PAR10_HUMAN - dbPTM
PAR10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAR10_HUMAN
UniProt AC Q53GL7
Protein Name Poly [ADP-ribose] polymerase 10
Gene Name PARP10
Organism Homo sapiens (Human).
Sequence Length 1025
Subcellular Localization Nucleus, nucleolus . Cytoplasm . Shuttles between the nuclear and cytoplasmic compartment. A subpopulation concentrates in the nucleolus during late G1/S phase.
Protein Description May play a role in cell proliferation. May be required for the maintenance of cell cycle progression..
Protein Sequence MVAMAEAEAGVAVEVRGLPPAVPDELLTLYFENRRRSGGGPVLSWQRLGCGGVLTFREPADAERVLAQADHELHGAQLSLRPAPPRAPARLLLQGLPPGTTPQRLEQHVQALLRASGLPVQPCCALASPRPDRALVQLPKPLSEADVRVLEEQAQNLGLEGTLVSLARVPQARAVRVVGDGASVDLLLLELYLENERRSGGGPLEDLQRLPGPLGTVASFQQWQVAERVLQQEHRLQGSELSLVPHYDILEPEELAENTSGGDHPSTQGPRATKHALLRTGGLVTALQGAGTVTMGSGEEPGQSGASLRTGPMVQGRGIMTTGSGQEPGQSGTSLRTGPMGSLGQAEQVSSMPMGSLEHEGLVSLRPVGLQEQEGPMSLGPVGSAGPVETSKGLLGQEGLVEIAMDSPEQEGLVGPMEITMGSLEKAGPVSPGCVKLAGQEGLVEMVLLMEPGAMRFLQLYHEDLLAGLGDVALLPLEGPDMTGFRLCGAQASCQAAEEFLRSLLGSISCHVLCLEHPGSARFLLGPEGQHLLQGLEAQFQCVFGTERLATATLDTGLEEVDPTEALPVLPGNAHTLWTPDSTGGDQEDVSLEEVRELLATLEGLDLDGEDWLPRELEEEGPQEQPEEEVTPGHEEEEPVAPSTVAPRWLEEEAALQLALHRSLEPQGQVAEQEEAAALRQALTLSLLEQPPLEAEEPPDGGTDGKAQLVVHSAFEQDVEELDRALRAALEVHVQEETVGPWRRTLPAELRARLERCHGVSVALRGDCTILRGFGAHPARAARHLVALLAGPWDQSLAFPLAASGPTLAGQTLKGPWNNLERLAENTGEFQEVVRAFYDTLDAARSSIRVVRVERVSHPLLQQQYELYRERLLQRCERRPVEQVLYHGTTAPAVPDICAHGFNRSFCGRNATVYGKGVYFARRASLSVQDRYSPPNADGHKAVFVARVLTGDYGQGRRGLRAPPLRGPGHVLLRYDSAVDCICQPSIFVIFHDTQALPTHLITCEHVPRASPDDPSGLPGRSPDT
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
37PhosphorylationYFENRRRSGGGPVLS
EECCCCCCCCCCCCC		39.7230108239
44PhosphorylationSGGGPVLSWQRLGCG
CCCCCCCCEEECCCC		22.77-
79PhosphorylationELHGAQLSLRPAPPR
HHHCCEEECCCCCCC		15.3924719451
101PhosphorylationQGLPPGTTPQRLEQH
CCCCCCCCHHHHHHH		24.2822817900
106ADP-ribosylationGTTPQRLEQHVQALL
CCCHHHHHHHHHHHH		40.6125043379
128PhosphorylationQPCCALASPRPDRAL
CCCEECCCCCCCCEE		23.4527251275
140ADP-ribosylationRALVQLPKPLSEADV
CEEECCCCCCCHHHH		68.1525043379
140UbiquitinationRALVQLPKPLSEADV
CEEECCCCCCCHHHH		68.15-
143PhosphorylationVQLPKPLSEADVRVL
ECCCCCCCHHHHHHH		38.9928348404
199PhosphorylationYLENERRSGGGPLED
HHHCCCCCCCCCHHH		48.2720071362
274UbiquitinationTQGPRATKHALLRTG
CCCCHHHHCHHHHHC		26.37-
304PhosphorylationSGEEPGQSGASLRTG
CCCCCCCCCCCCCCC		42.0927251275
307PhosphorylationEPGQSGASLRTGPMV
CCCCCCCCCCCCCCC		23.1627251275
310PhosphorylationQSGASLRTGPMVQGR
CCCCCCCCCCCCCCC		51.4320068231
321PhosphorylationVQGRGIMTTGSGQEP
CCCCCEEECCCCCCC		26.5320068231
322PhosphorylationQGRGIMTTGSGQEPG
CCCCEEECCCCCCCC		16.3920068231
324PhosphorylationRGIMTTGSGQEPGQS
CCEEECCCCCCCCCC		34.9020068231
331PhosphorylationSGQEPGQSGTSLRTG
CCCCCCCCCCCCCCC		50.3720068231
333PhosphorylationQEPGQSGTSLRTGPM
CCCCCCCCCCCCCCC		29.8120068231
334PhosphorylationEPGQSGTSLRTGPMG
CCCCCCCCCCCCCCC		21.2728857561
337PhosphorylationQSGTSLRTGPMGSLG
CCCCCCCCCCCCCCC		51.4324043423
342PhosphorylationLRTGPMGSLGQAEQV
CCCCCCCCCCCHHHC		24.0724043423
342O-linked_GlycosylationLRTGPMGSLGQAEQV
CCCCCCCCCCCHHHC		24.0729351928
350PhosphorylationLGQAEQVSSMPMGSL
CCCHHHCCCCCCCCC		22.1824043423
351PhosphorylationGQAEQVSSMPMGSLE
CCHHHCCCCCCCCCC		28.2224043423
356PhosphorylationVSSMPMGSLEHEGLV
CCCCCCCCCCCCCCE		25.0824043423
356O-linked_GlycosylationVSSMPMGSLEHEGLV
CCCCCCCCCCCCCCE		25.0829351928
364PhosphorylationLEHEGLVSLRPVGLQ
CCCCCCEEEEECCCC		24.5724719451
378PhosphorylationQEQEGPMSLGPVGSA
CCCCCCCCCCCCCCC		33.0527251275
407PhosphorylationLVEIAMDSPEQEGLV
CEEEECCCHHHCCCC		19.7727251275
420PhosphorylationLVGPMEITMGSLEKA
CCCCEEEEECCHHHC		11.3724275569
423PhosphorylationPMEITMGSLEKAGPV
CEEEEECCHHHCCCC		23.6427251275
431PhosphorylationLEKAGPVSPGCVKLA
HHHCCCCCCCCHHCC		20.7823401153
601PhosphorylationEVRELLATLEGLDLD
HHHHHHHHHHCCCCC		25.88-
663PhosphorylationLQLALHRSLEPQGQV
HHHHHHHHCCCCCCH		26.7426657352
882ADP-ribosylationRCERRPVEQVLYHGT
HHHHCCHHHHEECCC		37.3418851833
916UbiquitinationRNATVYGKGVYFARR
CCCEEECCCEEEEEE		27.7619608861
916AcetylationRNATVYGKGVYFARR
CCCEEECCCEEEEEE		27.7619608861
916ADP-ribosylationRNATVYGKGVYFARR
CCCEEECCCEEEEEE		27.7625043379
925PhosphorylationVYFARRASLSVQDRY
EEEEEEEECCCCCCC		21.2623401153
927PhosphorylationFARRASLSVQDRYSP
EEEEEECCCCCCCCC		18.4230108239
928UbiquitinationARRASLSVQDRYSPP
EEEEECCCCCCCCCC		9.2321890473
928UbiquitinationARRASLSVQDRYSPP
EEEEECCCCCCCCCC		9.2321890473
941UbiquitinationPPNADGHKAVFVARV
CCCCCCCCEEEEEEE		52.34-
953PhosphorylationARVLTGDYGQGRRGL
EEEHHCCCCCCCCCC		16.8223285258
986PhosphorylationVDCICQPSIFVIFHD
HCCEECCEEEEEEEC		11.6328348404
1011PhosphorylationCEHVPRASPDDPSGL
EECCCCCCCCCCCCC		30.0930266825
1016PhosphorylationRASPDDPSGLPGRSP
CCCCCCCCCCCCCCC		61.0230266825
1022PhosphorylationPSGLPGRSPDT----
CCCCCCCCCCC----		32.8030266825
1025PhosphorylationLPGRSPDT-------
CCCCCCCC-------		43.8430266825
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
101TPhosphorylationKinaseCDK2P24941
PSP
601TPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAR10_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 PAR10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYC_HUMANMYCphysical
15674325
H31_HUMANHIST1H3Aphysical
15674325
H2A2C_HUMANHIST2H2ACphysical
15674325
H2B2E_HUMANHIST2H2BEphysical
15674325
MYC_HUMANMYCphysical
22992334
SQSTM_HUMANSQSTM1physical
22992334
NEMO_HUMANIKBKGphysical
23575687
PCNA_HUMANPCNAphysical
24695737
UBC_HUMANUBCphysical
23575687
PAR14_MOUSEParp14physical
23473667
RAN_HUMANRANphysical
23473667
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 PAR10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-916, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"CDK-dependent activation of poly(ADP-ribose) polymerase member 10(PARP10).";
Chou H.Y., Chou H.T., Lee S.C.;
J. Biol. Chem. 281:15201-15207(2006).
Cited for: FUNCTION, AND PHOSPHORYLATION AT THR-101.

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