PATL1_HUMAN
ID PATL1_HUMAN Reviewed; 770 AA.
AC Q86TB9; B3KXT9; Q2TA86; Q6P166; Q8N9M6; Q8NI63;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein PAT1 homolog 1;
DE AltName: Full=PAT1-like protein 1;
DE AltName: Full=Protein PAT1 homolog b;
DE Short=Pat1b;
DE Short=hPat1b;
GN Name=PATL1; ORFNames=OK/KNS-cl.5;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Glial tumor;
RA Nonaka Y., Shichijo S., Itoh K.;
RT "Genes encoded epitopes recognized by CTL established from TIL of colon
RT cancer.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 66-770 (ISOFORM 1).
RC TISSUE=Eye, and Uterus;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17936923; DOI=10.1016/j.bbamcr.2007.08.009;
RA Scheller N., Resa-Infante P., de la Luna S., Galao R.P., Albrecht M.,
RA Kaestner L., Lipp P., Lengauer T., Meyerhans A., Diez J.;
RT "Identification of PatL1, a human homolog to yeast P body component Pat1.";
RL Biochim. Biophys. Acta 1773:1786-1792(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179 AND SER-184, AND
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 [8]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=19628699; DOI=10.1073/pnas.0906413106;
RA Scheller N., Mina L.B., Galao R.P., Chari A., Gimenez-Barcons M.,
RA Noueiry A., Fischer U., Meyerhans A., Diez J.;
RT "Translation and replication of hepatitis C virus genomic RNA depends on
RT ancient cellular proteins that control mRNA fates.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13517-13522(2009).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN REGION A, INTERACTION WITH THE
RP CCR4-NOT COMPLEX, AND INTERACTION WITH DCP1A; DCP2; DDX6; EDC3; EDC4; LSM1;
RP LSM4 AND XRN1.
RX PubMed=20584987; DOI=10.1128/mcb.00429-10;
RA Ozgur S., Chekulaeva M., Stoecklin G.;
RT "Human Pat1b connects deadenylation with mRNA decapping and controls the
RT assembly of processing bodies.";
RL Mol. Cell. Biol. 30:4308-4323(2010).
RN [11]
RP RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=20826699; DOI=10.1261/rna.2295410;
RA Marnef A., Maldonado M., Bugaut A., Balasubramanian S., Kress M., Weil D.,
RA Standart N.;
RT "Distinct functions of maternal and somatic Pat1 protein paralogs.";
RL RNA 16:2094-2107(2010).
RN [12]
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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LSM1.
RX PubMed=20852261; DOI=10.1093/nar/gkq797;
RA Totaro A., Renzi F., La Fata G., Mattioli C., Raabe M., Urlaub H.,
RA Achsel T.;
RT "The human Pat1b protein: a novel mRNA deadenylation factor identified by a
RT new immunoprecipitation technique.";
RL Nucleic Acids Res. 39:635-647(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP RNA-BINDING, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS
RP OF LEU-86; LEU-90; MET-93 AND ILE-95.
RX PubMed=22090346; DOI=10.1091/mbc.e11-05-0415;
RA Marnef A., Weil D., Standart N.;
RT "RNA-related nuclear functions of human Pat1b, the P-body mRNA decay
RT factor.";
RL Mol. Biol. Cell 23:213-224(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-184; THR-194 AND
RP SER-278, AND IDENTIFICATION BY 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 [17]
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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-217; ARG-223 AND ARG-263, AND
RP IDENTIFICATION BY MASS 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 [19]
RP INTERACTION WITH EIF4ENIF1.
RX PubMed=26027925; DOI=10.1016/j.celrep.2015.04.065;
RA Nishimura T., Padamsi Z., Fakim H., Milette S., Dunham W.H., Gingras A.C.,
RA Fabian M.R.;
RT "The eIF4E-Binding protein 4E-T is a component of the mRNA decay machinery
RT that bridges the 5' and 3' termini of target mRNAs.";
RL Cell Rep. 11:1425-1436(2015).
RN [20]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
RN [21]
RP INTERACTION WITH DDX6.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [22]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4ENIF1.
RX PubMed=32354837; DOI=10.1101/gad.336073.119;
RA Raesch F., Weber R., Izaurralde E., Igreja C.;
RT "4E-T-bound mRNAs are stored in a silenced and deadenylated form.";
RL Genes Dev. 34:847-860(2020).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 517-767, RNA-BINDING, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN REGION C, INTERACTION WITH THE LSM-CONTAINING
RP SMN-SM PROTEIN COMPLEX, INTERACTION WITH DCP2; DDX6 AND EDC4, AND
RP MUTAGENESIS OF ARG-519; ARG-520; LEU-523; GLU-527; TYR-530; LEU-534;
RP 539-TYR--ASP-557; ARG-591; ARG-595; LYS-625 AND LYS-626.
RX PubMed=20543818; DOI=10.1038/emboj.2010.124;
RA Braun J.E., Tritschler F., Haas G., Igreja C., Truffault V.,
RA Weichenrieder O., Izaurralde E.;
RT "The C-terminal alpha-alpha superhelix of Pat is required for mRNA
RT decapping in metazoa.";
RL EMBO J. 29:2368-2380(2010).
CC -!- FUNCTION: RNA-binding protein involved in deadenylation-dependent
CC decapping of mRNAs, leading to the degradation of mRNAs
CC (PubMed:17936923, PubMed:20543818, PubMed:20584987, PubMed:20852261).
CC Acts as a scaffold protein that connects deadenylation and decapping
CC machinery (PubMed:17936923, PubMed:20543818, PubMed:20584987,
CC PubMed:20852261). Required for cytoplasmic mRNA processing body (P-
CC body) assembly (PubMed:17936923, PubMed:20543818, PubMed:20584987,
CC PubMed:20852261). {ECO:0000269|PubMed:17936923,
CC ECO:0000269|PubMed:20543818, ECO:0000269|PubMed:20584987,
CC ECO:0000269|PubMed:20852261}.
CC -!- FUNCTION: (Microbial infection) In case of infection, required for
CC translation and replication of hepatitis C virus (HCV).
CC {ECO:0000269|PubMed:19628699}.
CC -!- SUBUNIT: Interacts (via region A) with DDX6/RCK (PubMed:20543818,
CC PubMed:20584987, PubMed:31422817, PubMed:31439631). Interacts (via
CC region H and region C) with LSM1 and LSM4 (PubMed:20584987,
CC PubMed:20852261). Interacts (via region N) with DCP1A, DCP2, EDC3, EDC4
CC and XRN1 (PubMed:20584987, PubMed:20543818). Interacts with the CCR4-
CC NOT complex (PubMed:20584987). Interacts with the Lsm-containing SMN-Sm
CC protein complex (PubMed:20543818). Interacts with EIF4ENIF1/4E-T
CC (PubMed:26027925, PubMed:32354837). {ECO:0000269|PubMed:20543818,
CC ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:20852261,
CC ECO:0000269|PubMed:26027925, ECO:0000269|PubMed:31422817,
CC ECO:0000269|PubMed:31439631, ECO:0000269|PubMed:32354837}.
