SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8QGV2

- WEE1B_XENLA

UniProt

Q8QGV2 - WEE1B_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Wee1-like protein kinase 1-B
Gene
wee1-b
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a zygotic negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed cdk1 before the onset of mitosis by mediating phosphorylation of cdk1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed cdk1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-cdk1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric cdk1 does not occur.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei277 – 2771ATP By similarity
Active sitei375 – 3751Proton acceptor By similarity
Metal bindingi380 – 3801Magnesium; via carbonyl oxygen By similarity
Metal bindingi412 – 4121Magnesium; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi254 – 2629ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein serine/threonine kinase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Wee1-like protein kinase 1-B (EC:2.7.10.2)
Alternative name(s):
Zygotic wee1-like protein kinase 1B
Short name:
Xe-Wee1B
Short name:
XeWee1B
Gene namesi
Name:wee1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254033. wee1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi181 – 1833NIN → AAA: Impairs without abolishing ability to phosphorylate cdk1. 1 Publication
Mutagenesisi186 – 1861T → A: Abolishes kinase activity inhibition during M-phase. Does not affect ability to phosphorylate cdk1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Wee1-like protein kinase 1-B
PRO_0000409523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphothreonine; by cdk11 Publication

Post-translational modificationi

Phosphorylation at Thr-186 during M-phase by cdk1 inhibits the kinase activity and leads to interaction with pin1.

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

Zygotically expressed. Present in oocytes and postgastrula embryos (at least until the tailbud stage). Expression begins at the midblastula stage and increases after the early gastrula stage.1 Publication

Interactioni

Subunit structurei

Interacts (when phosphorylated at Thr-186) with pin1.1 Publication

Protein-protein interaction databases

BioGridi100680. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8QGV2.
SMRiQ8QGV2. Positions 240-518.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini248 – 518271Protein kinase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili526 – 56338 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 757Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG005050.
KOiK06632.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8QGV2-1 [UniParc]FASTAAdd to Basket

« Hide

MNVQPRNMNV QPRNMNVQPV RHKLFFSDTD EEEEDGHSTG EDSAFQESDS    50
PVSRQREKQE GKPPGGTWEE LEEEEGFGSS PIKSPGDFFM SDSPSYRQLA 100
PASPTRSPQG PTSPIPECPG TPPHKTFRKL RLFDTPHTPK SLLSKARGIG 150
SSALRFRGGT LFREAEKAPK PEFVYSTPQV NINPFTPDSL EIQSSAGLCR 200
GRKRALLNDS CGEDMEGSDC ELEDEDIRPA KRIPITESNM KSRYATEFHE 250
LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA 300
VLGQHPHVVR YYSAWAEDDH MLIQNEYCNG GSLSDVISEN YRTMQYFTEP 350
ELKDLLLQVA RGLKYIHSMS LVHMDIKPSN IFISRTTLPN TAVEEADDEE 400
CGSGKVIYKI GDLGHVTRVS SPQVEEGDSR FLANEVLQEN YTHLAKADIF 450
ALALTVWSAA GAEPFPTNGD QWHEIRQGKL PRVPQLLSQE FVDLIKLMIS 500
PDPEKRPSSV ALVKHSVLLS ASRKSAEQLR IELDAEKFKN ALLQKELKKA 550
QIAKAAAEER AHFPDRIATR STTQNNRTTR LIGKKMNRSV SLTIY 595
Length:595
Mass (Da):66,600
Last modified:June 1, 2002 - v1
Checksum:i4E90E7FDA341CB1B
GO

Sequence cautioni

The sequence AAH82404.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671T → S in AAH82404. 1 Publication
Sequence conflicti367 – 3671H → Y in AAH82404. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB071983 mRNA. Translation: BAB86797.1.
BC082404 mRNA. Translation: AAH82404.1. Different initiation.
RefSeqiNP_001084186.1. NM_001090717.1.
UniGeneiXl.9986.

Genome annotation databases

GeneIDi399355.
KEGGixla:399355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB071983 mRNA. Translation: BAB86797.1 .
BC082404 mRNA. Translation: AAH82404.1 . Different initiation.
RefSeqi NP_001084186.1. NM_001090717.1.
UniGenei Xl.9986.

3D structure databases

ProteinModelPortali Q8QGV2.
SMRi Q8QGV2. Positions 240-518.
ModBasei Search...

Protein-protein interaction databases

BioGridi 100680. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399355.
KEGGi xla:399355.

Organism-specific databases

CTDi 399355.
Xenbasei XB-GENE-6254033. wee1.

Phylogenomic databases

HOVERGENi HBG005050.
KOi K06632.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The existence of two distinct Wee1 isoforms in Xenopus: implications for the developmental regulation of the cell cycle."
    Okamoto K., Nakajo N., Sagata N.
    EMBO J. 21:2472-2484(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase."
    Okamoto K., Sagata N.
    Proc. Natl. Acad. Sci. U.S.A. 104:3753-3758(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-186, INTERACTION WITH PIN1, MUTAGENESIS OF 181-ASN--ASN-183 AND THR-186.

Entry informationi

Entry nameiWEE1B_XENLA
AccessioniPrimary (citable) accession number: Q8QGV2
Secondary accession number(s): Q641D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi