373Combined sources
Helixi340 – 34910Combined sources
Turni354 – 3563Combined sources
Helixi360 – 3645Combined sources
Helixi367 – 3748Combined sources
Helixi379 – 3868Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9IX-ray3.20A/B55-400[»]
4H3QX-ray2.20B4-16[»]
ProteinModelPortaliP36507.
SMRiP36507. Positions 60-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36507.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 369298Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi266 – 31550Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
InParanoidiP36507.
KOiK04369.
OMAiEGASEAH.
OrthoDBiEOG7HF1KZ.
PhylomeDBiP36507.
TreeFamiTF105137.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELELDEQQ
60 70 80 90 100
KKRLEAFLTQ KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR
110 120 130 140 150
KLIHLEIKPA IRNQIIRELQ VLHECNSPYI VGFYGAFYSD GEISICMEHM
160 170 180 190 200
DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG LAYLREKHQI MHRDVKPSNI
210 220 230 240 250
LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMAPERLQ GTHYSVQSDI
260 270 280 290 300
WSMGLSLVEL AVGRYPIPPP DAKELEAIFG RPVVDGEEGE PHSISPRPRP
310 320 330 340 350
PGRPVSGHGM DSRPAMAIFE LLDYIVNEPP PKLPNGVFTP DFQEFVNKCL
360 370 380 390 400
IKNPAERADL KMLTNHTFIK RSEVEEVDFA GWLCKTLRLN QPGTPTRTAV
Length:400
Mass (Da):44,424
Last modified:June 1, 1994 - v1
Checksum:i3401D522515C30A5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571F → C in CFC4. 1 Publication
VAR_035095
Natural varianti57 – 571F → V in CFC4. 1 Publication
VAR_069781
Natural varianti128 – 1281P → Q in CFC4; results in increased kinase activity. 1 Publication
VAR_069782
Natural varianti134 – 1341Y → H in CFC4. 1 Publication
VAR_069783

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11285 mRNA. No translation available.
BC000471 mRNA. Translation: AAH00471.1.
BC018645 mRNA. Translation: AAH18645.1.
CCDSiCCDS12120.1.
PIRiA46723.
RefSeqiNP_109587.1. NM_030662.3.
UniGeneiHs.465627.

Genome annotation databases

EnsembliENST00000262948; ENSP00000262948; ENSG00000126934.
GeneIDi5605.
KEGGihsa:5605.
UCSCiuc002lzj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11285 mRNA. No translation available.
BC000471 mRNA. Translation: AAH00471.1.
BC018645 mRNA. Translation: AAH18645.1.
CCDSiCCDS12120.1.
PIRiA46723.
RefSeqiNP_109587.1. NM_030662.3.
UniGeneiHs.465627.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9IX-ray3.20A/B55-400[»]
4H3QX-ray2.20B4-16[»]
ProteinModelPortaliP36507.
SMRiP36507. Positions 60-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111591. 25 interactions.
DIPiDIP-29119N.
IntActiP36507. 15 interactions.
MINTiMINT-99667.
STRINGi9606.ENSP00000262948.

Chemistry

BindingDBiP36507.
ChEMBLiCHEMBL2111289.
DrugBankiDB06616. Bosutinib.
DB08911. Trametinib.
GuidetoPHARMACOLOGYi2063.

PTM databases

PhosphoSiteiP36507.

Polymorphism and mutation databases

BioMutaiMAP2K2.
DMDMi547915.

2D gel databases

REPRODUCTION-2DPAGEIPI00003783.

Proteomic databases

MaxQBiP36507.
PaxDbiP36507.
PeptideAtlasiP36507.
PRIDEiP36507.

Protocols and materials databases

DNASUi5605.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262948; ENSP00000262948; ENSG00000126934.
GeneIDi5605.
KEGGihsa:5605.
UCSCiuc002lzj.3. human.

Organism-specific databases

CTDi5605.
GeneCardsiGC19M004090.
GeneReviewsiMAP2K2.
H-InvDBHIX0033655.
HGNCiHGNC:6842. MAP2K2.
HPAiCAB003835.
HPA051993.
MIMi601263. gene.
615280. phenotype.
neXtProtiNX_P36507.
Orphaneti1340. Cardiofaciocutaneous syndrome.
638. Neurofibromatosis-Noonan syndrome.
PharmGKBiPA30587.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
InParanoidiP36507.
KOiK04369.
OMAiEGASEAH.
OrthoDBiEOG7HF1KZ.
PhylomeDBiP36507.
TreeFamiTF105137.

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiREACT_1183. ERK2 activation.
REACT_22272. Signal transduction by L1.
REACT_252852. Signaling by FGFR3.
REACT_264618. Uptake and function of anthrax toxins.
REACT_355200. Signaling by FGFR2.
REACT_355289. Signaling by FGFR1.
REACT_355408. Signaling by FGFR4.
REACT_614. RAF phosphorylates MEK.
REACT_962. MEK activation.
SignaLinkiP36507.

Miscellaneous databases

ChiTaRSiMAP2K2. human.
EvolutionaryTraceiP36507.
GeneWikiiMAP2K2.
GenomeRNAii5605.
NextBioi21780.
PMAP-CutDBP36507.
PROiP36507.
SOURCEiSearch...

Gene expression databases

BgeeiP36507.
CleanExiHS_MAP2K2.
ExpressionAtlasiP36507. baseline and differential.
GenevisibleiP36507. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2."
    Zheng C.-F., Guan K.-L.
    J. Biol. Chem. 268:11435-11439(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Muscle and Skin.
  3. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 40-51; 53-61; 64-100; 102-112; 164-172; 194-205; 265-297; 362-371 AND 389-397, PHOSPHORYLATION AT THR-394, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  4. "Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling."
    Mittal R., Peak-Chew S.Y., McMahon H.T.
    Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 210-231, INACTIVATION BY YERSINIA YOPJ, PHOSPHORYLATION AT SER-222 AND SER-226, ACETYLATION AT SER-222 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY.
  5. Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
  6. "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
    Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
    Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration."
    Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M.
    J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGK1.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome."
    Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A., Cruz M.S., McCormick F., Rauen K.A.
    Science 311:1287-1290(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CFC4 CYS-57.
  20. Cited for: VARIANTS CFC4 VAL-57 AND HIS-134.
  21. "Molecular and functional analysis of a novel MEK2 mutation in cardio-facio-cutaneous syndrome: transmission through four generations."
    Rauen K.A., Tidyman W.E., Estep A.L., Sampath S., Peltier H.M., Bale S.J., Lacassie Y.
    Am. J. Med. Genet. A 152:807-814(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CFC4 GLN-128, CHARACTERIZATION OF VARIANT CFC4 GLN-128.

Entry informationi

Entry nameiMP2K2_HUMAN
AccessioniPrimary (citable) accession number: P36507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 22, 2015
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.