HPF1_MOUSE
ID HPF1_MOUSE Reviewed; 346 AA.
AC Q8CFE2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Histone PARylation factor 1 {ECO:0000305};
GN Name=Hpf1 {ECO:0000312|MGI:MGI:1919862};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Initiates the repair of double-strand DNA breaks: recruited
CC to DNA damage sites by PARP1 and PARP2 and switches the amino acid
CC specificity of PARP1 and PARP2 from aspartate or glutamate to serine
CC residues, licensing serine ADP-ribosylation of target proteins. Serine
CC ADP-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. Serine ADP-ribosylation of
CC proteins constitutes the primary form of ADP-ribosylation of proteins
CC in response to DNA damage. HPF1 acts by completing the active site of
CC PARP1 and PARP2: forms a composite active site composed of residues
CC from HPF1 and PARP1 or PARP2. HPF1 also promotes tyrosine ADP-
CC ribosylation, probably by conferring tyrosine specificity on PARP1.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SUBUNIT: Interacts with PARP1 (via the PARP catalytic domain).
CC Interacts with PARP2 (via the PARP catalytic domain). Interacts with
CC core nucleosomes in a PARP1- and PARP2-dependent manner.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9NWY4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9NWY4}. Note=Localizes to DNA damage
CC sites; chromatin localization is dependent on PARP1 and PARP2.
CC {ECO:0000250|UniProtKB:Q9NWY4}.
CC -!- SIMILARITY: Belongs to the HPF1 family. {ECO:0000305}.
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DR EMBL; AK150453; BAE29573.1; -; mRNA.
DR EMBL; AK157260; BAE34015.1; -; mRNA.
DR EMBL; BC042740; AAH42740.1; -; mRNA.
DR CCDS; CCDS52553.1; -.
DR RefSeq; NP_082575.1; NM_028299.1.
DR PDB; 6M3H; X-ray; 1.71 A; A=1-346.
DR PDBsum; 6M3H; -.
DR AlphaFoldDB; Q8CFE2; -.
DR SMR; Q8CFE2; -.
DR BioGRID; 215471; 2.
DR IntAct; Q8CFE2; 1.
DR MINT; Q8CFE2; -.
DR STRING; 10090.ENSMUSP00000047235; -.
DR iPTMnet; Q8CFE2; -.
DR PhosphoSitePlus; Q8CFE2; -.
DR EPD; Q8CFE2; -.
DR jPOST; Q8CFE2; -.
DR MaxQB; Q8CFE2; -.
DR PaxDb; Q8CFE2; -.
DR PeptideAtlas; Q8CFE2; -.
DR PRIDE; Q8CFE2; -.
DR ProteomicsDB; 273190; -.
DR Antibodypedia; 50204; 61 antibodies from 11 providers.
DR Ensembl; ENSMUST00000037190; ENSMUSP00000047235; ENSMUSG00000038005.
DR GeneID; 72612; -.
DR KEGG; mmu:72612; -.
DR UCSC; uc009lti.2; mouse.
DR CTD; 54969; -.
DR MGI; MGI:1919862; Hpf1.
DR VEuPathDB; HostDB:ENSMUSG00000038005; -.
DR eggNOG; KOG3952; Eukaryota.
DR GeneTree; ENSGT00390000014876; -.
DR HOGENOM; CLU_053037_0_0_1; -.
DR InParanoid; Q8CFE2; -.
DR OMA; RPQFIAI; -.
DR OrthoDB; 1077112at2759; -.
DR PhylomeDB; Q8CFE2; -.
DR TreeFam; TF317026; -.
DR BioGRID-ORCS; 72612; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hpf1; mouse.
DR PRO; PR:Q8CFE2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CFE2; protein.
DR Bgee; ENSMUSG00000038005; Expressed in animal zygote and 254 other tissues.
DR ExpressionAtlas; Q8CFE2; baseline and differential.
DR Genevisible; Q8CFE2; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISS: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_0000294447"
FT REGION 242..346
FT /note="Interaction with PARP1"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT ACT_SITE 284
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT MOD_RES 238
FT /note="ADP-ribosyltyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWY4"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6M3H"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:6M3H"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6M3H"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6M3H"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6M3H"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6M3H"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 179..199
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:6M3H"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 261..283
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:6M3H"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:6M3H"
SQ SEQUENCE 346 AA; 39291 MW; 9B97648395692416 CRC64;
MVGGGGKRRT AGAGPQCEKT VEVKKSKFSE ADVSSDLRKE VENLYKLSLP EDFYHFWKFC
EELDPEKPAD ALATSLGLRL VGPYDILAGK HKMKKKPTGL NCNLHWRFYY DPPEFQTIII
GDNKTQYHMG YFRDSPDELP VYVGTNEAKK NCIIIQNGDN VFAAIKLFLM KKLKEVTDRK
KISILKNIDE KLTEAARKLG YSLEQRTVKM RQRDKKVVTK TFHGAGLVVP VDKNDVGYRE
LPETDADLKR ICKAVVDAAS DEERLKAFAP IQEMMTFVQF ANDECDYGMG LELGMDLFCY
GSHYFHKVAG QLLPLAYNLL KRDLFAKIIE DHLASRSEEN IDQLAG
