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Q9Y6F1

- PARP3_HUMAN

UniProt

Q9Y6F1 - PARP3_HUMAN

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Protein

Poly [ADP-ribose] polymerase 3

Gene

PARP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.1 Publication

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

GO - Molecular functioni

  1. catalytic activity Source: ProtInc
  2. NAD+ ADP-ribosyltransferase activity Source: MGI

GO - Biological processi

  1. DNA repair Source: ProtInc
  2. double-strand break repair Source: MGI
  3. positive regulation of DNA ligation Source: MGI
  4. protein ADP-ribosylation Source: MGI
  5. protein localization to site of double-strand break Source: MGI
  6. regulation of mitotic spindle organization Source: MGI
  7. telomere maintenance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.
SignaLinkiQ9Y6F1.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 3 (EC:2.4.2.30)
Short name:
PARP-3
Short name:
hPARP-3
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 3
Short name:
ARTD3
IRT1
NAD(+) ADP-ribosyltransferase 3
Short name:
ADPRT-3
Poly[ADP-ribose] synthase 3
Short name:
pADPRT-3
Gene namesi
Name:PARP3
Synonyms:ADPRT3, ADPRTL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:273. PARP3.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
Note: Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According to PubMed:16924674, it is almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
  4. site of double-strand break Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Poly [ADP-ribose] polymerase 3PRO_0000211329Add
BLAST

Post-translational modificationi

Auto-poly(ADP)-ribosylation.

Proteomic databases

MaxQBiQ9Y6F1.
PaxDbiQ9Y6F1.
PRIDEiQ9Y6F1.

PTM databases

PhosphoSiteiQ9Y6F1.

Expressioni

Tissue specificityi

Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.

Gene expression databases

BgeeiQ9Y6F1.
CleanExiHS_PARP3.
ExpressionAtlasiQ9Y6F1. baseline and differential.
GenevestigatoriQ9Y6F1.

Interactioni

Subunit structurei

Interacts with PRKDC and PARP1. Interacts with XRCC5; the interaction is dependent on nucleic acids. Interacts with XRCC6; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4.2 Publications

Protein-protein interaction databases

BioGridi115351. 10 interactions.
STRINGi9606.ENSP00000381740.

Structurei

Secondary structure

1
533
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 534
Turni54 – 563
Beta strandi61 – 7414
Turni75 – 784
Beta strandi79 – 8911
Beta strandi95 – 1006
Beta strandi111 – 1177
Helixi118 – 13316
Helixi140 – 1423
Beta strandi147 – 1493
Beta strandi151 – 1533
Helixi187 – 19610
Helixi199 – 20810
Turni213 – 2153
Turni218 – 2203
Helixi223 – 24018
Beta strandi246 – 2483
Helixi250 – 26011
Beta strandi265 – 2684
Helixi276 – 29823
Helixi303 – 3075
Beta strandi309 – 3113
Helixi314 – 3218
Beta strandi325 – 3284
Helixi336 – 34611
Beta strandi349 – 3513
Beta strandi354 – 3629
Turni364 – 3663
Helixi367 – 3715
Turni372 – 3754
Beta strandi379 – 3857
Helixi388 – 3903
Helixi391 – 3977
Beta strandi411 – 4188
Helixi419 – 4235
Beta strandi429 – 4313
Beta strandi434 – 44512
Beta strandi448 – 4547
Beta strandi467 – 4715
Beta strandi473 – 4775
Helixi479 – 4813
Beta strandi483 – 4875
Beta strandi490 – 4945
Beta strandi499 – 5013
Helixi503 – 5053
Beta strandi509 – 5124
Beta strandi514 – 5196
Helixi520 – 5223
Beta strandi523 – 53210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EOCNMR-A41-157[»]
3C49X-ray2.80A178-532[»]
3C4HX-ray2.10A178-532[»]
3CE0X-ray2.80A178-532[»]
3FHBX-ray2.30A178-532[»]
4GV0X-ray1.90A178-532[»]
4GV2X-ray1.80A178-532[»]
4GV4X-ray1.80A178-532[»]
4L6ZX-ray2.00A178-532[»]
4L70X-ray2.00A178-532[»]
4L7LX-ray2.10A178-532[»]
4L7NX-ray1.80A178-532[»]
4L7OX-ray2.00A178-532[»]
4L7PX-ray2.30A178-532[»]
4L7RX-ray2.20A178-532[»]
4L7UX-ray2.80A178-532[»]
ProteinModelPortaliQ9Y6F1.
SMRiQ9Y6F1. Positions 41-157, 178-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6F1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini182 – 300119PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini313 – 533221PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 207Nuclear localization signalSequence Analysis

Domaini

According to PubMed:10329013, the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.

