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Protein

Stress-activated protein kinase JNK-1

Gene

JNK-1

Organism
Ancylostoma caninum (Dog hookworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551ATPPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 386ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-activated protein kinase JNK-1 (EC:2.7.11.24)
Gene namesi
Name:JNK-1
OrganismiAncylostoma caninum (Dog hookworm)Imported
Taxonomic identifieri29170 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaAncylostomatoideaAncylostomatidaeAncylostomatinaeAncylostoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Stress-activated protein kinase JNK-1PRO_0000186269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831PhosphothreonineBy similarity
Modified residuei185 – 1851PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9U6D2.

Structurei

3D structure databases

ProteinModelPortaliQ9U6D2.
SMRiQ9U6D2. Positions 10-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 321296Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U6D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTSVPENY YVVPIGETQM VILKRYENLR LIGSGAQGIV CAATDMVTNK
60 70 80 90 100
PVAIKKLSRP FQNVTHAKRA YREFILMNLV NHKNIIGLLN AFSPQREVEE
110 120 130 140 150
FNDLYIVMEL MDANLCQVIQ MDLDHERLSY LLYQMLCGIK HLHSAGIIHR
160 170 180 190 200
DLKPSNIVVK SDCTLKILDF GLARTAVEAF MMTPYVVTRY YRAPEVILGM
210 220 230 240 250
GYGENVDVWS VGCIFGELIR GRVLFPGADH IDQWTRIIEL LGTPEPQFLA
260 270 280 290 300
RLQTTVRNYV ENRQKYQPVP FETLFADNMF PPGADNARLT AAKARDLLSR
310 320 330 340 350
MLVIDPEKRI SVDDALAHEY VNVWYDASRG SCSSAGPSTI LLVDGEHTVE
360 370
EWRAMLFAEL QNYYRTHDVY GVGQRR
Length:376
Mass (Da):42,770
Last modified:October 1, 2002 - v2
Checksum:i2EDFA15CC28AD3A4
GO

Sequence cautioni

The sequence AAF00539.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187690 mRNA. Translation: AAF00539.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187690 mRNA. Translation: AAF00539.1. Different initiation.

3D structure databases

ProteinModelPortaliQ9U6D2.
SMRiQ9U6D2. Positions 10-362.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9U6D2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "JNK-1 kinase of the hookworm nematode, Ancylostoma caninum."
    Arasu P.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiJNK1_ANCCA
AccessioniPrimary (citable) accession number: Q9U6D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.