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A4QPA9 (A4QPA9_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names

Mitogen-activated protein kinase kinase 1, isoform CRA_a EMBL EAW77765.1

cDNA FLJ76051, highly similar to Homo sapiens mitogen-activated protein kinase kinase 1 (MAP2K1), mRNA EMBL BAF84189.1
Gene names
Name:MAP2K1 EMBL AAI39730.1
ORF Names:hCG_24510 EMBL EAW77765.1
OrganismHomo sapiens (Human) EMBL AAI39730.1
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

Ontologies

Keywords
   LigandATP-binding RuleBase RU000304
Nucleotide-binding
   Molecular functionKinase EMBL AAI39730.1
Transferase
Gene Ontology (GO)
   Biological_processGolgi inheritance

Inferred from electronic annotation. Source: Compara

cell motility

Inferred from electronic annotation. Source: Compara

cell proliferation

Inferred from electronic annotation. Source: Compara

keratinocyte differentiation

Inferred from electronic annotation. Source: Compara

labyrinthine layer development

Inferred from electronic annotation. Source: Compara

melanosome transport

Inferred from electronic annotation. Source: Compara

mitosis

Inferred from electronic annotation. Source: Compara

negative regulation of homotypic cell-cell adhesion

Inferred from electronic annotation. Source: Compara

neuron projection morphogenesis

Inferred from electronic annotation. Source: Compara

placenta blood vessel development

Inferred from electronic annotation. Source: Compara

positive regulation of Ras GTPase activity

Inferred from electronic annotation. Source: Compara

positive regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Compara

positive regulation of cell differentiation

Inferred from electronic annotation. Source: Compara

positive regulation of cell migration

Inferred from electronic annotation. Source: Compara

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Compara

protein heterooligomerization

Inferred from electronic annotation. Source: Compara

regulation of vascular smooth muscle contraction

Inferred from electronic annotation. Source: Compara

response to axon injury

Inferred from electronic annotation. Source: Compara

response to glucocorticoid stimulus

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from electronic annotation. Source: Compara

vesicle transport along microtubule

Inferred from electronic annotation. Source: Compara

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Compara

axon part

Inferred from electronic annotation. Source: Compara

cell cortex

Inferred from electronic annotation. Source: Compara

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Compara

dendrite cytoplasm

Inferred from electronic annotation. Source: Compara

perikaryon

Inferred from electronic annotation. Source: Compara

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from electronic annotation. Source: Compara

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

receptor signaling protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A4QPA9 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 0344118FFC842D51

FASTA39343,439
        10         20         30         40         50         60 
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV 

        70         80         90        100        110        120 
GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE 

       130        140        150        160        170        180 
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL 

       190        200        210        220        230        240 
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY 

       250        260        270        280        290        300 
SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLSSY 

       310        320        330        340        350        360 
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF 

       370        380        390 
IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA AGV 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M. expand/collapse author list , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain EMBL AAI37460.1 and PCR rescued clones EMBL AAI39730.1.
[2]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"NEDO human cDNA sequencing project."
Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T. expand/collapse author list , Sugano S., Nomura N., Isogai T.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC137459 mRNA. Translation: AAI37460.1.
BC139729 mRNA. Translation: AAI39730.1.
AK291500 mRNA. Translation: BAF84189.1.
CH471082 Genomic DNA. Translation: EAW77765.1.
IPIIPI00219604.
RefSeqNP_002746.1. NM_002755.3.
UniGeneHs.145442.

3D structure databases

ProteinModelPortalA4QPA9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4QPA9.

Proteomic databases

PRIDEA4QPA9.

Protocols and materials databases

DNASU5604.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5604.
KEGGhsa:5604.

Organism-specific databases

CTD5604.
PharmGKBPA30584.

Phylogenomic databases

HOVERGENHBG108518.
KOK04368.
OMAELMFGCP.
PhylomeDBA4QPA9.

Gene expression databases

ArrayExpressA4QPA9.
BgeeA4QPA9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBA4QPA9.
ChiTaRSMAP2K1. human.
GenomeRNAi5604.
NextBio21776.

Entry information

Entry nameA4QPA9_HUMAN
AccessionPrimary (citable) accession number: A4QPA9
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.