CC -!- INTERACTION:
CC Q86TB9; A5YKK6: CNOT1; NbExp=3; IntAct=EBI-2562092, EBI-1222758;
CC Q86TB9; Q9ULM6: CNOT6; NbExp=3; IntAct=EBI-2562092, EBI-2104530;
CC Q86TB9; Q9UIV1: CNOT7; NbExp=5; IntAct=EBI-2562092, EBI-2105113;
CC Q86TB9; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-2562092, EBI-742299;
CC Q86TB9; Q9NPI6: DCP1A; NbExp=2; IntAct=EBI-2562092, EBI-374238;
CC Q86TB9; P26196: DDX6; NbExp=12; IntAct=EBI-2562092, EBI-351257;
CC Q86TB9; Q13643: FHL3; NbExp=8; IntAct=EBI-2562092, EBI-741101;
CC Q86TB9; Q08379: GOLGA2; NbExp=6; IntAct=EBI-2562092, EBI-618309;
CC Q86TB9; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2562092, EBI-11962084;
CC Q86TB9; O15116: LSM1; NbExp=17; IntAct=EBI-2562092, EBI-347619;
CC Q86TB9; Q9Y333: LSM2; NbExp=3; IntAct=EBI-2562092, EBI-347416;
CC Q86TB9; P62312: LSM6; NbExp=3; IntAct=EBI-2562092, EBI-373310;
CC Q86TB9; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2562092, EBI-10271199;
CC Q86TB9; P25788: PSMA3; NbExp=3; IntAct=EBI-2562092, EBI-348380;
CC Q86TB9; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2562092, EBI-12806590;
CC Q86TB9; Q9NZC7-5: WWOX; NbExp=5; IntAct=EBI-2562092, EBI-12040603;
CC Q86TB9; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2562092, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:17936923,
CC ECO:0000269|PubMed:20543818, ECO:0000269|PubMed:20584987,
CC ECO:0000269|PubMed:20826699, ECO:0000269|PubMed:20852261,
CC ECO:0000269|PubMed:22090346, ECO:0000269|PubMed:32354837}. Nucleus
CC {ECO:0000269|PubMed:22090346}. Nucleus, PML body
CC {ECO:0000269|PubMed:22090346}. Nucleus speckle
CC {ECO:0000269|PubMed:22090346}. Note=Predominantly cytoplasmic
CC (PubMed:22090346). Shuttles between the nucleus and the cytoplasm in a
CC CRM1-dependent manner (PubMed:22090346). Enriched in splicing speckles.
CC Localization to nuclear foci and speckles requires active
CC transcription. Excluded from the nucleolus (PubMed:22090346).
CC {ECO:0000269|PubMed:22090346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86TB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TB9-2; Sequence=VSP_031778;
CC Name=3;
CC IsoId=Q86TB9-3; Sequence=VSP_031777;
CC Name=4;
CC IsoId=Q86TB9-4; Sequence=VSP_040576, VSP_040577;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17936923}.
CC -!- DOMAIN: The region A, also named N-term, mediates the interaction with
CC DDX6/RCK and is required for cytoplasmic mRNA processing body assembly.
CC -!- DOMAIN: The region C, also named Pat-C, is required for RNA-binding and
CC mediates the binding with the Lsm-containing SMN-Sm protein complex and
CC the decapping machinery. It folds into an alpha-alpha superhelix,
CC exposing conserved and basic residues on one side of the domain.
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89916.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB065087; BAB93524.1; -; mRNA.
DR EMBL; AK094193; BAC04305.1; -; mRNA.
DR EMBL; AK127943; BAG54601.1; -; mRNA.
DR EMBL; AL831992; CAD89916.1; ALT_INIT; mRNA.
DR EMBL; AP000442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065264; AAH65264.2; -; mRNA.
DR EMBL; BC109038; AAI09039.1; -; mRNA.
DR EMBL; BC109039; AAI09040.1; -; mRNA.
DR EMBL; BC111047; AAI11048.1; -; mRNA.
DR CCDS; CCDS44613.1; -. [Q86TB9-1]
DR RefSeq; NP_689929.2; NM_152716.2. [Q86TB9-1]
DR PDB; 2XEQ; X-ray; 3.10 A; A/B/C/D=517-767.
DR PDB; 2XER; X-ray; 2.95 A; A/B/C=517-767.
DR PDB; 2XES; X-ray; 2.10 A; A/B=517-767.
DR PDBsum; 2XEQ; -.
DR PDBsum; 2XER; -.
DR PDBsum; 2XES; -.
DR AlphaFoldDB; Q86TB9; -.
DR SMR; Q86TB9; -.
DR BioGRID; 128613; 167.
DR IntAct; Q86TB9; 37.
DR STRING; 9606.ENSP00000300146; -.
DR GlyGen; Q86TB9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86TB9; -.
DR MetOSite; Q86TB9; -.
DR PhosphoSitePlus; Q86TB9; -.
DR BioMuta; PATL1; -.
DR DMDM; 182705251; -.
DR EPD; Q86TB9; -.
DR jPOST; Q86TB9; -.
DR MassIVE; Q86TB9; -.
DR MaxQB; Q86TB9; -.
DR PaxDb; Q86TB9; -.
DR PeptideAtlas; Q86TB9; -.
DR PRIDE; Q86TB9; -.
