KPRB_HUMAN - dbPTM
KPRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPRB_HUMAN
UniProt AC O60256
Protein Name Phosphoribosyl pyrophosphate synthase-associated protein 2
Gene Name PRPSAP2
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization
Protein Description Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis..
Protein Sequence MFCVTPPELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIHPSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRRIEESAIDEVVVTNTIPHEVQKLQCPKIKTVDISMILSEAIRRIHNGESMSYLFRNIGLDD
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
1Acetylation-------MFCVTPPE
-------CCCCCCHH		5.4619413330
5Phosphorylation---MFCVTPPELETK
---CCCCCCHHHCCC		34.0223401153
11PhosphorylationVTPPELETKMNITKG
CCCHHHCCCCCCCCC		48.4926552605
27PhosphorylationLVLFSANSNSSCMEL
EEEEECCCCCHHHHH		37.49-
29UbiquitinationLFSANSNSSCMELSK
EEECCCCCHHHHHHH		25.41-
48UbiquitinationRLGVEMGKVQVYQEP
HHCCCCCCEEEEECC		28.34-
48AcetylationRLGVEMGKVQVYQEP
HHCCCCCCEEEEECC		28.3425953088
52PhosphorylationEMGKVQVYQEPNRET
CCCCEEEEECCCCCC		7.0622817900
52NitrationEMGKVQVYQEPNRET
CCCCEEEEECCCCCC		7.06-
102UbiquitinationACKTSCAKSIIGVIP
HHHHHHHHHHHHEEC		46.6521906983
115UbiquitinationIPYFPYSKQCKMRKR
ECCCCCCCCCCCCCC		54.60-
115AcetylationIPYFPYSKQCKMRKR
ECCCCCCCCCCCCCC		54.6025953088
144PhosphorylationAGLTHLITMDLHQKE
HCCCEEEECCCCCCH		15.8218491316
165UbiquitinationIPVDNLRASPFLLQY
CCHHHCCCCHHHHHH		25.4019608861
165AcetylationIPVDNLRASPFLLQY
CCHHHCCCCHHHHHH		25.4019608861
165UbiquitinationIPVDNLRASPFLLQY
CCHHHCCCCHHHHHH		25.4021906983
188UbiquitinationRNAVIVAKSPASAKR
CCEEEEECCHHHHHH		46.182190698
188AcetylationRNAVIVAKSPASAKR
CCEEEEECCHHHHHH		46.18133515
189PhosphorylationNAVIVAKSPASAKRA
CEEEEECCHHHHHHH		18.8928857561
192PhosphorylationIVAKSPASAKRAQSF
EEECCHHHHHHHHHH		37.3923312004
194AcetylationAKSPASAKRAQSFAE
ECCHHHHHHHHHHHH		45.85133519
198PhosphorylationASAKRAQSFAERLRL
HHHHHHHHHHHHHHH		25.9926657352
211AcetylationRLGIAVIHGEAQDAE
HHCEEEEECCCCCCH		22.8019608861
211UbiquitinationRLGIAVIHGEAQDAE
HHCEEEEECCCCCCH		22.8019608861
219PhosphorylationGEAQDAESDLVDGRH
CCCCCCHHCCCCCCC		37.6623927012
227PhosphorylationDLVDGRHSPPMVRSV
CCCCCCCCCCCHHHH		29.3629255136
233PhosphorylationHSPPMVRSVAAIHPS
CCCCCHHHHEECCCC		12.5114702039
240PhosphorylationSVAAIHPSLEIPMLI
HHEECCCCCCCCEEC		25.1926074081
251UbiquitinationPMLIPKEKPPITVVG
CEECCCCCCCEEEEE		63.3221890473
251AcetylationPMLIPKEKPPITVVG
CEECCCCCCCEEEEE		63.3219608861
330UbiquitinationTIPHEVQKLQCPKIK
CCCHHHHHCCCCCCC		45.78-
335UbiquitinationVQKLQCPKIKTVDIS
HHHCCCCCCCEEEHH		65.54-
338PhosphorylationLQCPKIKTVDISMIL
CCCCCCCEEEHHHHH		27.2120068231
342PhosphorylationKIKTVDISMILSEAI
CCCEEEHHHHHHHHH		8.7020068231
346PhosphorylationVDISMILSEAIRRIH
EEHHHHHHHHHHHHH		17.6620068231
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 KPRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPRB_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 KPRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
IQGA1_HUMANIQGAP1physical
22863883
RU2B_HUMANSNRPB2physical
22863883
NS1BP_HUMANIVNS1ABPphysical
28514442
LZTR1_HUMANLZTR1physical
28514442
GLT16_HUMANGALNT16physical
28514442
PRPS3_HUMANPRPS1L1physical
28514442
CCNB1_HUMANCCNB1physical
28514442
FNTB_HUMANFNTBphysical
28514442
SNAG_HUMANNAPGphysical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
DOCK7_HUMANDOCK7physical
28514442
VTI1B_HUMANVTI1Bphysical
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 KPRB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-219 AND SER-227, AND MASS SPECTROMETRY.
"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-251, 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-227, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-219 AND SER-227, 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-227, AND MASSSPECTROMETRY.
"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-227, AND MASSSPECTROMETRY.

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