| Entry |
|
|---|
| Name |
NAD+ ADP-ribosyltransferase;
poly(ADP-ribose) synthase;
ADP-ribosyltransferase (polymerizing);
NAD ADP-ribosyltransferase;
PARP;
PARP-1;
NAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor
ADP-D-ribosyl-transferase (incorrect);
NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor
ADP-D-ribosyl-transferase |
|---|
| Class |
Transferases;
Glycosyltransferases;
Pentosyltransferases
 |
|---|
| Sysname |
NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase |
|---|
| Reaction(IUBMB) |
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide +
(ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176] |
|---|
| Reaction(KEGG) |
R04176
 |
|---|
| Substrate |
NAD+ [CPD:C00003];
(ADP-D-ribosyl)n-acceptor [CPD:C03245] |
|---|
| Product |
nicotinamide [CPD:C00153];
(ADP-D-ribosyl)n+1-acceptor [CPD:C03245];
H+ [CPD:C00080] |
|---|
| Comment |
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor
carboxy group on a histone or the enzyme itself, 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. |
|---|
| Orthology |
K10798 poly [ADP-ribose] polymerase
K10799 tankyrase |
|---|
| Genes |
HSA: 10038(PARP2) 10039(PARP3) 142(PARP1) 143(PARP4) 80351(TNKS2)
8658(TNKS)
PTR: 452486(PARP4) 460409(PARP3) 463982(TNKS) 465197(PARP2)
MCC: 698806(PARP1) 699004(TNKS) 699294(PARP3) 701955(PARP2) 717978
MMU: 11545(Parp1) 11546(Parp2) 21951(Tnks) 235587(Parp3)
328417(Parp4) 74493(Tnks2)
RNO: 25591(Parp1) 290027(Parp2) 300985(Parp3) 309512(Tnks2)
CFA: 475392(PARP2) 475603(TNKS) 477348(PARP4) 477767(TNKS2)
484745(PARP3) 490385(PARP1)
BTA: 286764(PARP1) 533901(TNKS2) 535030(TNKS) 615359(PARP4)
SSC: 100154520(TNKS2) 100157513
ECB: 100053202(PARP4) 100058499 100058523 100060729 100061968(TNKS2)
100072572(PARP2)
MDO: 100019495 100024392(TNKS2) 100029480 100031207
OAA: 100077716 100082297 100092246
GGA: 374252(TNKS) 374253(TNKS2) 396199(PARP1) 418958(PARP4)
TGU: 100223095 100226670 100227818
XLA: 397928(parp1) 446370(parp2) 495279(tnks2) 496154(parp3)
XTR: 100145803(parp3) 549762(tnks2)
DRE: 100007906 335495(parp3) 559022(tnks) 560788(parp1)
567533(wu:fe02c12)
BFO: BRAFLDRAFT_125321 BRAFLDRAFT_203655 BRAFLDRAFT_73983
CIN: 100178364 100179282
SPU: 575677 579954 581348 584303 752216 757518 763210
DME: Dmel_CG40411(Parp) Dmel_CG4719(tankyrase)
DPO: Dpse_GA18382 Dpse_GA25584
DAN: Dana_GF18240
DER: Dere_GG12231
DPE: Dper_GL12354 Dper_GL22305
DSE: Dsec_GM10230
DSI: Dsim_GD18183
DWI: Dwil_GK14355 Dwil_GK14394
DYA: Dyak_GE10679 Dyak_GE20224
DGR: Dgri_GH18604 Dgri_GH22365
DMO: Dmoj_GI10353 Dmoj_GI23619
DVI: Dvir_GJ10205 Dvir_GJ11149
AGA: AgaP_AGAP001947 AgaP_AGAP003230
AAG: AaeL_AAEL003391 AaeL_AAEL011815
CQU: CpipJ_CPIJ012304 CpipJ_CPIJ017909
AME: 413032(tankyrase) 552095(Parp)
NVI: 100121205(Parp) 100124046(NV10936)
TCA: 655924(Parp) 655990
API: 100158994(ACYPI000408) 100165409(ACYPI006362)
PHU: Phum_PHUM420090 Phum_PHUM498090
ISC: IscW_ISCW001797 IscW_ISCW017128 IscW_ISCW019519
CEL: E02H1.4(pme-2) Y71F9AL.18(pme-1)
CBR: CBG00959(Cbr-pme-2) CBG04221(Cbr-pme-1)
BMY: Bm1_07920 Bm1_32600 Bm1_50905
SMM: Smp_128950 Smp_129260 Smp_145810.1
NVE: NEMVE_v1g161451 NEMVE_v1g88355 NEMVE_v1g88877
HMG: 100201709 100207492 100214803
TAD: TRIADDRAFT_19562 TRIADDRAFT_23639 TRIADDRAFT_32651
TRIADDRAFT_61586
ATH: AT2G31320(PARP2) AT4G02390(APP)
POP: POPTR_1099156 POPTR_830081
RCU: RCOM_0993250
VVI: 100257212 100261796
OSA: 4326479(Os01g0351200) 4343013(Os07g0413700)
SBI: SORBI_02g009900 SORBI_03g013840
PPP: PHYPADRAFT_150949 PHYPADRAFT_188096
NCR: NCU08852
PAN: PODANSg151
MGR: MGG_08613(MG08613.4)
FGR: FG05924.1
ANI: AN3129.2
AFM: AFUA_5G07320
NFI: NFIA_079950
AOR: AO090003000350
ANG: An18g01170
AFV: AFLA_034670
ACT: ACLA_010570
PCS: Pc12g02720
URE: UREG_04297
PNO: SNOG_02255
TML: GSTUM_00005329001
PPL: POSPLDRAFT_103641
CCI: CC1G_04200
MBR: MONBRDRAFT_16448 MONBRDRAFT_26401 MONBRDRAFT_27847
NGR: NAEGRDRAFT_58866 NAEGRDRAFT_71853
DDI: DDB_G0278741(adprt1A) DDB_G0286613 DDB_G0292820(adprt2)
EDI: EDI_129890
TGO: TGME49_070840
TET: TTHERM_00030430 TTHERM_00726460 TTHERM_00726470 TTHERM_00823980
TTHERM_00865150
PTM: GSPATT00033128001 GSPATT00036444001
TBR: Tb927.5.3050
TCR: 509721.60 510173.90
AZO: azo2985(tnkS)
 |
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Reference
Authors
Title
Journal
|
1 [PMID:3927821]
Ueda K, Hayaishi O.
ADP-ribosylation.
Annu. Rev. Biochem. 54 (1985) 73-100. |
|---|
Reference
Authors
Title
Journal
|
2
Ueda, K., Kawaichi, M. and Hayaishi, O.
Poly(ADP-ribose) synthetase.
In: Hayaishi, O. and Ueda, K. (Eds.), ADP-Ribosylation Reactions:
Biology and Medicine, Academic Press, London, 1982, p. 117-155. |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:2434482]
Ushiro H, Yokoyama Y, Shizuta Y.
Purification and characterization of poly (ADP-ribose) synthetase
from human placenta.
J. Biol. Chem. 262 (1987) 2352-7.
Homo sapiens [GN:hsa] |
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| Other DBs |
ExplorEnz - The Enzyme Database: 2.4.2.30
IUBMB Enzyme Nomenclature: 2.4.2.30
ExPASy - ENZYME nomenclature database: 2.4.2.30
BRENDA, the Enzyme Database: 2.4.2.30
CAS: 58319-92-9 |
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