PMYT1_HUMAN - dbPTM
PMYT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMYT1_HUMAN
UniProt AC Q99640
Protein Name Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
Gene Name PKMYT1
Organism Homo sapiens (Human).
Sequence Length 499
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein . Golgi apparatus membrane
Peripheral membrane protein .
Protein Description 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..
Protein Sequence MLERPPALAMPMPTEGTPPPLSGTPIPVPAYFRHAEPGFSLKRPRGLSRSLPPPPPAKGSIPISRLFPPRTPGWHQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQPRAWGVLWCMAAEALSRGWALWQALLALLCWLWHGLAHPASWLQPLGPPATPPGSPPCSLLLDSSLSSNWDDDSLGPSLSPEAVLARTVGSTSTPRSRCTPRDALDLSDINSEPPRGSFPSFEPRNLLSLFEDTLDPT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MLERPPAL
-------CCCCCCCC		8.7120068231
14PhosphorylationALAMPMPTEGTPPPL
CCCCCCCCCCCCCCC		40.5722199227
17PhosphorylationMPMPTEGTPPPLSGT
CCCCCCCCCCCCCCC		26.7925159151
22PhosphorylationEGTPPPLSGTPIPVP
CCCCCCCCCCCCCCC		46.5222199227
24PhosphorylationTPPPLSGTPIPVPAY
CCCCCCCCCCCCCCC		18.0522199227
31PhosphorylationTPIPVPAYFRHAEPG
CCCCCCCCCCCCCCC		8.6227273156
40PhosphorylationRHAEPGFSLKRPRGL
CCCCCCCCCCCCCCC		38.6130266825
42MethylationAEPGFSLKRPRGLSR
CCCCCCCCCCCCCCC		60.1982981881
42UbiquitinationAEPGFSLKRPRGLSR
CCCCCCCCCCCCCCC		60.19-
48PhosphorylationLKRPRGLSRSLPPPP
CCCCCCCCCCCCCCC		23.7320068231
50PhosphorylationRPRGLSRSLPPPPPA
CCCCCCCCCCCCCCC		41.6830266825
58UbiquitinationLPPPPPAKGSIPISR
CCCCCCCCCCCCHHH		59.99-
60PhosphorylationPPPPAKGSIPISRLF
CCCCCCCCCCHHHCC		25.2020068231
64PhosphorylationAKGSIPISRLFPPRT
CCCCCCHHHCCCCCC		19.9920068231
71PhosphorylationSRLFPPRTPGWHQLQ
HHCCCCCCCCCCCCC		31.7423312004
89PhosphorylationVSFRGEASETLQSPG
EEECCCHHHHHCCCC		27.1530266825
91PhosphorylationFRGEASETLQSPGYD
ECCCHHHHHCCCCCC		27.8330266825
94PhosphorylationEASETLQSPGYDPSR
CHHHHHCCCCCCCCC		24.3330266825
97PhosphorylationETLQSPGYDPSRPES
HHHCCCCCCCCCCHH		28.2330266825
100PhosphorylationQSPGYDPSRPESFFQ
CCCCCCCCCCHHHHH		58.5330266825
104PhosphorylationYDPSRPESFFQQSFQ
CCCCCCHHHHHHHHH		33.7630266825
109PhosphorylationPESFFQQSFQRLSRL
CHHHHHHHHHHHHCC		16.7426055452
120PhosphorylationLSRLGHGSYGEVFKV
HHCCCCCCCCCEEEE		25.0425159151
121PhosphorylationSRLGHGSYGEVFKVR
HCCCCCCCCCEEEEE		23.1528796482
126UbiquitinationGSYGEVFKVRSKEDG
CCCCCEEEEEECCCC		41.7521906983
126MethylationGSYGEVFKVRSKEDG
CCCCCEEEEEECCCC		41.7542359113
136PhosphorylationSKEDGRLYAVKRSMS
ECCCCCEEEEEECCC		14.1620068231
139UbiquitinationDGRLYAVKRSMSPFR
CCCEEEEEECCCCCC		30.50-
141PhosphorylationRLYAVKRSMSPFRGP
CEEEEEECCCCCCCH		20.2130266825
143PhosphorylationYAVKRSMSPFRGPKD
EEEEECCCCCCCHHH		23.3325159151
149UbiquitinationMSPFRGPKDRARKLA
CCCCCCHHHHHHHHH		63.77-
154UbiquitinationGPKDRARKLAEVGSH
CHHHHHHHHHHHCCC		51.5721906983
160PhosphorylationRKLAEVGSHEKVGQH
HHHHHHCCCCCCCCC		33.3825159151
163UbiquitinationAEVGSHEKVGQHPCC
HHHCCCCCCCCCCCE		46.36-
330PhosphorylationEFTAGLSSELRSVLV
HHHCCCCHHHHHHHH		45.7724719451
345UbiquitinationMMLEPDPKLRATAEA
HHHCCCHHHHHHHHH		58.97-
412PhosphorylationQPLGPPATPPGSPPC
CCCCCCCCCCCCCCC		35.4726074081
416PhosphorylationPPATPPGSPPCSLLL
CCCCCCCCCCCCEEE		31.2926074081
420PhosphorylationPPGSPPCSLLLDSSL
CCCCCCCCEEECCCC		28.0326074081
426PhosphorylationCSLLLDSSLSSNWDD
CCEEECCCCCCCCCC		31.7522817900
441PhosphorylationDSLGPSLSPEAVLAR
CCCCCCCCHHHHHHH		25.6522817900
449PhosphorylationPEAVLARTVGSTSTP
HHHHHHHHCCCCCCC		24.5028102081
452PhosphorylationVLARTVGSTSTPRSR
HHHHHCCCCCCCCCC		18.1729396449
453PhosphorylationLARTVGSTSTPRSRC
HHHHCCCCCCCCCCC		30.5928985074
454PhosphorylationARTVGSTSTPRSRCT
HHHCCCCCCCCCCCC		37.8028176443
455PhosphorylationRTVGSTSTPRSRCTP
HHCCCCCCCCCCCCC		23.8625849741
458PhosphorylationGSTSTPRSRCTPRDA
CCCCCCCCCCCCCHH		32.6723312004
461PhosphorylationSTPRSRCTPRDALDL
CCCCCCCCCCHHCCH		21.9022817900
469PhosphorylationPRDALDLSDINSEPP
CCHHCCHHHCCCCCC		35.7930266825
473PhosphorylationLDLSDINSEPPRGSF
CCHHHCCCCCCCCCC		52.3823927012
479PhosphorylationNSEPPRGSFPSFEPR
CCCCCCCCCCCCCCH		34.9523401153
482PhosphorylationPPRGSFPSFEPRNLL
CCCCCCCCCCCHHHH		39.9930266825
490PhosphorylationFEPRNLLSLFEDTLD
CCCHHHHHHHHHCCC		33.8929485707
495PhosphorylationLLSLFEDTLDPT---
HHHHHHHCCCCC---		26.3412738781
499PhosphorylationFEDTLDPT-------
HHHCCCCC-------		51.4120873877
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
426SPhosphorylationKinasePLK1P53350
Uniprot
495TPhosphorylationKinasePLK1P53350
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMYT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PMYT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
9499405
MK08_HUMANMAPK8physical
19204086
MK10_HUMANMAPK10physical
19204086
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMYT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-50; SER-120;SER-469 AND SER-473, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-94; SER-120;SER-143; SER-160; SER-469 AND THR-495, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION AT SER-426 AND THR-495.

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