HPF1_HUMAN
ID HPF1_HUMAN Reviewed; 346 AA.
AC Q9NWY4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histone PARylation factor 1 {ECO:0000303|PubMed:27067600};
GN Name=HPF1 {ECO:0000303|PubMed:27067600, ECO:0000312|HGNC:HGNC:26051};
GN Synonyms=C4orf27 {ECO:0000303|PubMed:27067600,
GN ECO:0000312|HGNC:HGNC:26051};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-174.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-174.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-174.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186 AND LYS-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP1; PARP2; HISTONE H2A
RP AND HISTONE H3, AND MUTAGENESIS OF 238-TYR-ARG-239.
RX PubMed=27067600; DOI=10.1016/j.molcel.2016.03.008;
RA Gibbs-Seymour I., Fontana P., Rack J.G., Ahel I.;
RT "HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-
RT ribosylation activity.";
RL Mol. Cell 62:432-442(2016).
RN [9]
RP FUNCTION, INTERACTION WITH PARP1 AND PARP2, AND MUTAGENESIS OF
RP 238-TYR-ARG-239.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [10]
RP FUNCTION, ADP-RIBOSYLATION AT SER-97 AND TYR-238, AND MUTAGENESIS OF
RP ARG-239.
RX PubMed=30257210; DOI=10.1016/j.celrep.2018.08.092;
RA Bartlett E., Bonfiglio J.J., Prokhorova E., Colby T., Zobel F., Ahel I.,
RA Matic I.;
RT "Interplay of histone marks with serine ADP-ribosylation.";
RL Cell Rep. 24:3488-3502(2018).
RN [11]
RP FUNCTION.
RX PubMed=29480802; DOI=10.7554/elife.34334;
RA Palazzo L., Leidecker O., Prokhorova E., Dauben H., Matic I., Ahel I.;
RT "Serine is the major residue for ADP-ribosylation upon DNA damage.";
RL Elife 7:0-0(2018).
RN [12]
RP FUNCTION, AND ADP-RIBOSYLATION AT TYR-238.
RX PubMed=29954836; DOI=10.15252/embr.201745310;
RA Leslie Pedrioli D.M., Leutert M., Bilan V., Nowak K., Gunasekera K.,
RA Ferrari E., Imhof R., Malmstroem L., Hottiger M.O.;
RT "Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose
RT acceptor site.";
RL EMBO Rep. 19:0-0(2018).
RN [13]
RP FUNCTION.
RX PubMed=33186521; DOI=10.1016/j.cell.2020.09.055;
RA Bonfiglio J.J., Leidecker O., Dauben H., Longarini E.J., Colby T.,
RA San Segundo-Acosta P., Perez K.A., Matic I.;
RT "An HPF1/PARP1-based chemical biology strategy for exploring ADP-
RT ribosylation.";
RL Cell 183:1086-1102(2020).
RN [14]
RP INTERACTION WITH PARP2.
RX PubMed=33141820; DOI=10.1371/journal.pone.0240932;
RA Gaullier G., Roberts G., Muthurajan U.M., Bowerman S., Rudolph J.,
RA Mahadevan J., Jha A., Rae P.S., Luger K.;
RT "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances
RT its interaction with HPF1.";
RL PLoS ONE 15:e0240932-e0240932(2020).
RN [15] {ECO:0007744|PDB:6TX2, ECO:0007744|PDB:6TX3}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 37-346 IN COMPLEX WITH PARP2 AND
RP NUCLEOSOME CORE COMPLEX, FUNCTION, ACTIVE SITE, INTERACTION WITH PARP1 AND
RP PARP2, AND MUTAGENESIS OF ARG-239; GLU-243; ASP-283; GLU-284 AND ASP-286.
RX PubMed=32028527; DOI=10.1038/s41586-020-2013-6;
RA Suskiewicz M.J., Zobel F., Ogden T.E.H., Fontana P., Ariza A., Yang J.C.,
RA Zhu K., Bracken L., Hawthorne W.J., Ahel D., Neuhaus D., Ahel I.;
RT "HPF1 completes the PARP active site for DNA damage-induced ADP-
RT ribosylation.";
RL Nature 579:598-602(2020).
RN [16] {ECO:0007744|PDB:6X0L, ECO:0007744|PDB:6X0M, ECO:0007744|PDB:6X0N}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH PARP2 AND
RP NUCLEOSOME CORE COMPLEX, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH
RP PARP2, AND MUTAGENESIS OF 149-LYS-LYS-150 AND 179-LYS--LYS-181.
RX PubMed=32939087; DOI=10.1038/s41586-020-2725-7;
RA Bilokapic S., Suskiewicz M.J., Ahel I., Halic M.;
RT "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.";
RL Nature 585:609-613(2020).
CC -!- FUNCTION: Cofactor for serine ADP-ribosylation that confers serine
CC specificity on PARP1 and PARP2 and plays a key role in DNA damage
CC response (PubMed:28190768, PubMed:29480802, PubMed:29954836,
CC PubMed:33186521, PubMed:32028527, PubMed:32939087). Initiates the
CC repair of double-strand DNA breaks: recruited to DNA damage sites by
CC PARP1 and PARP2 and switches the amino acid specificity of PARP1 and
CC PARP2 from aspartate or glutamate to serine residues, licensing serine
CC ADP-ribosylation of target proteins (PubMed:28190768, PubMed:29480802,
CC PubMed:29954836, PubMed:32028527, PubMed:32939087). Serine ADP-
CC ribosylation of target proteins, such as histones, promotes
CC decompaction of chromatin and the recruitment of repair factors leading
CC to the reparation of DNA strand breaks (PubMed:27067600,
CC PubMed:28190768, PubMed:32939087). Serine ADP-ribosylation of proteins
CC constitutes the primary form of ADP-ribosylation of proteins in
CC response to DNA damage (PubMed:29480802). HPF1 acts by completing the
CC active site of PARP1 and PARP2: forms a composite active site composed
CC of residues from HPF1 and PARP1 or PARP2 (PubMed:32028527). HPF1 also
CC promotes tyrosine ADP-ribosylation, probably by conferring tyrosine
CC specificity on PARP1 (PubMed:30257210, PubMed:29954836).
CC {ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:28190768,
CC ECO:0000269|PubMed:29480802, ECO:0000269|PubMed:29954836,
CC ECO:0000269|PubMed:30257210, ECO:0000269|PubMed:32028527,
CC ECO:0000269|PubMed:32939087, ECO:0000269|PubMed:33186521}.
CC -!- SUBUNIT: Interacts with PARP1 (via the PARP catalytic domain)
CC (PubMed:27067600, PubMed:32028527). Interacts with PARP2 (via the PARP
CC catalytic domain) (PubMed:27067600, PubMed:33141820, PubMed:32028527,
CC PubMed:32939087). Interacts with core nucleosomes in a PARP1- and
CC PARP2-dependent manner (PubMed:27067600, PubMed:32939087).
CC {ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:32028527,
CC ECO:0000269|PubMed:32939087, ECO:0000269|PubMed:33141820}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:27067600,
CC ECO:0000269|PubMed:32939087}. Nucleus {ECO:0000269|PubMed:27067600}.
CC Note=Localizes to DNA damage sites; chromatin localization is dependent
CC on PARP1 and PARP2. {ECO:0000269|PubMed:27067600,
CC ECO:0000269|PubMed:32939087}.
CC -!- SIMILARITY: Belongs to the HPF1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Catalysis - Issue 235 of
CC April 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/235/";
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DR EMBL; AL136673; CAB66608.1; -; mRNA.
DR EMBL; AK000541; BAA91241.1; -; mRNA.
DR EMBL; AC106878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010367; AAH10367.1; -; mRNA.
DR CCDS; CCDS3813.1; -.
DR RefSeq; NP_060337.2; NM_017867.2.
DR PDB; 6M3G; X-ray; 1.57 A; A=1-346.
DR PDB; 6M3I; X-ray; 1.98 A; A=1-346.
DR PDB; 6TX2; X-ray; 2.09 A; A=37-346.
DR PDB; 6TX3; X-ray; 2.96 A; A=37-346.
DR PDB; 6X0L; EM; 3.90 A; O=1-346.
DR PDB; 6X0M; EM; 6.30 A; O/o=1-346.
DR PDB; 6X0N; EM; 10.00 A; O=1-346.
DR PDBsum; 6M3G; -.
DR PDBsum; 6M3I; -.
DR PDBsum; 6TX2; -.
DR PDBsum; 6TX3; -.
DR PDBsum; 6X0L; -.
DR PDBsum; 6X0M; -.
DR PDBsum; 6X0N; -.
DR AlphaFoldDB; Q9NWY4; -.
DR SMR; Q9NWY4; -.
DR BioGRID; 120306; 37.
DR IntAct; Q9NWY4; 6.
DR MINT; Q9NWY4; -.
DR STRING; 9606.ENSP00000406598; -.
DR iPTMnet; Q9NWY4; -.
DR PhosphoSitePlus; Q9NWY4; -.
DR BioMuta; HPF1; -.
DR DMDM; 296434433; -.
DR EPD; Q9NWY4; -.
DR jPOST; Q9NWY4; -.
DR MassIVE; Q9NWY4; -.
DR MaxQB; Q9NWY4; -.
DR PaxDb; Q9NWY4; -.
DR PeptideAtlas; Q9NWY4; -.
DR PRIDE; Q9NWY4; -.
DR ProteomicsDB; 82999; -.
DR Antibodypedia; 50204; 61 antibodies from 11 providers.
DR DNASU; 54969; -.
DR Ensembl; ENST00000393381.3; ENSP00000406598.1; ENSG00000056050.7.
DR GeneID; 54969; -.
DR KEGG; hsa:54969; -.
DR MANE-Select; ENST00000393381.3; ENSP00000406598.1; NM_017867.3; NP_060337.2.
DR UCSC; uc003isl.5; human.
DR CTD; 54969; -.
DR GeneCards; HPF1; -.
DR HGNC; HGNC:26051; HPF1.
DR HPA; ENSG00000056050; Low tissue specificity.
DR MIM; 616614; gene.
DR neXtProt; NX_Q9NWY4; -.
DR OpenTargets; ENSG00000056050; -.
DR PharmGKB; PA145149735; -.
DR VEuPathDB; HostDB:ENSG00000056050; -.
DR eggNOG; KOG3952; Eukaryota.
DR GeneTree; ENSGT00390000014876; -.
DR HOGENOM; CLU_053037_0_0_1; -.
DR InParanoid; Q9NWY4; -.
DR OMA; RPQFIAI; -.
DR OrthoDB; 1077112at2759; -.
DR PhylomeDB; Q9NWY4; -.
DR TreeFam; TF317026; -.
DR PathwayCommons; Q9NWY4; -.
DR SignaLink; Q9NWY4; -.
DR BioGRID-ORCS; 54969; 13 hits in 985 CRISPR screens.
DR ChiTaRS; HPF1; human.
DR GenomeRNAi; 54969; -.
DR Pharos; Q9NWY4; Tbio.
DR PRO; PR:Q9NWY4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NWY4; protein.
DR Bgee; ENSG00000056050; Expressed in oocyte and 207 other tissues.
DR Genevisible; Q9NWY4; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0031056; P:regulation of histone modification; IDA:UniProtKB.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:UniProtKB.
DR InterPro; IPR019361; HPF1.
DR PANTHER; PTHR13386; PTHR13386; 1.
DR Pfam; PF10228; DUF2228; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; DNA damage;
KW DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..346
FT /note="Histone PARylation factor 1"
FT /id="PRO_0000294446"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..346
FT /note="Interaction with PARP1"
FT /evidence="ECO:0000269|PubMed:27067600"
FT ACT_SITE 284
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:32028527"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CFE2"
FT MOD_RES 97
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:30257210"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 238
FT /note="ADP-ribosyltyrosine"
FT /evidence="ECO:0000269|PubMed:29954836,
FT ECO:0000269|PubMed:30257210"
FT VARIANT 174
FT /note="R -> K (in dbSNP:rs1047642)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_033183"
FT VARIANT 331
FT /note="E -> D (in dbSNP:rs1047706)"
FT /id="VAR_033184"
FT MUTAGEN 149..150
FT /note="KK->EE: Abolished interaction with PARP2, leading to
FT destabilize the PARP2-nucleosome complex."
FT /evidence="ECO:0000269|PubMed:32939087"
FT MUTAGEN 179..181
FT /note="KKK->EEE: Abolished interaction with PARP2, leading
FT to destabilize the PARP2-nucleosome complex."
FT /evidence="ECO:0000269|PubMed:32939087"
FT MUTAGEN 238..239
FT /note="YR->AA: Loss of ability to bind PARP1 and histones.
FT Abolishes PARP1 ability to mediate ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:27067600,
FT ECO:0000269|PubMed:28190768"
FT MUTAGEN 239
FT /note="R->A: Strongly reduced serine ADP-ribosylation by
FT PARP1 and PARP2. Decreases PARP1 ability to mediate
FT tyrosine ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:30257210,
FT ECO:0000269|PubMed:32028527"
FT MUTAGEN 243
FT /note="E->A: Does not affect serine ADP-ribosylation by
FT PARP1 and PARP2."
FT /evidence="ECO:0000269|PubMed:32028527"
FT MUTAGEN 283
FT /note="D->A: Strongly reduced serine ADP-ribosylation by
FT PARP1 and PARP2."
FT /evidence="ECO:0000269|PubMed:32028527"
FT MUTAGEN 284
FT /note="E->A: Abolished serine ADP-ribosylation by PARP1 and
FT PARP2."
FT /evidence="ECO:0000269|PubMed:32028527"
FT MUTAGEN 286
FT /note="D->A: Strongly reduced serine ADP-ribosylation by
FT PARP1 and PARP2."
FT /evidence="ECO:0000269|PubMed:32028527"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6M3G"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6TX3"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:6M3G"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6M3G"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:6M3I"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6M3G"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6M3G"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6M3G"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6M3G"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 179..199
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:6M3G"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:6M3G"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:6M3G"
SQ SEQUENCE 346 AA; 39436 MW; DF411C9AE254E1E1 CRC64;
MVGGGGKRRP GGEGPQCEKT TDVKKSKFCE ADVSSDLRKE VENHYKLSLP EDFYHFWKFC
EELDPEKPSD SLSASLGLQL VGPYDILAGK HKTKKKSTGL NFNLHWRFYY DPPEFQTIII
GDNKTQYHMG YFRDSPDEFP VYVGINEAKK NCIIVPNGDN VFAAVKLFLT KKLREITDKK
KINLLKNIDE KLTEAARELG YSLEQRTVKM KQRDKKVVTK TFHGAGLVVP VDKNDVGYRE
LPETDADLKR ICKTIVEAAS DEERLKAFAP IQEMMTFVQF ANDECDYGMG LELGMDLFCY
GSHYFHKVAG QLLPLAYNLL KRNLFAEIIE EHLANRSQEN IDQLAA
