PARI_HUMAN - dbPTM
PARI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARI_HUMAN
UniProt AC Q9NWS1
Protein Name PCNA-interacting partner
Gene Name PARPBP
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Cytoplasm. Nucleus . Localizes to chromatin in response to S phase arrest but not in mitosis. Targeted to chromatin via its interaction with PCNA.
Protein Description Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by interfering with the formation of the RAD51-DNA homologous recombination structure. Binds single-strand DNA and poly(A) homopolymers. Positively regulate the poly(ADP-ribosyl)ation activity of PARP1; however such function may be indirect..
Protein Sequence MAVFNQKSVSDMIKEFRKNWRALCNSERTTLCGADSMLLALQLSMAENNKQHSGEFTVSLSDVLLTWKYLLHEKLNLPVENMDVTDHYEDVRKIYDDFLKNSNMLDLIDVYQKCRALTSNCENYNTVSPSQLLDFLSGKQYAVGDETDLSIPTSPTSKYNRDNEKVQLLARKIIFSYLNLLVNSKNDLAVAYILNIPDRGLGREAFTDLKHAAREKQMSIFLVATSFIRTIELGGKGYAPPPSDPLRTHVKGLSNFINFIDKLDEILGEIPNPSIAGGQILSVIKMQLIKGQNSRDPFCKAIEEVAQDLDLRIKNIINSQEGVVALSTTDISPARPKSHAINHGTAYCGRDTVKALLVLLDEEAANAPTKNKAELLYDEENTIHHHGTSILTLFRSPTQVNNSIKPLRERICVSMQEKKIKMKQTLIRSQFACTYKDDYMISKDNWNNVNLASKPLCVLYMENDLSEGVNPSVGRSTIGTSFGNVHLDRSKNEKVSRKSTSQTGNKSSKRKQVDLDGENILCDNRNEPPQHKNAKIPKKSNDSQNRLYGKLAKVAKSNKCTAKDKLISGQAKLTQFFRL
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
7Ubiquitination-MAVFNQKSVSDMIK
-CCCCCCCCHHHHHH		54.66-
8PhosphorylationMAVFNQKSVSDMIKE
CCCCCCCCHHHHHHH		19.65-
10PhosphorylationVFNQKSVSDMIKEFR
CCCCCCHHHHHHHHH		28.6629396449
14UbiquitinationKSVSDMIKEFRKNWR
CCHHHHHHHHHHHHH		44.13-
19 (in isoform 2)Ubiquitination-29.2521906983
57PhosphorylationKQHSGEFTVSLSDVL
CCCCCEEEEEHHHHH		12.6018767875
59PhosphorylationHSGEFTVSLSDVLLT
CCCEEEEEHHHHHHH		21.0618767875
61PhosphorylationGEFTVSLSDVLLTWK
CEEEEEHHHHHHHHH		20.4018767875
77 (in isoform 2)Ubiquitination-7.9221906983
93UbiquitinationDHYEDVRKIYDDFLK
CCHHHHHHHHHHHHH		45.53-
100 (in isoform 7)Ubiquitination-59.3221906983
100 (in isoform 1)Ubiquitination-59.3221906983
100 (in isoform 6)Ubiquitination-59.3221906983
100MethylationKIYDDFLKNSNMLDL
HHHHHHHHHCCHHHH		59.3242341061
100 (in isoform 5)Ubiquitination-59.3221906983
100 (in isoform 4)Ubiquitination-59.3221906983
100UbiquitinationKIYDDFLKNSNMLDL
HHHHHHHHHCCHHHH		59.3221906983
104 (in isoform 3)Ubiquitination-2.8621906983
113UbiquitinationDLIDVYQKCRALTSN
HHHHHHHHHHHHHCC		14.17-
147PhosphorylationQYAVGDETDLSIPTS
CEECCCCCCCCCCCC		47.1629978859
150PhosphorylationVGDETDLSIPTSPTS
CCCCCCCCCCCCCCC		29.3629978859
153PhosphorylationETDLSIPTSPTSKYN
CCCCCCCCCCCCCCC		45.7422210691
154PhosphorylationTDLSIPTSPTSKYNR
CCCCCCCCCCCCCCC		22.3325159151
155 (in isoform 2)Ubiquitination-43.0721906983
156PhosphorylationLSIPTSPTSKYNRDN
CCCCCCCCCCCCCCC		37.3022210691
157PhosphorylationSIPTSPTSKYNRDNE
