PARP2_HUMAN - dbPTM
PARP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP2_HUMAN
UniProt AC Q9UGN5
Protein Name Poly [ADP-ribose] polymerase 2
Gene Name PARP2
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization Nucleus .
Protein Description Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. [PubMed: 10364231]
Protein Sequence MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
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
8PhosphorylationMAARRRRSTGGGRAR
CCCCCCCCCCCHHHH		29.5923882029
9PhosphorylationAARRRRSTGGGRARA
CCCCCCCCCCHHHHH		37.7323882029
20PhosphorylationRARALNESKRVNNGN
HHHHCCCCCCCCCCC		25.3723882029
28PhosphorylationKRVNNGNTAPEDSSP
CCCCCCCCCCCCCCH		45.0123403867
33PhosphorylationGNTAPEDSSPAKKTR
CCCCCCCCCHHHHHH		36.2423401153
33 (in isoform 2)Phosphorylation-36.24-
34PhosphorylationNTAPEDSSPAKKTRR
CCCCCCCCHHHHHHH		40.9923401153
34 (in isoform 2)Phosphorylation-40.99-
37AcetylationPEDSSPAKKTRRCQR
CCCCCHHHHHHHHHH		59.0518436469
38AcetylationEDSSPAKKTRRCQRQ
CCCCHHHHHHHHHHH		49.7418436469
39PhosphorylationDSSPAKKTRRCQRQE
CCCHHHHHHHHHHHH		23.7328111955
47PhosphorylationRRCQRQESKKMPVAG
HHHHHHHHCCCCCCC		29.2824719451
71UbiquitinationDKQDGMPGRSWASKR
CCCCCCCCCHHHHHH		27.6229967540
82PhosphorylationASKRVSESVKALLLK
HHHHHHHHHHHHHHC		22.7833259812
88UbiquitinationESVKALLLKGKAPVD
HHHHHHHHCCCCCCC		7.7529967540
91UbiquitinationKALLLKGKAPVDPEC
HHHHHCCCCCCCHHH		48.1833845483
101UbiquitinationVDPECTAKVGKAHVY
CCHHHCCEECCEEEE		33.1129967540
104UbiquitinationECTAKVGKAHVYCEG
HHCCEECCEEEEECC		38.0029967540
115PhosphorylationYCEGNDVYDVMLNQT
EECCCCHHEEEECCE		12.99-
158UbiquitinationWGRVGKMGQHSLVAC
ECCCCCCCCCCEEEE		26.0729967540
160UbiquitinationRVGKMGQHSLVACSG
CCCCCCCCCEEEECC		19.8529967540
171UbiquitinationACSGNLNKAKEIFQK
EECCCHHHHHHHHHH		65.0929967540
173UbiquitinationSGNLNKAKEIFQKKF
CCCHHHHHHHHHHHH		53.6129967540
183UbiquitinationFQKKFLDKTKNNWED
HHHHHHHHHCCCHHH		64.6429967540
196UbiquitinationEDREKFEKVPGKYDM
HHHHHHHCCCCCCCE		57.7929967540
201PhosphorylationFEKVPGKYDMLQMDY
HHCCCCCCCEEECCC		16.7022468782
208PhosphorylationYDMLQMDYATNTQDE
CCEEECCCCCCCCCH		15.2426552605
210PhosphorylationMLQMDYATNTQDEEE
EEECCCCCCCCCHHH		32.3526552605
212PhosphorylationQMDYATNTQDEEETK
ECCCCCCCCCHHHHH		32.8026552605
212UbiquitinationQMDYATNTQDEEETK
ECCCCCCCCCHHHHH		32.8029967540
216UbiquitinationATNTQDEEETKKEES
CCCCCCHHHHHHHHH		78.3133845483
218PhosphorylationNTQDEEETKKEESLK
CCCCHHHHHHHHHHC		51.1722468782
223PhosphorylationEETKKEESLKSPLKP
HHHHHHHHHCCCCCC		42.0425850435
225UbiquitinationTKKEESLKSPLKPES
HHHHHHHCCCCCCHH		60.3429967540
226PhosphorylationKKEESLKSPLKPESQ
HHHHHHCCCCCCHHH		40.5325159151
229UbiquitinationESLKSPLKPESQLDL
HHHCCCCCCHHHHHH		50.5533845483
232PhosphorylationKSPLKPESQLDLRVQ
CCCCCCHHHHHHHHH		44.5721406692
256UbiquitinationQAMEEMMMEMKYNTK
HHHHHHHHHHCCCCC		4.3729967540
260PhosphorylationEMMMEMKYNTKKAPL
HHHHHHCCCCCCCCC		27.1023663014
262PhosphorylationMMEMKYNTKKAPLGK
HHHHCCCCCCCCCCC		30.7223663014
263UbiquitinationMEMKYNTKKAPLGKL
HHHCCCCCCCCCCCE		43.2121890473
263 (in isoform 2)Ubiquitination-43.2121890473
269UbiquitinationTKKAPLGKLTVAQIK
CCCCCCCCEEHHHHH		48.9829967540
271PhosphorylationKAPLGKLTVAQIKAG
CCCCCCEEHHHHHHH		19.7921406692
276UbiquitinationKLTVAQIKAGYQSLK
CEEHHHHHHHHHHHH		24.5522817900
276 (in isoform 1)Ubiquitination-24.5521890473
279PhosphorylationVAQIKAGYQSLKKIE
HHHHHHHHHHHHHHH		10.3728796482
317PhosphorylationPHDFGLRTPPLIRTQ
CCCCCCCCCCCCCCH		34.0124719451
328PhosphorylationIRTQKELSEKIQLLE
CCCHHHHHHHHHHHH		37.6224719451
332UbiquitinationKELSEKIQLLEALGD
HHHHHHHHHHHHHCC		51.5722817900
335 (in isoform 2)Ubiquitination-50.9021890473
335UbiquitinationSEKIQLLEALGDIEI
HHHHHHHHHHCCHHH		50.9021890473
345UbiquitinationGDIEIAIKLVKTELQ
CCHHHHHHHHHHHHC		37.9022817900
348 (in isoform 1)Ubiquitination-46.8721890473
348UbiquitinationEIAIKLVKTELQSPE
HHHHHHHHHHHCCCC		46.8722817900
353PhosphorylationLVKTELQSPEHPLDQ
HHHHHHCCCCCCCHH		44.9025159151
383PhosphorylationSYEFKVISQYLQSTH
CHHHHHHHHHHHHCC		18.76-
389PhosphorylationISQYLQSTHAPTHSD
HHHHHHHCCCCCCCC		14.75-
430PhosphorylationRMLLWHGSRMSNWVG
HHHHHCHHHHHHHHH		16.3620068231
456UbiquitinationEAPITGYMFGKGIYF
CCCCCEEECCCCEEE		3.6532015554
467PhosphorylationGIYFADMSSKSANYC
CEEEEECCCCCCCCC		34.85-
469UbiquitinationYFADMSSKSANYCFA
EEEECCCCCCCCCHH		46.4032015554
473PhosphorylationMSSKSANYCFASRLK
CCCCCCCCCHHHHCH		6.6728152594
480UbiquitinationYCFASRLKNTGLLLL
CCHHHHCHHHCCHHH		51.89-
499UbiquitinationLGQCNELLEANPKAE
HHHHHHHHHHCCCCC		4.8129967540
512UbiquitinationAEGLLQGKHSTKGLG
CCCCCCCCCCCCCCC		22.7829967540
514PhosphorylationGLLQGKHSTKGLGKM
CCCCCCCCCCCCCCC		34.9922964224
516UbiquitinationLQGKHSTKGLGKMAP
CCCCCCCCCCCCCCC		55.97-
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 PARP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP2_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 PARP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC1_HUMANXRCC1physical
11948190
STP2_HUMANTNP2physical
19607827
HSP72_HUMANHSPA2physical
19607827
TIF1B_HUMANTRIM28physical
18676401
CBX5_HUMANCBX5physical
18676401
NPM_MOUSENpm1physical
15615785
UHRF1_HUMANUHRF1physical
24782312
HPF1_HUMANC4orf27physical
27067600
H31T_HUMANHIST3H3physical
28190768
H15_HUMANHIST1H1Bphysical
28190768
H31_HUMANHIST1H3Aphysical
28190768
H33_HUMANH3F3Aphysical
28190768
H10_HUMANH1F0physical
28190768
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 PARP2_HUMAN

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Related Literatures of Post-Translational Modification

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