WBP2_HUMAN - dbPTM
WBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WBP2_HUMAN
UniProt AC Q969T9
Protein Name WW domain-binding protein 2
Gene Name WBP2
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Cytoplasm . Nucleus . Translocates from cytoplasm to nucleus when phosphorylated.
Protein Description Acts as transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation. [PubMed: 16772533 In presence of estrogen, binds to ESR1-responsive promoters]
Protein Sequence MALNKNHSEGGGVIVNNTESILMSYDHVELTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSASYKLTFTAGGAIEFGQRMLQVASQASRGEVPSGAYGYSYMPSGAYVYPPPVANGMYPCPPGYPYPPPPPEFYPGPPMMDGAMGYVQPPPPPYPGPMEPPVSGPDVPSTPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQ
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
36UbiquitinationELTFNDMKNVPEAFK
EEEHHHHCCCCHHHC		58.62-
43UbiquitinationKNVPEAFKGTKKGTV
CCCCHHHCCCCCCEE		73.12-
49PhosphorylationFKGTKKGTVYLTPYR
HCCCCCCEEEECCEE		18.1720068231
51PhosphorylationGTKKGTVYLTPYRVI
CCCCCEEEECCEEEE		12.5120068231
53PhosphorylationKKGTVYLTPYRVIFL
CCCEEEECCEEEEEE		10.6920068231
55PhosphorylationGTVYLTPYRVIFLSK
CEEEECCEEEEEECC		16.5720068231
61PhosphorylationPYRVIFLSKGKDAMQ
CEEEEEECCCHHHHH		28.7220068231
62UbiquitinationYRVIFLSKGKDAMQS
EEEEEECCCHHHHHH		72.61-
64UbiquitinationVIFLSKGKDAMQSFM
EEEECCCHHHHHHCH		46.15-
69PhosphorylationKGKDAMQSFMMPFYL
CCHHHHHHCHHCHHH		11.30-
83UbiquitinationLMKDCEIKQPVFGAN
HCCCCCCCCCCCCCE		26.68-
91PhosphorylationQPVFGANYIKGTVKA
CCCCCCEEEEEEEEE		11.9523532336
93UbiquitinationVFGANYIKGTVKAEA
CCCCEEEEEEEEEEE		37.86-
126SulfoxidationAIEFGQRMLQVASQA
HHHHHHHHHHHHHHH		2.0621406390
131PhosphorylationQRMLQVASQASRGEV
HHHHHHHHHHHCCCC		27.6728857561
134PhosphorylationLQVASQASRGEVPSG
HHHHHHHHCCCCCCC		32.9320068231
143PhosphorylationGEVPSGAYGYSYMPS
CCCCCCCCCCCCCCC		21.81-
192PhosphorylationMMDGAMGYVQPPPPP
CCCCCCCCCCCCCCC		5.2621642474
222UbiquitinationSTPAAEAKAAEAAAS
CCHHHHHHHHHHHHH		39.37-
229PhosphorylationKAAEAAASAYYNPGN
HHHHHHHHHHCCCCC		16.4521945579
231PhosphorylationAEAAASAYYNPGNPH
HHHHHHHHCCCCCCC		10.9821945579
232PhosphorylationEAAASAYYNPGNPHN
HHHHHHHCCCCCCCC		18.0121945579
241PhosphorylationPGNPHNVYMPTSQPP
CCCCCCCCCCCCCCC		11.6021945579
244O-linked_GlycosylationPHNVYMPTSQPPPPP
CCCCCCCCCCCCCCC		24.38OGP
244PhosphorylationPHNVYMPTSQPPPPP
CCCCCCCCCCCCCCC		24.3821945579
245PhosphorylationHNVYMPTSQPPPPPY
CCCCCCCCCCCCCCC		34.5221945579
252PhosphorylationSQPPPPPYYPPEDKK
CCCCCCCCCCCCCCC		34.0821945579
253PhosphorylationQPPPPPYYPPEDKKT
CCCCCCCCCCCCCCC		20.3421945579
258UbiquitinationPYYPPEDKKTQ----
CCCCCCCCCCC----		56.9321906983
259UbiquitinationYYPPEDKKTQ-----
CCCCCCCCCC-----		65.56-
260PhosphorylationYPPEDKKTQ------
CCCCCCCCC------		45.3027251275
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
192YPhosphorylationKinaseSRCP12931
Uniprot
192YPhosphorylationKinaseYES1P07947
GPS
231YPhosphorylationKinaseSRCP12931
Uniprot
231YPhosphorylationKinaseYES1P07947
GPS
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:26371805
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WBP2_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 WBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WWP1_HUMANWWP1physical
9169421
WWP2_HUMANWWP2physical
9169421
MAGI1_HUMANMAGI1physical
9169421
NEDD4_HUMANNEDD4physical
19953087
NED4L_HUMANNEDD4Lphysical
19953087
MAGA4_HUMANMAGEA4physical
21516116
CTNB1_HUMANCTNNB1physical
27578003
ITCH_HUMANITCHphysical
27578003
EGFR_HUMANEGFRphysical
27578003
WWTR1_HUMANWWTR1physical
27578003
YAP1_HUMANYAP1physical
27578003
WWP1_HUMANWWP1physical
27578003
WWP2_HUMANWWP2physical
27578003
UBC_HUMANUBCphysical
27578003
MYO6_HUMANMYO6physical
27578003
AN13A_HUMANANKRD13Aphysical
27578003
RL40_HUMANUBA52physical
27578003
TOLIP_HUMANTOLLIPphysical
27578003
RS27A_HUMANRPS27Aphysical
27578003
RHBD3_HUMANRHBDD3physical
27578003
UBQL1_HUMANUBQLN1physical
27578003
AN13D_HUMANANKRD13Dphysical
27578003
EPN2_HUMANEPN2physical
27578003
APC1_HUMANANAPC1physical
27578003
CUED1_HUMANCUEDC1physical
27578003
HUWE1_HUMANHUWE1physical
27578003
NED4L_HUMANNEDD4Lphysical
27578003
POLH_HUMANPOLHphysical
27578003
RN168_HUMANRNF168physical
27578003
TM1L2_HUMANTOM1L2physical
27578003
TYDP2_HUMANTDP2physical
27578003
UIMC1_HUMANUIMC1physical
27578003
COPE_HUMANCOPEphysical
27578003
COPA_HUMANCOPAphysical
27578003
COPG1_HUMANCOPG1physical
27578003
K2C8_HUMANKRT8physical
27578003
K1C18_HUMANKRT18physical
27578003
COPB_HUMANCOPB1physical
27578003
GRPE1_HUMANGRPEL1physical
27578003
COPB2_HUMANCOPB2physical
27578003
COPD_HUMANARCN1physical
27578003
RS3_HUMANRPS3physical
27578003
K1C9_HUMANKRT9physical
27578003
SDHA_HUMANSDHAphysical
27578003
DDX17_HUMANDDX17physical
27578003
EF1B_HUMANEEF1B2physical
27578003
UBE3A_HUMANUBE3Aphysical
16772533
ESR1_HUMANESR1physical
16772533
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 WBP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-232, AND MASSSPECTROMETRY.

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