PDIP3_MOUSE
ID PDIP3_MOUSE Reviewed; 420 AA.
AC Q8BG81; B2FDB4; Q6PE83; Q80X99; Q8CI28;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Polymerase delta-interacting protein 3;
DE AltName: Full=S6K1 Aly/REF-like target;
DE Short=SKAR;
GN Name=Poldip3;
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; TISSUE=Cerebellum, Embryonic spinal ganglion, and Eye;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Liver, Olfactory epithelium, and Salivary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic
CC shuttling protein. {ECO:0000250}.
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DR EMBL; AK081139; BAC38144.1; -; mRNA.
DR EMBL; AK083924; BAC39068.1; -; mRNA.
DR EMBL; AK087446; BAC39877.1; -; mRNA.
DR EMBL; AL591952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037652; AAH37652.2; -; mRNA.
DR EMBL; BC046505; AAH46505.2; -; mRNA.
DR EMBL; BC058225; AAH58225.2; -; mRNA.
DR CCDS; CCDS27697.1; -.
DR RefSeq; NP_001334011.1; NM_001347082.1.
DR RefSeq; NP_848742.1; NM_178627.3.
DR AlphaFoldDB; Q8BG81; -.
DR SMR; Q8BG81; -.
DR BioGRID; 216286; 27.
DR IntAct; Q8BG81; 2.
DR STRING; 10090.ENSMUSP00000054548; -.
DR iPTMnet; Q8BG81; -.
DR PhosphoSitePlus; Q8BG81; -.
DR EPD; Q8BG81; -.
DR MaxQB; Q8BG81; -.
DR PaxDb; Q8BG81; -.
DR PeptideAtlas; Q8BG81; -.
DR PRIDE; Q8BG81; -.
DR ProteomicsDB; 288022; -.
DR Antibodypedia; 13265; 263 antibodies from 30 providers.
DR DNASU; 73826; -.
DR Ensembl; ENSMUST00000058793; ENSMUSP00000054548; ENSMUSG00000041815.
DR GeneID; 73826; -.
DR KEGG; mmu:73826; -.
DR UCSC; uc007wzz.1; mouse.
DR CTD; 84271; -.
DR MGI; MGI:1921076; Poldip3.
DR VEuPathDB; HostDB:ENSMUSG00000041815; -.
DR eggNOG; KOG0533; Eukaryota.
DR GeneTree; ENSGT00390000018868; -.
DR InParanoid; Q8BG81; -.
DR OMA; VNFQRTF; -.
DR OrthoDB; 1462536at2759; -.
DR TreeFam; TF313312; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 73826; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Poldip3; mouse.
DR PRO; PR:Q8BG81; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BG81; protein.
DR Bgee; ENSMUSG00000041815; Expressed in internal carotid artery and 246 other tissues.
DR ExpressionAtlas; Q8BG81; baseline and differential.
DR Genevisible; Q8BG81; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
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; Cytoplasm; Isopeptide bond; Methylation; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Translation regulation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CHAIN 2..420
FT /note="Polymerase delta-interacting protein 3"
FT /id="PRO_0000081723"
FT DOMAIN 280..351
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 256..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 33
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BY77"
SQ SEQUENCE 420 AA; 46132 MW; B898C54D485CF5FE CRC64;
MADLSLDELI RKRGTAAKGR LSVRPGIGGV RSRVGIQHSL VNQPARTATF QQRFDARQKI
GLSDARLKLG VKDAREKLLQ KDARFRIKGK VQDAREMLNS RKQQGTVPQK PRQVADAREK
ISLKRRSPAA FTSPPIGTVT PALKLTKTIQ VPQQKAMVPL HAHPAGMRIN VVNNHQAKQN
LYDLDEDDDI VVPVPPKQMK FAATGSLVHH MTGLSSSKLS MSKALPLTKV VQNDAYTAPV
LPSSVRTKAL TSMSRTLVNK EEPPKELPPA EPVLSPLEGT KMTVNNLHPR VTEEDIVELF
CVCGALKRAR LVHPGVAEVV FVKKDDAITA YKKYNNRCLD GQPMKCNLHM NGNVITSDQP
ILLRLSDSPS VKKESELPRR GNPASSNPPA EVDPDTVLRA LFKSSGASVT TQPTEFKIKL
