PDIP2_HUMAN
ID PDIP2_HUMAN Reviewed; 368 AA.
AC Q9Y2S7; B2R846; Q96JE4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Polymerase delta-interacting protein 2 {ECO:0000303|PubMed:26984527};
DE AltName: Full=38 kDa DNA polymerase delta interaction protein {ECO:0000303|PubMed:12522211};
DE Short=p38 {ECO:0000303|PubMed:12522211};
DE Flags: Precursor;
GN Name=POLDIP2 {ECO:0000303|PubMed:26984527, ECO:0000312|HGNC:HGNC:23781};
GN Synonyms=PDIP38 {ECO:0000303|PubMed:12522211, ECO:0000303|PubMed:16428295},
GN POLD4; ORFNames=HSPC017;
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 [MRNA], AND INTERACTION WITH PCNA AND POLD2.
RC TISSUE=Placenta;
RX PubMed=12522211; DOI=10.1074/jbc.m208694200;
RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
RT "Identification of a novel protein, PDIP38, that interacts with the p50
RT subunit of DNA polymerase delta and proliferating cell nuclear antigen.";
RL J. Biol. Chem. 278:10041-10047(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lung;
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 SUBCELLULAR LOCATION, AND INTERACTION WITH SSBP1.
RX PubMed=16428295; DOI=10.1093/jb/mvi169;
RA Cheng X., Kanki T., Fukuoh A., Ohgaki K., Takeya R., Aoki Y., Hamasaki N.,
RA Kang D.;
RT "PDIP38 associates with proteins constituting the mitochondrial DNA
RT nucleoid.";
RL J. Biochem. 138:673-678(2005).
RN [6]
RP INTERACTION WITH POLH.
RX PubMed=20554254; DOI=10.1016/j.dnarep.2010.04.010;
RA Tissier A., Janel-Bintz R., Coulon S., Klaile E., Kannouche P., Fuchs R.P.,
RA Cordonnier A.M.;
RT "Crosstalk between replicative and translesional DNA polymerases: PDIP38
RT interacts directly with Poleta.";
RL DNA Repair 9:922-928(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH POLD1.
RX PubMed=24191025; DOI=10.1073/pnas.1308760110;
RA Maga G., Crespan E., Markkanen E., Imhof R., Furrer A., Villani G.,
RA Huebscher U., van Loon B.;
RT "DNA polymerase delta-interacting protein 2 is a processivity factor for
RT DNA polymerase lambda during 8-oxo-7,8-dihydroguanine bypass.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18850-18855(2013).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, AND INTERACTION WITH PRIMPOL.
RX PubMed=26984527; DOI=10.1093/nar/gkw175;
RA Guilliam T.A., Bailey L.J., Brissett N.C., Doherty A.J.;
RT "PolDIP2 interacts with human PrimPol and enhances its DNA polymerase
RT activities.";
RL Nucleic Acids Res. 44:3317-3329(2016).
CC -!- FUNCTION: Involved in DNA damage tolerance by regulating translesion
CC synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG
CC and abasic sites (PubMed:24191025). May act by stimulating activity of
CC DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta
CC (POLD1) (PubMed:24191025, PubMed:26984527).
CC {ECO:0000269|PubMed:24191025, ECO:0000269|PubMed:26984527}.
CC -!- SUBUNIT: Interacts with PCNA and POLD2 (PubMed:12522211). Interacts
CC with SSBP1 (PubMed:16428295). Interacts with PRIMPOL; leading to
CC enhance DNA polymerase activity of PRIMPOL (PubMed:26984527). Interacts
CC with POLH (PubMed:20554254). Interacts with POLD1; leading to stimulate
CC DNA polymerase activity of POLD1 (PubMed:24191025).
CC {ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:16428295,
CC ECO:0000269|PubMed:20554254, ECO:0000269|PubMed:24191025,
CC ECO:0000269|PubMed:26984527}.
CC -!- INTERACTION:
CC Q9Y2S7; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-713000, EBI-11522760;
CC Q9Y2S7; P13196: ALAS1; NbExp=4; IntAct=EBI-713000, EBI-3905054;
CC Q9Y2S7; Q9Y6H1: CHCHD2; NbExp=7; IntAct=EBI-713000, EBI-2321769;
CC Q9Y2S7; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-713000, EBI-10239299;
CC Q9Y2S7; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-713000, EBI-742948;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:16428295}. Nucleus {ECO:0000269|PubMed:16428295}.
CC Note=Mainly localizes to the mitochondrial matrix; a small fraction
CC localizes in the nucleus. {ECO:0000269|PubMed:16428295}.
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DR EMBL; AF179891; AAK92018.1; -; mRNA.
DR EMBL; AF077203; AAD26998.1; -; mRNA.
DR EMBL; AK313232; BAG36043.1; -; mRNA.
DR EMBL; BC000655; AAH00655.1; -; mRNA.
DR EMBL; BC009265; AAH09265.1; -; mRNA.
DR CCDS; CCDS74018.1; -.
DR RefSeq; NP_001277074.1; NM_001290145.1.
DR RefSeq; NP_056399.1; NM_015584.4.
DR PDB; 6Z9C; X-ray; 2.80 A; A=51-368.
DR PDB; 6ZLX; X-ray; 3.39 A; A=67-359.
DR PDBsum; 6Z9C; -.
DR PDBsum; 6ZLX; -.
DR AlphaFoldDB; Q9Y2S7; -.
DR SASBDB; Q9Y2S7; -.
DR SMR; Q9Y2S7; -.
DR BioGRID; 117531; 210.
DR IntAct; Q9Y2S7; 93.
DR MINT; Q9Y2S7; -.
DR STRING; 9606.ENSP00000475924; -.
DR GlyGen; Q9Y2S7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2S7; -.
DR PhosphoSitePlus; Q9Y2S7; -.
DR BioMuta; POLDIP2; -.
DR EPD; Q9Y2S7; -.
DR jPOST; Q9Y2S7; -.
DR MassIVE; Q9Y2S7; -.
DR MaxQB; Q9Y2S7; -.
DR PeptideAtlas; Q9Y2S7; -.
DR PRIDE; Q9Y2S7; -.
DR ProteomicsDB; 85887; -.
DR Antibodypedia; 69152; 221 antibodies from 30 providers.
DR DNASU; 26073; -.
DR Ensembl; ENST00000540200.6; ENSP00000475924.2; ENSG00000004142.12.
DR GeneID; 26073; -.
DR KEGG; hsa:26073; -.
DR MANE-Select; ENST00000540200.6; ENSP00000475924.2; NM_015584.5; NP_056399.1.
DR UCSC; uc032ezc.2; human.
DR CTD; 26073; -.
DR DisGeNET; 26073; -.
DR GeneCards; POLDIP2; -.
DR HGNC; HGNC:23781; POLDIP2.
DR HPA; ENSG00000004142; Low tissue specificity.
DR MIM; 611519; gene.
DR neXtProt; NX_Q9Y2S7; -.
DR OpenTargets; ENSG00000004142; -.
DR PharmGKB; PA134866227; -.
DR VEuPathDB; HostDB:ENSG00000004142; -.
DR eggNOG; KOG4408; Eukaryota.
DR GeneTree; ENSGT00940000153571; -.
DR HOGENOM; CLU_051858_0_0_1; -.
DR InParanoid; Q9Y2S7; -.
DR OMA; MGCRESQ; -.
DR OrthoDB; 805515at2759; -.
DR PhylomeDB; Q9Y2S7; -.
DR PathwayCommons; Q9Y2S7; -.
DR SignaLink; Q9Y2S7; -.
DR BioGRID-ORCS; 26073; 13 hits in 253 CRISPR screens.
DR ChiTaRS; POLDIP2; human.
DR GeneWiki; POLDIP2; -.
DR GenomeRNAi; 26073; -.
DR Pharos; Q9Y2S7; Tbio.
DR PRO; PR:Q9Y2S7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2S7; protein.
DR Bgee; ENSG00000004142; Expressed in gastrocnemius and 198 other tissues.
DR ExpressionAtlas; Q9Y2S7; baseline and differential.
DR Genevisible; Q9Y2S7; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070987; P:error-free translesion synthesis; IDA:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:1904531; P:positive regulation of actin filament binding; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR Gene3D; 2.60.40.1470; -; 1.
DR InterPro; IPR007474; ApaG_domain.
DR InterPro; IPR036767; ApaG_sf.
DR InterPro; IPR011722; Hemimethylated_DNA-bd_dom.
DR InterPro; IPR036623; Hemimethylated_DNA-bd_sf.
DR Pfam; PF04379; DUF525; 1.
DR Pfam; PF08755; YccV-like; 1.
DR SMART; SM00992; YccV-like; 1.
DR SUPFAM; SSF110069; SSF110069; 1.
DR SUPFAM; SSF141255; SSF141255; 1.
DR PROSITE; PS51087; APAG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 52..368
FT /note="Polymerase delta-interacting protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000197975"
FT DOMAIN 235..360
FT /note="ApaG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00412"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 9
FT /note="A -> P (in Ref. 1; AAK92018)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="R -> K (in Ref. 1; AAK92018)"
FT /evidence="ECO:0000305"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6Z9C"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 91..105
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6Z9C"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6Z9C"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6Z9C"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 241..252
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6ZLX"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 277..288
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6ZLX"
FT STRAND 314..326
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:6Z9C"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:6Z9C"
SQ SEQUENCE 368 AA; 42033 MW; 1882F93273542CCF CRC64;
MAACTARRAL AVGSRWWSRS LTGARWPRPL CAAAGAGAFS PASTTTTRRH LSSRNRPEGK
VLETVGVFEV PKQNGKYETG QLFLHSIFGY RGVVLFPWQA RLYDRDVASA APEKAENPAG
HGSKEVKGKT HTYYQVLIDA RDCPHISQRS QTEAVTFLAN HDDSRALYAI PGLDYVSHED
ILPYTSTDQV PIQHELFERF LLYDQTKAPP FVARETLRAW QEKNHPWLEL SDVHRETTEN
IRVTVIPFYM GMREAQNSHV YWWRYCIRLE NLDSDVVQLR ERHWRIFSLS GTLETVRGRG
VVGREPVLSK EQPAFQYSSH VSLQASSGHM WGTFRFERPD GSHFDVRIPP FSLESNKDEK
TPPSGLHW
