SART3_HUMAN
ID SART3_HUMAN Reviewed; 963 AA.
AC Q15020; A8K2E4; B7ZKM0; Q2M2H0; Q58F06; Q8IUS1; Q96J95;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
DE Short=SART-3 {ECO:0000312|EMBL:BAA78384.1};
DE AltName: Full=Tat-interacting protein of 110 kDa {ECO:0000303|PubMed:11959860};
DE Short=Tip110 {ECO:0000303|PubMed:11959860};
DE AltName: Full=p110 nuclear RNA-binding protein {ECO:0000303|PubMed:12032085};
GN Name=SART3 {ECO:0000312|HGNC:HGNC:16860};
GN Synonyms=KIAA0156 {ECO:0000312|EMBL:BAA09929.1},
GN TIP110 {ECO:0000303|PubMed:11959860};
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=10463607;
RA Yang D., Nakao M., Shichijo S., Sasatomi T., Takasu H., Matsumoto H.,
RA Mori K., Hayashi A., Yamana H., Shirouzu K., Itoh K.;
RT "Identification of a gene coding for a protein possessing shared tumor
RT epitopes capable of inducing HLA-A24-restricted cytotoxic T lymphocytes in
RT cancer patients.";
RL Cancer Res. 59:4056-4063(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, FUNCTION, INTERACTION WITH TAT, AND REGION.
RC TISSUE=Fetal brain;
RX PubMed=11959860; DOI=10.1074/jbc.m200773200;
RA Liu Y., Li J., Kim B.O., Pace B.S., He J.J.;
RT "HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal
RT repeat promoter is potentiated by a novel nuclear Tat-interacting protein
RT of 110 kDa, Tip110.";
RL J. Biol. Chem. 277:23854-23863(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-23.
RC TISSUE=Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Eye, Skin, 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 [7]
RP FUNCTION.
RX PubMed=12032085; DOI=10.1093/emboj/21.11.2724;
RA Bell M., Schreiner S., Damianov A., Reddy R., Bindereif A.;
RT "p110, a novel human U6 snRNP protein and U4/U6 snRNP recycling factor.";
RL EMBO J. 21:2724-2735(2002).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12578909; DOI=10.1083/jcb.200210087;
RA Stanek D., Rader S.D., Klingauf M., Neugebauer K.M.;
RT "Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal
RT bodies.";
RL J. Cell Biol. 160:505-516(2003).
RN [9]
RP FUNCTION.
RX PubMed=14749385; DOI=10.1128/mcb.24.4.1700-1708.2004;
RA Damianov A., Schreiner S., Bindereif A.;
RT "Recycling of the U12-type spliceosome requires p110, a component of the
RT U6atac snRNP.";
RL Mol. Cell. Biol. 24:1700-1708(2004).
RN [10]
RP FUNCTION (ISOFORM 2), INTERACTION WITH PRPF3, AND REGION.
RX PubMed=15314151; DOI=10.1128/mcb.24.17.7392-7401.2004;
RA Medenbach J., Schreiner S., Liu S., Luhrmann R., Bindereif A.;
RT "Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the
RT function of the tetratricopeptide repeat domain in recycling.";
RL Mol. Cell. Biol. 24:7392-7401(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [13]
RP PROTEIN SEQUENCE OF 2-17; 121-130; 233-243; 295-322; 329-335; 350-356;
RP 360-370; 452-463; 494-502; 555-568; 646-669; 758-768 AND 911-918, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [14]
RP IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, AND IDENTIFICATION BY
RP 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 [16]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
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=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP FUNCTION, INTERACTION WITH PRPF3 AND USP4, AND REGION.
RX PubMed=20595234; DOI=10.1101/gad.1925010;
RA Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
RA Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
RT "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
RT reversible ubiquitination at the spliceosome.";
RL Genes Dev. 24:1434-1447(2010).
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].
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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [22]
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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-215; SER-650;
RP THR-657; SER-769 AND SER-795, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [25]
RP FUNCTION, AND INTERACTION WITH USP15.
RX PubMed=24526689; DOI=10.1074/jbc.m114.551754;
RA Long L., Thelen J.P., Furgason M., Haj-Yahya M., Brik A., Cheng D.,
RA Peng J., Yao T.;
RT "The U4/U6 recycling factor SART3 has histone chaperone activity and
RT associates with USP15 to regulate H2B deubiquitination.";
RL J. Biol. Chem. 289:8916-8930(2014).
RN [26]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-906, 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 [27]
RP STRUCTURE BY NMR OF 791-877.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain of squamous cell carcinoma
RT antigen recognized by T cells 3.";
RL Submitted (APR-2007) to the PDB data bank.
RN [28]
RP VARIANT MET-591.
RX PubMed=15840095; DOI=10.1111/j.1365-2133.2005.06443.x;
RA Zhang Z.H., Niu Z.M., Yuan W.T., Zhao J.J., Jiang F.X., Zhang J., Chai B.,
RA Cui F., Chen W., Lian C.H., Xiang L.H., Xu S.J., Liu W.D., Zheng Z.Z.,
RA Huang W.;
RT "A mutation in SART3 gene in a Chinese pedigree with disseminated
RT superficial actinic porokeratosis.";
RL Br. J. Dermatol. 152:658-663(2005).