Sequence similaritiesi

Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG243963.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiQ9Y6F1.
KOiK10798.
OMAiFSKEMFK.
OrthoDBiEOG7RV9G0.
PhylomeDBiQ9Y6F1.
TreeFamiTF315407.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTiSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6F1-1) [UniParc]FASTAAdd to Basket

Also known as: Short

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP
60 70 80 90 100
TCPLSSNPGT QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNH
110 120 130 140 150
WGRVGEVGQS KINHFTRLED AKKDFEKKFR EKTKNNWAER DHFVSHPGKY
160 170 180 190 200
TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV QPCSLDPATQ KLITNIFSKE
210 220 230 240 250
MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL KGPTDGGQSL
260 270 280 290 300
EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
310 320 330 340 350
VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH
360 370 380 390 400
RCPTLQHIWK VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR
410 420 430 440 450
IMPHSGGRVG KGIYFASENS KSAGYVIGMK CGAHHVGYMF LGEVALGREH
460 470 480 490 500
HINTDNPSLK SPPPGFDSVI ARGHTEPDPT QDTELELDGQ QVVVPQGQPV
510 520 530
PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL

Note: More abundant according to PubMed:16924674.

Length:533
Mass (Da):60,070
Last modified:March 3, 2009 - v3
Checksum:iBF728C3D88722029
GO
Isoform 2 (identifier: Q9Y6F1-2) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSLLFLAM

Show »
Length:540
Mass (Da):60,846
Checksum:iAF68D80A50A78BC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801N → K in AAD29855. (PubMed:10329013)Curated
Sequence conflicti171 – 1711G → A in AAD29855. (PubMed:10329013)Curated
Sequence conflicti411 – 4111K → E in CAB43246. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911S → N.
Corresponds to variant rs34224216 [ dbSNP | Ensembl ].
VAR_056643
Natural varianti100 – 1001H → R.5 Publications
Corresponds to variant rs28547534 [ dbSNP | Ensembl ].
VAR_054622
Natural varianti269 – 2691Q → R.
Corresponds to variant rs323870 [ dbSNP | Ensembl ].
VAR_056644

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSLLFLAM in isoform 2. 2 PublicationsVSP_007863

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y16836 mRNA. Translation: CAC79988.1.
AF083068 mRNA. Translation: AAD29855.1.
AY126341 mRNA. Translation: AAM95460.1.
AC115284 Genomic DNA. No translation available.
BC014260 mRNA. Translation: AAH14260.1.
AL050034 mRNA. Translation: CAB43246.1.
CCDSiCCDS43097.1. [Q9Y6F1-1]
CCDS46839.1. [Q9Y6F1-2]
PIRiT08713.
RefSeqiNP_001003931.2. NM_001003931.2. [Q9Y6F1-2]
NP_005476.3. NM_005485.4. [Q9Y6F1-1]
XP_005264836.2. XM_005264779.2.
XP_006712977.1. XM_006712914.1.
UniGeneiHs.271742.

Genome annotation databases

EnsembliENST00000398755; ENSP00000381740; ENSG00000041880.
GeneIDi10039.
KEGGihsa:10039.
UCSCiuc003dby.3. human. [Q9Y6F1-1]
uc003dbz.3. human. [Q9Y6F1-2]

