MUTYH_HUMAN - dbPTM
MUTYH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUTYH_HUMAN
UniProt AC Q9UIF7
Protein Name Adenine DNA glycosylase
Gene Name MUTYH
Organism Homo sapiens (Human).
Sequence Length 546
Subcellular Localization Nucleus . Mitochondrion .
Protein Description Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities..
Protein Sequence MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ
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
2Phosphorylation------MTPLVSRLS
------CCHHHHHHH
25.9029083192
6Phosphorylation--MTPLVSRLSRLWA
--CCHHHHHHHHHHH
34.8826552605
9PhosphorylationTPLVSRLSRLWAIMR
CHHHHHHHHHHHHHC
24.9827422710
24PhosphorylationKPRAAVGSGHRKQAA
CCCCCCCCCHHHHHH
25.48-
28 (in isoform 1)Ubiquitination-38.3222053931
28UbiquitinationAVGSGHRKQAASQEG
CCCCCHHHHHHHHHH
38.3222053931
41 (in isoform 3)Ubiquitination-57.28-
47 (in isoform 3)Ubiquitination-31.69-
94 (in isoform 3)Ubiquitination-31.18-
105UbiquitinationLSWYDQEKRDLPWRR
HHHHCHHCCCCCCHH
45.65-
178 (in isoform 3)Ubiquitination-21.56-
189UbiquitinationRLQEGARKVVEELGG
HHHHHHHHHHHHHCC
50.53-
360PhosphorylationVNFPRKASRKPPREE
CCCCCCCCCCCCCCC
43.8222817900
404 (in isoform 3)Ubiquitination-8.00-
415UbiquitinationPSEQLQRKALLQELQ
CCHHHHHHHHHHHHH
30.35-
494PhosphorylationMKKVFRVYQGQQPGT
HHHHHHHHCCCCCCC
11.5829978859
495 (in isoform 3)Ubiquitination-40.12-
501PhosphorylationYQGQQPGTCMGSKRS
HCCCCCCCCCCCCCC
13.1529978859
505PhosphorylationQPGTCMGSKRSQVSS
CCCCCCCCCCCCCCC
9.6729978859
506UbiquitinationPGTCMGSKRSQVSSP
CCCCCCCCCCCCCCC
50.79-
508PhosphorylationTCMGSKRSQVSSPCS
CCCCCCCCCCCCCCC
38.3728102081
511PhosphorylationGSKRSQVSSPCSRKK
CCCCCCCCCCCCCCC
22.4126552605
512PhosphorylationSKRSQVSSPCSRKKP
CCCCCCCCCCCCCCC
30.9426552605
515PhosphorylationSQVSSPCSRKKPRMG
CCCCCCCCCCCCCHH
50.9826552605
535PhosphorylationNFFRSHISTDAHSLN
HHHHHHHCCCHHHHH
18.1422817900
540PhosphorylationHISTDAHSLNSAAQ-
HHCCCHHHHHHHCC-
30.8528555341

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
-KUbiquitinationE3 ubiquitin ligaseHUWE1Q7Z6Z7
PMID:24443563

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUTYH_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 MUTYH_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APEX1_HUMANAPEX1physical
11092888
PCNA_HUMANPCNAphysical
11092888
RFA1_HUMANRPA1physical
11092888
MSH2_HUMANMSH2physical
11801590
MSH6_HUMANMSH6physical
11801590
APEX1_HUMANAPEX1physical
24209961
HUWE1_HUMANHUWE1physical
24443563
ATRAP_HUMANAGTRAPphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608456Familial adenomatous polyposis 2 (FAP2)
613659Gastric cancer (GASC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MUTYH_HUMAN

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Related Literatures of Post-Translational Modification

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