DR ProteomicsDB; 69679; -. [Q86TB9-1]
DR ProteomicsDB; 69680; -. [Q86TB9-2]
DR ProteomicsDB; 69681; -. [Q86TB9-3]
DR ProteomicsDB; 69682; -. [Q86TB9-4]
DR Antibodypedia; 49853; 90 antibodies from 20 providers.
DR DNASU; 219988; -.
DR Ensembl; ENST00000300146.10; ENSP00000300146.9; ENSG00000166889.14. [Q86TB9-1]
DR GeneID; 219988; -.
DR KEGG; hsa:219988; -.
DR MANE-Select; ENST00000300146.10; ENSP00000300146.9; NM_152716.3; NP_689929.2.
DR UCSC; uc001noe.6; human. [Q86TB9-1]
DR CTD; 219988; -.
DR GeneCards; PATL1; -.
DR HGNC; HGNC:26721; PATL1.
DR HPA; ENSG00000166889; Low tissue specificity.
DR MIM; 614660; gene.
DR neXtProt; NX_Q86TB9; -.
DR OpenTargets; ENSG00000166889; -.
DR PharmGKB; PA162398769; -.
DR VEuPathDB; HostDB:ENSG00000166889; -.
DR eggNOG; KOG4592; Eukaryota.
DR GeneTree; ENSGT00520000055649; -.
DR HOGENOM; CLU_009778_1_0_1; -.
DR InParanoid; Q86TB9; -.
DR OMA; LPQHPLM; -.
DR OrthoDB; 950451at2759; -.
DR PhylomeDB; Q86TB9; -.
DR TreeFam; TF323322; -.
DR PathwayCommons; Q86TB9; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; Q86TB9; -.
DR BioGRID-ORCS; 219988; 15 hits in 1088 CRISPR screens.
DR ChiTaRS; PATL1; human.
DR EvolutionaryTrace; Q86TB9; -.
DR GenomeRNAi; 219988; -.
DR Pharos; Q86TB9; Tbio.
DR PRO; PR:Q86TB9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86TB9; protein.
DR Bgee; ENSG00000166889; Expressed in ileal mucosa and 175 other tissues.
DR Genevisible; Q86TB9; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0034046; F:poly(G) binding; IDA:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IDA:UniProtKB.
DR InterPro; IPR039900; Pat1-like.
DR InterPro; IPR019167; PAT1_dom.
DR PANTHER; PTHR21551; PTHR21551; 1.
DR Pfam; PF09770; PAT1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..770
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000320963"
FT REGION 1..397
FT /note="Involved in nuclear foci localization"
FT REGION 1..84
FT /note="Region A; interaction with DDX6/RCK"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..388
FT /note="Region N; interaction with decapping machinery"
FT REGION 223..397
FT /note="Involved in RNA-binding"
FT REGION 314..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..448
FT /note="Region H"
FT REGION 398..770
FT /note="Involved in nuclear speckle localization"
FT REGION 449..770
FT /note="Region C"
FT MOTIF 86..95
FT /note="Nuclear export signal"
FT COMPBIAS 9..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 223
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 263
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
FT VAR_SEQ 1..659
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_031777"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031778"
FT VAR_SEQ 242..271
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040576"
FT VAR_SEQ 662..698
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040577"
FT MUTAGEN 86
FT /note="L->A: Loss of nuclear export; when associated with
FT A-90, A-93 and A-95."
FT /evidence="ECO:0000269|PubMed:22090346"
FT MUTAGEN 90
FT /note="L->A: Loss of nuclear export; when associated with
FT A-86, A-93 and A-95."
FT /evidence="ECO:0000269|PubMed:22090346"
FT MUTAGEN 93
FT /note="M->A: Loss of nuclear export; when associated with
FT A-86, A-90 and A-95."
FT /evidence="ECO:0000269|PubMed:22090346"
FT MUTAGEN 95
FT /note="I->A: Loss of nuclear export; when associated with
FT A-86, A-90 and A-93."
FT /evidence="ECO:0000269|PubMed:22090346"
FT MUTAGEN 519
FT /note="R->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-520; A-591; A-595; A-625 and A-626."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 520
FT /note="R->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-519; A-591; A-595; A-625 and A-626."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 523
FT /note="L->A: In mut2; Abolishes interaction with the
FT decapping machinery and localization to P-body; when
FT associated with A-527; A-530 and S-534."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 527
FT /note="E->A: In mut2; Abolishes interaction with the
FT decapping machinery and localization to P-body; when
FT associated with S-523; A-530 and S-534."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 530
FT /note="Y->A: In mut2; Abolishes interaction with the
FT decapping machinery and localization to P-body; when
FT associated with S-523; A-527 and S-534."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 534
FT /note="L->S: In mut2; Abolishes interaction with the
FT decapping machinery and localization to P-body; when
FT associated with S-523; A-527 and A-530."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 539..557
FT /note="YERRYLLSLEEERPALMDD->GSGSGSG: In mut3; does not
FT affect neither RNA-binding,interaction with the decapping
FT machinery, nor localization to P-body."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 591
FT /note="R->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-519; A-520; A-595; A-625 and A-626."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 595
FT /note="R->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-519; A-520; A-591; A-625 and A-626."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 625
FT /note="K->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-519; A-520; A-591; A-595 and A-626."
FT /evidence="ECO:0000269|PubMed:20543818"
FT MUTAGEN 626
FT /note="K->A: In mut1; Abolishes RNA-binding, localization
FT to P-body and interaction with the decapping machinery;
FT when associated with A-519; A-520; A-591; A-595 and A-625."
FT /evidence="ECO:0000269|PubMed:20543818"
FT CONFLICT 160
FT /note="Q -> H (in Ref. 2; BAG54601)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="K -> R (in Ref. 2; BAC04305 and 3; CAD89916)"
FT /evidence="ECO:0000305"
FT HELIX 518..544
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 551..570
FT /evidence="ECO:0007829|PDB:2XES"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:2XEQ"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 591..600
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 606..618
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:2XES"
FT TURN 627..630
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 637..644
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:2XES"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 683..700
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 712..727
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 743..750
FT /evidence="ECO:0007829|PDB:2XES"
FT HELIX 753..762
FT /evidence="ECO:0007829|PDB:2XES"
SQ SEQUENCE 770 AA; 86850 MW; 65F7038C4AAC356B CRC64;
MFRYESLEDC PLDEDEDAFQ GLGEEDEEID QFNDDTFGSG AVDDDWQEAH ERLAELEEKL
PVAVNEQTGN GERDEMDLLG DHEENLAERL SKMVIENELE DPAIMRAVQT RPVLQPQPGS
LNSSIWDGSE VLRRIRGPLL AQEMPTVSVL EYALPQRPPQ GPEDDRDLSE RALPRRSTSP
IIGSPPVRAV PIGTPPKQMA VPSFTQQILC PKPVHVRPPM PPRYPAPYGE RMSPNQLCSV
PNSSLLGHPF PPSVPPVLSP LQRAQLLGGA QLQPGRMSPS QFARVPGFVG SPLAAMNPKL
LQGRVGQMLP PAPGFRAFFS APPSATPPPQ QHPPGPGPHL QNLRSQAPMF RPDTTHLHPQ
HRRLLHQRQQ QNRSQHRNLN GAGDRGSHRS SHQDHLRKDP YANLMLQREK DWVSKIQMMQ
LQSTDPYLDD FYYQNYFEKL EKLSAAEEIQ GDGPKKERTK LITPQVAKLE HAYKPVQFEG
SLGKLTVSSV NNPRKMIDAV VTSRSEDDET KEKQVRDKRR KTLVIIEKTY SLLLDVEDYE
RRYLLSLEEE RPALMDDRKH KICSMYDNLR GKLPGQERPS DDHFVQIMCI RKGKRMVARI
LPFLSTEQAA DILMTTARNL PFLIKKDAQD EVLPCLLSPF SLLLYHLPSV SITSLLRQLM
NLPQSAATPA LSNPHLTAVL QNKFGLSLLL ILLSRGEDLQ SSDPATESTQ NNQWTEVMFM
ATRELLRIPQ AALAKPISIP TNLVSLFSRY VDRQKLNLLE TKLQLVQGIR
