PWP2_HUMAN - dbPTM
PWP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PWP2_HUMAN
UniProt AC Q15269
Protein Name Periodic tryptophan protein 2 homolog
Gene Name PWP2
Organism Homo sapiens (Human).
Sequence Length 919
Subcellular Localization Nucleus, nucleolus .
Protein Description
Protein Sequence MKFAYRFSNLLGTVYRRGNLNFTCDGNSVISPVGNRVTVFDLKNNKSDTLPLATRYNVKCVGLSPDGRLAIIVDEGGDALLVSLVCRSVLHHFHFKGSVHSVSFSPDGRKFVVTKGNIAQMYHAPGKKREFNAFVLDKTYFGPYDETTCIDWTDDSRCFVVGSKDMSTWVFGAERWDNLIYYALGGHKDAIVACFFESNSLDLYSLSQDGVLCMWQCDTPPEGLRLKPPAGWKADLLQREEEEEEEEDQEGDRETTIRGKATPAEEEKTGKVKYSRLAKYFFNKEGDFNNLTAAAFHKKSHLLVTGFASGIFHLHELPEFNLIHSLSISDQSIASVAINSSGDWIAFGCSGLGQLLVWEWQSESYVLKQQGHFNSMVALAYSPDGQYIVTGGDDGKVKVWNTLSGFCFVTFTEHSSGVTGVTFTATGYVVVTSSMDGTVRAFDLHRYRNFRTFTSPRPTQFSCVAVDASGEIVSAGAQDSFEIFVWSMQTGRLLDVLSGHEGPISGLCFNPMKSVLASASWDKTVRLWDMFDSWRTKETLALTSDALAVTFRPDGAELAVATLNSQITFWDPENAVQTGSIEGRHDLKTGRKELDKITAKHAAKGKAFTALCYSADGHSILAGGMSKFVCIYHVREQILMKRFEISCNLSLDAMEEFLNRRKMTEFGNLALIDQDAGQEDGVAIPLPGVRKGDMSSRHFKPEIRVTSLRFSPTGRCWAATTTEGLLIYSLDTRVLFDPFELDTSVTPGRVREALRQQDFTRAILMALRLNESKLVQEALEAVPRGEIEVVTSSLPELYVEKVLEFLASSFEVSRHLEFYLLWTHKLLMLHGQKLKSRAGTLLPVIQFLQKSIQRHLDDLSKLCSWNHYNMQYALAVSKQRGTKRSLDPLGSEEEAEASEDDSLHLLGGGGRDSEEEMLA
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
2Methylation------MKFAYRFSN
------CCHHHHHHH		38.41115975955
432-HydroxyisobutyrylationRVTVFDLKNNKSDTL
EEEEEECCCCCCCCC		61.39-
43UbiquitinationRVTVFDLKNNKSDTL
EEEEEECCCCCCCCC		61.3921906983
43AcetylationRVTVFDLKNNKSDTL
EEEEEECCCCCCCCC		61.3925953088
43MethylationRVTVFDLKNNKSDTL
EEEEEECCCCCCCCC		61.3942365565
46UbiquitinationVFDLKNNKSDTLPLA
EEECCCCCCCCCCEE		60.1322817900
47PhosphorylationFDLKNNKSDTLPLAT
EECCCCCCCCCCEEE		37.6420068231
49PhosphorylationLKNNKSDTLPLATRY
CCCCCCCCCCEEEEE		37.0520068231
54PhosphorylationSDTLPLATRYNVKCV
CCCCCEEEEECEEEE		41.1720068231
54O-linked_GlycosylationSDTLPLATRYNVKCV
CCCCCEEEEECEEEE		41.1730379171
56PhosphorylationTLPLATRYNVKCVGL
CCCEEEEECEEEEEE		21.6924719451
592-HydroxyisobutyrylationLATRYNVKCVGLSPD
EEEEECEEEEEECCC		21.40-
59AcetylationLATRYNVKCVGLSPD
EEEEECEEEEEECCC		21.4026051181
59UbiquitinationLATRYNVKCVGLSPD
EEEEECEEEEEECCC		21.4024816145
64PhosphorylationNVKCVGLSPDGRLAI
CEEEEEECCCCCEEE		18.2824719451
114PhosphorylationDGRKFVVTKGNIAQM
CCCEEEEEECCCEEE		28.12-
115UbiquitinationGRKFVVTKGNIAQMY
CCEEEEEECCCEEEE		38.0529967540
115AcetylationGRKFVVTKGNIAQMY
CCEEEEEECCCEEEE		38.0526051181
127UbiquitinationQMYHAPGKKREFNAF
EEEECCCCCCEEEEE		47.8227667366
163PhosphorylationSRCFVVGSKDMSTWV
CCEEEEECCCCCEEE		17.5520068231
181PhosphorylationERWDNLIYYALGGHK
HHHHHHHHHHHCCCC		5.9523917254
227UbiquitinationPPEGLRLKPPAGWKA
CCCCCCCCCCCCHHH		42.39-
233UbiquitinationLKPPAGWKADLLQRE
CCCCCCHHHHHHHHH		30.9821890473
253MethylationEEDQEGDRETTIRGK
HHHCCCCCCEECCCC		54.76115489707
255PhosphorylationDQEGDRETTIRGKAT
HCCCCCCEECCCCCC		28.5424732914
256PhosphorylationQEGDRETTIRGKATP
CCCCCCEECCCCCCC		12.1524732914
262PhosphorylationTTIRGKATPAEEEKT
EECCCCCCCHHHHCC		26.9028985074
268UbiquitinationATPAEEEKTGKVKYS
CCCHHHHCCCCCCHH		66.8924816145
268AcetylationATPAEEEKTGKVKYS
CCCHHHHCCCCCCHH		66.8926051181
273AcetylationEEKTGKVKYSRLAKY
HHCCCCCCHHHHHHH		40.787697081
279AcetylationVKYSRLAKYFFNKEG
CCHHHHHHHHCCCCC		47.3725825284
279UbiquitinationVKYSRLAKYFFNKEG
CCHHHHHHHHCCCCC		47.3722817900
284UbiquitinationLAKYFFNKEGDFNNL
HHHHHCCCCCCCCCC		58.9021906983
284AcetylationLAKYFFNKEGDFNNL
HHHHHCCCCCCCCCC		58.9026051181
298AcetylationLTAAAFHKKSHLLVT
CCHHHHHCCCCEEEE		49.9026051181
514PhosphorylationLCFNPMKSVLASASW
CCCCCHHHHHHHCCC		18.9920860994
518PhosphorylationPMKSVLASASWDKTV
CHHHHHHHCCCCCCC		20.7620860994
520PhosphorylationKSVLASASWDKTVRL
HHHHHHCCCCCCCHH		33.0620860994
523UbiquitinationLASASWDKTVRLWDM
HHHCCCCCCCHHHHH		42.5322817900
543O-linked_GlycosylationTKETLALTSDALAVT
CHHHEEEECCEEEEE		20.9630379171
592AcetylationHDLKTGRKELDKITA
CCCCCCCHHHHHHHH		65.0626051181
600AcetylationELDKITAKHAAKGKA
HHHHHHHHHHHCCCC		25.7325953088
600UbiquitinationELDKITAKHAAKGKA
HHHHHHHHHHHCCCC		25.7329967540
609PhosphorylationAAKGKAFTALCYSAD
HHCCCCEEEEEECCC		24.47-
632PhosphorylationMSKFVCIYHVREQIL
CCEEEEEHHHHHHHH		6.8020068231
662UbiquitinationEEFLNRRKMTEFGNL
HHHHHHCCCCCCCCE		47.1122817900
691MethylationIPLPGVRKGDMSSRH
EECCCCCCCCCCCCC		57.7823644510
700UbiquitinationDMSSRHFKPEIRVTS
CCCCCCCCCEEEEEE		35.3019608861
700AcetylationDMSSRHFKPEIRVTS
CCCCCCCCCEEEEEE		35.3023749302
707PhosphorylationKPEIRVTSLRFSPTG
CCEEEEEEEEECCCC		18.07-
711PhosphorylationRVTSLRFSPTGRCWA
EEEEEEECCCCCEEE		18.3427067055
743PhosphorylationFDPFELDTSVTPGRV
CCCCCCCCCCCHHHH		37.4124732914
744PhosphorylationDPFELDTSVTPGRVR
CCCCCCCCCCHHHHH		24.5424732914
746PhosphorylationFELDTSVTPGRVREA
CCCCCCCCHHHHHHH		21.5721712546
773UbiquitinationALRLNESKLVQEALE
HHHCCHHHHHHHHHH		46.6421906983
791PhosphorylationRGEIEVVTSSLPELY
CCCEEEEECCCCHHH		20.1320068231
792PhosphorylationGEIEVVTSSLPELYV
CCEEEEECCCCHHHH		20.4720068231
793PhosphorylationEIEVVTSSLPELYVE
CEEEEECCCCHHHHH		38.2820068231
798PhosphorylationTSSLPELYVEKVLEF
ECCCCHHHHHHHHHH		12.6120068231
850UbiquitinationPVIQFLQKSIQRHLD
HHHHHHHHHHHHHHH		52.2332015554
860PhosphorylationQRHLDDLSKLCSWNH
HHHHHHHHHHHHCCC		30.4920860994
885PhosphorylationKQRGTKRSLDPLGSE
HHCCCCCCCCCCCCH		38.3823663014
891PhosphorylationRSLDPLGSEEEAEAS
CCCCCCCCHHHHHCC		49.9021955146
898PhosphorylationSEEEAEASEDDSLHL
CHHHHHCCCCCCEEC		32.8225159151
902PhosphorylationAEASEDDSLHLLGGG
HHCCCCCCEECCCCC		29.9721955146
913PhosphorylationLGGGGRDSEEEMLA-
CCCCCCCCHHHHCC-		45.6125159151
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

Oops, there are no upstream regulatory protein records of PWP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PWP2_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 PWP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM1L1_HUMANTOM1L1physical
16169070
WDR36_HUMANWDR36physical
22939629
U3IP2_HUMANRRP9physical
22939629
MPP10_HUMANMPHOSPH10physical
26344197
TBL3_HUMANTBL3physical
26344197
WDR36_HUMANWDR36physical
26344197
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 PWP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-700, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891 AND SER-898, ANDMASS SPECTROMETRY.
"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 THR-746; SER-891; SER-898;SER-902 AND SER-913, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891 AND SER-913, ANDMASS SPECTROMETRY.

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