PDIP3_HUMAN
ID PDIP3_HUMAN Reviewed; 421 AA.
AC Q9BY77; A8K6F8; A8K6V9; Q009A7; Q5H972; Q6PGN6; Q7Z6Z0; Q9NSP5; Q9NSP6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Polymerase delta-interacting protein 3;
DE AltName: Full=46 kDa DNA polymerase delta interaction protein;
DE Short=p46;
DE AltName: Full=S6K1 Aly/REF-like target;
DE Short=SKAR;
GN Name=POLDIP3; Synonyms=KIAA1649, PDIP46;
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 [GENOMIC DNA] (ISOFORM 1), AND INTERACTION WITH POLD2.
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] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 2-11; 34-46; 148-155; 311-323 AND 405-418, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-421, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH NCBP1 AND EIF4A3.
RX PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
RA Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
RT "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation
RT efficiency of spliced mRNAs.";
RL Cell 133:303-313(2008).
RN [10]
RP INTERACTION WITH RPS6KB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-127;
RP SER-275; SER-383 AND SER-385, MUTAGENESIS OF SER-383 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15341740; DOI=10.1016/j.cub.2004.08.061;
RA Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A.,
RA Gygi S., Blenis J.;
RT "SKAR is a specific target of S6 kinase 1 in cell growth control.";
RL Curr. Biol. 14:1540-1549(2004).
RN [11]
RP INTERACTION WITH ERH, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16984396; DOI=10.1111/j.1742-4658.2006.05477.x;
RA Smyk A., Szuminska M., Uniewicz K.A., Graves L.M., Kozlowski P.;
RT "Human enhancer of rudimentary is a molecular partner of PDIP46/SKAR, a
RT protein interacting with DNA polymerase delta and S6K1 and regulating cell
RT growth.";
RL FEBS J. 273:4728-4741(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ASSOCIATION WITH THE TREX COMPLEX.
RX PubMed=20844015; DOI=10.1101/gad.1898610;
RA Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.;
RT "ATP is required for interactions between UAP56 and two conserved mRNA
RT export proteins, Aly and CIP29, to assemble the TREX complex.";
RL Genes Dev. 24:2043-2053(2010).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5; SER-127 AND SER-275, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THOC2; DDX39B AND ZC3H11A,
RP AND ASSOCIATION WITH THE TREX COMPLEX.
RX PubMed=22928037; DOI=10.1371/journal.pone.0043804;
RA Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.;
RT "The proteins PDIP3 and ZC11A associate with the human TREX complex in an
RT ATP-dependent manner and function in mRNA export.";
RL PLoS ONE 7:E43804-E43804(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-44; SER-127; SER-204;
RP SER-215; SER-217; SER-244 AND SER-275, AND IDENTIFICATION BY MASS
RP 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 [23]
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 [24]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-372, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-223; LYS-248; LYS-372
RP AND LYS-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Is involved in regulation of translation. Is preferentially
CC associated with CBC-bound spliced mRNA-protein complexes during the
CC pioneer round of mRNA translation. Contributes to enhanced
CC translational efficiency of spliced over nonspliced mRNAs. Recruits
CC activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly
CC synthesized mRNA. Involved in nuclear mRNA export; probably mediated by
CC association with the TREX complex. {ECO:0000269|PubMed:18423201,
CC ECO:0000269|PubMed:22928037}.
CC -!- SUBUNIT: Interacts with POLD2. Interacts with NCBP1 and EIF4A3.
CC Associates with the multiprotein exon junction complex (EJC). Interacts
CC with RPS6KB1 (activated). Interacts with ERH. Interacts with THOC2,
CC DDX39B and ZC3H11A; the interactions are ATP-dependent and indicative
CC for an association with the TREX complex. {ECO:0000269|PubMed:12522211,
CC ECO:0000269|PubMed:15341740, ECO:0000269|PubMed:16984396,
CC ECO:0000269|PubMed:18423201, ECO:0000269|PubMed:22928037}.
CC -!- INTERACTION:
CC Q9BY77; Q09161: NCBP1; NbExp=3; IntAct=EBI-1776152, EBI-464743;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC Note=Nucleocytoplasmic shuttling protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BY77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BY77-2; Sequence=VSP_011056;
CC -!- PTM: Phosphorylated at Ser-383 and Ser-385 by RPS6KB1.
CC {ECO:0000269|PubMed:15341740}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB33368.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY422990; AAQ94604.1; -; Genomic_DNA.
DR EMBL; AB055760; BAB33368.2; ALT_INIT; mRNA.
DR EMBL; AL160111; CAB77058.1; -; mRNA.
DR EMBL; AL160112; CAB77059.1; -; mRNA.
DR EMBL; CR456456; CAG30342.1; -; mRNA.
DR EMBL; AK291623; BAF84312.1; -; mRNA.
DR EMBL; AK291774; BAF84463.1; -; mRNA.
DR EMBL; Z93241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049840; AAH49840.1; -; mRNA.
DR EMBL; BC056912; AAH56912.2; -; mRNA.
DR EMBL; BC095411; AAH95411.1; -; mRNA.
DR EMBL; DQ887818; ABI74675.1; -; mRNA.
DR CCDS; CCDS14038.1; -. [Q9BY77-1]
DR CCDS; CCDS14039.1; -. [Q9BY77-2]
DR RefSeq; NP_115687.2; NM_032311.4. [Q9BY77-1]
DR RefSeq; NP_835237.1; NM_178136.2. [Q9BY77-2]
DR AlphaFoldDB; Q9BY77; -.
DR SMR; Q9BY77; -.
DR BioGRID; 123998; 227.
DR IntAct; Q9BY77; 61.
DR MINT; Q9BY77; -.
DR STRING; 9606.ENSP00000397927; -.
DR GlyGen; Q9BY77; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BY77; -.
DR PhosphoSitePlus; Q9BY77; -.
DR SwissPalm; Q9BY77; -.
DR BioMuta; POLDIP3; -.
DR DMDM; 50403796; -.
DR EPD; Q9BY77; -.
DR jPOST; Q9BY77; -.
DR MassIVE; Q9BY77; -.
DR MaxQB; Q9BY77; -.
DR PaxDb; Q9BY77; -.
DR PeptideAtlas; Q9BY77; -.
DR PRIDE; Q9BY77; -.
DR ProteomicsDB; 79598; -. [Q9BY77-1]
DR ProteomicsDB; 79599; -. [Q9BY77-2]
DR Antibodypedia; 13265; 263 antibodies from 30 providers.
DR DNASU; 84271; -.
DR Ensembl; ENST00000252115.10; ENSP00000252115.5; ENSG00000100227.19. [Q9BY77-1]
DR Ensembl; ENST00000348657.6; ENSP00000252116.5; ENSG00000100227.19. [Q9BY77-2]
DR GeneID; 84271; -.
DR KEGG; hsa:84271; -.
DR MANE-Select; ENST00000252115.10; ENSP00000252115.5; NM_032311.5; NP_115687.2.
DR UCSC; uc003bcu.4; human. [Q9BY77-1]
DR CTD; 84271; -.
DR DisGeNET; 84271; -.
DR GeneCards; POLDIP3; -.
DR HGNC; HGNC:23782; POLDIP3.
DR HPA; ENSG00000100227; Low tissue specificity.
DR MIM; 611520; gene.
DR neXtProt; NX_Q9BY77; -.
DR OpenTargets; ENSG00000100227; -.
DR PharmGKB; PA134899124; -.
DR VEuPathDB; HostDB:ENSG00000100227; -.
DR eggNOG; KOG0533; Eukaryota.
DR GeneTree; ENSGT00390000018868; -.
DR HOGENOM; CLU_049890_0_0_1; -.
DR InParanoid; Q9BY77; -.
DR OMA; VNFQRTF; -.
DR PhylomeDB; Q9BY77; -.
DR TreeFam; TF313312; -.
DR PathwayCommons; Q9BY77; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q9BY77; -.
DR SIGNOR; Q9BY77; -.
DR BioGRID-ORCS; 84271; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; POLDIP3; human.
DR GeneWiki; POLDIP3; -.
DR GenomeRNAi; 84271; -.
DR Pharos; Q9BY77; Tbio.
DR PRO; PR:Q9BY77; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9BY77; protein.
DR Bgee; ENSG00000100227; Expressed in ventricular zone and 213 other tissues.
DR ExpressionAtlas; Q9BY77; baseline and differential.
DR Genevisible; Q9BY77; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR CDD; cd12681; RRM_SKAR; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034784; PDIP3_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Translation regulation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..421
FT /note="Polymerase delta-interacting protein 3"
FT /id="PRO_0000081722"
FT DOMAIN 280..351
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 370..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15341740,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15341740,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:15341740"
FT MOD_RES 385
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:15341740"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 151..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_011056"
FT MUTAGEN 383
FT /note="S->A: Reduces in vitro phosphorylation by RPS6KB1.
FT Abolishes in vitro phosphorylation by RPS6KB1; when
FT associated with A-385."
FT /evidence="ECO:0000269|PubMed:15341740"
FT MUTAGEN 385
FT /note="S->A: Reduces in vitro phosphorylation by RPS6KB1.
FT Reduces in vitro phosphorylation by RPS6KB1; when
FT associated with A-383."
FT /evidence="ECO:0000269|PubMed:15341740"
SQ SEQUENCE 421 AA; 46089 MW; 39A4A2362852E020 CRC64;
MADISLDELI RKRGAAAKGR LNARPGVGGV RSRVGIQQGL LSQSTRTATF QQRFDARQKI
GLSDARLKLG VKDAREKLLQ KDARFRIKGK VQDAREMLNS RKQQTTVPQK PRQVADAREK
ISLKRSSPAA FINPPIGTVT PALKLTKTIQ VPQQKAMAPL HPHPAGMRIN VVNNHQAKQN
LYDLDEDDDG IASVPTKQMK FAASGGFLHH MAGLSSSKLS MSKALPLTKV VQNDAYTAPA
LPSSIRTKAL TNMSRTLVNK EEPPKELPAA EPVLSPLEGT KMTVNNLHPR VTEEDIVELF
CVCGALKRAR LVHPGVAEVV FVKKDDAITA YKKYNNRCLD GQPMKCNLHM NGNVITSDQP
ILLRLSDSPS MKKESELPRR VNSASSSNPP AEVDPDTILK ALFKSSGASV TTQPTEFKIK
L
