PELO_HUMAN - dbPTM
PELO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PELO_HUMAN
UniProt AC Q9BRX2
Protein Name Protein pelota homolog
Gene Name PELO
Organism Homo sapiens (Human).
Sequence Length 385
Subcellular Localization Nucleus . Cytoplasm.
Protein Description Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential)..
Protein Sequence MKLVRKNIEKDNAGQVTLVPEEPEDMWHTYNLVQVGDSLRASTIRKVQTESSTGSVGSNRVRTTLTLCVEAIDFDSQACQLRVKGTNIQENEYVKMGAYHTIELEPNRQFTLAKKQWDSVVLERIEQACDPAWSADVAAVVMQEGLAHICLVTPSMTLTRAKVEVNIPRKRKGNCSQHDRALERFYEQVVQAIQRHIHFDVVKCILVASPGFVREQFCDYLFQQAVKTDNKLLLENRSKFLQVHASSGHKYSLKEALCDPTVASRLSDTKAAGEVKALDDFYKMLQHEPDRAFYGLKQVEKANEAMAIDTLLISDELFRHQDVATRSRYVRLVDSVKENAGTVRIFSSLHVSGEQLSQLTGVAAILRFPVPELSDQEGDSSSEED
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
10UbiquitinationLVRKNIEKDNAGQVT
CCCCCCCCCCCCCEE		53.1129967540
17PhosphorylationKDNAGQVTLVPEEPE
CCCCCCEEECCCCCC		17.7227690223
46UbiquitinationLRASTIRKVQTESST
HCHHHEEEEEECCCC		34.5421906983
46SumoylationLRASTIRKVQTESST
HCHHHEEEEEECCCC		34.54-
46SumoylationLRASTIRKVQTESST
HCHHHEEEEEECCCC		34.54-
49PhosphorylationSTIRKVQTESSTGSV
HHEEEEEECCCCCCC		40.6021406692
51PhosphorylationIRKVQTESSTGSVGS
EEEEEECCCCCCCCC		36.2728450419
52PhosphorylationRKVQTESSTGSVGSN
EEEEECCCCCCCCCC		30.4729255136
53PhosphorylationKVQTESSTGSVGSNR
EEEECCCCCCCCCCC		42.6329255136
55PhosphorylationQTESSTGSVGSNRVR
EECCCCCCCCCCCCE		24.3229255136
58PhosphorylationSSTGSVGSNRVRTTL
CCCCCCCCCCCEEEE		21.2129255136
84MalonylationQACQLRVKGTNIQEN
CEEEEEECCCCCCCC		54.2926320211
84SumoylationQACQLRVKGTNIQEN
CEEEEEECCCCCCCC		54.29-
84UbiquitinationQACQLRVKGTNIQEN
CEEEEEECCCCCCCC		54.2921906983
84SumoylationQACQLRVKGTNIQEN
CEEEEEECCCCCCCC		54.29-
93PhosphorylationTNIQENEYVKMGAYH
CCCCCCCEEEECCEE		19.5628796482
95UbiquitinationIQENEYVKMGAYHTI
CCCCCEEEECCEEEE		30.6221906983
99PhosphorylationEYVKMGAYHTIELEP
CEEEECCEEEEEECC		8.1828796482
101PhosphorylationVKMGAYHTIELEPNR
EEECCEEEEEECCCC		11.9420068231
108MethylationTIELEPNRQFTLAKK
EEEECCCCEEEECHH		43.64115486977
111PhosphorylationLEPNRQFTLAKKQWD
ECCCCEEEECHHHHH		19.9128060719
1142-HydroxyisobutyrylationNRQFTLAKKQWDSVV
CCEEEECHHHHHHHH		48.92-
114UbiquitinationNRQFTLAKKQWDSVV
CCEEEECHHHHHHHH		48.9227667366
115UbiquitinationRQFTLAKKQWDSVVL
CEEEECHHHHHHHHH		51.5229967540
119PhosphorylationLAKKQWDSVVLERIE
ECHHHHHHHHHHHHH		15.92-
162UbiquitinationSMTLTRAKVEVNIPR
CCEEEEEEEEECCCC		35.3227667366
162SumoylationSMTLTRAKVEVNIPR
CCEEEEEEEEECCCC		35.3228112733
186PhosphorylationDRALERFYEQVVQAI
HHHHHHHHHHHHHHH		16.2127642862
203UbiquitinationHIHFDVVKCILVASP
HCCCCEEEEEEECCC		18.5322817900
220PhosphorylationVREQFCDYLFQQAVK
HHHHHHHHHHHHHHH		15.5929255136
227UbiquitinationYLFQQAVKTDNKLLL
HHHHHHHHHCCEEHH		53.8522817900
231UbiquitinationQAVKTDNKLLLENRS
HHHHHCCEEHHHCHH		43.2321906983
231SumoylationQAVKTDNKLLLENRS
HHHHHCCEEHHHCHH		43.23-
231SumoylationQAVKTDNKLLLENRS
HHHHHCCEEHHHCHH		43.23-
239UbiquitinationLLLENRSKFLQVHAS
EHHHCHHHHEEEECC		47.0229967540
250UbiquitinationVHASSGHKYSLKEAL
EECCCCCCCCHHHHH		39.8123000965
252PhosphorylationASSGHKYSLKEALCD
CCCCCCCCHHHHHCC		37.4624719451
254MethylationSGHKYSLKEALCDPT
CCCCCCHHHHHCCHH		34.6924627023
254UbiquitinationSGHKYSLKEALCDPT
CCCCCCHHHHHCCHH		34.6923000965
261PhosphorylationKEALCDPTVASRLSD
HHHHCCHHHHHHHCC		18.5630622161
264PhosphorylationLCDPTVASRLSDTKA
HCCHHHHHHHCCCCC		29.4420068231
267PhosphorylationPTVASRLSDTKAAGE
HHHHHHHCCCCCHHH		41.9728634298
269PhosphorylationVASRLSDTKAAGEVK
HHHHHCCCCCHHHHC		21.1428634298
270SumoylationASRLSDTKAAGEVKA
HHHHCCCCCHHHHCH		41.03-
270UbiquitinationASRLSDTKAAGEVKA
HHHHCCCCCHHHHCH		41.0321906983
270SumoylationASRLSDTKAAGEVKA
HHHHCCCCCHHHHCH		41.03-
276UbiquitinationTKAAGEVKALDDFYK
CCCHHHHCHHHHHHH		38.6421906983
283UbiquitinationKALDDFYKMLQHEPD
CHHHHHHHHHCCCCC		32.8821906983
291MethylationMLQHEPDRAFYGLKQ
HHCCCCCHHHHCHHH		36.99115486985
297UbiquitinationDRAFYGLKQVEKANE
CHHHHCHHHHHHHHH		48.1921906983
301UbiquitinationYGLKQVEKANEAMAI
HCHHHHHHHHHHHHH		58.6222817900
306SulfoxidationVEKANEAMAIDTLLI
HHHHHHHHHHCHHHH		2.4721406390
337UbiquitinationVRLVDSVKENAGTVR
HHHHHHHHHHCCEEE		49.5622817900
337AcetylationVRLVDSVKENAGTVR
HHHHHHHHHHCCEEE		49.5626051181
342PhosphorylationSVKENAGTVRIFSSL
HHHHHCCEEEEEEEE		12.2826853621
374PhosphorylationRFPVPELSDQEGDSS
CCCCCCCCCCCCCCC		35.2730631047
380PhosphorylationLSDQEGDSSSEED--
CCCCCCCCCCCCC--		46.7730631047
381PhosphorylationSDQEGDSSSEED---
CCCCCCCCCCCC---		46.6522115753
382PhosphorylationDQEGDSSSEED----
CCCCCCCCCCC----		49.2910810093
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 PELO_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PELO_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
231Ubiquitination221 (10)L ⇒ Mrs1499280
  • Reticulocyte fraction of red cells
  • Immature fraction of reticulocytes
  • Reticulocyte count
  • High light scatter reticulocyte count
  • High light scatter reticulocyte percentage of red cells
27863252
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB1_HUMANRUVBL1physical
17353931
AIFM1_HUMANAIFM1physical
17353931
ABCD3_HUMANABCD3physical
17353931
HEAT1_HUMANHEATR1physical
17353931
HACD3_HUMANPTPLAD1physical
17353931
TIM50_HUMANTIMM50physical
17353931
FANCI_HUMANFANCIphysical
17353931
CMC1_HUMANSLC25A12physical
17353931
MYO1D_HUMANMYO1Dphysical
17353931
MCM7_HUMANMCM7physical
17353931
ANM6_HUMANPRMT6physical
23455924
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 PELO_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-374, AND MASSSPECTROMETRY.
"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-374; SER-380; SER-381AND SER-382, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381AND SER-382, 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-374; SER-380; SER-381AND SER-382, AND MASS SPECTROMETRY.

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