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Q99640

- PMYT1_HUMAN

UniProt

Q99640 - PMYT1_HUMAN

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Protein
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
Gene
PKMYT1, MYT1
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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.2 Publications

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391ATP By similarity
Active sitei233 – 2331Proton acceptor By similarity
Metal bindingi238 – 2381Magnesium; via carbonyl oxygen By similarity
Metal bindingi251 – 2511Magnesium; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1249ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: HGNC
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: IntAct
  5. protein kinase activity Source: ProtInc
  6. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: Reactome
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: ProtInc
  5. negative regulation of phosphatase activity Source: UniProtKB
  6. regulation of cell cycle Source: Reactome
  7. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  8. regulation of mitosis Source: ProtInc
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

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
SignaLinkiQ99640.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:29650. PKMYT1.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: ProtInc
  2. Golgi membrane Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. endoplasmic reticulum Source: ProtInc
  5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  6. membrane Source: ProtInc
  7. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi238 – 2381N → A: Loss of kinase activity. 1 Publication
Mutagenesisi251 – 2511D → A: Loss of kinase activity. 1 Publication
Mutagenesisi486 – 4883RNL → AAA: Loss of CDC2-CCNB1 interaction. 1 Publication

Organism-specific databases

PharmGKBiPA385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
PRO_0000086573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei17 – 171Phosphothreonine2 Publications
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei160 – 1601Phosphoserine1 Publication
Modified residuei426 – 4261Phosphoserine; by PLK11 Publication
Modified residuei469 – 4691Phosphoserine2 Publications
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei495 – 4951Phosphothreonine; by PLK12 Publications

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99640.
PaxDbiQ99640.
PRIDEiQ99640.

PTM databases

PhosphoSiteiQ99640.

Expressioni

Gene expression databases

ArrayExpressiQ99640.
BgeeiQ99640.
CleanExiHS_MYT1.
HS_PKMYT1.
GenevestigatoriQ99640.

Organism-specific databases

HPAiCAB046000.

Interactioni

Subunit structurei

Interacts with CDC2-CCNB1 complex. Can also interact with PIN1 when phosphorylated by CDC2-CCNB1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1P146354EBI-495308,EBI-495332
CDK1P064933EBI-495308,EBI-444308

Protein-protein interaction databases

BioGridi114544. 9 interactions.
IntActiQ99640. 6 interactions.
MINTiMINT-3059438.
STRINGi9606.ENSP00000262300.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi101 – 1033
Helixi105 – 1095
Beta strandi110 – 11910
Beta strandi122 – 1298
Turni130 – 1323
Beta strandi135 – 14410
Helixi148 – 16417
Beta strandi173 – 1797
Beta strandi182 – 1887
Helixi194 – 2018
Helixi207 – 22620
Helixi236 – 2383
Beta strandi239 – 2413
Helixi243 – 2453
Beta strandi247 – 2493
Helixi271 – 2733
Helixi276 – 2805
Helixi286 – 30116
Helixi309 – 3157
Turni316 – 3183
Helixi322 – 3254
Helixi330 – 33910
Turni344 – 3463
Helixi350 – 3545
Helixi357 – 3593

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P1AX-ray1.70A75-362[»]
ProteinModelPortaliQ99640.
SMRiQ99640. Positions 76-362.

Miscellaneous databases

EvolutionaryTraceiQ99640.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 359250Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni398 – 499102Interaction with PIN1
Add
BLAST
Regioni437 – 49963Interaction with CDC2-CCNB1
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi382 – 39817Membrane-association motif
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 7268Pro-rich
Add
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 is however unproven.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000293277.
HOVERGENiHBG053623.
InParanoidiQ99640.
KOiK06633.
PhylomeDBiQ99640.
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.
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99640-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLERPPALAM PMPTEGTPPP LSGTPIPVPA YFRHAEPGFS LKRPRGLSRS    50
LPPPPPAKGS IPISRLFPPR TPGWHQLQPR RVSFRGEASE TLQSPGYDPS 100
RPESFFQQSF QRLSRLGHGS YGEVFKVRSK EDGRLYAVKR SMSPFRGPKD 150
RARKLAEVGS HEKVGQHPCC VRLEQAWEEG GILYLQTELC GPSLQQHCEA 200
WGASLPEAQV WGYLRDTLLA LAHLHSQGLV HLDVKPANIF LGPRGRCKLG 250
DFGLLVELGT AGAGEVQEGD PRYMAPELLQ GSYGTAADVF SLGLTILEVA 300
CNMELPHGGE GWQQLRQGYL PPEFTAGLSS ELRSVLVMML EPDPKLRATA 350
EALLALPVLR QPRAWGVLWC MAAEALSRGW ALWQALLALL CWLWHGLAHP 400
ASWLQPLGPP ATPPGSPPCS LLLDSSLSSN WDDDSLGPSL SPEAVLARTV 450
GSTSTPRSRC TPRDALDLSD INSEPPRGSF PSFEPRNLLS LFEDTLDPT 499
Length:499
Mass (Da):54,521
Last modified:May 1, 1997 - v1
Checksum:i4DF28A5965265567
GO
Isoform 2 (identifier: Q99640-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     439-499: SLSPEAVLAR...SLFEDTLDPT → GHPPCLACPP...AGAHPGMPWT

Note: No experimental confirmation available.

Show »
Length:480
Mass (Da):52,146
Checksum:iE3A040B3858812A6
GO
Isoform 3 (identifier: Q99640-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Note: No experimental confirmation available.

Show »
Length:490
Mass (Da):53,542
Checksum:i0D60B306B464E780
GO
Isoform 4 (identifier: Q99640-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-73: Missing.

Note: No experimental confirmation available.

Show »
Length:430
Mass (Da):47,284
Checksum:iCD5FC8DADE1E8E7E
GO

Sequence cautioni

The sequence CAD28540.1 differs from that shown. Reason: Chimeric cDNA.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031E → Q.1 Publication
Corresponds to variant rs55834293 [ dbSNP | Ensembl ].
VAR_041034
Natural varianti140 – 1401R → C.2 Publications
Corresponds to variant rs4149796 [ dbSNP | Ensembl ].
VAR_019928
Natural varianti246 – 2461R → H.1 Publication
Corresponds to variant rs35192104 [ dbSNP | Ensembl ].
VAR_041035
Natural varianti351 – 3511E → K.1 Publication
Corresponds to variant rs56382954 [ dbSNP | Ensembl ].
VAR_041036
Natural varianti417 – 4171P → R.1 Publication
Corresponds to variant rs4149800 [ dbSNP | Ensembl ].
VAR_019929
Natural varianti445 – 4451V → A.1 Publication
Corresponds to variant rs10546 [ dbSNP | Ensembl ].
VAR_019930

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform 3.
VSP_046846
Alternative sequencei5 – 7369Missing in isoform 4.
VSP_046847Add
BLAST
Alternative sequencei439 – 49961SLSPE…TLDPT → GHPPCLACPPAGLHSPLRLS WPGLWGAPPPPGAGAHPGMP WT in isoform 2.
VSP_045699Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311E → A in BAG53500. 1 Publication
Sequence conflicti415 – 4151G → D in AAB71843. 1 Publication
Sequence conflicti427 – 4271L → F in AAB71843. 1 Publication
Sequence conflicti491 – 4911L → M in AAB71843. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014118 mRNA. Translation: AAB71843.1.
U56816 mRNA. Translation: AAC50949.1.
AK097642 mRNA. Translation: BAG53500.1.
AK098452 mRNA. No translation available.
AK301926 mRNA. Translation: BAG63346.1.
AF549406 Genomic DNA. Translation: AAN40703.1.
AC004233 Genomic DNA. Translation: AAC04478.1.
AC004235 Genomic DNA. Translation: AAC04477.1.
CH471112 Genomic DNA. Translation: EAW85439.1.
CH471112 Genomic DNA. Translation: EAW85440.1.
AL713779 mRNA. Translation: CAD28540.1. Sequence problems.
CCDSiCCDS10486.1. [Q99640-1]
CCDS45391.1. [Q99640-2]
CCDS58414.1. [Q99640-3]
CCDS58415.1. [Q99640-4]
RefSeqiNP_001245379.1. NM_001258450.1. [Q99640-4]
NP_001245380.1. NM_001258451.1. [Q99640-3]
NP_004194.3. NM_004203.4. [Q99640-1]
NP_872629.1. NM_182687.2. [Q99640-2]
XP_006721039.1. XM_006720976.1. [Q99640-1]
UniGeneiHs.732385.

Genome annotation databases

EnsembliENST00000262300; ENSP00000262300; ENSG00000127564. [Q99640-1]
ENST00000440027; ENSP00000397739; ENSG00000127564. [Q99640-2]
ENST00000573944; ENSP00000459123; ENSG00000127564. [Q99640-3]
ENST00000574385; ENSP00000458943; ENSG00000127564. [Q99640-3]
ENST00000574730; ENSP00000460868; ENSG00000127564. [Q99640-4]
GeneIDi9088.
KEGGihsa:9088.
UCSCiuc002csn.3. human. [Q99640-1]

Polymorphism databases

DMDMi55976573.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014118 mRNA. Translation: AAB71843.1 .
U56816 mRNA. Translation: AAC50949.1 .
AK097642 mRNA. Translation: BAG53500.1 .
AK098452 mRNA. No translation available.
AK301926 mRNA. Translation: BAG63346.1 .
AF549406 Genomic DNA. Translation: AAN40703.1 .
AC004233 Genomic DNA. Translation: AAC04478.1 .
AC004235 Genomic DNA. Translation: AAC04477.1 .
CH471112 Genomic DNA. Translation: EAW85439.1 .
CH471112 Genomic DNA. Translation: EAW85440.1 .
AL713779 mRNA. Translation: CAD28540.1 . Sequence problems.
CCDSi CCDS10486.1. [Q99640-1 ]
CCDS45391.1. [Q99640-2 ]
CCDS58414.1. [Q99640-3 ]
CCDS58415.1. [Q99640-4 ]
RefSeqi NP_001245379.1. NM_001258450.1. [Q99640-4 ]
NP_001245380.1. NM_001258451.1. [Q99640-3 ]
NP_004194.3. NM_004203.4. [Q99640-1 ]
NP_872629.1. NM_182687.2. [Q99640-2 ]
XP_006721039.1. XM_006720976.1. [Q99640-1 ]
UniGenei Hs.732385.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P1A X-ray 1.70 A 75-362 [» ]
ProteinModelPortali Q99640.
SMRi Q99640. Positions 76-362.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114544. 9 interactions.
IntActi Q99640. 6 interactions.
MINTi MINT-3059438.
STRINGi 9606.ENSP00000262300.

Chemistry

BindingDBi Q99640.
ChEMBLi CHEMBL3984.
GuidetoPHARMACOLOGYi 2167.

PTM databases

PhosphoSitei Q99640.

Polymorphism databases

DMDMi 55976573.

Proteomic databases

MaxQBi Q99640.
PaxDbi Q99640.
PRIDEi Q99640.

Protocols and materials databases

DNASUi 9088.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262300 ; ENSP00000262300 ; ENSG00000127564 . [Q99640-1 ]
ENST00000440027 ; ENSP00000397739 ; ENSG00000127564 . [Q99640-2 ]
ENST00000573944 ; ENSP00000459123 ; ENSG00000127564 . [Q99640-3 ]
ENST00000574385 ; ENSP00000458943 ; ENSG00000127564 . [Q99640-3 ]
ENST00000574730 ; ENSP00000460868 ; ENSG00000127564 . [Q99640-4 ]
GeneIDi 9088.
KEGGi hsa:9088.
UCSCi uc002csn.3. human. [Q99640-1 ]

Organism-specific databases

CTDi 9088.
GeneCardsi GC16M002995.
HGNCi HGNC:29650. PKMYT1.
HPAi CAB046000.
MIMi 602474. gene.
neXtProti NX_Q99640.
PharmGKBi PA385.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000293277.
HOVERGENi HBG053623.
InParanoidi Q99640.
KOi K06633.
PhylomeDBi Q99640.
TreeFami TF101087.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
SignaLinki Q99640.

Miscellaneous databases

ChiTaRSi PKMYT1. human.
EvolutionaryTracei Q99640.
GeneWikii PKMYT1.
GenomeRNAii 9088.
NextBioi 34055.
PROi Q99640.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99640.
Bgeei Q99640.
CleanExi HS_MYT1.
HS_PKMYT1.
Genevestigatori Q99640.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000567. TYPK_Myt1. 1 hit.
SUPFAMi SSF56112. SSF56112. 2 hits.
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. "Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity."
    Booher R.N., Holman P.S., Fattaey A.
    J. Biol. Chem. 272:22300-22306(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION.
  2. "The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex."
    Liu F., Stanton J.J., Wu Z., Piwnica-Worms H.
    Mol. Cell. Biol. 17:571-583(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Tissue: Testis and Thyroid.
  4. NIEHS SNPs program
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-140; ARG-417 AND ALA-445.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-499 (ISOFORM 1).
    Tissue: Brain.
  8. "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins."
    Shen M., Stukenberg P.T., Kirschner M.W., Lu K.P.
    Genes Dev. 12:706-720(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIN1.
  9. "The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression."
    Wells N.J., Watanabe N., Tokusumi T., Jiang W., Verdecia M.A., Hunter T.
    J. Cell Sci. 112:3361-3371(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, COMPONENT OF CDC2-CCNB1 COMPLEX, INTERACTION WITH PIN1, MUTAGENESIS OF ASP-251.
  10. "Overproduction of human Myt1 kinase induces a G2 cell cycle delay by interfering with the intracellular trafficking of Cdc2-cyclin B1 complexes."
    Liu F., Rothblum-Oviatt C., Ryan C.E., Piwnica-Worms H.
    Mol. Cell. Biol. 19:5113-5123(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-238 AND 486-ARG--LEU-488.
  11. "Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate."
    Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E.
    J. Biol. Chem. 278:25277-25280(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-426 AND THR-495.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-94; SER-469 AND THR-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-469 AND SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-103; CYS-140; HIS-246 AND LYS-351.

Entry informationi

Entry nameiPMYT1_HUMAN
AccessioniPrimary (citable) accession number: Q99640
Secondary accession number(s): B3KUN8
, B4DXD4, D3DUA4, F8W164, I3L1V2, O14731, Q7LE24, Q8TCM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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