APTX_HUMAN - dbPTM
APTX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APTX_HUMAN
UniProt AC Q7Z2E3
Protein Name Aprataxin
Gene Name APTX
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Nucleus, nucleoplasm . Nucleus, nucleolus . Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage (PubMed:15380105). Colocalizes with MDC1 at sites of DNA double-strand breaks (PubMed:20008512). Interaction with NCL is required for nuc
Protein Description DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. [PubMed: 15380105]
Protein Sequence MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKDQEVKLQPGQVLHMVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ
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
26PhosphorylationCWLVRQDSRHQRIRL
HHHHCCCCCCCCCCC		24.2727067055
30 (in isoform 4)Phosphorylation-15.18-
39UbiquitinationRLPHLEAVVIGRGPE
CCCCEEEEEECCCCC		2.0524816145
53UbiquitinationETKITDKKCSRQQVQ
CCCCCCCCCCHHHHH		40.0124816145
62SumoylationSRQQVQLKAECNKGY
CHHHHHHHHHCCCCE		25.66-
62SumoylationSRQQVQLKAECNKGY
CHHHHHHHHHCCCCE		25.66-
67PhosphorylationQLKAECNKGYVKVKQ
HHHHHCCCCEEEEEE		64.3833259812
75UbiquitinationGYVKVKQVGVNPTSI
CEEEEEEECCCCCCC		8.3929967540
84O-linked_GlycosylationVNPTSIDSVVIGKDQ
CCCCCCCEEEECCCC		19.3329351928
89UbiquitinationIDSVVIGKDQEVKLQ
CCEEEECCCCCEEEC		45.15-
98UbiquitinationQEVKLQPGQVLHMVN
CCEEECCCCHHHHHH		19.7829967540
107UbiquitinationVLHMVNELYPYIVEF
HHHHHHHHHHHHHHC		4.3829967540
118UbiquitinationIVEFEEEAKNPGLET
HHHCHHHHCCCCCHH		21.8729967540
118 (in isoform 7)Phosphorylation-21.87-
121PhosphorylationFEEEAKNPGLETHRK
CHHHHCCCCCHHHHH		48.3033259812
125PhosphorylationAKNPGLETHRKRKRS
HCCCCCHHHHHHHCC		31.8322817900
132PhosphorylationTHRKRKRSGNSDSIE
HHHHHHCCCCCCCHH		45.4129255136
132 (in isoform 11)Phosphorylation-45.41-
135PhosphorylationKRKRSGNSDSIERDA
HHHCCCCCCCHHHHH		35.9422167270
137PhosphorylationKRSGNSDSIERDAAQ
HCCCCCCCHHHHHHH		26.6022167270
138UbiquitinationRSGNSDSIERDAAQE
CCCCCCCHHHHHHHH		6.3733845483
150PhosphorylationAQEAEAGTGLEPGSN
HHHHHCCCCCCCCCC		45.7130576142
152UbiquitinationEAEAGTGLEPGSNSG
HHHCCCCCCCCCCCC		7.8329967540
156PhosphorylationGTGLEPGSNSGQCSV
CCCCCCCCCCCCCCC		38.2429632367
158PhosphorylationGLEPGSNSGQCSVPL
CCCCCCCCCCCCCEE		31.7529632367
161UbiquitinationPGSNSGQCSVPLKKG
CCCCCCCCCCEECCC		5.1629967540
162PhosphorylationGSNSGQCSVPLKKGK
CCCCCCCCCEECCCC		20.9129632367
166AcetylationGQCSVPLKKGKDAPI
CCCCCEECCCCCCCC		54.1026051181
166UbiquitinationGQCSVPLKKGKDAPI
CCCCCEECCCCCCCC		54.10-
171UbiquitinationPLKKGKDAPIKKESL
EECCCCCCCCCHHHH		15.9429967540
172UbiquitinationLKKGKDAPIKKESLG
ECCCCCCCCCHHHHC		49.4129967540
175UbiquitinationGKDAPIKKESLGHWS
CCCCCCCHHHHCCHH		53.94-
177PhosphorylationDAPIKKESLGHWSQG
CCCCCHHHHCCHHCC		48.8325159151
182PhosphorylationKESLGHWSQGLKISM
HHHHCCHHCCCEEEE		14.5429449344
186UbiquitinationGHWSQGLKISMQDPK
CCHHCCCEEEECCCC		39.29-
189UbiquitinationSQGLKISMQDPKMQV
HCCCEEEECCCCCCE		6.2833845483
192UbiquitinationLKISMQDPKMQVYKD
CEEEECCCCCCEECC		19.6833845483
198SumoylationDPKMQVYKDEQVVVI
CCCCCEECCCEEEEE		56.80-
198AcetylationDPKMQVYKDEQVVVI
CCCCCEECCCEEEEE		56.8026051181
198SumoylationDPKMQVYKDEQVVVI
CCCCCEECCCEEEEE		56.80-
198UbiquitinationDPKMQVYKDEQVVVI
CCCCCEECCCEEEEE		56.80-
208AcetylationQVVVIKDKYPKARYH
EEEEEECCCCCCCEE		59.4526051181
209PhosphorylationVVVIKDKYPKARYHW
EEEEECCCCCCCEEE		21.79-
214PhosphorylationDKYPKARYHWLVLPW
CCCCCCCEEEEEEEC		11.3823898821
225UbiquitinationVLPWTSISSLKAVAR
EEECCCHHHHHHHHH		29.4129967540
225PhosphorylationVLPWTSISSLKAVAR
EEECCCHHHHHHHHH		29.4124719451
239UbiquitinationREHLELLKHMHTVGE
HHHHHHHHHHCCCCC		52.05-
243UbiquitinationELLKHMHTVGEKVIV
HHHHHHCCCCCEEEE		23.7233845483
257AcetylationVDFAGSSKLRFRLGY
EECCCCCCEEEEEEC		45.4325953088
328UbiquitinationDGMPELLKLPLRCHE
CCCHHHHHCCCCHHH		61.76-
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
125TPhosphorylationKinasePRKCGP05129
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APTX_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 APTX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC1_HUMANXRCC1physical
15555565
PARP1_HUMANPARP1physical
15555565
P53_HUMANTP53physical
15044383
XRCC1_HUMANXRCC1physical
15044383
PARP1_HUMANPARP1physical
15044383
TRI37_HUMANTRIM37physical
16713569
XRCC4_HUMANXRCC4physical
16713569
CE350_HUMANCEP350physical
16713569
ZEP1_HUMANHIVEP1physical
16713569
CACO1_HUMANCALCOCO1physical
16713569
CNTRB_HUMANCNTROBphysical
16713569
SYT17_HUMANSYT17physical
16713569
MABP1_HUMANMAPKBP1physical
16713569
MBP_HUMANMBPphysical
16713569
TSYL2_HUMANTSPYL2physical
16713569
XRCC1_HUMANXRCC1physical
16713569
ZN639_HUMANZNF639physical
16713569
PICK1_HUMANPICK1physical
16713569
DNLI3_HUMANLIG3physical
15367657
DDX21_HUMANDDX21physical
15367657
XRCC1_HUMANXRCC1physical
15367657
HSP74_HUMANHSPA4physical
15367657
BAD_HUMANBADphysical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
208920Ataxia-oculomotor apraxia syndrome (AOA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APTX_HUMAN

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Related Literatures of Post-Translational Modification

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