PARP9_HUMAN - dbPTM
PARP9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP9_HUMAN
UniProt AC Q8IXQ6
Protein Name Poly [ADP-ribose] polymerase 9
Gene Name PARP9
Organism Homo sapiens (Human).
Sequence Length 854
Subcellular Localization Cytoplasm, cytosol . Nucleus . Shuttles between the nucleus and the cytosol (PubMed:16809771). Translocates to the nucleus in response to IFNG or IFNB1 stimulation (PubMed:26479788). Export to the cytosol depends on the interaction with DTX3L (PubMed
Protein Description ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses. [PubMed: 16809771]
Protein Sequence MDFSMVAGAAAYNEKSGRITSLSLLFQKVFAQIFPQWRKGNTEECLPYKCSETGALGENYSWQIPINHNDFKILKNNERQLCEVLQNKFGCISTLVSPVQEGNSKSLQVFRKMLTPRIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPMMSNLKEIHLVSNEDPTVAAFKAASEFILGKSELGQETTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSVPQSTREEKRENGLEARSPAINLMGFNVEEMYEAHAWIQRILSLQNHHIIENNHILYLGRKEHDILSQLQKTSSVSITEIISPGRTELEIEGARADLIEVVMNIEDMLCKVQEEMARKKERGLWRSLGQWTIQQQKTQDEMKENIIFLKCPVPPTQELLDQKKQFEKCGLQVLKVEKIDNEVLMAAFQRKKKMMEEKLHRQPVSHRLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVPPPLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTCTQEYVQSQDYSSGPMRPFAQHPWRGFASGSPVD
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
4Phosphorylation----MDFSMVAGAAA
----CCHHHHCCHHH		14.2125850435
12PhosphorylationMVAGAAAYNEKSGRI
HHCCHHHCCCCCCCC		21.0925850435
18 (in isoform 2)Phosphorylation-35.7827251275
49UbiquitinationTEECLPYKCSETGAL
CCCCCCEECCCCCCC		29.37-
51PhosphorylationECLPYKCSETGALGE
CCCCEECCCCCCCCC		33.7627251275
53PhosphorylationLPYKCSETGALGENY
CCEECCCCCCCCCCE		16.0927251275
61PhosphorylationGALGENYSWQIPINH
CCCCCCEEEEEECCC		24.8824247654
72UbiquitinationPINHNDFKILKNNER
ECCCCCCHHHCCCHH		50.41-
75UbiquitinationHNDFKILKNNERQLC
CCCCHHHCCCHHHHH		62.29-
88UbiquitinationLCEVLQNKFGCISTL
HHHHHHHHCCHHHCC		30.12-
105UbiquitinationPVQEGNSKSLQVFRK
CCCCCCCCHHHHHHH		60.22-
121PhosphorylationLTPRIELSVWKDDLT
HCCCEEEEEECCHHH		17.0922496350
166UbiquitinationFEIQEESKQFVARYG
CCCCHHHHHHHHHHC		51.54-
172PhosphorylationSKQFVARYGKVSAGE
HHHHHHHHCCCCHHE		16.1522817900
174UbiquitinationQFVARYGKVSAGEIA
HHHHHHCCCCHHEEE		24.87-
191UbiquitinationGAGRLPCKQIIHAVG
CCCCCCHHHHHHHHC		42.46-
206UbiquitinationPRWMEWDKQGCTGKL
CCHHCCCCCCCCHHH		50.06-
273UbiquitinationKPMMSNLKEIHLVSN
CCCCCCCEEEEEECC		59.89-
279PhosphorylationLKEIHLVSNEDPTVA
CEEEEEECCCCHHHH		40.6422210691
289UbiquitinationDPTVAAFKAASEFIL
CHHHHHHHHHHHHHC		38.01-
361UbiquitinationQQAGVEMKSEFLATK
HHHCCCHHHHHHHHH		33.07-
362PhosphorylationQAGVEMKSEFLATKA
HHCCCHHHHHHHHHH		32.0724719451
368UbiquitinationKSEFLATKAKQFQRS
HHHHHHHHHHHHCHH		48.24-
368MalonylationKSEFLATKAKQFQRS
HHHHHHHHHHHHCHH		48.2432601280
411UbiquitinationQILKHAMKECLEKCI
HHHHHHHHHHHHHHH		46.16-
455UbiquitinationDEVLTFAKDHVKHQL
HHHHHHHHHHHHCCE		44.14-
459UbiquitinationTFAKDHVKHQLTVKF
HHHHHHHHCCEEEEE		23.39-
477UbiquitinationPTDLEIYKAFSSEMA
ECCHHHHHHHCHHHH		48.92-
485UbiquitinationAFSSEMAKRSKMLSL
HHCHHHHHHHCCCCC		56.76-
487PhosphorylationSSEMAKRSKMLSLNN
CHHHHHHHCCCCCCC		23.0128634298
488UbiquitinationSEMAKRSKMLSLNNY
HHHHHHHCCCCCCCC		48.14-
491PhosphorylationAKRSKMLSLNNYSVP
HHHHCCCCCCCCCCC		26.0821945579
495PhosphorylationKMLSLNNYSVPQSTR
CCCCCCCCCCCHHHH		15.2421945579
496PhosphorylationMLSLNNYSVPQSTRE
CCCCCCCCCCHHHHH		29.4621945579
500PhosphorylationNNYSVPQSTREEKRE
CCCCCCHHHHHHHHH		24.3021945579
501PhosphorylationNYSVPQSTREEKREN
CCCCCHHHHHHHHHC		36.5321945579
563PhosphorylationRKEHDILSQLQKTSS
CCHHHHHHHHHHCCC		29.2228122231
569PhosphorylationLSQLQKTSSVSITEI
HHHHHHCCCCEEEEE		35.4628985074
572PhosphorylationLQKTSSVSITEIISP
HHHCCCCEEEEEECC		26.2428985074
574PhosphorylationKTSSVSITEIISPGR
HCCCCEEEEEECCCC		17.3928985074
597 (in isoform 2)Ubiquitination-1.2521890473
627PhosphorylationWRSLGQWTIQQQKTQ
HHHHHHHHHHCCCCH		10.8728857561
632UbiquitinationQWTIQQQKTQDEMKE
HHHHHCCCCHHHHHH		43.7621890473
632UbiquitinationQWTIQQQKTQDEMKE
HHHHHCCCCHHHHHH		43.7621890473
632UbiquitinationQWTIQQQKTQDEMKE
HHHHHCCCCHHHHHH		43.7621890473
632 (in isoform 1)Ubiquitination-43.7621890473
637SulfoxidationQQKTQDEMKENIIFL
CCCCHHHHHHCEEEE		9.9321406390
638UbiquitinationQKTQDEMKENIIFLK
CCCHHHHHHCEEEEE		45.63-
645UbiquitinationKENIIFLKCPVPPTQ
HHCEEEEECCCCCHH		26.24-
651PhosphorylationLKCPVPPTQELLDQK
EECCCCCHHHHHHHH		28.7123532336
659UbiquitinationQELLDQKKQFEKCGL
HHHHHHHHHHHHHCC		55.37-
663UbiquitinationDQKKQFEKCGLQVLK
HHHHHHHHHCCEEEE		34.59-
680SulfoxidationKIDNEVLMAAFQRKK
ECCHHHHHHHHHHHH		2.8221406390
693AcetylationKKKMMEEKLHRQPVS
HHHHHHHHHHCCCCH		35.977355457
705 (in isoform 2)Ubiquitination-48.2121890473
740UbiquitinationGAGIYFTKNLKNLAE
CCCEECCCCHHHHHH		50.8421890473
740UbiquitinationGAGIYFTKNLKNLAE
CCCEECCCCHHHHHH		50.8421890473
740UbiquitinationGAGIYFTKNLKNLAE
CCCEECCCCHHHHHH		50.8421890473
740 (in isoform 1)Ubiquitination-50.8421890473
743UbiquitinationIYFTKNLKNLAEKAK
EECCCCHHHHHHHHH		60.35-
849PhosphorylationHPWRGFASGSPVD--
CCCCCCCCCCCCC--		37.2323090842
851PhosphorylationWRGFASGSPVD----
CCCCCCCCCCC----		21.1823403867
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 PARP9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP9_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 PARP9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DTX3L_HUMANDTX3Lphysical
12670957
PARP1_HUMANPARP1physical
24886089
PAR14_HUMANPARP14physical
24886089
DTX3L_HUMANDTX3Lphysical
24886089
STAT1_HUMANSTAT1physical
26479788
DTX3L_HUMANDTX3Lphysical
26479788
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 PARP9_HUMAN

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Related Literatures of Post-Translational Modification

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