PWP2B_HUMAN - dbPTM
PWP2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PWP2B_HUMAN
UniProt AC Q6NUJ5
Protein Name PWWP domain-containing protein 2B
Gene Name PWWP2B
Organism Homo sapiens (Human).
Sequence Length 590
Subcellular Localization
Protein Description
Protein Sequence MEPRAGCRLPVRVEQVVNGALVVTVSCGERSFAGILLDCTKKSGLFGLPPLAPLPQVDESPVNDSHGRAPEEGDAEVMQLGSSSPPPARGVQPPETTRPEPPPPLVPPLPAGSLPPYPPYFEGAPFPHPLWLRDTYKLWVPQPPPRTIKRTRRRLSRNRDPGRLILSTIRLRPRQVLCEKCKSTLSPPEASPGPPAAPRARRRLGSGPDRELRKPEEPENGEPTAAATARRSKRERREEDRAPAEQVPRSPVIKISYSTPQGKGEVVKIPSRVHGSLEPFRPQQAPQDDGSQDPEVLDRESRDRPSCAPSASIPKLKLTRPVPAGADLPPPKIRLKPHRLGDSEHEPVYRAELVGELNGYLRDSSPAPCADGPAGGLADLSSGSSGEDDDFKSCPQGPQGREGLAFLVSCPEGRADCASESACSSDSLDEARSSGSEGTPADTGDLSPGHGASAPSVSREARQTVPPLTVRLHTQSVSECITEDGRTVAVGDIVWGKIHGFPWWPARVLDISLGQKEDGEPSWREAKVSWFGSPTTSFLSISKLSPFSEFFKLRFNRKKKGMYRKAITEAANAARHVAPEIRELLTQFET
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
43PhosphorylationLLDCTKKSGLFGLPP
EEECCCCCCCCCCCC
42.14-
60PhosphorylationPLPQVDESPVNDSHG
CCCCCCCCCCCCCCC
29.6825849741
65PhosphorylationDESPVNDSHGRAPEE
CCCCCCCCCCCCCCC
23.7222210691
82PhosphorylationAEVMQLGSSSPPPAR
CCHHCCCCCCCCCCC
35.9123401153
83PhosphorylationEVMQLGSSSPPPARG
CHHCCCCCCCCCCCC
45.1026657352
84PhosphorylationVMQLGSSSPPPARGV
HHCCCCCCCCCCCCC
43.0226657352
167PhosphorylationDPGRLILSTIRLRPR
CCCCEEEEEEECCCH
18.1320068231
168PhosphorylationPGRLILSTIRLRPRQ
CCCEEEEEEECCCHH
13.4820068231
183PhosphorylationVLCEKCKSTLSPPEA
HHHHHHHHCCCCCCC
44.0122199227
184PhosphorylationLCEKCKSTLSPPEAS
HHHHHHHCCCCCCCC
19.4222199227
186PhosphorylationEKCKSTLSPPEASPG
HHHHHCCCCCCCCCC
38.2025159151
191PhosphorylationTLSPPEASPGPPAAP
CCCCCCCCCCCCCCH
28.8225159151
206PhosphorylationRARRRLGSGPDRELR
HHHHHCCCCCCHHHC
52.3127794612
250PhosphorylationPAEQVPRSPVIKISY
CHHHCCCCCEEEEEE
19.9023401153
256PhosphorylationRSPVIKISYSTPQGK
CCCEEEEEEECCCCC
14.1826852163
257PhosphorylationSPVIKISYSTPQGKG
CCEEEEEEECCCCCC
21.7526852163
258PhosphorylationPVIKISYSTPQGKGE
CEEEEEEECCCCCCC
27.1625159151
259PhosphorylationVIKISYSTPQGKGEV
EEEEEEECCCCCCCE
16.0525159151
271PhosphorylationGEVVKIPSRVHGSLE
CCEEECCCCCCCCCC
50.8620068231
276PhosphorylationIPSRVHGSLEPFRPQ
CCCCCCCCCCCCCCC
18.0625159151
291PhosphorylationQAPQDDGSQDPEVLD
CCCCCCCCCCHHHHC
38.1017525332
312PhosphorylationPSCAPSASIPKLKLT
CCCCCCCCCCCCEEC
43.7028555341
360PhosphorylationLVGELNGYLRDSSPA
HHHHHCCEECCCCCC
9.4827050516
433PhosphorylationDSLDEARSSGSEGTP
CCHHHHHHCCCCCCC
46.2123927012
434PhosphorylationSLDEARSSGSEGTPA
CHHHHHHCCCCCCCC
40.5623927012
436PhosphorylationDEARSSGSEGTPADT
HHHHHCCCCCCCCCC
34.5023927012
439PhosphorylationRSSGSEGTPADTGDL
HHCCCCCCCCCCCCC
15.9723927012
443PhosphorylationSEGTPADTGDLSPGH
CCCCCCCCCCCCCCC
34.4026657352
447PhosphorylationPADTGDLSPGHGASA
CCCCCCCCCCCCCCC
33.3123401153
453PhosphorylationLSPGHGASAPSVSRE
CCCCCCCCCCCCCHH
45.3528450419
456PhosphorylationGHGASAPSVSREARQ
CCCCCCCCCCHHHHH
32.2328450419
458PhosphorylationGASAPSVSREARQTV
CCCCCCCCHHHHHCC
28.8328450419
474PhosphorylationPLTVRLHTQSVSECI
CEEEEEECCCHHHHC
27.4223312004
476PhosphorylationTVRLHTQSVSECITE
EEEEECCCHHHHCCC
28.8524719451
478PhosphorylationRLHTQSVSECITEDG
EEECCCHHHHCCCCC
31.8123532336
482PhosphorylationQSVSECITEDGRTVA
CCHHHHCCCCCCEEE
39.4223532336
522PhosphorylationQKEDGEPSWREAKVS
CCCCCCCCCCEEEEE
34.1726091039
540PhosphorylationSPTTSFLSISKLSPF
CCCCEEEEHHHCCCH
23.8624719451
558AcetylationFKLRFNRKKKGMYRK
HHHHHCCCCCCHHHH
61.007684987
559AcetylationKLRFNRKKKGMYRKA
HHHHCCCCCCHHHHH
51.857684995
565AcetylationKKKGMYRKAITEAAN
CCCCHHHHHHHHHHH
27.017685203

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 PWP2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PWP2B_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 PWP2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PWP2B_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 PWP2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY.

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