CCCCCCCCCCCCCCH		36.2029978859
158UbiquitinationIPTSPTSKYNRDNEK
CCCCCCCCCCCCCHH		49.3621906983
158 (in isoform 7)Ubiquitination-49.3621906983
158 (in isoform 5)Ubiquitination-49.3621906983
158 (in isoform 6)Ubiquitination-49.3621906983
158 (in isoform 1)Ubiquitination-49.3621906983
162 (in isoform 3)Ubiquitination-65.0921906983
165UbiquitinationKYNRDNEKVQLLARK
CCCCCCHHHHHHHHH		41.35-
184PhosphorylationYLNLLVNSKNDLAVA
HHHHHHCCCCHHHHH		25.9227732954
210UbiquitinationREAFTDLKHAAREKQ
HHHHHCHHHHHHHHH		33.73-
236 (in isoform 1)Ubiquitination-47.1221906983
236 (in isoform 5)Ubiquitination-47.1221906983
236 (in isoform 6)Ubiquitination-47.1221906983
236 (in isoform 7)Ubiquitination-47.1221906983
236UbiquitinationRTIELGGKGYAPPPS
HHHHCCCCCCCCCCC		47.1221906983
273 (in isoform 2)Ubiquitination-23.0421906983
289 (in isoform 2)Ubiquitination-2.3721906983
314UbiquitinationQDLDLRIKNIINSQE
HHHHHHHHHHHCCCC		35.34-
327PhosphorylationQEGVVALSTTDISPA
CCCEEEEECCCCCCC		21.3728348404
328PhosphorylationEGVVALSTTDISPAR
CCEEEEECCCCCCCC		29.3628348404
329PhosphorylationGVVALSTTDISPARP
CEEEEECCCCCCCCC		28.1428348404
332PhosphorylationALSTTDISPARPKSH
EEECCCCCCCCCCCC		18.4728348404
337UbiquitinationDISPARPKSHAINHG
CCCCCCCCCCCCCCC		49.69-
345PhosphorylationSHAINHGTAYCGRDT
CCCCCCCCCCCCHHH		13.60-
347PhosphorylationAINHGTAYCGRDTVK
CCCCCCCCCCHHHHH		8.69-
354 (in isoform 1)Ubiquitination-35.1021906983
354UbiquitinationYCGRDTVKALLVLLD
CCCHHHHHHHHHHHC		35.1021906983
354 (in isoform 5)Ubiquitination-35.1021906983
370 (in isoform 5)Ubiquitination-56.2321906983
370UbiquitinationEAANAPTKNKAELLY
HHHCCCCCCHHHHHC		56.2321906983
370 (in isoform 1)Ubiquitination-56.2321906983
405UbiquitinationTQVNNSIKPLRERIC
CCCCCCCHHHHHHHH		37.512190698
405 (in isoform 5)Ubiquitination-37.5121906983
425PhosphorylationKKIKMKQTLIRSQFA
HHHHHHHHHHHHHHC		20.7321964256
453PhosphorylationWNNVNLASKPLCVLY
CCCCCCCCCCEEEEE		37.6624719451
499PhosphorylationNEKVSRKSTSQTGNK
CCCCCCCCCCCCCCC		31.9822964224
500PhosphorylationEKVSRKSTSQTGNKS
CCCCCCCCCCCCCCC		28.0822964224
501PhosphorylationKVSRKSTSQTGNKSS
CCCCCCCCCCCCCCC		32.6022964224
506AcetylationSTSQTGNKSSKRKQV
CCCCCCCCCCCCEEE		58.417826245
508PhosphorylationSQTGNKSSKRKQVDL
CCCCCCCCCCEEECC		37.7822964224
568PhosphorylationTAKDKLISGQAKLTQ
CHHHHHHCCHHHHHH		34.9829449344
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 PARI_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARI_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 PARI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
22153967
RAD51_HUMANRAD51physical
22153967
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 PARI_HUMAN

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Related Literatures of Post-Translational Modification

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