[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). STRAIN=Bristol N2; PubMed=8299935 [NCBI, ExPASy, EBI, Israel, Japan] Wu Y., Han M.; "Suppression of activated Let-60 ras protein defines a role of Caenorhabditis elegans Sur-1 MAP kinase in vulval differentiation."; Genes Dev. 8:147-159(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). STRAIN=Bristol N2; PubMed=8299936 [NCBI, ExPASy, EBI, Israel, Japan] Lackner M.R., Kornfeld K., Miller L.M., Horvitz H.R., Kim S.K.; "A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of vulval cell fates in Caenorhabditis elegans."; Genes Dev. 8:160-173(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).

Comments

FUNCTION: Function in let-60 Ras signaling pathway; acts downstream of lin-45 raf kinase, but before the lin-1 gene product in controlling vulval cell differentiation.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
COFACTOR: Magnesium (By similarity).
ENZYME REGULATION: Activated by tyrosine and threonine phosphorylation (By similarity).
INTERACTION:
O17109:-; NbExp=1; IntAct=EBI-321013, EBI-322062;
O17285:-; NbExp=2; IntAct=EBI-321013, EBI-322126;
O18687:-; NbExp=1; IntAct=EBI-321013, EBI-322003;
Q20772:-; NbExp=1; IntAct=EBI-321013, EBI-313068;
Q21229:-; NbExp=2; IntAct=EBI-321013, EBI-322054;
Q21648:-; NbExp=1; IntAct=EBI-321013, EBI-314179;
Q22836:-; NbExp=1; IntAct=EBI-321013, EBI-322121;
Q9N3Y1:-; NbExp=1; IntAct=EBI-321013, EBI-315848;
Q9N5V2:-; NbExp=1; IntAct=EBI-321013, EBI-311836;
Q9XUF2:-; NbExp=2; IntAct=EBI-321013, EBI-321986;
Q9XXJ0:-; NbExp=1; IntAct=EBI-321013, EBI-322139;
P91249:col-20; NbExp=1; IntAct=EBI-321013, EBI-313893;
P91001:csn-5; NbExp=1; IntAct=EBI-321013, EBI-313007;
P19826:deb-1; NbExp=1; IntAct=EBI-321013, EBI-322152;
O02289:gla-3; NbExp=1; IntAct=EBI-321013, EBI-317795;
O61899:kel-8; NbExp=1; IntAct=EBI-321013, EBI-312469;
P91820:lst-1; NbExp=1; IntAct=EBI-321013, EBI-313618;
P91829:nhr-69; NbExp=2; IntAct=EBI-321013, EBI-322112;
Q86G90:npp-9; NbExp=1; IntAct=EBI-321013, EBI-313076;
Q21734:rskn-1; NbExp=1; IntAct=EBI-321013, EBI-322085;
Q17695:spdl-1; NbExp=2; IntAct=EBI-321013, EBI-321960;
Q19203:unc-98; NbExp=2; IntAct=EBI-321013, EBI-319640;
Q8MPS9:zfp-3; NbExp=1; IntAct=EBI-321013, EBI-311975;
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name b

Isoform ID P39745-1

This is the isoform sequence displayed in this entry.

Name a

Isoform ID P39745-2

Features which should be applied to build the isoform sequence: VSP_004848.
DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
PTM: Dually phosphorylated on Thr-256 and Tyr-258, which activates the enzyme (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U03879; AAA18956.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U27124; AAA73482.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46937; CAA87057.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46937; CAB60996.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36977; A36977.
A36978; A36978.

RefSeq

NP_001022584.1; -.

UniGene

Cel.34032

3D structure databases

HSSP

P28482; 1PME. [HSSP ENTRY / PDB]

SMR

P39745; 83-421.

ModBase

P39745.

Protein-protein interaction databases

DIP

DIP:26227N; -.

IntAct

P39745; -.

Organism-specific databases

WormBase

WBGene00003401; mpk-1.

WormPep

F43C1.2a; CE01583. [WormPep / WorfDB]
F43C1.2b; CE24971. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

P39745; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004707;	Molecular function: MAP kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0040035;	Biological process: hermaphrodite genitalia development (inferred from mutant phenotype from WormBase).
GO:0040010;	Biological process: positive regulation of growth rate (inferred from mutant phenotype from WormBase).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0040025;	Biological process: vulval development (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR008349; Erk_1_2_MAPK.
IPR003527; MAP_kin_CS.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

PRINTS

PR01770; ERK1ERK2MAPK.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS01351; MAPK; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P39745.

Genome annotation databases

Ensembl

F43C1.2; Caenorhabditis elegans. [Contig view]

GeneID

175545; -.

Other

NextBio

888610; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Cell cycle; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 444`	`444`	`Mitogen-activated protein kinase mpk-1.`	`PRO_0000186306`
`DOMAIN`	`96 384`	`289`	`Protein kinase.`
`NP_BIND`	`102 110`	`9`	`ATP (By similarity).`
`MOTIF`	`256 258`	`3`	`TXY.`
`ACT_SITE`	`220 220`		`Proton acceptor (By similarity).`
`BINDING`	`125 125`		`ATP (By similarity).`
`MOD_RES`	`256 256`		`Phosphothreonine (By similarity).`
`MOD_RES`	`258 258`		`Phosphotyrosine (By similarity).`
`VAR_SEQ`	`1 68`		`Missing (in isoform a).`	`VSP_004848`
`MUTAGEN`	`106 106`		`A->V: Loss of function and ATP-binding.`
`CONFLICT`	`9 10`		`LC -> FF (in Ref. 2; AAA18956).`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 50663 Da [This is the MW of the unprocessed precursor]

CRC64: 11BA27D17641980D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTWIPNNLC AQPTTRNAKP PSNGHPQATQ QQSAPGSLAY RNSSNIPNGA TNHVRQQKWQ 

        70         80         90        100        110        120 
YTRSGHRKMA DGEAVISTVN NVEEVHGQLF EVAPRYVNLS YIGEGAYGMV ASALDTITRD 

       130        140        150        160        170        180 
RVAIKKISPF EHQTFCQRTL REIKILNRFK HENIINIQEI IRSETVDSLK DIYIVQCLME 

       190        200        210        220        230        240 
TDLYKLLKTQ KLSNDHVCYF LYQILRGLKY IHSANVLHRD LKPSNLLLNT TCDLKICDFG 

       250        260        270        280        290        300 
LARVTDPQTD HTGFLTEYVA TRWYRAPEIM LNSKGYTKSI DVWSVGCILA EMLSNRPLFP 

       310        320        330        340        350        360 
GKHYLDQLNL ILAVVGSPSN ADLQCIINDK ARSYLISLPH KPKQPWARLY PGADPRALDL 

       370        380        390        400        410        420 
LDKMLTFNPH NRIDIEQALA HPYLEQYYDP GDEPVCEEPF TLEMEFDDLP KEKLKELIWE 

       430        440 
EAEAHHRRME AEAAARNNGG QNPV

P39745 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools