PRCC_HUMAN - dbPTM
PRCC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRCC_HUMAN
UniProt AC Q92733
Protein Name Proline-rich protein PRCC
Gene Name PRCC
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Nucleus .
Protein Description May regulate cell cycle progression through interaction with MAD2L2..
Protein Sequence MSLVAYASSDESEPDEAEPEPEEEEAVAPTSGPALGGLFASLPAPKGPALLPPPPQMLAPAFPPPLLLPPPTGDPRLQPPPPLPFGLGGFPPPPGVSPAEAAGVGEGLGLGLPSPRGPGLNLPPPIGGAGPPLGLPKPKKRKEPVKIAAPELHKGDSDSEEDEPTKKKTILQGSSEGTGLSALLPQPKNLTVKETNRLLLPHAFSRKPSDGSPDTKPSRLASKTKTSSLAPVVGTTTTTPSPSAIKAAAKSAALQVTKQITQEEDDSDEEVAPENFFSLPEKAEPPGVEPYPYPIPTVPEELPPGTEPEPAFQDDAANAPLEFKMAAGSSGAPWMPKPGDDYSYNQFSTYGDANAAGAYYQDYYSGGYYPAQDPALVPPQEIAPDASFIDDEAFKRLQGKRNRGREEINFVEIKGDDQLSGAQQWMTKSLTEEKTMKSFSKKKGEQPTGQQRRKHQITYLIHQAKERELELKNTWSENKLSRRQTQAKYGF
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
2Phosphorylation------MSLVAYASS
------CCCEEEECC		31.3920873877
6Phosphorylation--MSLVAYASSDESE
--CCCEEEECCCCCC		10.2726029660
8PhosphorylationMSLVAYASSDESEPD
CCCEEEECCCCCCCC		26.1620873877
9PhosphorylationSLVAYASSDESEPDE
CCEEEECCCCCCCCC		36.9120873877
12PhosphorylationAYASSDESEPDEAEP
EEECCCCCCCCCCCC		60.4620873877
30PhosphorylationEEEAVAPTSGPALGG
HHHCCCCCCCCCCHH		36.2627251275
31PhosphorylationEEAVAPTSGPALGGL
HHCCCCCCCCCCHHH		41.5427251275
41PhosphorylationALGGLFASLPAPKGP
CCHHHHHCCCCCCCC		27.7924719451
72PhosphorylationPLLLPPPTGDPRLQP
CCCCCCCCCCCCCCC		61.0525022875
97PhosphorylationFPPPPGVSPAEAAGV
CCCCCCCCHHHHCCC		25.0620068231
114PhosphorylationGLGLGLPSPRGPGLN
CCCCCCCCCCCCCCC		32.0728355574
157PhosphorylationPELHKGDSDSEEDEP
CCCCCCCCCCCCCCC		52.2729255136
159PhosphorylationLHKGDSDSEEDEPTK
CCCCCCCCCCCCCCC		47.0029255136
165PhosphorylationDSEEDEPTKKKTILQ
CCCCCCCCCCEEEEC		54.1422167270
169PhosphorylationDEPTKKKTILQGSSE
CCCCCCEEEECCCCC		35.4826074081
174PhosphorylationKKTILQGSSEGTGLS
CEEEECCCCCCCCHH		16.5626074081
175PhosphorylationKTILQGSSEGTGLSA
EEEECCCCCCCCHHH		47.0426074081
178PhosphorylationLQGSSEGTGLSALLP
ECCCCCCCCHHHHCC		30.7828111955
181PhosphorylationSSEGTGLSALLPQPK
CCCCCCHHHHCCCCC		20.4428111955
193AcetylationQPKNLTVKETNRLLL
CCCCCCHHHCCCEEC		54.2927452117
205PhosphorylationLLLPHAFSRKPSDGS
EECCCCCCCCCCCCC		39.9328555341
209PhosphorylationHAFSRKPSDGSPDTK
CCCCCCCCCCCCCCC		58.6022167270
212PhosphorylationSRKPSDGSPDTKPSR
CCCCCCCCCCCCHHH		25.2922167270
215PhosphorylationPSDGSPDTKPSRLAS
CCCCCCCCCHHHHHH		48.5223898821
216AcetylationSDGSPDTKPSRLASK
CCCCCCCCHHHHHHC		48.6626051181
218PhosphorylationGSPDTKPSRLASKTK
CCCCCCHHHHHHCCC		41.2921082442
225MethylationSRLASKTKTSSLAPV
HHHHHCCCCCCCCCC		50.58100290781
226PhosphorylationRLASKTKTSSLAPVV
HHHHCCCCCCCCCCC		28.8728450419
226O-linked_GlycosylationRLASKTKTSSLAPVV
HHHHCCCCCCCCCCC		28.8730379171
227PhosphorylationLASKTKTSSLAPVVG
HHHCCCCCCCCCCCC		25.5528450419
227O-linked_GlycosylationLASKTKTSSLAPVVG
HHHCCCCCCCCCCCC		25.5530379171
228O-linked_GlycosylationASKTKTSSLAPVVGT
HHCCCCCCCCCCCCC		33.5130379171
228PhosphorylationASKTKTSSLAPVVGT
HHCCCCCCCCCCCCC		33.5128450419
235PhosphorylationSLAPVVGTTTTTPSP
CCCCCCCCCCCCCCH		14.9021712546
236PhosphorylationLAPVVGTTTTTPSPS
CCCCCCCCCCCCCHH		19.0622115753
237PhosphorylationAPVVGTTTTTPSPSA
CCCCCCCCCCCCHHH		28.6321712546
238PhosphorylationPVVGTTTTTPSPSAI
CCCCCCCCCCCHHHH		34.3225159151
239PhosphorylationVVGTTTTTPSPSAIK
CCCCCCCCCCHHHHH		21.4825159151
241PhosphorylationGTTTTTPSPSAIKAA
CCCCCCCCHHHHHHH		29.4225159151
243PhosphorylationTTTTPSPSAIKAAAK
CCCCCCHHHHHHHHH		47.1421712546
250AcetylationSAIKAAAKSAALQVT
HHHHHHHHHHHHHHH		35.5830591513
261PhosphorylationLQVTKQITQEEDDSD
HHHHHHHHHCCCCCC		27.6829255136
267PhosphorylationITQEEDDSDEEVAPE
HHHCCCCCCCCCCCC		60.2829255136
278PhosphorylationVAPENFFSLPEKAEP
CCCCHHCCCCCCCCC		38.5923927012
414SumoylationEINFVEIKGDDQLSG
CCCEEEECCCCCCHH		42.66-
428UbiquitinationGAQQWMTKSLTEEKT
HHHHHHHHHCCHHHH		27.62-
434AcetylationTKSLTEEKTMKSFSK
HHHCCHHHHHHHHHH		47.9225953088
438PhosphorylationTEEKTMKSFSKKKGE
CHHHHHHHHHHHCCC		24.7524719451
440PhosphorylationEKTMKSFSKKKGEQP
HHHHHHHHHHCCCCC		51.13-
442AcetylationTMKSFSKKKGEQPTG
HHHHHHHHCCCCCCH		65.8930591519
443AcetylationMKSFSKKKGEQPTGQ
HHHHHHHCCCCCCHH		71.9930591525
458PhosphorylationQRRKHQITYLIHQAK
HHHHHHHHHHHHHHH		13.0020068231
459PhosphorylationRRKHQITYLIHQAKE
HHHHHHHHHHHHHHH		12.8027642862
472UbiquitinationKERELELKNTWSENK
HHHHHHHHCCCCCHH		42.85-
476PhosphorylationLELKNTWSENKLSRR
HHHHCCCCCHHHHHH		29.2929449344
476O-linked_GlycosylationLELKNTWSENKLSRR
HHHHCCCCCHHHHHH		29.2930379171
479UbiquitinationKNTWSENKLSRRQTQ
HCCCCCHHHHHHHHH		43.73-
481PhosphorylationTWSENKLSRRQTQAK
CCCCHHHHHHHHHHH		27.3329449344
488UbiquitinationSRRQTQAKYGF----
HHHHHHHHHCC----		35.77-
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 PRCC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRCC_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 PRCC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD2L2_HUMANMAD2L2physical
11717438
SOSB1_HUMANNABP2physical
22939629
RBM10_HUMANRBM10physical
22365833
LSM2_HUMANLSM2physical
22365833
PRP19_HUMANPRPF19physical
22365833
PPIL2_HUMANPPIL2physical
22365833
TOE1_HUMANTOE1physical
22365833
CS057_HUMANC19orf57physical
28514442
FA11_HUMANF11physical
28514442
TKTL2_HUMANTKTL2physical
28514442
BCAM_HUMANBCAMphysical
28514442
FAF1_HUMANFAF1physical
28514442
SPF27_HUMANBCAS2physical
28514442
GRP75_HUMANHSPA9physical
28514442
CARM1_HUMANCARM1physical
28514442
CRNL1_HUMANCRNKL1physical
28514442
GORS2_HUMANGORASP2physical
27173435
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 PRCC_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-157 AND SER-159, ANDMASS SPECTROMETRY.
"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 THR-239; SER-241; SER-243AND SER-267, 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-157; SER-159 ANDSER-267, AND MASS 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 SER-157 AND SER-159, ANDMASS 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-8; SER-9; SER-12;SER-157; SER-159 AND SER-218, AND MASS SPECTROMETRY.

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