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P46734 (MP2K3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 3

Short name=MAP kinase kinase 3
Short name=MAPKK 3
EC=2.7.12.2
Alternative name(s):
MAPK/ERK kinase 3
Short name=MEK 3
Stress-activated protein kinase kinase 2
Short name=SAPK kinase 2
Short name=SAPKK-2
Short name=SAPKK2
Gene names
Name:MAP2K3
Synonyms:MEK3, MKK3, PRKMK3, SKK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by dual phosphorylation on Ser-218 and Thr-222.

Subunit structure

Binds to DYRK1B/MIRK and increases its kinase activity. Part of a complex with MAP3K3, RAC1 and CCM2. Interacts with ARRB1. Interacts with Yersinia yopJ. Ref.8 Ref.9 Ref.10

Tissue specificity

Abundant expression is seen in the skeletal muscle. It is also widely expressed in other tissues.

Post-translational modification

Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity. Phosphorylated by TAOK2. Ref.6 Ref.7

Yersinia yopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, thus blocking the MAPK signaling pathway. Ref.10

Involvement in disease

Defects in MAP2K3 may be involved in colon cancer.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

positive regulation of protein kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of cytokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P46734-1)

Also known as: 3b;

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 1 (identifier: P46734-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
Isoform 2 (identifier: P46734-3)

Also known as: 3c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MESPASSQPASMPQSK → MGVQGTLMSRDSQTPHLLSIL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Dual specificity mitogen-activated protein kinase kinase 3
PRO_0000086378

Regions

Domain64 – 325262Protein kinase
Nucleotide binding70 – 789ATP By similarity

Sites

Active site1901Proton acceptor By similarity
Binding site931ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.12 Ref.14
Modified residue31Phosphoserine Ref.12
Modified residue151Phosphoserine Ref.12
Modified residue2181Phosphoserine Ref.6
Modified residue2221Phosphothreonine Ref.6

Natural variations

Alternative sequence1 – 2929Missing in isoform 1.
VSP_004878
Alternative sequence1 – 1616MESPA…MPQSK → MGVQGTLMSRDSQTPHLLSI L in isoform 2.
VSP_004877
Natural variant261R → T. Ref.16
VAR_040817
Natural variant401P → T.
Corresponds to variant rs33911218 [ dbSNP | Ensembl ].
VAR_046062
Natural variant551R → T.
Corresponds to variant rs36047035 [ dbSNP | Ensembl ].
VAR_061742
Natural variant681S → P. Ref.16
Corresponds to variant rs34105301 [ dbSNP | Ensembl ].
VAR_046063
Natural variant841A → T. Ref.16
Corresponds to variant rs2305873 [ dbSNP | Ensembl ].
VAR_046064
Natural variant901M → I. Ref.16
Corresponds to variant rs36076766 [ dbSNP | Ensembl ].
VAR_046065
Natural variant941R → L. Ref.16
Corresponds to variant rs56067280 [ dbSNP | Ensembl ].
VAR_046066
Natural variant961R → W. Ref.16
Corresponds to variant rs56216806 [ dbSNP | Ensembl ].
VAR_046067
Natural variant1751R → W in colon cancer. Ref.15
VAR_014208
Natural variant2151L → V in colon cancer. Ref.15
VAR_014209
Natural variant2931R → H. Ref.16
Corresponds to variant rs35206134 [ dbSNP | Ensembl ].
VAR_046068
Natural variant3391V → M. Ref.16
Corresponds to variant rs2363198 [ dbSNP | Ensembl ].
VAR_046069

Experimental info

Mutagenesis2181S → A: Inactivation. Ref.6
Mutagenesis2181S → E: Constitutive activation. Ref.6
Mutagenesis2221T → A: Inactivation. Ref.6
Mutagenesis2221T → E: Constitutive activation. Ref.6
Sequence conflict3411E → K Ref.1
Sequence conflict3411E → K Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (3b) [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: A80BA4FDFF8F75A2

FASTA34739,318
        10         20         30         40         50         60 
MESPASSQPA SMPQSKGKSK RKKDLRISCM SKPPAPNPTP PRNLDSRTFI TIGDRNFEVE 

        70         80         90        100        110        120 
ADDLVTISEL GRGAYGVVEK VRHAQSGTIM AVKRIRATVN SQEQKRLLMD LDINMRTVDC 

       130        140        150        160        170        180 
FYTVTFYGAL FREGDVWICM ELMDTSLDKF YRKVLDKNMT IPEDILGEIA VSIVRALEHL 

       190        200        210        220        230        240 
HSKLSVIHRD VKPSNVLINK EGHVKMCDFG ISGYLVDSVA KTMDAGCKPY MAPERINPEL 

       250        260        270        280        290        300 
NQKGYNVKSD VWSLGITMIE MAILRFPYES WGTPFQQLKQ VVEEPSPQLP ADRFSPEFVD 

       310        320        330        340 
FTAQCLRKNP AERMSYLELM EHPFFTLHKT KKTDIAAFVK EILGEDS 

« Hide

Isoform 1 [UniParc].

