PAR12_HUMAN - dbPTM
PAR12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAR12_HUMAN
UniProt AC Q9H0J9
Protein Name Poly [ADP-ribose] polymerase 12
Gene Name PARP12
Organism Homo sapiens (Human).
Sequence Length 701
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MAQAGVVGEVTQVLCAAGGALELPELRRRLRMGLSADALERLLRQRGRFVVAVRAGGAAAAPERVVLAASPLRLCRAHQGSKPGCVGLCAQLHLCRFMVYGACKFLRAGKNCRNSHSLTTEHNLSVLRTHGVDHLSYNELCQLLFQNDPWLLPEICQHYNKGDGPHGSCAFQKQCIKLHICQYFLQGECKFGTSCKRSHDFSNSENLEKLEKLGMSSDLVSRLPTIYRNAHDIKNKSSAPSRVPPLFVPQGTSERKDSSGSVSPNTLSQEEGDQICLYHIRKSCSFQDKCHRVHFHLPYRWQFLDRGKWEDLDNMELIEEAYCNPKIERILCSESASTFHSHCLNFNAMTYGATQARRLSTASSVTKPPHFILTTDWIWYWSDEFGSWQEYGRQGTVHPVTTVSSSDVEKAYLAYCTPGSDGQAATLKFQAGKHNYELDFKAFVQKNLVYGTTKKVCRRPKYVSPQDVTTMQTCNTKFPGPKSIPDYWDSSALPDPGFQKITLSSSSEEYQKVWNLFNRTLPFYFVQKIERVQNLALWEVYQWQKGQMQKQNGGKAVDERQLFHGTSAIFVDAICQQNFDWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQTHTMFLARVLVGEFVRGNASFVRPPAKEGWSNAFYDSCVNSVSDPSIFVIFEKHQVYPEYVIQYTTSSKPSVTPSILLALGSLFSSRQ
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
11PhosphorylationAGVVGEVTQVLCAAG
CCCHHHHHHHHHHCC		14.5224043423
70PhosphorylationERVVLAASPLRLCRA
CEEEEEECHHHHHHH		20.8927067055
115PhosphorylationAGKNCRNSHSLTTEH
CCCCCCCCCCCCCCC		8.6320873877
117PhosphorylationKNCRNSHSLTTEHNL
CCCCCCCCCCCCCCH		27.5120873877
119PhosphorylationCRNSHSLTTEHNLSV
CCCCCCCCCCCCHHH		32.9020873877
120PhosphorylationRNSHSLTTEHNLSVL
CCCCCCCCCCCHHHH		40.3120873877
125PhosphorylationLTTEHNLSVLRTHGV
CCCCCCHHHHHHHCC		25.1524719451
173UbiquitinationHGSCAFQKQCIKLHI
CCCCHHHHHHHHHHH		40.46-
183PhosphorylationIKLHICQYFLQGECK
HHHHHHHHHHCCCCC		11.2220090780
196UbiquitinationCKFGTSCKRSHDFSN
CCCCCCCCCCCCCCC		57.62-
209UbiquitinationSNSENLEKLEKLGMS
CCCHHHHHHHHCCCC		66.18-
212UbiquitinationENLEKLEKLGMSSDL
HHHHHHHHCCCCHHH		61.86-
216PhosphorylationKLEKLGMSSDLVSRL
HHHHCCCCHHHHHHC		20.9228857561
234UbiquitinationYRNAHDIKNKSSAPS
HHCHHHHCCCCCCCC		65.46-
252PhosphorylationPLFVPQGTSERKDSS
CCCCCCCCCCCCCCC		23.3623312004
253PhosphorylationLFVPQGTSERKDSSG
CCCCCCCCCCCCCCC		42.0823312004
256UbiquitinationPQGTSERKDSSGSVS
CCCCCCCCCCCCCCC		58.89-
258PhosphorylationGTSERKDSSGSVSPN
CCCCCCCCCCCCCCC		39.3723401153
259PhosphorylationTSERKDSSGSVSPNT
CCCCCCCCCCCCCCC		45.2630266825
261PhosphorylationERKDSSGSVSPNTLS
CCCCCCCCCCCCCCC		22.7530266825
263PhosphorylationKDSSGSVSPNTLSQE
CCCCCCCCCCCCCHH		17.7130266825
266PhosphorylationSGSVSPNTLSQEEGD
CCCCCCCCCCHHHCC		31.0430266825
268PhosphorylationSVSPNTLSQEEGDQI
CCCCCCCCHHHCCEE		33.2430266825
278PhosphorylationEGDQICLYHIRKSCS
HCCEEEEEEHHHHCC		7.2626074081
285PhosphorylationYHIRKSCSFQDKCHR
EEHHHHCCCCCCCEE		32.7927499020
289UbiquitinationKSCSFQDKCHRVHFH
HHCCCCCCCEEEEEE		22.58-
326UbiquitinationEEAYCNPKIERILCS
HHHHCCHHHHEEEEC		43.11-
360PhosphorylationATQARRLSTASSVTK
HHHHHHHCCCCCCCC		21.8120068231
361PhosphorylationTQARRLSTASSVTKP
HHHHHHCCCCCCCCC		34.8430177828
363PhosphorylationARRLSTASSVTKPPH
HHHHCCCCCCCCCCE		25.9830177828
364PhosphorylationRRLSTASSVTKPPHF
HHHCCCCCCCCCCEE		31.2030177828
366PhosphorylationLSTASSVTKPPHFIL
HCCCCCCCCCCEEEE		39.5230177828
410UbiquitinationVSSSDVEKAYLAYCT
CCHHHHCEEEEEEEC		42.03-
428UbiquitinationDGQAATLKFQAGKHN
CCCEEEEEEECCCCC		30.95-
428AcetylationDGQAATLKFQAGKHN
CCCEEEEEEECCCCC		30.9526051181
433UbiquitinationTLKFQAGKHNYELDF
EEEEECCCCCEEEEE		31.52-
441UbiquitinationHNYELDFKAFVQKNL
CCEEEEEHHHHHHHC		40.35-
446UbiquitinationDFKAFVQKNLVYGTT
EEHHHHHHHCCCCCC		47.12-
454UbiquitinationNLVYGTTKKVCRRPK
HCCCCCCHHHCCCCC		42.94-
455UbiquitinationLVYGTTKKVCRRPKY
CCCCCCHHHCCCCCC		44.46-
461AcetylationKKVCRRPKYVSPQDV
HHHCCCCCCCCHHHC		57.3726051181
461UbiquitinationKKVCRRPKYVSPQDV
HHHCCCCCCCCHHHC		57.37-
464PhosphorylationCRRPKYVSPQDVTTM
CCCCCCCCHHHCCCC		17.4724114839
469PhosphorylationYVSPQDVTTMQTCNT
CCCHHHCCCCCCCCC		25.4924114839
473PhosphorylationQDVTTMQTCNTKFPG
HHCCCCCCCCCCCCC		9.2624114839
474ADP-ribosylationDVTTMQTCNTKFPGP
HCCCCCCCCCCCCCC		3.2425043379
476PhosphorylationTTMQTCNTKFPGPKS
CCCCCCCCCCCCCCC		35.8924114839
477UbiquitinationTMQTCNTKFPGPKSI
CCCCCCCCCCCCCCC		35.25-
477AcetylationTMQTCNTKFPGPKSI
CCCCCCCCCCCCCCC		35.2526051181
482UbiquitinationNTKFPGPKSIPDYWD
CCCCCCCCCCCCCCC		67.92-
483PhosphorylationTKFPGPKSIPDYWDS
CCCCCCCCCCCCCCC		42.3527251275
487PhosphorylationGPKSIPDYWDSSALP
CCCCCCCCCCCCCCC		13.0327642862
500UbiquitinationLPDPGFQKITLSSSS
CCCCCCCEEECCCCC		35.08-
512UbiquitinationSSSEEYQKVWNLFNR
CCCHHHHHHHHHHCC		48.60-
528UbiquitinationLPFYFVQKIERVQNL
CCHHHHHHHHHHHHH		41.03-
545UbiquitinationWEVYQWQKGQMQKQN
HHHHHHHHHCHHHCC		48.42-
593UbiquitinationVHGTSYGKGSYFARD
EECCCCCCCCCCHHH		36.13-
600ADP-ribosylationKGSYFARDAAYSHHY
CCCCCHHHHHHCCCC		31.9225043379
611ADP-ribosylationSHHYSKSDTQTHTMF
CCCCCCCHHHHHHHH		46.7125043379
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 PAR12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAR12_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 PAR12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BHA15_HUMANBHLHA15physical
28514442
RN166_HUMANRNF166physical
28514442
GSH0_HUMANGCLMphysical
28514442
MKRN2_HUMANMKRN2physical
28514442
RN114_HUMANRNF114physical
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 PAR12_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-258 AND SER-263, ANDMASS SPECTROMETRY.

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