PAWR_HUMAN - dbPTM
PAWR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAWR_HUMAN
UniProt AC Q96IZ0
Protein Name PRKC apoptosis WT1 regulator protein
Gene Name PAWR
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization Cytoplasm. Nucleus. Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis (By similarity). Nuclear localization includes nucleopl
Protein Description Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1..
Protein Sequence MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANELNNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR
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
3Phosphorylation-----MATGGYRTSS
-----CCCCCCCCCC		29.8222199227
6Phosphorylation--MATGGYRTSSGLG
--CCCCCCCCCCCCC		16.4422199227
8PhosphorylationMATGGYRTSSGLGGS
CCCCCCCCCCCCCCC		20.8225159151
9PhosphorylationATGGYRTSSGLGGST
CCCCCCCCCCCCCCH		17.2623403867
10PhosphorylationTGGYRTSSGLGGSTT
CCCCCCCCCCCCCHH		37.1123403867
15PhosphorylationTSSGLGGSTTDFLEE
CCCCCCCCHHHHHHH		26.7423403867
16PhosphorylationSSGLGGSTTDFLEEW
CCCCCCCHHHHHHHH		33.3923403867
17PhosphorylationSGLGGSTTDFLEEWK
CCCCCCHHHHHHHHH		26.8423403867
24AcetylationTDFLEEWKAKREKMR
HHHHHHHHHHHHHHH		47.5126051181
95PhosphorylationGVNCAVGSAMLTRAA
CCCHHHCHHHHHCCC		12.14-
99PhosphorylationAVGSAMLTRAAPGPR
HHCHHHHHCCCCCCC		12.74-
108O-linked_GlycosylationAAPGPRRSEDEPPAA
CCCCCCCCCCCCCCC		51.1628411811
108PhosphorylationAAPGPRRSEDEPPAA
CCCCCCCCCCCCCCC		51.1630266825
116PhosphorylationEDEPPAASASAAPPP
CCCCCCCCCCCCCCC		25.5123663014
118PhosphorylationEPPAASASAAPPPQR
CCCCCCCCCCCCCCC		23.5923663014
146MethylationSSGPSARKGKGQIEK
CCCCCCCCCCCHHHH		65.77116253451
148UbiquitinationGPSARKGKGQIEKRK
CCCCCCCCCHHHHHH		51.1524816145
153UbiquitinationKGKGQIEKRKLREKR
CCCCHHHHHHHHHHH		57.3627667366
162PhosphorylationKLREKRRSTGVVNIP
HHHHHHHHCCCCCCC		33.2825159151
163PhosphorylationLREKRRSTGVVNIPA
HHHHHHHCCCCCCCH		31.9825159151
177PhosphorylationAAECLDEYEDDEAGQ
HHHHHHHHCCCHHHH		25.0722322096
211PhosphorylationVNLLDPGSSYLLQEP
HHHCCCCCCCCCCCC		22.6228102081
212PhosphorylationNLLDPGSSYLLQEPP
HHCCCCCCCCCCCCC		26.2228102081
213PhosphorylationLLDPGSSYLLQEPPR
HCCCCCCCCCCCCCC		17.0927642862
221PhosphorylationLLQEPPRTVSGRYKS
CCCCCCCEECCCCCC		25.4628102081
223PhosphorylationQEPPRTVSGRYKSTT
CCCCCEECCCCCCCC		19.5519651622
226PhosphorylationPRTVSGRYKSTTSVS
CCEECCCCCCCCCCC		16.9022617229
227UbiquitinationRTVSGRYKSTTSVSE
CEECCCCCCCCCCCH		39.7124816145
227MethylationRTVSGRYKSTTSVSE
CEECCCCCCCCCCCH		39.71115974615
228PhosphorylationTVSGRYKSTTSVSEE
EECCCCCCCCCCCHH		28.1625159151
229PhosphorylationVSGRYKSTTSVSEED
ECCCCCCCCCCCHHH		20.9522322096
230PhosphorylationSGRYKSTTSVSEEDV
CCCCCCCCCCCHHHH		33.9325159151
231PhosphorylationGRYKSTTSVSEEDVS
CCCCCCCCCCHHHHH		24.5922322096
233PhosphorylationYKSTTSVSEEDVSSR
CCCCCCCCHHHHHHC		34.7322322096
233O-linked_GlycosylationYKSTTSVSEEDVSSR
CCCCCCCCHHHHHHC		34.7328411811
238PhosphorylationSVSEEDVSSRYSRTD
CCCHHHHHHCCCCCC		22.7823403867
238O-linked_GlycosylationSVSEEDVSSRYSRTD
CCCHHHHHHCCCCCC		22.7828411811
239PhosphorylationVSEEDVSSRYSRTDR
CCHHHHHHCCCCCCC		34.7823403867
241PhosphorylationEEDVSSRYSRTDRSG
HHHHHHCCCCCCCCC		12.4022817900
242PhosphorylationEDVSSRYSRTDRSGF
HHHHHCCCCCCCCCC		27.8227251275
252PhosphorylationDRSGFPRYNRDANVS
CCCCCCCCCCCCCCC		18.1323090842
259PhosphorylationYNRDANVSGTLVSSS
CCCCCCCCCEEECHH		26.3519664994
261PhosphorylationRDANVSGTLVSSSTL
CCCCCCCEEECHHHH		19.2429255136
264PhosphorylationNVSGTLVSSSTLEKK
CCCCEEECHHHHHHH		22.9929255136
265PhosphorylationVSGTLVSSSTLEKKI
CCCEEECHHHHHHHH		21.6229255136
266PhosphorylationSGTLVSSSTLEKKIE
CCEEECHHHHHHHHH		29.5229255136
267PhosphorylationGTLVSSSTLEKKIED
CEEECHHHHHHHHHH		40.6729255136
271AcetylationSSSTLEKKIEDLEKE
CHHHHHHHHHHHHHH		41.7926051181
2772-HydroxyisobutyrylationKKIEDLEKEVVRERQ
HHHHHHHHHHHHHHH		64.21-
277UbiquitinationKKIEDLEKEVVRERQ
HHHHHHHHHHHHHHH		64.2129967540
296UbiquitinationLVRLMQDKEEMIGKL
HHHHHCCHHHHHHHH		38.3929967540
2962-HydroxyisobutyrylationLVRLMQDKEEMIGKL
HHHHHCCHHHHHHHH		38.39-
296AcetylationLVRLMQDKEEMIGKL
HHHHHCCHHHHHHHH		38.3926051181
302UbiquitinationDKEEMIGKLKEEIDL
CHHHHHHHHHHHHHH		45.5227667366
302AcetylationDKEEMIGKLKEEIDL
CHHHHHHHHHHHHHH		45.527374293
304UbiquitinationEEMIGKLKEEIDLLN
HHHHHHHHHHHHHHC		57.7129967540
325UbiquitinationEDENEQLKQENKTLL
HHHHHHHHHHHHHHH		56.0924816145
325AcetylationEDENEQLKQENKTLL
HHHHHHHHHHHHHHH		56.0926051181
329UbiquitinationEQLKQENKTLLKVVG
HHHHHHHHHHHHHHH		39.5323000965
333UbiquitinationQENKTLLKVVGQLTR
HHHHHHHHHHHHHCC		37.6823000965
333MalonylationQENKTLLKVVGQLTR
HHHHHHHHHHHHHCC		37.6826320211
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
163TPhosphorylationKinasePKA-Uniprot
231SPhosphorylationKinaseCSNK2A1P68400
GPS
231SPhosphorylationKinaseCK2A1P19139
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXO45P0C2W1
PMID:24992930
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
163TPhosphorylation

-
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 PAWR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC5A7_HUMANSLC5A7physical
15090548
SC5A1_HUMANSLC5A1physical
15090548
AATF_HUMANAATFphysical
14627703
DAPK3_HUMANDAPK3physical
12917339
THAP1_HUMANTHAP1physical
12717420
KPCZ_HUMANPRKCZphysical
8797824
WT1_HUMANWT1physical
8943350
GRP78_HUMANHSPA5physical
19632185
SPSB4_MOUSESpsb4physical
20561531
SPSB2_MOUSESpsb2physical
20561531
KPCZ_HUMANPRKCZphysical
11755531
SQSTM_HUMANSQSTM1physical
11755531
ACPH_HUMANAPEHphysical
22863883
CAND1_HUMANCAND1physical
22863883
SYCC_HUMANCARSphysical
22863883
NIBL1_HUMANFAM129Bphysical
22863883
H33_HUMANH3F3Aphysical
22863883
IDE_HUMANIDEphysical
22863883
JMJD6_HUMANJMJD6physical
22863883
PPM1G_HUMANPPM1Gphysical
22863883
GLYM_HUMANSHMT2physical
22863883
SNX2_HUMANSNX2physical
22863883
SNX6_HUMANSNX6physical
22863883
STAT1_HUMANSTAT1physical
22863883
VPS29_HUMANVPS29physical
22863883
FBSP1_HUMANFBXO45physical
24992930
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 PAWR_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-233, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-226; SER-228; THR-229AND SER-231, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory