Reviewed, UniProtKB/Swiss-Prot Q9UGN5 (PARP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Poly [ADP-ribose] polymerase 2
      Short name=PARP-2
      Short name=hPARP-2
    EC=2.4.2.30
Alternative name(s):
    NAD(+) ADP-ribosyltransferase 2
      Short name=ADPRT-2
    Poly[ADP-ribose] synthetase 2
      Short name=pADPRT-2

Gene names

Name:	PARP2
Synonyms:	ADPRT2, ADPRTL2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	583 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subunit structure	Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LIG3. Homo- and heterodimer with PARP1.
Subcellular location	Nucleus.
Tissue specificity	Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus.
Post-translational modification	Poly-ADP-ribosylated by PARP1 By similarity.
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.
Sequence caution	The sequence AAL77437.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding NAD
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid ADP-ribosylation Traceable author statement. Source: ProtInc
Cellular component	nucleolus Inferred from direct assay. Source: MGI nucleoplasm Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UGN5-1)

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.

Isoform 2 (identifier: Q9UGN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-80: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 583	583	Poly [ADP-ribose] polymerase 2		PRO_0000211327
Regions
	Domain	231 – 348	118	PARP alpha-helical
	Domain	356 – 583	228	PARP catalytic
	DNA binding	1 – 88	88	Potential
	Motif	4 – 7	4	Nuclear localization signal Potential
	Motif	35 – 40	6	Nuclear localization signal Potential
Natural variations
	Alternative sequence	68 – 80	13	Missing in isoform 2.		VSP_004537
	Natural variant	161	1	S → N: dbSNP rs3093905. Ref.5		VAR_019174
	Natural variant	168	1	N → S: dbSNP rs3093906. Ref.5		VAR_019175
	Natural variant	235	1	D → G: dbSNP rs3093921. Ref.5		VAR_019176
	Natural variant	285	1	I → V: dbSNP rs3093925. Ref.5		VAR_019177
	Natural variant	296	1	R → Q: dbSNP rs3093926. Ref.5		VAR_019178
	Natural variant	331	1	I → T: dbSNP rs2275010.		VAR_050462
Experimental info
	Sequence conflict	447	1	P → H in AAD29857. Ref.2
	Sequence conflict	481	1	N → H in BAA92017. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 5B7AE8AE531836AF	FASTA	583	66,206
	10 20 30 40 50 60 MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD 70 80 90 100 110 120 RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA KVGKAHVYCE GNDVYDVMLN 130 140 150 160 170 180 QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKMGQH SLVACSGNLN KAKEIFQKKF 190 200 210 220 230 240 LDKTKNNWED REKFEKVPGK YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE 250 260 270 280 290 300 LIKLICNVQA MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME 310 320 330 340 350 360 ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE LQSPEHPLDQ 370 380 390 400 410 420 HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT LLDLFEVEKD GEKEAFREDL 430 440 450 460 470 480 HNRMLLWHGS RMSNWVGILS HGLRIAPPEA PITGYMFGKG IYFADMSSKS ANYCFASRLK 490 500 510 520 530 540 NTGLLLLSEV ALGQCNELLE ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP 550 560 570 580 ASDTGILNPD GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW
	Isoform 2. Checksum: 335A5B64E758FDFF	FASTA	570	64,805
	10 20 30 40 50 60 MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD 70 80 90 100 110 120 RTEDKQDESV KALLLKGKAP VDPECTAKVG KAHVYCEGND VYDVMLNQTN LQFNNNKYYL 130 140 150 160 170 180 IQLLEDDAQR NFSVWMRWGR VGKMGQHSLV ACSGNLNKAK EIFQKKFLDK TKNNWEDREK 190 200 210 220 230 240 FEKVPGKYDM LQMDYATNTQ DEEETKKEES LKSPLKPESQ LDLRVQELIK LICNVQAMEE 250 260 270 280 290 300 MMMEMKYNTK KAPLGKLTVA QIKAGYQSLK KIEDCIRAGQ HGRALMEACN EFYTRIPHDF 310 320 330 340 350 360 GLRTPPLIRT QKELSEKIQL LEALGDIEIA IKLVKTELQS PEHPLDQHYR NLHCALRPLD 370 380 390 400 410 420 HESYEFKVIS QYLQSTHAPT HSDYTMTLLD LFEVEKDGEK EAFREDLHNR MLLWHGSRMS 430 440 450 460 470 480 NWVGILSHGL RIAPPEAPIT GYMFGKGIYF ADMSSKSANY CFASRLKNTG LLLLSEVALG 490 500 510 520 530 540 QCNELLEANP KAEGLLQGKH STKGLGKMAP SSAHFVTLNG STVPLGPASD TGILNPDGYT 550 560 570 LNYNEYIVYN PNQVRMRYLL KVQFNFLQLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase." Ame J.-C., Rolli V., Schreiber V., Niedergang C., Apiou F., Decker P., Muller S., Hoeger T., Menissier-de Murcia J., de Murcia G.M. J. Biol. Chem. 274:17860-17868(1999) [PubMed: 10364231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Fetal brain.
[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: 10329013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-583 (ISOFORM 1). Tissue: Fetal brain.
[3]	"pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans." Berghammer H., Ebner M., Marksteiner R., Auer B. FEBS Lett. 449:259-263(1999) [PubMed: 10338144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-583 (ISOFORM 1). Tissue: Fibroblast.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[5]	NIEHS SNPs program Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-161; SER-168; GLY-235; VAL-285 AND GLN-296.
[6]	"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1." Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M. J. Biol. Chem. 277:23028-23036(2002) [PubMed: 11948190] [Abstract] Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LIG3.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ236912 mRNA. Translation: CAB65088.1.
AF085734 mRNA. Translation: AAD29857.1. Different initiation.
AJ236876 mRNA. Translation: CAB41505.2. Different initiation.
AK001980 mRNA. Translation: BAA92017.1. Different termination.
AF479321 Genomic DNA. Translation: AAL77437.1. Sequence problems.

IPI

IPI00026497.
IPI00220995.

RefSeq

NP_001036083.1.
NP_005475.2.

UniGene

Hs.409412

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KCZ	X-ray	2.00	A/B	235-579	[»]
3KJD	X-ray	1.95	A/B	235-579	[»]

SMR

Q9UGN5. Positions 79-209.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UGN5.

PTM databases

PhosphoSite

Q9UGN5.

Proteomic databases

PRIDE

Q9UGN5.

Genome annotation databases

Ensembl

ENST00000250416; ENSP00000250416; ENSG00000129484; Homo sapiens. [Genome view]

GeneID

10038.

KEGG

hsa:10038.

UCSC

uc001vxb.1. human.
uc001vxd.1. human.

Organism-specific databases

CTD

10038.

GeneCards

GC14P019881.

HGNC

HGNC:272. PARP2.

MIM

607725. gene.

PharmGKB

PA24592.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05958.

HOGENOM

HBG713287.

HOVERGEN

Q9UGN5.

InParanoid

Q9UGN5.

OMA

CALHPLD.

OrthoDB

EOG9K3PG4.

PhylomeDB

Q9UGN5.

Enzyme and pathway databases

BRENDA

2.4.2.30. 247.

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

Q9UGN5.

Bgee

Q9UGN5.

CleanEx

HS_PARP2.

Genevestigator

Q9UGN5.

GermOnline

ENSG00000129484. Homo sapiens.

Family and domain databases

InterPro

IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR.
[Graphical view]

Gene3D

G3DSA:1.20.142.10. PARP_reg. 1 hit.

Pfam

PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]

SMART

SM00773. WGR. 1 hit.
[Graphical view]

PROSITE

PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

37907.

SOURCE

Search...

Entry information

Entry name

PARP2_HUMAN

Accession

Primary (citable) accession number: Q9UGN5
Secondary accession number(s): Q8TEU4 , Q9NUV2, Q9UMR4, Q9Y6C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.