PWP2A_HUMAN - dbPTM
PWP2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PWP2A_HUMAN
UniProt AC Q96N64
Protein Name PWWP domain-containing protein 2A
Gene Name PWWP2A
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization Nucleus .
Protein Description H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. Also required for proper mitosis progression..
Protein Sequence MAAVAAEAAATAASPGEGGAGEAEPEMEPIPGSEAGTDPLPVTATEASVPDGETDGQQSAPQADEPPLPPPPPPPGELARSPEAVGPELEAEEKLSVRVAESAAAAPQGGPELPPSPASPPEQPPAPEEREEPPLPQPVAPALVPPAGGDSTVSQLIPGSEVRVTLDHIIEDALVVSFRFGEKLFSGVLMDLSKRFGPHGIPVTVFPKREYKDKPEAMPLQSNTFQEGTEVKCEANGAVPDDPSPVPHPELSLAESLWTSKPPPLFHEGAPYPPPLFIRDTYNQSIPQPPPRKIKRPKRKMYREEPTSIMNAIKLRPRQVLCDKCKNSVVAEKKEIRKGSSATDSSKYEDKKRRNESVTTVNKKLKTDHKVDGKNQNESQKRNAVVKVSNIAHSRGRVVKVSAQANTSKAQLSTKKVLQSKNMDHAKAREVLKIAKEKAQKKQNETSTSKNAHSKVHFTRRYQNPSSGSLPPRVRLKPQRYRNEENDSSLKTGLEKMRSGKMAPKPQSRCTSTRSAGEAPSENQSPSKGPEEASSEVQDTNEVHVPGDQDEPQTLGKKGSKNNISVYMTLNQKKSDSSSASVCSIDSTDDLKSSNSECSSSESFDFPPGSMHAPSTSSTSSSSKEEKKLSNSLKMKVFSKNVSKCVTPDGRTICVGDIVWAKIYGFPWWPARILTITVSRKDNGLLVRQEARISWFGSPTTSFLALSQLSPFLENFQSRFNKKRKGLYRKAITEAAKAAKQLTPEVRALLTQFET
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
81PhosphorylationPPGELARSPEAVGPE
CCCCCCCCCCCCCCC		22.8329255136
102PhosphorylationLSVRVAESAAAAPQG
HHHHHHHHHHHCCCC		17.3030108239
116PhosphorylationGGPELPPSPASPPEQ
CCCCCCCCCCCCCCC		31.0330266825
119PhosphorylationELPPSPASPPEQPPA
CCCCCCCCCCCCCCC		44.3530266825
186PhosphorylationRFGEKLFSGVLMDLS
ECCCHHHHHHHHHHH		38.1324719451
190SulfoxidationKLFSGVLMDLSKRFG
HHHHHHHHHHHHHHC		4.5321406390
193PhosphorylationSGVLMDLSKRFGPHG
HHHHHHHHHHHCCCC		19.9520068231
204PhosphorylationGPHGIPVTVFPKREY
CCCCCEEEECCCCCC		15.8624719451
208SumoylationIPVTVFPKREYKDKP
CEEEECCCCCCCCCC		46.5328112733
302PhosphorylationKRPKRKMYREEPTSI
CCCCCHHCCCCCCCH		20.2225690035
307PhosphorylationKMYREEPTSIMNAIK
HHCCCCCCCHHHHHH		33.8825690035
308PhosphorylationMYREEPTSIMNAIKL
HCCCCCCCHHHHHHC		30.4725690035
338AcetylationAEKKEIRKGSSATDS
HHHHHHHCCCCCCCH		69.6612436571
352AcetylationSSKYEDKKRRNESVT
HHHHHHHHHCCCCCH		69.7612436581
357PhosphorylationDKKRRNESVTTVNKK
HHHHCCCCCHHHHHH		28.4529083192
359PhosphorylationKRRNESVTTVNKKLK
HHCCCCCHHHHHHHC		34.0129083192
360PhosphorylationRRNESVTTVNKKLKT
HCCCCCHHHHHHHCC		21.6729083192
416AcetylationKAQLSTKKVLQSKNM
HHHHHHHHHHHHCCC		48.557297939
420PhosphorylationSTKKVLQSKNMDHAK
HHHHHHHHCCCCHHH		23.10-
427AcetylationSKNMDHAKAREVLKI
HCCCCHHHHHHHHHH		44.557297949
436AcetylationREVLKIAKEKAQKKQ
HHHHHHHHHHHHHHH		64.3211793477
438AcetylationVLKIAKEKAQKKQNE
HHHHHHHHHHHHHCC		56.257617887
441AcetylationIAKEKAQKKQNETST
HHHHHHHHHHCCCCC		62.277469387
442AcetylationAKEKAQKKQNETSTS
HHHHHHHHHCCCCCC		46.4011793487
446PhosphorylationAQKKQNETSTSKNAH
HHHHHCCCCCCCCHH		44.8724144214
447PhosphorylationQKKQNETSTSKNAHS
HHHHCCCCCCCCHHH		25.2224144214
448PhosphorylationKKQNETSTSKNAHSK
HHHCCCCCCCCHHHH		51.6624144214
449PhosphorylationKQNETSTSKNAHSKV
HHCCCCCCCCHHHHH		24.5525690035
450UbiquitinationQNETSTSKNAHSKVH
HCCCCCCCCHHHHHE		59.2433845483
462PhosphorylationKVHFTRRYQNPSSGS
HHEEEECCCCCCCCC		14.8922817900
469PhosphorylationYQNPSSGSLPPRVRL
CCCCCCCCCCCCCCC		39.3824719451
492PhosphorylationENDSSLKTGLEKMRS
CCCHHHHHHHHHHHC		52.9021406692
499PhosphorylationTGLEKMRSGKMAPKP
HHHHHHHCCCCCCCC		38.9920068231
501AcetylationLEKMRSGKMAPKPQS
HHHHHCCCCCCCCCC		32.8925953088
511PhosphorylationPKPQSRCTSTRSAGE
CCCCCCCCCCCCCCC		31.8328348404
515PhosphorylationSRCTSTRSAGEAPSE
CCCCCCCCCCCCCCC		40.4923663014
521PhosphorylationRSAGEAPSENQSPSK
CCCCCCCCCCCCCCC		57.1130278072
525PhosphorylationEAPSENQSPSKGPEE
CCCCCCCCCCCCHHH		42.6030278072
527PhosphorylationPSENQSPSKGPEEAS
CCCCCCCCCCHHHHH		56.3330278072
534PhosphorylationSKGPEEASSEVQDTN
CCCHHHHHHCCCCCC		30.2523663014
535PhosphorylationKGPEEASSEVQDTNE
CCHHHHHHCCCCCCC		49.1623663014
540PhosphorylationASSEVQDTNEVHVPG
HHHCCCCCCCCCCCC		19.0423663014
554PhosphorylationGDQDEPQTLGKKGSK
CCCCCCCCCCCCCCC		48.4721406692
575PhosphorylationMTLNQKKSDSSSASV
EEECCCCCCCCCCCE		50.1630177828
577PhosphorylationLNQKKSDSSSASVCS
ECCCCCCCCCCCEEE		33.0324667141
578PhosphorylationNQKKSDSSSASVCSI
CCCCCCCCCCCEEEC		34.6125159151
579PhosphorylationQKKSDSSSASVCSID
CCCCCCCCCCEEECC		28.6330177828
581PhosphorylationKSDSSSASVCSIDST
CCCCCCCCEEECCCC		26.1323663014
584PhosphorylationSSSASVCSIDSTDDL
CCCCCEEECCCCCHH		27.5523663014
587PhosphorylationASVCSIDSTDDLKSS
CCEEECCCCCHHHHC		31.8723663014
588PhosphorylationSVCSIDSTDDLKSSN
CEEECCCCCHHHHCC		29.7723663014
630PhosphorylationSKEEKKLSNSLKMKV
CHHHHHHHHHHHHHH		33.0021406692
632PhosphorylationEEKKLSNSLKMKVFS
HHHHHHHHHHHHHHH		26.4521406692
634AcetylationKKLSNSLKMKVFSKN
HHHHHHHHHHHHHCC		36.1718604569
636AcetylationLSNSLKMKVFSKNVS
HHHHHHHHHHHCCHH		38.2418604577
652PhosphorylationCVTPDGRTICVGDIV
CCCCCCCEEEECCEE		25.0223403867
701PhosphorylationSWFGSPTTSFLALSQ
ECCCCCHHHHHHHHH		22.3622210691
702PhosphorylationWFGSPTTSFLALSQL
CCCCCHHHHHHHHHH		22.2722210691
718PhosphorylationPFLENFQSRFNKKRK
HHHHHHHHHHHHHCH		34.4022210691
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 PWP2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PWP2A_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 PWP2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PWP2A_HUMAN !!
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 PWP2A_HUMAN

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Related Literatures of Post-Translational Modification
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-116 AND SER-119, 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 SER-81, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-499, AND MASSSPECTROMETRY.

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