WBP11_HUMAN - dbPTM
WBP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WBP11_HUMAN
UniProt AC Q9Y2W2
Protein Name WW domain-binding protein 11
Gene Name WBP11
Organism Homo sapiens (Human).
Sequence Length 641
Subcellular Localization Nucleus. Cytoplasm. Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cy
Protein Description Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity..
Protein Sequence MGRRSTSSTKSGKFMNPTDQARKEARKRELKKNKKQRMMVRAAVLKMKDPKQIIRDMEKLDEMEFNPVQQPQLNEKVLKDKRKKLRETFERILRLYEKENPDIYKELRKLEVEYEQKRAQLSQYFDAVKNAQHVEVESIPLPDMPHAPSNILIQDIPLPGAQPPSILKKTSAYGPPTRAVSILPLLGHGVPRLPPGRKPPGPPPGPPPPQVVQMYGRKVGFALDLPPRRRDEDMLYSPELAQRGHDDDVSSTSEDDGYPEDMDQDKHDDSTDDSDTDKSDGESDGDEFVHRDNGERDNNEEKKSGLSVRFADMPGKSRKKKKNMKELTPLQAMMLRMAGQEIPEEGREVEEFSEDDDEDDSDDSEAEKQSQKQHKEESHSDGTSTASSQQQAPPQSVPPSQIQAPPMPGPPPLGPPPAPPLRPPGPPTGLPPGPPPGAPPFLRPPGMPGLRGPLPRLLPPGPPPGRPPGPPPGPPPGLPPGPPPRGPPPRLPPPAPPGIPPPRPGMMRPPLVPPLGPAPPGLFPPAPLPNPGVLSAPPNLIQRPKADDTSAATIEKKATATISAKPQITNPKAEITRFVPTALRVRRENKGATAAPQRKSEDDSAVPLAKAAPKSGPSVPVSVQTKDDVYEAFMKEMEGLL
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
13UbiquitinationTSSTKSGKFMNPTDQ
CCCCCCCCCCCHHHH		48.8319608861
13AcetylationTSSTKSGKFMNPTDQ
CCCCCCCCCCCHHHH		48.8319608861
15SulfoxidationSTKSGKFMNPTDQAR
CCCCCCCCCHHHHHH		7.1821406390
48UbiquitinationRAAVLKMKDPKQIIR
HHHHHHCCCHHHHHH		70.10-
51UbiquitinationVLKMKDPKQIIRDME
HHHCCCHHHHHHCHH		65.35-
512-HydroxyisobutyrylationVLKMKDPKQIIRDME
HHHCCCHHHHHHCHH		65.35-
59AcetylationQIIRDMEKLDEMEFN
HHHHCHHHHHCCCCC		55.3826051181
98AcetylationRILRLYEKENPDIYK
HHHHHHHHHCHHHHH		49.5926051181
104PhosphorylationEKENPDIYKELRKLE
HHHCHHHHHHHHHHH		13.04-
105AcetylationKENPDIYKELRKLEV
HHCHHHHHHHHHHHH		51.0826051181
105UbiquitinationKENPDIYKELRKLEV
HHCHHHHHHHHHHHH		51.0821890473
109UbiquitinationDIYKELRKLEVEYEQ
HHHHHHHHHHHHHHH		62.72-
114PhosphorylationLRKLEVEYEQKRAQL
HHHHHHHHHHHHHHH		28.9220068231
117UbiquitinationLEVEYEQKRAQLSQY
HHHHHHHHHHHHHHH		37.45-
1172-HydroxyisobutyrylationLEVEYEQKRAQLSQY
HHHHHHHHHHHHHHH		37.45-
122PhosphorylationEQKRAQLSQYFDAVK
HHHHHHHHHHHHHHH		15.6828152594
124NitrationKRAQLSQYFDAVKNA
HHHHHHHHHHHHHCC		10.47-
124PhosphorylationKRAQLSQYFDAVKNA
HHHHHHHHHHHHHCC		10.4728152594
165PhosphorylationLPGAQPPSILKKTSA
CCCCCCCHHHHHCCC		47.4324719451
169MethylationQPPSILKKTSAYGPP
CCCHHHHHCCCCCCC		44.2483136403
170PhosphorylationPPSILKKTSAYGPPT
CCHHHHHCCCCCCCC		19.5927732954
171PhosphorylationPSILKKTSAYGPPTR
CHHHHHCCCCCCCCC		28.5127732954
173PhosphorylationILKKTSAYGPPTRAV
HHHHCCCCCCCCCEE		29.9027642862
173NitrationILKKTSAYGPPTRAV
HHHHCCCCCCCCCEE		29.90-
178MethylationSAYGPPTRAVSILPL
CCCCCCCCEEEHHHH		38.4782954715
181PhosphorylationGPPTRAVSILPLLGH
CCCCCEEEHHHHCCC		19.8830266825
192MethylationLLGHGVPRLPPGRKP
HCCCCCCCCCCCCCC		58.3724129315
214SulfoxidationPPPQVVQMYGRKVGF
CCCHHHHCCCCEEEE		2.3028183972
215PhosphorylationPPQVVQMYGRKVGFA
CCHHHHCCCCEEEEE		9.1828111955
236PhosphorylationRRDEDMLYSPELAQR
CCCCCCCCCHHHHHC		18.6221945579
237PhosphorylationRDEDMLYSPELAQRG
CCCCCCCCHHHHHCC		14.1329255136
250PhosphorylationRGHDDDVSSTSEDDG
CCCCCCCCCCCCCCC		34.5925850435
251PhosphorylationGHDDDVSSTSEDDGY
CCCCCCCCCCCCCCC		35.4821082442
252PhosphorylationHDDDVSSTSEDDGYP
CCCCCCCCCCCCCCC		28.7321082442
253PhosphorylationDDDVSSTSEDDGYPE
CCCCCCCCCCCCCCC		40.7621082442
258PhosphorylationSTSEDDGYPEDMDQD
CCCCCCCCCCCCCCC		15.5025850435
270PhosphorylationDQDKHDDSTDDSDTD
CCCCCCCCCCCCCCC		39.5325137130
271PhosphorylationQDKHDDSTDDSDTDK
CCCCCCCCCCCCCCC		51.3125022875
274PhosphorylationHDDSTDDSDTDKSDG
CCCCCCCCCCCCCCC		45.2625022875
276PhosphorylationDSTDDSDTDKSDGES
CCCCCCCCCCCCCCC		49.6425022875
279PhosphorylationDDSDTDKSDGESDGD
CCCCCCCCCCCCCCC		54.3720164059
283PhosphorylationTDKSDGESDGDEFVH
CCCCCCCCCCCCCCC		53.0428355574
307PhosphorylationEEKKSGLSVRFADMP
HHHHCCCEEECCCCC		18.1224719451
316AcetylationRFADMPGKSRKKKKN
ECCCCCCCCHHCCCC		41.0125953088
319AcetylationDMPGKSRKKKKNMKE
CCCCCCHHCCCCHHH		75.847663221
325AcetylationRKKKKNMKELTPLQA
HHCCCCHHHCHHHHH		59.9925953088
328PhosphorylationKKNMKELTPLQAMML
CCCHHHCHHHHHHHH		24.0421712546
353PhosphorylationGREVEEFSEDDDEDD
CCCCHHCCCCCCCCC		43.3123927012
361PhosphorylationEDDDEDDSDDSEAEK
CCCCCCCCCCHHHHH		56.4923927012
364PhosphorylationDEDDSDDSEAEKQSQ
CCCCCCCHHHHHHHH		43.6323927012
370PhosphorylationDSEAEKQSQKQHKEE
CHHHHHHHHHHHHHH		50.8725137130
485MethylationLPPGPPPRGPPPRLP
CCCCCCCCCCCCCCC		75.83-
508MethylationPPRPGMMRPPLVPPL
CCCCCCCCCCCCCCC		22.3152718131
508DimethylationPPRPGMMRPPLVPPL
CCCCCCCCCCCCCCC		22.31-
556AcetylationTSAATIEKKATATIS
CCCCEEEEHHHEEEE		43.8025953088
557SumoylationSAATIEKKATATISA
CCCEEEEHHHEEEEC		37.8728112733
561PhosphorylationIEKKATATISAKPQI
EEEHHHEEEECCCCC		15.8825954137
563PhosphorylationKKATATISAKPQITN
EHHHEEEECCCCCCC		26.3625954137
565AcetylationATATISAKPQITNPK
HHEEEECCCCCCCCC		30.5723954790
572SumoylationKPQITNPKAEITRFV
CCCCCCCCHHHEEEC		61.8028112733
572AcetylationKPQITNPKAEITRFV
CCCCCCCCHHHEEEC		61.8026051181
577MethylationNPKAEITRFVPTALR
CCCHHHEEECCHHHH		35.91115919897
593PhosphorylationRRENKGATAAPQRKS
HHHCCCCCCCCCCCC		31.8323403867
600PhosphorylationTAAPQRKSEDDSAVP
CCCCCCCCCCCCCCC		48.7429255136
604PhosphorylationQRKSEDDSAVPLAKA
CCCCCCCCCCCHHHC		43.4125159151
610AcetylationDSAVPLAKAAPKSGP
CCCCCHHHCCCCCCC		53.4125953088
610UbiquitinationDSAVPLAKAAPKSGP
CCCCCHHHCCCCCCC		53.41-
614AcetylationPLAKAAPKSGPSVPV
CHHHCCCCCCCCCCC		64.4226051181
614UbiquitinationPLAKAAPKSGPSVPV
CHHHCCCCCCCCCCC		64.42-
615PhosphorylationLAKAAPKSGPSVPVS
HHHCCCCCCCCCCCE		55.6825159151
626AcetylationVPVSVQTKDDVYEAF
CCCEEECCHHHHHHH		34.5426051181
626UbiquitinationVPVSVQTKDDVYEAF
CCCEEECCHHHHHHH		34.54-
630PhosphorylationVQTKDDVYEAFMKEM
EECCHHHHHHHHHHH		14.4528796482
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 WBP11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WBP11_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 WBP11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT4I1_HUMANRTN4IP1physical
16189514
CE022_HUMANC5orf22physical
16189514
PQBP1_HUMANPQBP1physical
11054566
ZC3HD_HUMANZC3H13physical
22939629
RBM5_HUMANRBM5physical
22365833
CTBL1_HUMANCTNNBL1physical
22365833
PP1A_HUMANPPP1CAphysical
22365833
DDX17_HUMANDDX17physical
22365833
DDX5_HUMANDDX5physical
22365833
CHP3_HUMANTESCphysical
25416956
MED16_HUMANMED16physical
26344197
PQBP1_HUMANPQBP1physical
26344197
SFPQ_HUMANSFPQphysical
26344197
CE022_HUMANC5orf22physical
28514442
PQBP1_HUMANPQBP1physical
28514442
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 WBP11_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-13, 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-353; SER-361 ANDSER-364, AND MASS 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-237; THR-328; SER-353;SER-361 AND SER-364, AND MASS SPECTROMETRY.
"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-237; SER-251; THR-252;SER-253; SER-270; THR-271; SER-274; THR-276; SER-279; SER-283;SER-353; SER-361 AND SER-364, AND MASS SPECTROMETRY.

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