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Protein

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

Gene

Myt1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of Cdk1 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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei131 – 1311ATPPROSITE-ProRule annotation
Active sitei224 – 2241Proton acceptorPROSITE-ProRule annotation
Metal bindingi229 – 2291Magnesium; via carbonyl oxygenBy similarity
Metal bindingi243 – 2431Magnesium; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1169ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: FlyBase
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • female meiotic division Source: FlyBase
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • germarium-derived cystoblast division Source: FlyBase
  • male germ-line stem cell asymmetric division Source: FlyBase
  • male meiosis Source: FlyBase
  • meiotic nuclear division Source: FlyBase
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • negative regulation of mitotic cell cycle Source: UniProtKB
  • positive regulation of cell size Source: FlyBase
  • protein phosphorylation Source: UniProtKB
  • spermatocyte division Source: FlyBase
  • spermatogonial cell division Source: FlyBase
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-DME-156711. Polo-like kinase mediated events.
R-DME-69202. Cyclin E associated events during G1/S transition.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69478. G2/M DNA replication checkpoint.
SignaLinkiQ9NI63.

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
dMyt1
Gene namesi
Name:Myt1
ORF Names:CG32417
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0040298. Myt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinasePRO_0000086577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei504 – 5041Phosphoserine1 Publication
Modified residuei519 – 5191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NI63.

PTM databases

iPTMnetiQ9NI63.

Expressioni

Gene expression databases

BgeeiQ9NI63.
GenevisibleiQ9NI63. DM.

Interactioni

Protein-protein interaction databases

BioGridi64110. 6 interactions.
STRINGi7227.FBpp0076824.

Structurei

3D structure databases

ProteinModelPortaliQ9NI63.
SMRiQ9NI63. Positions 24-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 351250Protein kinasePROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ9NI63.
KOiK06633.
OMAiHHATEGD.
OrthoDBiEOG7J70FR.
PhylomeDBiQ9NI63.

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.

Q9NI63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKHHRLPLP ELHDDKHRHK QCNGENSNRF RPPKYKTRGY VAVDNNNLNR
60 70 80 90 100
SQSLGSCSTN SSQIAHAISF RDAGCSDSST LPSSPVQAEL STLSLSHFEQ
110 120 130 140 150
CFERLAKLGE GSFGEVFQVR DRSDGQLYAV KISKQLFRGE QYRAERLEEV
160 170 180 190 200
RRYEEFSGHE NCIRFIRAWE QYDRLYMQME LCRESLEQYL LRCQRIPEER
210 220 230 240 250
IWHILLDLLR GLKSLHDRNL IHLDIKLDNV LIGEDDETCK LADFGLVIDV
260 270 280 290 300
DRANSHHATE GDSRYMAPEI LQGHFSKAAD IFSLGIAMLE LACYMDLPSN
310 320 330 340 350
GPLWHELRHG ILPEEFINKI SLELQSVIKS MMKPDPAQRP TAEQLLSHPK
360 370 380 390 400
LQYLQKKRKS LMNFSMLSRS FRRSRRAVWG RMCNWKTAAF RYLLYFLEVL
410 420 430 440 450
HLCKPITASQ PNINIVPSSP SSKGVPLVPQ VEFQLVGSTP IANRDCYASD
460 470 480 490 500
FLSGEDPLDL SNQGSPNVIN STPLNTNQGK SRLDLLKNNV DSMGRYVHVH
510 520 530
DFESPCSALS SAKVLDTSSF RRKKLFVLEY DDE
Length:533
Mass (Da):61,131
Last modified:November 23, 2004 - v2
Checksum:i3DCD3458914D0645
GO

Sequence cautioni

The sequence AAF32288.1 differs from that shown. Reason: Frameshift at position 526. Curated
The sequence AAK77309.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF215861 mRNA. Translation: AAF32288.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF50747.3.
AY047577 mRNA. Translation: AAK77309.1. Different initiation.
RefSeqiNP_647987.2. NM_139730.3.
UniGeneiDm.4639.

Genome annotation databases

EnsemblMetazoaiFBtr0077118; FBpp0076824; FBgn0040298.
GeneIDi38649.
KEGGidme:Dmel_CG32417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF215861 mRNA. Translation: AAF32288.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF50747.3.
AY047577 mRNA. Translation: AAK77309.1. Different initiation.
RefSeqiNP_647987.2. NM_139730.3.
UniGeneiDm.4639.

3D structure databases

ProteinModelPortaliQ9NI63.
SMRiQ9NI63. Positions 24-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64110. 6 interactions.
STRINGi7227.FBpp0076824.

PTM databases

iPTMnetiQ9NI63.

Proteomic databases

PaxDbiQ9NI63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077118; FBpp0076824; FBgn0040298.
GeneIDi38649.
KEGGidme:Dmel_CG32417.

Organism-specific databases

CTDi4661.
FlyBaseiFBgn0040298. Myt1.

Phylogenomic databases

eggNOGiKOG0601. Eukaryota.
ENOG410XS1M. LUCA.
GeneTreeiENSGT00530000063230.
InParanoidiQ9NI63.
KOiK06633.
OMAiHHATEGD.
OrthoDBiEOG7J70FR.
PhylomeDBiQ9NI63.

Enzyme and pathway databases

ReactomeiR-DME-156711. Polo-like kinase mediated events.
R-DME-69202. Cyclin E associated events during G1/S transition.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69478. G2/M DNA replication checkpoint.
SignaLinkiQ9NI63.

Miscellaneous databases

GenomeRNAii38649.
PROiQ9NI63.

Gene expression databases

BgeeiQ9NI63.
GenevisibleiQ9NI63. DM.

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. "Identification of Drosophila Myt1 kinase and its role in Golgi during mitosis."
    Cornwell W.D., Kaminski P.J., Jackson J.R.
    Cell. Signal. 14:467-476(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Ectopic expression of the Drosophila Cdk1 inhibitory kinases, Wee1 and Myt1, interferes with the second mitotic wave and disrupts pattern formation during eye development."
    Price D.M., Jin Z., Rabinovitch S., Campbell S.D.
    Genetics 161:721-731(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-533.
    Strain: Berkeley.
    Tissue: Head.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-519, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiPMYT1_DROME
AccessioniPrimary (citable) accession number: Q9NI63
Secondary accession number(s): Q961T4, Q9VRP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.