PRR5_HUMAN - dbPTM
PRR5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRR5_HUMAN
UniProt AC P85299
Protein Name Proline-rich protein 5
Gene Name PRR5
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization
Protein Description Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer..
Protein Sequence MRTLRRLKFMSSPSLSDLGKREPAAAADERGTQQRRACANATWNSIHNGVIAVFQRKGLPDQELFSLNEGVRQLLKTELGSFFTEYLQNQLLTKGMVILRDKIRFYEGQKLLDSLAETWDFFFSDVLPMLQAIFYPVQGKEPSVRQLALLHFRNAITLSVKLEDALARAHARVPPAIVQMLLVLQGVHESRGVTEDYLRLETLVQKVVSPYLGTYGLHSSEGPFTHSCILEKRLLRRSRSGDVLAKNPVVRSKSYNTPLLNPVQEHEAEGAAAGGTSIRRHSVSEMTSCPEPQGFSDPPGQGPTGTFRSSPAPHSGPCPSRLYPTTQPPEQGLDPTRSSLPRSSPENLVDQILESVDSDSEGIFIDFGRGRGSGMSDLEGSGGRQSVV
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
6 (in isoform 2)Phosphorylation-45.3930622161
11PhosphorylationLRRLKFMSSPSLSDL
HHHHHCCCCCCHHHH		42.0830266825
12PhosphorylationRRLKFMSSPSLSDLG
HHHHCCCCCCHHHHC		13.5130266825
14PhosphorylationLKFMSSPSLSDLGKR
HHCCCCCCHHHHCCC		42.3130266825
16PhosphorylationFMSSPSLSDLGKREP
CCCCCCHHHHCCCCC		34.8230266825
20AcetylationPSLSDLGKREPAAAA
CCHHHHCCCCCCHHH		61.9712431423
34PhosphorylationADERGTQQRRACANA
HCHHHHHHHHHHHHC		36.3424719451
35PhosphorylationDERGTQQRRACANAT
CHHHHHHHHHHHHCC		20.5327251275
37PhosphorylationRGTQQRRACANATWN
HHHHHHHHHHHCCHH		10.0427251275
77PhosphorylationGVRQLLKTELGSFFT
HHHHHHHHHHHHHHH		36.0924719451
161SumoylationNAITLSVKLEDALAR
CCEEEEEEHHHHHHH		42.66-
161SumoylationNAITLSVKLEDALAR
CCEEEEEEHHHHHHH		42.66-
238PhosphorylationEKRLLRRSRSGDVLA
HHHHHHHCCCCCCCC		25.1023401153
240PhosphorylationRLLRRSRSGDVLAKN
HHHHHCCCCCCCCCC		40.3630266825
246UbiquitinationRSGDVLAKNPVVRSK
CCCCCCCCCCCCCCC		58.59-
252PhosphorylationAKNPVVRSKSYNTPL
CCCCCCCCCCCCCCC		17.8423401153
254PhosphorylationNPVVRSKSYNTPLLN
CCCCCCCCCCCCCCC		25.5123401153
255PhosphorylationPVVRSKSYNTPLLNP
CCCCCCCCCCCCCCC		27.1330266825
257PhosphorylationVRSKSYNTPLLNPVQ
CCCCCCCCCCCCCHH		13.6930266825
263PhosphorylationNTPLLNPVQEHEAEG
CCCCCCCHHHCHHHH		11.5324719451
275PhosphorylationAEGAAAGGTSIRRHS
HHHHHCCCCCEECCC		16.1524719451
276PhosphorylationEGAAAGGTSIRRHSV
HHHHCCCCCEECCCC		21.7723927012
277PhosphorylationGAAAGGTSIRRHSVS
HHHCCCCCEECCCCC		19.8526074081
282PhosphorylationGTSIRRHSVSEMTSC
CCCEECCCCCCCCCC		26.0623401153
284PhosphorylationSIRRHSVSEMTSCPE
CEECCCCCCCCCCCC		25.3523927012
287PhosphorylationRHSVSEMTSCPEPQG
CCCCCCCCCCCCCCC		24.1123663014
288PhosphorylationHSVSEMTSCPEPQGF
CCCCCCCCCCCCCCC		26.7723663014
296PhosphorylationCPEPQGFSDPPGQGP
CCCCCCCCCCCCCCC		56.9128450419
299PhosphorylationPQGFSDPPGQGPTGT
CCCCCCCCCCCCCCC		53.3724719451
304PhosphorylationDPPGQGPTGTFRSSP
CCCCCCCCCCCCCCC		56.5327422710
305PhosphorylationPPGQGPTGTFRSSPA
CCCCCCCCCCCCCCC		26.4524719451
306PhosphorylationPGQGPTGTFRSSPAP
CCCCCCCCCCCCCCC		20.5327251275
307PhosphorylationGQGPTGTFRSSPAPH
CCCCCCCCCCCCCCC		8.2527251275
309PhosphorylationGPTGTFRSSPAPHSG
CCCCCCCCCCCCCCC		36.1630266825
310PhosphorylationPTGTFRSSPAPHSGP
CCCCCCCCCCCCCCC		22.3330266825
315PhosphorylationRSSPAPHSGPCPSRL
CCCCCCCCCCCCCCC		43.2926552605
320PhosphorylationPHSGPCPSRLYPTTQ
CCCCCCCCCCCCCCC		41.4526552605
325PhosphorylationCPSRLYPTTQPPEQG
CCCCCCCCCCCCCCC		25.2227251275
326PhosphorylationPSRLYPTTQPPEQGL
CCCCCCCCCCCCCCC		34.2829449344
327PhosphorylationSRLYPTTQPPEQGLD
CCCCCCCCCCCCCCC		54.7727251275
333PhosphorylationTQPPEQGLDPTRSSL
CCCCCCCCCCCCCCC		7.7227251275
336PhosphorylationPEQGLDPTRSSLPRS
CCCCCCCCCCCCCCC		42.7330266825
338PhosphorylationQGLDPTRSSLPRSSP
CCCCCCCCCCCCCCH		38.4130266825
339PhosphorylationGLDPTRSSLPRSSPE
CCCCCCCCCCCCCHH		38.8230266825
343PhosphorylationTRSSLPRSSPENLVD
CCCCCCCCCHHHHHH		48.5927732954
344PhosphorylationRSSLPRSSPENLVDQ
CCCCCCCCHHHHHHH		37.2027732954
355PhosphorylationLVDQILESVDSDSEG
HHHHHHHHCCCCCCC		27.9827732954
358PhosphorylationQILESVDSDSEGIFI
HHHHHCCCCCCCEEE		40.6627732954
360PhosphorylationLESVDSDSEGIFIDF
HHHCCCCCCCEEEEC		41.4927732954
362PhosphorylationSVDSDSEGIFIDFGR
HCCCCCCCEEEECCC		24.8624719451
371MethylationFIDFGRGRGSGMSDL
EEECCCCCCCCCCCC		34.44115488975
373PhosphorylationDFGRGRGSGMSDLEG
ECCCCCCCCCCCCCC		29.9329255136
376PhosphorylationRGRGSGMSDLEGSGG
CCCCCCCCCCCCCCC		42.4429255136
381PhosphorylationGMSDLEGSGGRQSVV
CCCCCCCCCCCCCCC		28.7929255136
386PhosphorylationEGSGGRQSVV-----
CCCCCCCCCC-----		24.4029255136
396Phosphorylation---------------
---------------		27251275
404Phosphorylation-----------------------
-----------------------		24719451
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
240SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRR5_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 PRR5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN1_HUMANMAPKAP1physical
17461779
MTOR_HUMANMTORphysical
17461779
RICTR_HUMANRICTORphysical
17461779
LST8_HUMANMLST8physical
17461779
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 PRR5_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-11, AND MASSSPECTROMETRY.

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