Overview
| Uniprot ID | Q9UGN5 |
|---|
| Protein Name | Poly [ADP-ribose] polymerase 2 |
|---|
| Gene Name | PARP2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 84 |
KRVSESVKALLLKGK |
Function
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231, PubMed:25043379, PubMed:27471034, PubMed:30104678, PubMed:32028527, PubMed:32939087, PubMed:34108479, PubMed:34486521, PubMed:34874266). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:25043379, PubMed:30104678, PubMed:30321391). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:32939087). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed:25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (PubMed:28190768, PubMed:32028527, PubMed:34108479, PubMed:34486521, PubMed:34874266). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:10364231, PubMed:32939087, PubMed:34108479). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed:34732825, PubMed:34795260). Specifically mediates formation of branched poly-ADP-ribosylation (PubMed:30104678). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (PubMed:30104678). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (PubMed:27471034, PubMed:29361132)
Protein Sequence
10
MAARRRRSTG
20
GGRARALNES
30
KRVNNGNTAP
40
EDSSPAKKTR
50
RCQRQESKKM
60
PVAGGKANKD
70
RTEDKQDGMP
80
GRSWASKRVS
90
ESVKALLLKG
100
KAPVDPECTA
110
KVGKAHVYCE
120
GNDVYDVMLN
130
QTNLQFNNNK
140
YYLIQLLEDD
150
AQRNFSVWMR
160
WGRVGKMGQH
170
SLVACSGNLN
180
KAKEIFQKKF
190
LDKTKNNWED
200
REKFEKVPGK
210
YDMLQMDYAT
220
NTQDEEETKK
230
EESLKSPLKP
240
ESQLDLRVQE
250
LIKLICNVQA
260
MEEMMMEMKY
270
NTKKAPLGKL
280
TVAQIKAGYQ
290
SLKKIEDCIR
300
AGQHGRALME
310
ACNEFYTRIP
320
HDFGLRTPPL
330
IRTQKELSEK
340
IQLLEALGDI
350
EIAIKLVKTE
360
LQSPEHPLDQ
370
HYRNLHCALR
380
PLDHESYEFK
390
VISQYLQSTH
400
APTHSDYTMT
410
LLDLFEVEKD
420
GEKEAFREDL
430
HNRMLLWHGS
440
RMSNWVGILS
450
HGLRIAPPEA
460
PITGYMFGKG
470
IYFADMSSKS
480
ANYCFASRLK
490
NTGLLLLSEV
500
ALGQCNELLE
510
ANPKAEGLLQ
520
GKHSTKGLGK
530
MAPSSAHFVT
540
LNGSTVPLGP
550
ASDTGILNPD
560
GYTLNYNEYI
570
VYNPNQVRMR
580
YLLKVQFNFL
QLW
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0090734 |
site of DNA damage |
| Molecular Function |
GO:0003682 |
chromatin binding |
| Molecular Function |
GO:0003684 |
damaged DNA binding |
| Molecular Function |
GO:0140294 |
NAD DNA ADP-ribosyltransferase activity |
| Molecular Function |
GO:0003950 |
NAD+ poly-ADP-ribosyltransferase activity |
| Molecular Function |
GO:1990404 |
NAD+-protein mono-ADP-ribosyltransferase activity |
| Molecular Function |
GO:0140806 |
NAD+-protein-aspartate ADP-ribosyltransferase activity |
| Molecular Function |
GO:0140807 |
NAD+-protein-glutamate ADP-ribosyltransferase activity |
| Molecular Function |
GO:0140805 |
NAD+-protein-serine ADP-ribosyltransferase activity |
| Molecular Function |
GO:0031491 |
nucleosome binding |
| Molecular Function |
GO:0016779 |
nucleotidyltransferase activity |
| Molecular Function |
GO:0072572 |
poly-ADP-D-ribose binding |
| Molecular Function |
GO:0160004 |
poly-ADP-D-ribose modification-dependent protein binding |
| Biological Process |
GO:0046697 |
decidualization |
| Biological Process |
GO:0030592 |
DNA ADP-ribosylation |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0140861 |
DNA repair-dependent chromatin remodeling |
| Biological Process |
GO:0006302 |
double-strand break repair |
| Biological Process |
GO:0070213 |
protein auto-ADP-ribosylation |
| Biological Process |
GO:0070212 |
protein poly-ADP-ribosylation |
Reference
PMID: N/A