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Protein

Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase

Gene

Pkmyt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Negatively regulated by hyperphosphorylation during mitosis. The hyperphosphorylated form does not associate with CCNB1-CDC2 complexes. The PLK1 protein kinase may be required for mitotic phosphorylation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301ATPPROSITE-ProRule annotation
Active sitei224 – 2241Proton acceptorPROSITE-ProRule annotation
Metal bindingi229 – 2291Magnesium; via carbonyl oxygenBy similarity
Metal bindingi242 – 2421Magnesium; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1159ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-156711. Polo-like kinase mediated events.
R-MMU-69202. Cyclin E associated events during G1/S transition.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-69478. G2/M DNA replication checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (EC:2.7.11.1)
Alternative name(s):
Myt1 kinase
Gene namesi
Name:Pkmyt1
Synonyms:Myt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2137630. Pkmyt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
  • membrane Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinasePRO_0000086574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei417 – 4171Phosphothreonine; by PLK1By similarity
Modified residuei464 – 4641PhosphoserineBy similarity
Modified residuei486 – 4861Phosphoserine; by PLK1By similarity

Post-translational modificationi

Autophosphorylated. Phosphorylated by CDC2-CCNB1 complexes on undefined serine and threonine residues. The phosphorylation by CDC2-CCNB1 complexes may inhibit the catalytic activity (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ESG9.
PaxDbiQ9ESG9.
PRIDEiQ9ESG9.

PTM databases

iPTMnetiQ9ESG9.
PhosphoSiteiQ9ESG9.

Expressioni

Gene expression databases

BgeeiQ9ESG9.
CleanExiMM_MYT1.
GenevisibleiQ9ESG9. MM.

Interactioni

Subunit structurei

Interacts with CDC2-CCNB1 complex. Can also interact with PIN1 when phosphorylated by CDC2-CCNB1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024701.

Structurei

3D structure databases

ProteinModelPortaliQ9ESG9.
SMRiQ9ESG9. Positions 67-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 350250Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni389 – 490102Interaction with PIN1By similarityAdd
BLAST
Regioni428 – 49063Interaction with CDC2-CCNB1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi373 – 38917Membrane-association motifBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 9390Pro-richAdd
BLAST

Domaini

The membrane-association motif is essential for the localization to membrane of Golgi stack. According to some authors, it is a transmembrane domain; the existence of a transmembrane region of such is however unsure (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0601. Eukaryota.
ENOG410XS1M. LUCA.
GeneTreeiENSGT00530000063230.
HOGENOMiHOG000293277.
HOVERGENiHBG053623.
InParanoidiQ9ESG9.
KOiK06633.
OMAiFRGPQDR.
OrthoDBiEOG7J70FR.
TreeFamiTF101087.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR016235. Tyr/Thr_kinase_Cdc2_inhib.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000567. TYPK_Myt1. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
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.

Q9ESG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMPTEGTPP PLSGTPIPVP AYFRHAEPGF SLKRPGGLSR SLPPRPPAKG
60 70 80 90 100
CIPVSRLFPP RTPGWHQPQP RRVSFLCETS EPLQSPGYDP SRPESFFQQN
110 120 130 140 150
FQRLSRLGHG SYGEVFKVRS KEDGRLYAVK RYMSPFRGPK DRTRKLAEVG
160 170 180 190 200
GHEKVGQHPH CVRLERAWEE GGILYLQTEL CGPSLQQHCE AWGASLPEAQ
210 220 230 240 250
VWGYLRDILL ALDHLHSQGL VHLDVKPANI FLGPRGRCKL GDFGLLVELG
260 270 280 290 300
SAGAGEAQEG DPRYMAPELL QGSYGTAADV FSLGLTILEV ACNMELPHGG
310 320 330 340 350
EGWQQLRQGY LPPEFTAGLS SELRSVLAMM LEPDPQLRAT AEALLALPML
360 370 380 390 400
RQPRPWNVLW YMAAEALSRG WALWQALVTL LCWLWHGLVH PASWLQPPGP
410 420 430 440 450
PATPPGSPPC SPLLDSTLSS SWDNDSIGPS LSPETVLSRI TRRTSTPRGR
460 470 480 490
YIPRDALDLT DVDSEPPRGP CPTFEPRNLL SLFEDSLDPA
Length:490
Mass (Da):54,053
Last modified:July 27, 2011 - v3
Checksum:i1308CD1F9D0293B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521A → T in AAG09210 (Ref. 1) Curated
Sequence conflicti252 – 2521A → T in AAH25061 (PubMed:15489334).Curated
Sequence conflicti405 – 4051P → L in AAG09210 (Ref. 1) Curated
Sequence conflicti414 – 4152LD → MN in AAG09210 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175892 mRNA. Translation: AAG09210.1.
AK158550 mRNA. Translation: BAE34554.1.
AK165164 mRNA. Translation: BAE38056.1.
BC025061 mRNA. Translation: AAH25061.1.
CCDSiCCDS28460.1.
RefSeqiNP_075545.2. NM_023058.3.
UniGeneiMm.182193.

Genome annotation databases

EnsembliENSMUST00000024701; ENSMUSP00000024701; ENSMUSG00000023908.
GeneIDi268930.
KEGGimmu:268930.
UCSCiuc008asz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175892 mRNA. Translation: AAG09210.1.
AK158550 mRNA. Translation: BAE34554.1.
AK165164 mRNA. Translation: BAE38056.1.
BC025061 mRNA. Translation: AAH25061.1.
CCDSiCCDS28460.1.
RefSeqiNP_075545.2. NM_023058.3.
UniGeneiMm.182193.

3D structure databases

ProteinModelPortaliQ9ESG9.
SMRiQ9ESG9. Positions 67-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024701.

PTM databases

iPTMnetiQ9ESG9.
PhosphoSiteiQ9ESG9.

Proteomic databases

EPDiQ9ESG9.
PaxDbiQ9ESG9.
PRIDEiQ9ESG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024701; ENSMUSP00000024701; ENSMUSG00000023908.
GeneIDi268930.
KEGGimmu:268930.
UCSCiuc008asz.1. mouse.

Organism-specific databases

CTDi9088.
MGIiMGI:2137630. Pkmyt1.

Phylogenomic databases

eggNOGiKOG0601. Eukaryota.
ENOG410XS1M. LUCA.
GeneTreeiENSGT00530000063230.
HOGENOMiHOG000293277.
HOVERGENiHBG053623.
InParanoidiQ9ESG9.
KOiK06633.
OMAiFRGPQDR.
OrthoDBiEOG7J70FR.
TreeFamiTF101087.

Enzyme and pathway databases

ReactomeiR-MMU-156711. Polo-like kinase mediated events.
R-MMU-69202. Cyclin E associated events during G1/S transition.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-69478. G2/M DNA replication checkpoint.

Miscellaneous databases

ChiTaRSiPkmyt1. mouse.
PROiQ9ESG9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESG9.
CleanExiMM_MYT1.
GenevisibleiQ9ESG9. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR016235. Tyr/Thr_kinase_Cdc2_inhib.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000567. TYPK_Myt1. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Van de Putte T., Francis A., Zwijsen A., Huylebroeck D.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Visual cortex.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiPMYT1_MOUSE
AccessioniPrimary (citable) accession number: Q9ESG9
Secondary accession number(s): Q3TNN2, Q8R3L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.