Q9U8Q4
Gene name |
|
Protein name |
Pierisin |
Names |
EC 2.4.2.- , NAD--DNA ADP-ribosyltransferase , Pierisin-1 |
Species |
Pieris rapae (Small white butterfly) (Artogeia rapae) |
KEGG Pathway |
|
EC number |
2.4.2.-: Pentosyltransferases |
Protein Class |
|

Descriptions
Pierisin-1 is an ADP-ribosyltransferase that induces apoptosis of various types of cancer cell lines such as HeLa and TMK-1 cells. Segments 245-256 of the linker region mask the putative DNA-binding region and inhibit DNA binding, affecting ADP-ribosylation and apoptosis. This segment can also interact with the PN loop and induce a β4’ strand to form a β’-sheet, stabilizing the PN loop and relieving the autoinhibition of Pierisin-1.
Autoinhibitory domains (AIDs)
Target domain |
1-233 (Catalytic domain) |
Relief mechanism |
Others |
Assay |
Structural analysis, Deletion assay, Mutagenesis experiment |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
No variants for Q9U8Q4
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q9U8Q4 |
No associated diseases with Q9U8Q4
4 regional properties for Q9U8Q4
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Ricin B, lectin domain | 267 - 408 | IPR000772-1 |
domain | Ricin B, lectin domain | 418 - 560 | IPR000772-2 |
domain | Ricin B, lectin domain | 569 - 707 | IPR000772-3 |
domain | Ricin B, lectin domain | 716 - 848 | IPR000772-4 |
Functions
Description | ||
---|---|---|
EC Number | 2.4.2.- | Pentosyltransferases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
No GO annotations of cellular component
Name | Definition |
---|---|
No GO annotations for cellular component |
3 GO annotations of molecular function
Name | Definition |
---|---|
2'-deoxyguanosine DNA ADP-ribosyltransferase activity | Catalysis of the transfer of the ADP-ribose group of NAD+ to the amino group at N2 of 2'-deoxyguanosine to yield N2-(alpha-ADP-ribos-1-yl)-2'-deoxyguanosine and its beta form. |
DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
nucleotidyltransferase activity | Catalysis of the transfer of a nucleotidyl group to a reactant. |
2 GO annotations of biological process
Name | Definition |
---|---|
apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
DNA ADP-ribosylation | The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MADRQPYMTN | GIQAAVVEWI | RALDLEIISL | LLSRAWPMAL | LATSELRWRP | TVLTDTDNVV |
70 | 80 | 90 | 100 | 110 | 120 |
RLDRRQRLVR | WDRRPPNEIF | LDGFVPIVTR | ENPDWEETDL | YGFAKNNHPS | IFVSTTKTQR |
130 | 140 | 150 | 160 | 170 | 180 |
NKKKYVWTPR | NANRGIVYQY | EIYAPGGVDV | NDSFSDASPW | PNQMEVAFPG | GIQNIYIRSA |
190 | 200 | 210 | 220 | 230 | 240 |
RELHNGRIQR | IWINPNFLDP | GDLEPIVSSS | RTPQVIWRMN | HPDGGHRDQR | SERSASSYDD |
250 | 260 | 270 | 280 | 290 | 300 |
LMYGGTGNVQ | EDTFGDEPNN | PKPIAAGEFM | IESIKDKNSF | LDLSKNVNGG | VIHSNLYSGG |
310 | 320 | 330 | 340 | 350 | 360 |
DNQIWVFSYD | DNKKAYRIQS | YQNSYLYLSW | DSNASSKEMI | LRGYTNSGSN | NQYWQIEQTG |
370 | 380 | 390 | 400 | 410 | 420 |
KNYRLRNLLN | LDMIITAQDK | PSAFGGKEVI | VNTEISNSNT | KISQEWKMIP | FDFRPIIDGD |
430 | 440 | 450 | 460 | 470 | 480 |
YNIFNVDLSN | QVVDFSNQPD | LLVHGHIFCD | NENQTWHFTY | NSTYHAYKIW | SGRKSNLLLT |
490 | 500 | 510 | 520 | 530 | 540 |
WDSNAASKEM | VVRAYTESRS | KNQYWRIEQT | GSKSYKVRNL | ENSSMILGLT | RVSTPYGGLN |
550 | 560 | 570 | 580 | 590 | 600 |
LMVEDDSDGH | SDLHSDWDIK | PIFYQDIPDG | DYNIFNDNFP | NIAIDFTNQE | GSLIHGHNFC |
610 | 620 | 630 | 640 | 650 | 660 |
SNNNQKWSFV | FDGKRKAYRI | KSGVRSNLWL | SWDSNASSKE | MVLRAYTESG | SSNQYWRLDE |
670 | 680 | 690 | 700 | 710 | 720 |
ANDGSYRIRN | LQDYYKLIAL | TNKNTPYGGK | ELIVSDNKES | GNTWYLKKLG | EVPLPNRKFR |
730 | 740 | 750 | 760 | 770 | 780 |
IATKLNYKKV | IDSSTSYNLI | ITHDLNFASS | IWELVYDSSK | KAYNIYSSDI | NNLGWIYQNK |
790 | 800 | 810 | 820 | 830 | 840 |
NFFVKLGNID | GPDHGDLRYF | WTIEYSMQTG | CYLIRSLHDP | ANAVGYTDSE | SVITDTSTYS |
DNQLFHFILM |