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Q13163

- MP2K5_HUMAN

UniProt

Q13163 - MP2K5_HUMAN

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Protein

Dual specificity mitogen-activated protein kinase kinase 5

Gene

MAP2K5

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

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951ATP
Active sitei283 – 2831Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1809ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: UniProtKB-KW
  5. protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of MAPK activity Source: BHF-UCL
  2. cellular response to growth factor stimulus Source: BHF-UCL
  3. cellular response to laminar fluid shear stress Source: BHF-UCL
  4. ERK5 cascade Source: Ensembl
  5. heart development Source: Ensembl
  6. negative regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  7. negative regulation of chemokine (C-X-C motif) ligand 2 production Source: BHF-UCL
  8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  9. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  10. negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  11. negative regulation of interleukin-8 biosynthetic process Source: BHF-UCL
  12. negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  13. negative regulation of response to cytokine stimulus Source: BHF-UCL
  14. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. neurotrophin TRK receptor signaling pathway Source: Reactome
  16. positive regulation of cell growth Source: Ensembl
  17. positive regulation of epithelial cell proliferation Source: Ensembl
  18. positive regulation of protein metabolic process Source: BHF-UCL
  19. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  20. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiREACT_12020. Signalling to ERK5.
SignaLinkiQ13163.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity mitogen-activated protein kinase kinase 5 (EC:2.7.12.2)
Short name:
MAP kinase kinase 5
Short name:
MAPKK 5
Alternative name(s):
MAPK/ERK kinase 5
Short name:
MEK 5
Gene namesi
Name:MAP2K5
Synonyms:MEK5, MKK5, PRKMK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6845. MAP2K5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nucleus Source: Ensembl
  3. spindle Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951K → M: Inactivation. 1 Publication
Mutagenesisi311 – 3111S → A: Inactivation. 1 Publication
Mutagenesisi315 – 3151T → A: Inactivation. 1 Publication

Organism-specific databases

PharmGKBiPA30590.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Dual specificity mitogen-activated protein kinase kinase 5PRO_0000086383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei311 – 3111Phosphoserine2 Publications
Modified residuei315 – 3151Phosphothreonine1 Publication

Post-translational modificationi

Activated by phosphorylation on Ser/Thr by MAP kinase kinase kinases.By similarity
Yersinia yopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, thus blocking the MAPK signaling pathway.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13163.
PaxDbiQ13163.
PRIDEiQ13163.

PTM databases

PhosphoSiteiQ13163.

Expressioni

Tissue specificityi

Expressed in many adult tissues. Abundant in heart and skeletal muscle.

Gene expression databases

BgeeiQ13163.
CleanExiHS_MAP2K5.
ExpressionAtlasiQ13163. baseline and differential.
GenevestigatoriQ13163.

Organism-specific databases

HPAiCAB022094.
HPA027347.
HPA027755.

Interactioni

Subunit structurei

Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with SQSTM1 and PRKCZ or PRKCI (By similarity). Interacts with Yersinia yopJ.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629932EBI-307294,EBI-401755
MAP3K3Q997592EBI-307294,EBI-307281
MAPK7Q131642EBI-307294,EBI-1213983

Protein-protein interaction databases

BioGridi111593. 19 interactions.
DIPiDIP-27558N.
IntActiQ13163. 13 interactions.
MINTiMINT-1155433.
STRINGi9606.ENSP00000178640.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 237
Turni24 – 263
Beta strandi27 – 337
Helixi41 – 5111
Beta strandi58 – 636
Beta strandi65 – 673
Beta strandi69 – 724
Helixi75 – 9319
Turni94 – 963
Beta strandi102 – 1076

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPTX-ray1.75A/C5-108[»]
2O2VX-ray1.83A5-108[»]
4IC7X-ray2.60B/E16-130[»]
ProteinModelPortaliQ13163.
SMRiQ13163. Positions 16-130, 141-445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13163.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9780OPRAdd
BLAST
Domaini166 – 409244Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 258Interaction with MAPK7By similarity
Regioni64 – 685Interaction with MAP3K2/MAP3K3By similarity
Regioni117 – 13115Interaction with MAPK7By similarityAdd
BLAST

Domaini

Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues of the OPR domain. This domain also mediates interactions with SQSTM1 and PARD6A (By similarity).By similarity

Sequence similaritiesi

Contains 1 OPR domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
InParanoidiQ13163.
KOiK04463.
OMAiEVVSMWV.
OrthoDBiEOG7HF1KZ.
PhylomeDBiQ13163.
TreeFamiTF106468.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00220. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q13163) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLWLALGPFP AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ
60 70 80 90 100
VLPEATTTAF EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE
110 120 130 140 150
PLQIFPRACK PPGERNIHGL KVNTRAGPSQ HSSPAVSDSL PSNSLKKSSA
160 170 180 190 200
ELKKILANGQ MNEQDIRYRD TLGHGNGGTV YKAYHVPSGK ILAVKVILLD
210 220 230 240 250
ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC TEFMDGGSLD
260 270 280 290 300
VYRKMPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTRGQVKLC
310 320 330 340 350
DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA
360 370 380 390 400
LGRFPYPQIQ KNQGSLMPLQ LLQCIVDEDS PVLPVGEFSE PFVHFITQCM
410 420 430 440
RKQPKERPAP EELMGHPFIV QFNDGNAAVV SMWVCRALEE RRSQQGPP
Length:448
Mass (Da):50,112
Last modified:November 28, 2006 - v2
Checksum:iF23BB327E2A9C7DC
GO
Isoform A (identifier: Q13163-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-358: Missing.

Show »
Length:438
Mass (Da):48,968
Checksum:i21246312F1640EE2
GO
Isoform C (identifier: Q13163-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-358: Missing.
     444-448: QQGPP → LASLPSPSPSV

Note: Incomplete sequence.

Show »
Length:444
Mass (Da):49,497
Checksum:i574D15B06FD49134
GO
Isoform 4 (identifier: Q13163-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVL → MMEGHFPQS

Note: No experimental confirmation available.

Show »
Length:412
Mass (Da):46,131
Checksum:i7B00956329FCAEDB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181H → R.1 Publication
Corresponds to variant rs56241934 [ dbSNP | Ensembl ].
VAR_040823
Natural varianti427 – 4271A → V.1 Publication
VAR_040824
Natural varianti428 – 4281A → T.1 Publication
Corresponds to variant rs55811347 [ dbSNP | Ensembl ].
VAR_046070

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545MLWLA…FRDVL → MMEGHFPQS in isoform 4. 1 PublicationVSP_043333Add
BLAST
Alternative sequencei349 – 35810Missing in isoform A and isoform C. 2 PublicationsVSP_021825
Alternative sequencei444 – 4485QQGPP → LASLPSPSPSV in isoform C. 1 PublicationVSP_021826

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25265 mRNA. Translation: AAA96146.1.
U71087 mRNA. Translation: AAB16851.1.
U71088 mRNA. Translation: AAB16852.2.
BT006780 mRNA. Translation: AAP35426.1.
AK293459 mRNA. Translation: BAG56954.1.
CR542229 mRNA. Translation: CAG47025.1.
AC009292 Genomic DNA. No translation available.
AC016355 Genomic DNA. No translation available.
AC103753 Genomic DNA. No translation available.
BC008838 mRNA. Translation: AAH08838.1.
CCDSiCCDS10224.1. [Q13163-1]
CCDS42051.1. [Q13163-2]
CCDS55970.1. [Q13163-4]
RefSeqiNP_001193733.1. NM_001206804.1. [Q13163-4]
NP_002748.1. NM_002757.3. [Q13163-2]
NP_660143.1. NM_145160.2. [Q13163-1]
UniGeneiHs.114198.

Genome annotation databases

EnsembliENST00000178640; ENSP00000178640; ENSG00000137764. [Q13163-1]
ENST00000354498; ENSP00000346493; ENSG00000137764. [Q13163-4]
ENST00000395476; ENSP00000378859; ENSG00000137764. [Q13163-2]
GeneIDi5607.
KEGGihsa:5607.
UCSCiuc002aqu.3. human. [Q13163-1]
uc002aqv.3. human. [Q13163-2]
uc010ujw.2. human. [Q13163-4]

Polymorphism databases

DMDMi118572669.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25265 mRNA. Translation: AAA96146.1 .
U71087 mRNA. Translation: AAB16851.1 .
U71088 mRNA. Translation: AAB16852.2 .
BT006780 mRNA. Translation: AAP35426.1 .
AK293459 mRNA. Translation: BAG56954.1 .
CR542229 mRNA. Translation: CAG47025.1 .
AC009292 Genomic DNA. No translation available.
AC016355 Genomic DNA. No translation available.
AC103753 Genomic DNA. No translation available.
BC008838 mRNA. Translation: AAH08838.1 .
CCDSi CCDS10224.1. [Q13163-1 ]
CCDS42051.1. [Q13163-2 ]
CCDS55970.1. [Q13163-4 ]
RefSeqi NP_001193733.1. NM_001206804.1. [Q13163-4 ]
NP_002748.1. NM_002757.3. [Q13163-2 ]
NP_660143.1. NM_145160.2. [Q13163-1 ]
UniGenei Hs.114198.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NPT X-ray 1.75 A/C 5-108 [» ]
2O2V X-ray 1.83 A 5-108 [» ]
4IC7 X-ray 2.60 B/E 16-130 [» ]
ProteinModelPortali Q13163.
SMRi Q13163. Positions 16-130, 141-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111593. 19 interactions.
DIPi DIP-27558N.
IntActi Q13163. 13 interactions.
MINTi MINT-1155433.
STRINGi 9606.ENSP00000178640.

Chemistry

BindingDBi Q13163.
ChEMBLi CHEMBL4948.
GuidetoPHARMACOLOGYi 2066.

PTM databases

PhosphoSitei Q13163.

Polymorphism databases

DMDMi 118572669.

Proteomic databases

MaxQBi Q13163.
PaxDbi Q13163.
PRIDEi Q13163.

Protocols and materials databases

DNASUi 5607.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000178640 ; ENSP00000178640 ; ENSG00000137764 . [Q13163-1 ]
ENST00000354498 ; ENSP00000346493 ; ENSG00000137764 . [Q13163-4 ]
ENST00000395476 ; ENSP00000378859 ; ENSG00000137764 . [Q13163-2 ]
GeneIDi 5607.
KEGGi hsa:5607.
UCSCi uc002aqu.3. human. [Q13163-1 ]
uc002aqv.3. human. [Q13163-2 ]
uc010ujw.2. human. [Q13163-4 ]

Organism-specific databases

CTDi 5607.
GeneCardsi GC15P067835.
HGNCi HGNC:6845. MAP2K5.
HPAi CAB022094.
HPA027347.
HPA027755.
MIMi 602520. gene.
neXtProti NX_Q13163.
PharmGKBi PA30590.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119199.
HOGENOMi HOG000234206.
HOVERGENi HBG108518.
InParanoidi Q13163.
KOi K04463.
OMAi EVVSMWV.
OrthoDBi EOG7HF1KZ.
PhylomeDBi Q13163.
TreeFami TF106468.

Enzyme and pathway databases

BRENDAi 2.7.12.2. 2681.
Reactomei REACT_12020. Signalling to ERK5.
SignaLinki Q13163.

Miscellaneous databases

ChiTaRSi MAP2K5. human.
EvolutionaryTracei Q13163.
GeneWikii MAP2K5.
GenomeRNAii 5607.
NextBioi 21792.
PROi Q13163.
SOURCEi Search...

Gene expression databases

Bgeei Q13163.
CleanExi HS_MAP2K5.
ExpressionAtlasi Q13163. baseline and differential.
Genevestigatori Q13163.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH ERK5 AND MAPK7, MUTAGENESIS OF LYS-195; SER-311 AND THR-315, PHOSPHORYLATION AT SER-311 AND THR-315.
    Tissue: Fetal brain.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION.
    Tissue: Placenta.
  3. Lee J.D.
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS OF ISOFORM C.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Cerebellum.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
  7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 B).
    Tissue: Brain.
  9. "Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation."
    Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., Orth K.
    Science 312:1211-1214(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YOPJ, ACETYLATION.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of the complex of human mitogen activated protein kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated protein kinase kinase kinase 3 (MAP3K2B-Phox)."
    Structural genomics consortium (SGC)
    Submitted (NOV-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 4-108 IN COMPLEX WITH MAP3K2.
  14. "Crystal structure of the complex of human mitogen activated protein kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated protein kinase kinase kinase 3 (MAP3K3B-Phox)."
    Structural genomics consortium (SGC)
    Submitted (NOV-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 4-108 IN COMPLEX WITH MAP3K3.
  15. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-118; VAL-427 AND THR-428.

Entry informationi

Entry nameiMP2K5_HUMAN
AccessioniPrimary (citable) accession number: Q13163
Secondary accession number(s): B4DE43, Q92961, Q92962
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 150 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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