Polymorphism databases

DMDMi224471880.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y16836 mRNA. Translation: CAC79988.1 .
AF083068 mRNA. Translation: AAD29855.1 .
AY126341 mRNA. Translation: AAM95460.1 .
AC115284 Genomic DNA. No translation available.
BC014260 mRNA. Translation: AAH14260.1 .
AL050034 mRNA. Translation: CAB43246.1 .
CCDSi CCDS43097.1. [Q9Y6F1-1 ]
CCDS46839.1. [Q9Y6F1-2 ]
PIRi T08713.
RefSeqi NP_001003931.2. NM_001003931.2. [Q9Y6F1-2 ]
NP_005476.3. NM_005485.4. [Q9Y6F1-1 ]
XP_005264836.2. XM_005264779.2.
XP_006712977.1. XM_006712914.1.
UniGenei Hs.271742.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EOC NMR - A 41-157 [» ]
3C49 X-ray 2.80 A 178-532 [» ]
3C4H X-ray 2.10 A 178-532 [» ]
3CE0 X-ray 2.80 A 178-532 [» ]
3FHB X-ray 2.30 A 178-532 [» ]
4GV0 X-ray 1.90 A 178-532 [» ]
4GV2 X-ray 1.80 A 178-532 [» ]
4GV4 X-ray 1.80 A 178-532 [» ]
4L6Z X-ray 2.00 A 178-532 [» ]
4L70 X-ray 2.00 A 178-532 [» ]
4L7L X-ray 2.10 A 178-532 [» ]
4L7N X-ray 1.80 A 178-532 [» ]
4L7O X-ray 2.00 A 178-532 [» ]
4L7P X-ray 2.30 A 178-532 [» ]
4L7R X-ray 2.20 A 178-532 [» ]
4L7U X-ray 2.80 A 178-532 [» ]
ProteinModelPortali Q9Y6F1.
SMRi Q9Y6F1. Positions 41-157, 178-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115351. 10 interactions.
STRINGi 9606.ENSP00000381740.

Chemistry

BindingDBi Q9Y6F1.
ChEMBLi CHEMBL5083.

PTM databases

PhosphoSitei Q9Y6F1.

Polymorphism databases

DMDMi 224471880.

Proteomic databases

MaxQBi Q9Y6F1.
PaxDbi Q9Y6F1.
PRIDEi Q9Y6F1.

Protocols and materials databases

DNASUi 10039.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398755 ; ENSP00000381740 ; ENSG00000041880 .
GeneIDi 10039.
KEGGi hsa:10039.
UCSCi uc003dby.3. human. [Q9Y6F1-1 ]
uc003dbz.3. human. [Q9Y6F1-2 ]

Organism-specific databases

CTDi 10039.
GeneCardsi GC03P051951.
HGNCi HGNC:273. PARP3.
MIMi 607726. gene.
neXtProti NX_Q9Y6F1.
PharmGKBi PA24593.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243963.
GeneTreei ENSGT00390000017341.
HOGENOMi HOG000173055.
HOVERGENi HBG053514.
InParanoidi Q9Y6F1.
KOi K10798.
OMAi FSKEMFK.
OrthoDBi EOG7RV9G0.
PhylomeDBi Q9Y6F1.
TreeFami TF315407.

Enzyme and pathway databases

BRENDAi 2.4.2.30. 2681.
SignaLinki Q9Y6F1.

Miscellaneous databases

EvolutionaryTracei Q9Y6F1.
GeneWikii PARP3.
GenomeRNAii 10039.
NextBioi 37913.
PROi Q9Y6F1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6F1.
CleanExi HS_PARP3.
ExpressionAtlasi Q9Y6F1. baseline and differential.
Genevestigatori Q9Y6F1.

Family and domain databases

Gene3Di 1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view ]
Pfami PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view ]
SMARTi SM00773. WGR. 1 hit.
[Graphical view ]
SUPFAMi SSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEi PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Koch-Nolte F.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100.
  2. "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues."
    Johansson M.
    Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-100.
    Tissue: Fetal brain.
  3. "PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression."
    Augustin A., Spenlehauer C., Dumond H., Menissier-de Murcia J., Piel M., Schmit A.-C., Apiou F., Vonesch J.-L., Kock M., Bornens M., de Murcia G.M.
    J. Cell Sci. 116:1551-1562(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100, SUBCELLULAR LOCATION.
    Tissue: Frontal cortex.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-100.
    Tissue: B-cell.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1), VARIANT ARG-100.
    Tissue: Kidney.
  7. "PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery."
    Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A., Hunter J.M., Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.
    J. Cell. Biochem. 100:385-401(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKDC; PARP1; EZH2; HDAC1; HDAC2; SUZ12; YY1; LRIG3 AND LIG4.
  8. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
    Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
    Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  9. "Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor 3-aminobenzoic acid."
    Structural genomics consortium (SGC)
    Submitted (APR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE INHIBITOR 3-AMINOBENZOIC ACID.
  10. "Solution structure of the WGR domain from human poly [ADP-ribose] polymerase-3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 41-157.

Entry informationi

Entry nameiPARP3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6F1
Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 3, 2009
Last modified: October 29, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3