Checksum: 966821BE4B76E8FA
Show »

FASTA31836,173
Isoform 2 (3c) [UniParc].

Checksum: F59612D9001EA9C5
Show »

FASTA35239,940

References

« Hide 'large scale' references
[1]"Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms."
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J.
Science 267:682-685(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Purification and identification of a major activator for p38 from osmotically shocked cells: activation of mitogen-activated protein kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and H2O2."
Moriguchi T., Toyoshima F., Gotoh Y., Iwamatsu A., Irie K., Mori E., Kuroyanagi N., Hagiwara M., Matsumoto K., Nishida E.
J. Biol. Chem. 271:26981-26988(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]Han J.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3).
[4]"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 1).
Tissue: Trachea.
[5]"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 3).
Tissue: Leukocyte.
[6]"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway."
Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.
Mol. Cell. Biol. 16:1247-1255(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-218 AND THR-222, MUTAGENESIS OF SER-218 AND THR-222.
[7]"Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2."
Chen Z., Cobb M.H.
J. Biol. Chem. 276:16070-16075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY TAOK2.
[8]"Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1alpha."
Lim S., Jin K., Friedman E.
J. Biol. Chem. 277:25040-25046(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYRK1B.
Tissue: Muscle.
[9]"Platelet-activating factor-induced clathrin-mediated endocytosis requires beta-arrestin-1 recruitment and activation of the p38 MAPK signalosome at the plasma membrane for actin bundle formation."
McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C.
J. Immunol. 176:7039-7050(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1.
[10]"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.
[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]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Mutation analyses of 268 candidate genes in human tumor cell lines."
Teng D.-H., Chen Y., Lian L., Ha P.C., Tavtigian S.V., Wong A.K.C.
Genomics 74:352-364(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS COLON CANCER TRP-175 AND VAL-215.
[16]"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] THR-26; PRO-68; THR-84; ILE-90; LEU-94; TRP-96; HIS-293 AND MET-339.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36719 mRNA. Translation: AAC41718.1.
D87116 mRNA. Translation: BAA13248.1.
U66839 mRNA. Translation: AAB40652.1.
U66840 Genomic DNA. Translation: AAB40653.1.
AK093838 mRNA. Translation: BAG52769.1.
BC032478 mRNA. Translation: AAH32478.1.
CCDSCCDS11217.1. [P46734-1]
CCDS11218.1. [P46734-2]
RefSeqNP_002747.2. NM_002756.4. [P46734-2]
NP_659731.1. NM_145109.2. [P46734-1]
XP_005256779.1. XM_005256722.1. [P46734-2]
XP_005256780.1. XM_005256723.1. [P46734-2]
UniGeneHs.514012.

3D structure databases

ProteinModelPortalP46734.
SMRP46734. Positions 16-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111592. 28 interactions.
DIPDIP-34242N.
IntActP46734. 8 interactions.
MINTMINT-4300215.
STRING9606.ENSP00000345083.

Chemistry

BindingDBP46734.
ChEMBLCHEMBL2109.
GuidetoPHARMACOLOGY2064.

PTM databases

PhosphoSiteP46734.

Polymorphism databases

DMDM24638466.

Proteomic databases

MaxQBP46734.
PaxDbP46734.
PRIDEP46734.

Protocols and materials databases

DNASU5606.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316920; ENSP00000319139; ENSG00000034152. [P46734-2]
ENST00000342679; ENSP00000345083; ENSG00000034152. [P46734-1]
ENST00000361818; ENSP00000355081; ENSG00000034152. [P46734-2]
GeneID5606.
KEGGhsa:5606.
UCSCuc002gys.3. human. [P46734-1]

Organism-specific databases

CTD5606.
GeneCardsGC17P021187.
HGNCHGNC:6843. MAP2K3.
HPACAB018548.
HPA044497.
MIM602315. gene.
neXtProtNX_P46734.
PharmGKBPA30588.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234206.
HOVERGENHBG108518.
KOK04432.
OMANYLELME.
PhylomeDBP46734.
TreeFamTF350701.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP46734.

Gene expression databases

ArrayExpressP46734.
BgeeP46734.
CleanExHS_MAP2K3.
GenevestigatorP46734.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. 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

ChiTaRSMAP2K3. human.
GeneWikiMAP2K3.
GenomeRNAi5606.
NextBio21784.
PMAP-CutDBP46734.
PROP46734.
SOURCESearch...

Entry information

Entry nameMP2K3_HUMAN
AccessionPrimary (citable) accession number: P46734
Secondary accession number(s): B3KSK7 expand/collapse secondary AC list , Q99441, Q9UE71, Q9UE72
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 2002
Last modified: July 9, 2014
This is version 152 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM