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

Q13163 (MP2K5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity mitogen-activated protein kinase kinase 5

Short name=MAP kinase kinase 5
Short name=MAPKK 5
EC=2.7.12.2
Alternative name(s):
MAPK/ERK kinase 5
Short name=MEK 5
Gene names
Name:MAP2K5
Synonyms:MEK5, MKK5, PRKMK5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Subunit structure

Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with SQSTM1 and PRKCZ or PRKCI By similarity. Interacts with Yersinia yopJ. Ref.1 Ref.9

Tissue specificity

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

Domain

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

Post-translational modification

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. Ref.9

Sequence similarities

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

Contains 1 OPR domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK5 cascade

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

cellular response to growth factor stimulus

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

cellular response to laminar fluid shear stress

Traceable author statement PubMed 20551324. Source: BHF-UCL

heart development

Inferred from electronic annotation. Source: Ensembl

negative regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of cell migration involved in sprouting angiogenesis

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of chemokine (C-X-C motif) ligand 2 production

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of heterotypic cell-cell adhesion

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of interleukin-8 biosynthetic process

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of response to cytokine stimulus

Inferred from sequence or structural similarity PubMed 20551324. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q13163-1)

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 A (identifier: Q13163-2)

The sequence of this isoform differs from the canonical sequence as follows:
     349-358: Missing.
Isoform C (identifier: Q13163-3)

The sequence of this isoform differs from the canonical sequence as follows:
     349-358: Missing.
     444-448: QQGPP → LASLPSPSPSV
Note: Incomplete sequence.
Isoform 4 (identifier: Q13163-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVL → MMEGHFPQS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Dual specificity mitogen-activated protein kinase kinase 5
PRO_0000086383

Regions

Domain18 – 9780OPR
Domain166 – 409244Protein kinase
Nucleotide binding172 – 1809ATP By similarity
Region18 – 258Interaction with MAPK7 By similarity
Region64 – 685Interaction with MAP3K2/MAP3K3 By similarity
Region117 – 13115Interaction with MAPK7 By similarity

Sites

Active site2831Proton acceptor By similarity
Binding site1951ATP

Amino acid modifications

Modified residue3111Phosphoserine Ref.1 Ref.11
Modified residue3151Phosphothreonine Ref.1

Natural variations

Alternative sequence1 – 4545MLWLA…FRDVL → MMEGHFPQS in isoform 4.
VSP_043333
Alternative sequence349 – 35810Missing in isoform A and isoform C.
VSP_021825
Alternative sequence444 – 4485QQGPP → LASLPSPSPSV in isoform C.
VSP_021826
Natural variant1181H → R. Ref.15
Corresponds to variant rs56241934 [ dbSNP | Ensembl ].
VAR_040823
Natural variant4271A → V. Ref.15
VAR_040824
Natural variant4281A → T. Ref.15
Corresponds to variant rs55811347 [ dbSNP | Ensembl ].
VAR_046070

Experimental info

Mutagenesis1951K → M: Inactivation. Ref.1
Mutagenesis3111S → A: Inactivation. Ref.1
Mutagenesis3151T → A: Inactivation. Ref.1

Secondary structure

.................. 448
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: F23BB327E2A9C7DC

FASTA44850,112
        10         20         30         40         50         60 
MLWLALGPFP AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ VLPEATTTAF 

        70         80         90        100        110        120 
EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE PLQIFPRACK PPGERNIHGL 

       130        140        150        160        170        180 
KVNTRAGPSQ HSSPAVSDSL PSNSLKKSSA ELKKILANGQ MNEQDIRYRD TLGHGNGGTV 

       190        200        210        220        230        240 
YKAYHVPSGK ILAVKVILLD ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC 

       250        260        270        280        290        300 
TEFMDGGSLD VYRKMPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTRGQVKLC 

       310        320        330        340        350        360 
DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA LGRFPYPQIQ 

       370        380        390        400        410        420 
KNQGSLMPLQ LLQCIVDEDS PVLPVGEFSE PFVHFITQCM RKQPKERPAP EELMGHPFIV 

       430        440 
QFNDGNAAVV SMWVCRALEE RRSQQGPP 

« Hide

Isoform A [UniParc].

Checksum: 21246312F1640EE2
Show »

FASTA43848,968
Isoform C [UniParc].

Checksum: 574D15B06FD49134
Show »

FASTA44449,497
Isoform 4 [UniParc].

Checksum: 7B00956329FCAEDB
Show »

FASTA41246,131

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001193733.1. NM_001206804.1.
NP_002748.1. NM_002757.3.
NP_660143.1. NM_145160.2.
UniGeneHs.114198.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPTX-ray1.75A/C5-108[»]
2O2VX-ray1.83A5-108[»]
4IC7X-ray2.60B/E16-130[»]
ProteinModelPortalQ13163.
SMRQ13163. Positions 16-130, 160-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111593. 19 interactions.
DIPDIP-27558N.
IntActQ13163. 13 interactions.
MINTMINT-1155433.
STRING9606.ENSP00000178640.

Chemistry

BindingDBQ13163.
ChEMBLCHEMBL4948.
GuidetoPHARMACOLOGY2066.

PTM databases

PhosphoSiteQ13163.

Polymorphism databases

DMDM118572669.

Proteomic databases

PaxDbQ13163.
PRIDEQ13163.

Protocols and materials databases

DNASU5607.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000178640; ENSP00000178640; ENSG00000137764. [Q13163-1]
ENST00000354498; ENSP00000346493; ENSG00000137764. [Q13163-4]
ENST00000395476; ENSP00000378859; ENSG00000137764. [Q13163-2]
GeneID5607.
KEGGhsa:5607.
UCSCuc002aqu.3. human. [Q13163-1]
uc002aqv.3. human. [Q13163-2]
uc010ujw.2. human. [Q13163-4]

Organism-specific databases

CTD5607.
GeneCardsGC15P067835.
HGNCHGNC:6845. MAP2K5.
HPACAB022094.
HPA027347.
HPA027755.
MIM602520. gene.
neXtProtNX_Q13163.
PharmGKBPA30590.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234206.
HOVERGENHBG108518.
InParanoidQ13163.
KOK04463.
OMAEVVSMWV.
OrthoDBEOG7HF1KZ.
PhylomeDBQ13163.
TreeFamTF106468.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkQ13163.

Gene expression databases

ArrayExpressQ13163.
BgeeQ13163.
CleanExHS_MAP2K5.
GenevestigatorQ13163.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP2K5. human.
EvolutionaryTraceQ13163.
GeneWikiMAP2K5.
GenomeRNAi5607.
NextBio21792.
PROQ13163.
SOURCESearch...

Entry information

Entry nameMP2K5_HUMAN
AccessionPrimary (citable) accession number: Q13163
Secondary accession number(s): B4DE43, Q92961, Q92962
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM