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Q99640 (PMYT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase

EC=2.7.11.1
Alternative name(s):
Myt1 kinase
Gene names
Name:PKMYT1
Synonyms:MYT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.1

Subunit structure

Interacts with CDC2-CCNB1 complex. Can also interact with PIN1 when phosphorylated by CDC2-CCNB1. Ref.8 Ref.9

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein Ref.2.

Domain

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.

Post-translational modification

Autophosphorylated. Phosphorylated by CDC2-CCNB1 complexes on undefined serine and threonine residues. The phosphorylation by CDC2-CCNB1 complexes may inhibit the catalytic activity. Ref.9 Ref.11

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Traceable author statement Ref.2. Source: ProtInc

negative regulation of phosphatase activity

Inferred from direct assay PubMed 19389623. Source: UniProtKB

regulation of cell cycle

Traceable author statement. Source: Reactome

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: ProtInc

regulation of mitosis

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentGolgi apparatus

Traceable author statement Ref.2. Source: ProtInc

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Traceable author statement Ref.2. Source: ProtInc

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Traceable author statement Ref.2. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase activity

Inferred from direct assay Ref.1. Source: HGNC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10PubMed 23397142PubMed 23602568. Source: IntAct

protein kinase activity

Traceable author statement Ref.2. Source: ProtInc

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCNB1P146354EBI-495308,EBI-495332
CDK1P064933EBI-495308,EBI-444308

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99640-1)

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.
Isoform 2 (identifier: Q99640-2)

The sequence of this isoform differs from the canonical sequence as follows:
     439-499: SLSPEAVLAR...SLFEDTLDPT → GHPPCLACPP...AGAHPGMPWT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q99640-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q99640-4)

The sequence of this isoform differs from the canonical sequence as follows:
     5-73: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
PRO_0000086573

Regions

Domain110 – 359250Protein kinase
Nucleotide binding116 – 1249ATP By similarity
Region398 – 499102Interaction with PIN1
Region437 – 49963Interaction with CDC2-CCNB1
Motif382 – 39817Membrane-association motif
Compositional bias5 – 7268Pro-rich

Sites

Active site2331Proton acceptor By similarity
Metal binding2381Magnesium; via carbonyl oxygen By similarity
Metal binding2511Magnesium; via carbonyl oxygen By similarity
Binding site1391ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14
Modified residue171Phosphothreonine Ref.12 Ref.14
Modified residue941Phosphoserine Ref.12
Modified residue1201Phosphoserine Ref.13
Modified residue1601Phosphoserine Ref.14
Modified residue4261Phosphoserine; by PLK1 Ref.11
Modified residue4691Phosphoserine Ref.12 Ref.13
Modified residue4731Phosphoserine Ref.13
Modified residue4951Phosphothreonine; by PLK1 Ref.11 Ref.12

Natural variations

Alternative sequence1 – 99Missing in isoform 3.
VSP_046846
Alternative sequence5 – 7369Missing in isoform 4.
VSP_046847
Alternative sequence439 – 49961SLSPE…TLDPT → GHPPCLACPPAGLHSPLRLS WPGLWGAPPPPGAGAHPGMP WT in isoform 2.
VSP_045699
Natural variant1031E → Q. Ref.15
Corresponds to variant rs55834293 [ dbSNP | Ensembl ].
VAR_041034
Natural variant1401R → C. Ref.4 Ref.15
Corresponds to variant rs4149796 [ dbSNP | Ensembl ].
VAR_019928
Natural variant2461R → H. Ref.15
Corresponds to variant rs35192104 [ dbSNP | Ensembl ].
VAR_041035
Natural variant3511E → K. Ref.15
Corresponds to variant rs56382954 [ dbSNP | Ensembl ].
VAR_041036
Natural variant4171P → R. Ref.4
Corresponds to variant rs4149800 [ dbSNP | Ensembl ].
VAR_019929
Natural variant4451V → A. Ref.4
Corresponds to variant rs10546 [ dbSNP | Ensembl ].
VAR_019930

Experimental info

Mutagenesis2381N → A: Loss of kinase activity. Ref.10
Mutagenesis2511D → A: Loss of kinase activity. Ref.9
Mutagenesis486 – 4883RNL → AAA: Loss of CDC2-CCNB1 interaction. Ref.10
Sequence conflict1311E → A in BAG53500. Ref.4
Sequence conflict4151G → D in AAB71843. Ref.1
Sequence conflict4271L → F in AAB71843. Ref.1
Sequence conflict4911L → M in AAB71843. Ref.1

Secondary structure

............................................... 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4DF28A5965265567

FASTA49954,521
        10         20         30         40         50         60 
MLERPPALAM PMPTEGTPPP LSGTPIPVPA YFRHAEPGFS LKRPRGLSRS LPPPPPAKGS 

        70         80         90        100        110        120 
IPISRLFPPR TPGWHQLQPR RVSFRGEASE TLQSPGYDPS RPESFFQQSF QRLSRLGHGS 

       130        140        150        160        170        180 
YGEVFKVRSK EDGRLYAVKR SMSPFRGPKD RARKLAEVGS HEKVGQHPCC VRLEQAWEEG 

       190        200        210        220        230        240 
GILYLQTELC GPSLQQHCEA WGASLPEAQV WGYLRDTLLA LAHLHSQGLV HLDVKPANIF 

       250        260        270        280        290        300 
LGPRGRCKLG DFGLLVELGT AGAGEVQEGD PRYMAPELLQ GSYGTAADVF SLGLTILEVA 

       310        320        330        340        350        360 
CNMELPHGGE GWQQLRQGYL PPEFTAGLSS ELRSVLVMML EPDPKLRATA EALLALPVLR 

       370        380        390        400        410        420 
QPRAWGVLWC MAAEALSRGW ALWQALLALL CWLWHGLAHP ASWLQPLGPP ATPPGSPPCS 

       430        440        450        460        470        480 
LLLDSSLSSN WDDDSLGPSL SPEAVLARTV GSTSTPRSRC TPRDALDLSD INSEPPRGSF 

       490 
PSFEPRNLLS LFEDTLDPT 

« Hide

Isoform 2 [UniParc].

Checksum: E3A040B3858812A6
Show »

FASTA48052,146
Isoform 3 [UniParc].

Checksum: 0D60B306B464E780
Show »

FASTA49053,542
Isoform 4 [UniParc].

Checksum: CD5FC8DADE1E8E7E
Show »

FASTA43047,284

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10486.1. [Q99640-1]
CCDS45391.1. [Q99640-2]
CCDS58414.1. [Q99640-3]
CCDS58415.1. [Q99640-4]
RefSeqNP_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]
UniGeneHs.732385.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P1AX-ray1.70A75-362[»]
ProteinModelPortalQ99640.
SMRQ99640. Positions 76-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114544. 9 interactions.
IntActQ99640. 6 interactions.
MINTMINT-3059438.
STRING9606.ENSP00000262300.

Chemistry

BindingDBQ99640.
ChEMBLCHEMBL3984.
GuidetoPHARMACOLOGY2167.

PTM databases

PhosphoSiteQ99640.

Polymorphism databases

DMDM55976573.

Proteomic databases

MaxQBQ99640.
PaxDbQ99640.
PRIDEQ99640.

Protocols and materials databases

DNASU9088.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262300; ENSP00000262300; ENSG00000127564. [Q99640-1]
ENST00000440027; ENSP00000397739; ENSG00000127564. [Q99640-2]
ENST00000573944; ENSP00000459123; ENSG00000127564. [Q99640-3]
ENST00000574385; ENSP00000458943; ENSG00000127564. [Q99640-3]
ENST00000574730; ENSP00000460868; ENSG00000127564. [Q99640-4]
GeneID9088.
KEGGhsa:9088.
UCSCuc002csn.3. human. [Q99640-1]

Organism-specific databases

CTD9088.
GeneCardsGC16M002995.
HGNCHGNC:29650. PKMYT1.
HPACAB046000.
MIM602474. gene.
neXtProtNX_Q99640.
PharmGKBPA385.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000293277.
HOVERGENHBG053623.
InParanoidQ99640.
KOK06633.
PhylomeDBQ99640.
TreeFamTF101087.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkQ99640.

Gene expression databases

ArrayExpressQ99640.
BgeeQ99640.
CleanExHS_MYT1.
HS_PKMYT1.
GenevestigatorQ99640.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000567. TYPK_Myt1. 1 hit.
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPKMYT1. human.
EvolutionaryTraceQ99640.
GeneWikiPKMYT1.
GenomeRNAi9088.
NextBio34055.
PROQ99640.
SOURCESearch...

Entry information

Entry namePMYT1_HUMAN
AccessionPrimary (citable) accession number: Q99640
Secondary accession number(s): B3KUN8 expand/collapse secondary AC list , B4DXD4, D3DUA4, F8W164, I3L1V2, O14731, Q7LE24, Q8TCM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM