| UniProt ID | APEX2_HUMAN | |
|---|---|---|
| UniProt AC | Q9UBZ4 | |
| Protein Name | DNA-(apurinic or apyrimidinic site) lyase 2 | |
| Gene Name | APEX2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 518 | |
| Subcellular Localization | Nucleus. Cytoplasm. Mitochondrion . Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. | |
| Protein Description | Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.. | |
| Protein Sequence | MLRVVSWNINGIRRPLQGVANQEPSNCAAVAVGRILDELDADIVCLQETKVTRDALTEPLAIVEGYNSYFSFSRNRSGYSGVATFCKDNATPVAAEEGLSGLFATQNGDVGCYGNMDEFTQEELRALDSEGRALLTQHKIRTWEGKEKTLTLINVYCPHADPGRPERLVFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNLECFEEDPGRKWMDSLLSNLGCQSASHVGPFIDSYRCFQPKQEGAFTCWSAVTGARHLNYGSRLDYVLGDRTLVIDTFQASFLLPEVMGSDHCPVGAVLSVSSVPAKQCPPLCTRFLPEFAGTQLKILRFLVPLEQSPVLEQSTLQHNNQTRVQTCQNKAQVRSTRPQPSQVGSSRGQKNLKSYFQPSPSCPQASPDIELPSLPLMSALMTPKTPEEKAVAKVVKGQAKTSEAKDEKELRTSFWKSVLAGPLRTPLCGGHREPCVMRTVKKPGPNLGRRFYMCARPRGPPTDPSSRCNFFLWSRPS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 49 | Phosphorylation | DIVCLQETKVTRDAL CEEEEECCCCCHHHC | 20.18 | 29083192 | |
| 66 | Phosphorylation | PLAIVEGYNSYFSFS CEEEEECCCCCEECC | 6.34 | 22817900 | |
| 69 | Phosphorylation | IVEGYNSYFSFSRNR EEECCCCCEECCCCC | 10.29 | 22817900 | |
| 136 | Phosphorylation | SEGRALLTQHKIRTW HHHHHHHHHCEEECC | 29.49 | 28634120 | |
| 139 | Ubiquitination | RALLTQHKIRTWEGK HHHHHHCEEECCCCC | 24.86 | - | |
| 146 | Ubiquitination | KIRTWEGKEKTLTLI EEECCCCCCEEEEEE | 44.51 | - | |
| 149 | Phosphorylation | TWEGKEKTLTLINVY CCCCCCEEEEEEEEE | 26.52 | - | |
| 175 | Phosphorylation | LVFKMRFYRLLQIRA HHHHHHHHHHHHHHH | 7.03 | - | |
| 253 | Ubiquitination | SYRCFQPKQEGAFTC CEECCCCCCCCCCCH | 50.64 | - | |
| 338 | Ubiquitination | EFAGTQLKILRFLVP HHCCCHHHHHHHHCC | 29.85 | 21890473 | |
| 349 | Phosphorylation | FLVPLEQSPVLEQST HHCCHHHCCCCCHHH | 13.96 | 29496963 | |
| 355 | Phosphorylation | QSPVLEQSTLQHNNQ HCCCCCHHHHCCCCC | 23.01 | 29523821 | |
| 371 | Ubiquitination | RVQTCQNKAQVRSTR CHHHCCCHHHHHCCC | 17.83 | - | |
| 386 | Phosphorylation | PQPSQVGSSRGQKNL CCCHHCCCCCCCCCH | 20.29 | 28555341 | |
| 400 | Phosphorylation | LKSYFQPSPSCPQAS HHHHCCCCCCCCCCC | 20.75 | 27251275 | |
| 407 | Phosphorylation | SPSCPQASPDIELPS CCCCCCCCCCCCCCC | 20.18 | 24719451 | |
| 414 | Phosphorylation | SPDIELPSLPLMSAL CCCCCCCCHHHHHHH | 56.07 | 28348404 | |
| 449 | Ubiquitination | TSEAKDEKELRTSFW CCCCCCHHHHHHHHH | 72.66 | - | |
| 457 | Ubiquitination | ELRTSFWKSVLAGPL HHHHHHHHHHHHCCC | 28.77 | 21890473 | |
| 518 | Phosphorylation | FFLWSRPS------- EEEEECCC------- | 52.31 | 21712546 |
| 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 APEX2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APEX2_HUMAN !! | ||||||
* 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 APEX2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| HOOK2_HUMAN | HOOK2 | physical | 16189514 | |
| FBLN4_HUMAN | EFEMP2 | physical | 16189514 | |
| PCNA_HUMAN | PCNA | physical | 11376153 | |
| A4_HUMAN | APP | physical | 21832049 | |
| PDE12_HUMAN | PDE12 | physical | 22939629 | |
| CUL9_HUMAN | CUL9 | physical | 28514442 | |
| APBA2_HUMAN | APBA2 | physical | 28514442 | |
| SIR1_HUMAN | SIRT1 | physical | 28514442 | |
| WDR54_HUMAN | WDR54 | physical | 28514442 | |
| DDB2_HUMAN | DDB2 | physical | 28514442 | |
| CUL7_HUMAN | CUL7 | physical | 28514442 | |
| CTU2_HUMAN | CTU2 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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