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Polymerase delta-interacting protein 3 (46 kDa DNA polymerase delta interaction protein) (p46) (S6K1 Aly/REF-like target) (SKAR)

 PDIP3_HUMAN             Reviewed;         421 AA.
Q9BY77; A8K6F8; A8K6V9; Q009A7; Q5H972; Q6PGN6; Q7Z6Z0; Q9NSP5;
Q9NSP6;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
10-OCT-2018, entry version 148.
RecName: Full=Polymerase delta-interacting protein 3;
AltName: Full=46 kDa DNA polymerase delta interaction protein;
Short=p46;
AltName: Full=S6K1 Aly/REF-like target;
Short=SKAR;
Name=POLDIP3; Synonyms=KIAA1649, PDIP46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND INTERACTION WITH
POLD2.
PubMed=12522211; DOI=10.1074/jbc.M208694200;
Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
"Identification of a novel protein, PDIP38, that interacts with the
p50 subunit of DNA polymerase delta and proliferating cell nuclear
antigen.";
J. Biol. Chem. 278:10041-10047(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
PubMed=11258795; DOI=10.1093/dnares/8.1.1;
Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
"Identification of novel transcribed sequences on human chromosome 22
by expressed sequence tag mapping.";
DNA Res. 8:1-9(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=12529303; DOI=10.1101/gr.695703;
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J.,
Knowles S., Bye J.M., Beare D.M., Dunham I.;
"Reevaluating human gene annotation: a second-generation analysis of
chromosome 22.";
Genome Res. 13:27-36(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-11; 34-46; 148-155; 311-323 AND 405-418,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 259-421, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH NCBP1 AND EIF4A3.
PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
"SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced
translation efficiency of spliced mRNAs.";
Cell 133:303-313(2008).
[10]
INTERACTION WITH RPS6KB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
SER-127; SER-275; SER-383 AND SER-385, MUTAGENESIS OF SER-383 AND
SER-385, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15341740; DOI=10.1016/j.cub.2004.08.061;
Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A.,
Gygi S., Blenis J.;
"SKAR is a specific target of S6 kinase 1 in cell growth control.";
Curr. Biol. 14:1540-1549(2004).
[11]
INTERACTION WITH ERH, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16984396; DOI=10.1111/j.1742-4658.2006.05477.x;
Smyk A., Szuminska M., Uniewicz K.A., Graves L.M., Kozlowski P.;
"Human enhancer of rudimentary is a molecular partner of PDIP46/SKAR,
a protein interacting with DNA polymerase delta and S6K1 and
regulating cell growth.";
FEBS J. 273:4728-4741(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ASSOCIATION WITH THE TREX COMPLEX.
PubMed=20844015; DOI=10.1101/gad.1898610;
Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A.,
Reed R.;
"ATP is required for interactions between UAP56 and two conserved mRNA
export proteins, Aly and CIP29, to assemble the TREX complex.";
Genes Dev. 24:2043-2053(2010).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-5; SER-127 AND SER-275, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THOC2; DDX39B AND
ZC3H11A, AND ASSOCIATION WITH THE TREX COMPLEX.
PubMed=22928037; DOI=10.1371/journal.pone.0043804;
Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.;
"The proteins PDIP3 and ZC11A associate with the human TREX complex in
an ATP-dependent manner and function in mRNA export.";
PLoS ONE 7:E43804-E43804(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-44; SER-127;
SER-204; SER-215; SER-217; SER-244 AND SER-275, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-33, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-372, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-223; LYS-248;
LYS-372 AND LYS-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Is involved in regulation of translation. Is
preferentially associated with CBC-bound spliced mRNA-protein
complexes during the pioneer round of mRNA translation.
Contributes to enhanced translational efficiency of spliced over
nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase
beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear
mRNA export; probably mediated by association with the TREX
complex. {ECO:0000269|PubMed:18423201,
ECO:0000269|PubMed:22928037}.
-!- SUBUNIT: Interacts with POLD2. Interacts with NCBP1 and EIF4A3.
Associates with the multiprotein exon junction complex (EJC).
Interacts with RPS6KB1 (activated). Interacts with ERH. Interacts
with THOC2, DDX39B and ZC3H11A; the interactions are ATP-dependent
and indicative for an association with the TREX complex.
{ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:15341740,
ECO:0000269|PubMed:16984396, ECO:0000269|PubMed:18423201,
ECO:0000269|PubMed:22928037}.
-!- INTERACTION:
Q09161:NCBP1; NbExp=3; IntAct=EBI-1776152, EBI-464743;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
Note=Nucleocytoplasmic shuttling protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BY77-1; Sequence=Displayed;
Name=2;
IsoId=Q9BY77-2; Sequence=VSP_011056;
-!- PTM: Phosphorylated at Ser-383 and Ser-385 by RPS6KB1.
{ECO:0000269|PubMed:15341740}.
-!- SEQUENCE CAUTION:
Sequence=BAB33368.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY422990; AAQ94604.1; -; Genomic_DNA.
EMBL; AB055760; BAB33368.2; ALT_INIT; mRNA.
EMBL; AL160111; CAB77058.1; -; mRNA.
EMBL; AL160112; CAB77059.1; -; mRNA.
EMBL; CR456456; CAG30342.1; -; mRNA.
EMBL; AK291623; BAF84312.1; -; mRNA.
EMBL; AK291774; BAF84463.1; -; mRNA.
EMBL; Z93241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC049840; AAH49840.1; -; mRNA.
EMBL; BC056912; AAH56912.2; -; mRNA.
EMBL; BC095411; AAH95411.1; -; mRNA.
EMBL; DQ887818; ABI74675.1; -; mRNA.
CCDS; CCDS14038.1; -. [Q9BY77-1]
CCDS; CCDS14039.1; -. [Q9BY77-2]
RefSeq; NP_115687.2; NM_032311.4. [Q9BY77-1]
RefSeq; NP_835237.1; NM_178136.2. [Q9BY77-2]
UniGene; Hs.505802; -.
ProteinModelPortal; Q9BY77; -.
SMR; Q9BY77; -.
BioGrid; 123998; 56.
IntAct; Q9BY77; 29.
MINT; Q9BY77; -.
STRING; 9606.ENSP00000252115; -.
iPTMnet; Q9BY77; -.
PhosphoSitePlus; Q9BY77; -.
BioMuta; POLDIP3; -.
DMDM; 50403796; -.
EPD; Q9BY77; -.
MaxQB; Q9BY77; -.
PaxDb; Q9BY77; -.
PeptideAtlas; Q9BY77; -.
PRIDE; Q9BY77; -.
ProteomicsDB; 79598; -.
ProteomicsDB; 79599; -. [Q9BY77-2]
DNASU; 84271; -.
Ensembl; ENST00000252115; ENSP00000252115; ENSG00000100227. [Q9BY77-1]
Ensembl; ENST00000348657; ENSP00000252116; ENSG00000100227. [Q9BY77-2]
GeneID; 84271; -.
KEGG; hsa:84271; -.
UCSC; uc003bcu.4; human. [Q9BY77-1]
CTD; 84271; -.
DisGeNET; 84271; -.
EuPathDB; HostDB:ENSG00000100227.17; -.
GeneCards; POLDIP3; -.
HGNC; HGNC:23782; POLDIP3.
HPA; HPA018419; -.
HPA; HPA048790; -.
MIM; 611520; gene.
neXtProt; NX_Q9BY77; -.
OpenTargets; ENSG00000100227; -.
PharmGKB; PA134899124; -.
eggNOG; KOG0533; Eukaryota.
eggNOG; ENOG4111JAW; LUCA.
GeneTree; ENSGT00390000018868; -.
HOVERGEN; HBG053550; -.
InParanoid; Q9BY77; -.
KO; K22414; -.
PhylomeDB; Q9BY77; -.
TreeFam; TF313312; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72187; mRNA 3'-end processing.
SIGNOR; Q9BY77; -.
ChiTaRS; POLDIP3; human.
GeneWiki; POLDIP3; -.
GenomeRNAi; 84271; -.
PMAP-CutDB; Q9BY77; -.
PRO; PR:Q9BY77; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100227; Expressed in 230 organ(s), highest expression level in right ovary.
CleanEx; HS_POLDIP3; -.
ExpressionAtlas; Q9BY77; baseline and differential.
Genevisible; Q9BY77; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
CDD; cd12681; RRM_SKAR; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034785; PDIP3.
InterPro; IPR034784; PDIP3_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR19965:SF34; PTHR19965:SF34; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Methylation;
mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Translation regulation; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 421 Polymerase delta-interacting protein 3.
/FTId=PRO_0000081722.
DOMAIN 280 351 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 33 33 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15341740}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15341740}.
MOD_RES 383 383 Phosphoserine; by RPS6KB1.
{ECO:0000269|PubMed:15341740}.
MOD_RES 385 385 Phosphoserine; by RPS6KB1.
{ECO:0000269|PubMed:15341740}.
CROSSLNK 200 200 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 151 179 Missing (in isoform 2).
{ECO:0000303|PubMed:12529303,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011056.
MUTAGEN 383 383 S->A: Reduces in vitro phosphorylation by
RPS6KB1. Abolishes in vitro
phosphorylation by RPS6KB1; when
associated with A-385.
{ECO:0000269|PubMed:15341740}.
MUTAGEN 385 385 S->A: Reduces in vitro phosphorylation by
RPS6KB1. Reduces in vitro phosphorylation
by RPS6KB1; when associated with A-383.
{ECO:0000269|PubMed:15341740}.
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


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