CC -!- FUNCTION: U6 snRNP-binding protein that functions as a recycling factor
CC of the splicing machinery. Promotes the initial reassembly of U4 and U6
CC snRNPs following their ejection from the spliceosome during its
CC maturation (PubMed:12032085). Also binds U6atac snRNPs and may function
CC as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial
CC step in the assembly of U12-type spliceosomal complex. The U12-type
CC spliceosomal complex plays a role in the splicing of introns with non-
CC canonical splice sites (PubMed:14749385). May also function as a
CC substrate-targeting factor for deubiquitinases like USP4 and USP15.
CC Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP
CC complex, promoting PRPF3 deubiquitination and thereby regulating the
CC spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly
CC (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone
CC H2B and mediate histone deubiquitination, thereby regulating gene
CC expression and/or DNA repair (PubMed:24526689). May play a role in
CC hematopoiesis probably through transcription regulation of specific
CC genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8,
CC ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385,
CC ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.
CC -!- FUNCTION: Regulates Tat transactivation activity through direct
CC interaction. May be a cellular factor for HIV-1 gene expression and
CC viral replication. {ECO:0000269|PubMed:11959860}.
CC -!- SUBUNIT: Component of the 7SK snRNP complex at least composed of P-TEFb
CC (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3
CC proteins and 7SK and U6 snRNAs (PubMed:17643375). Interacts with AGO1
CC and AGO2 (PubMed:17932509). Interacts with PRPF3 and USP4; the
CC interaction with PRPF3 is direct and recruits USP4 to its substrate
CC PRPF3 (PubMed:15314151, PubMed:20595234). Interacts with USP15; the
CC interaction is direct (PubMed:24526689). Interacts with HIV-1 Tat
CC (PubMed:11959860). {ECO:0000269|PubMed:11959860,
CC ECO:0000269|PubMed:15314151, ECO:0000269|PubMed:17643375,
CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:20595234,
CC ECO:0000269|PubMed:24526689}.
CC -!- INTERACTION:
CC Q15020; Q15287: RNPS1; NbExp=5; IntAct=EBI-308619, EBI-395959;
CC Q15020; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-308619, EBI-4395669;
CC Q15020; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-308619, EBI-7138235;
CC Q15020; F5HFL9: K4; Xeno; NbExp=2; IntAct=EBI-308619, EBI-14032776;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10463607, ECO:0000269|PubMed:11959860,
CC ECO:0000269|PubMed:12578909}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:12578909}. Nucleus speckle
CC {ECO:0000269|PubMed:11959860}. Cytoplasm {ECO:0000269|PubMed:10463607,
CC ECO:0000269|PubMed:11959860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q15020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15020-2; Sequence=VSP_017250, VSP_017251;
CC Name=3;
CC IsoId=Q15020-3; Sequence=VSP_017248, VSP_017249;
CC Name=4;
CC IsoId=Q15020-4; Sequence=VSP_057284;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11959860}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. Inactive in U4/U6 snRNP recycling.
CC {ECO:0000269|PubMed:15314151}.
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DR EMBL; AB020880; BAA78384.1; -; mRNA.
DR EMBL; AF387506; AAK69347.1; -; mRNA.
DR EMBL; D63879; BAA09929.1; -; mRNA.
DR EMBL; AK290209; BAF82898.1; -; mRNA.
DR EMBL; AC008119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032601; AAH32601.1; -; mRNA.
DR EMBL; BC041638; AAH41638.1; -; mRNA.
DR EMBL; BC093784; AAH93784.1; -; mRNA.
DR EMBL; BC103706; AAI03707.1; -; mRNA.
DR EMBL; BC111983; AAI11984.1; -; mRNA.
DR EMBL; BC143253; AAI43254.1; -; mRNA.
DR CCDS; CCDS9117.1; -. [Q15020-1]
DR RefSeq; NP_055521.1; NM_014706.3. [Q15020-1]
DR PDB; 2DO4; NMR; -; A=791-877.
DR PDB; 5CTQ; X-ray; 2.60 A; A/B/C/D=94-611.
DR PDB; 5CTR; X-ray; 3.01 A; A/B=278-611.
DR PDB; 5CTT; X-ray; 1.70 A; B=601-649.
DR PDB; 5JJW; X-ray; 3.01 A; A=280-578.
DR PDB; 5JJX; X-ray; 2.00 A; A=81-393.
DR PDB; 5JPZ; X-ray; 3.04 A; A/B=96-574.
DR PDBsum; 2DO4; -.
DR PDBsum; 5CTQ; -.
DR PDBsum; 5CTR; -.
DR PDBsum; 5CTT; -.
DR PDBsum; 5JJW; -.
DR PDBsum; 5JJX; -.
DR PDBsum; 5JPZ; -.
DR AlphaFoldDB; Q15020; -.
DR SMR; Q15020; -.
DR BioGRID; 115082; 243.
DR IntAct; Q15020; 128.
DR MINT; Q15020; -.
DR STRING; 9606.ENSP00000228284; -.
DR GlyGen; Q15020; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15020; -.
DR MetOSite; Q15020; -.
DR PhosphoSitePlus; Q15020; -.
DR SwissPalm; Q15020; -.
DR BioMuta; SART3; -.
DR DMDM; 74762140; -.
DR EPD; Q15020; -.
DR jPOST; Q15020; -.
DR MassIVE; Q15020; -.
DR MaxQB; Q15020; -.
DR PaxDb; Q15020; -.
DR PeptideAtlas; Q15020; -.
DR PRIDE; Q15020; -.
DR ProteomicsDB; 60370; -. [Q15020-1]
DR ProteomicsDB; 60371; -. [Q15020-2]
DR ProteomicsDB; 60372; -. [Q15020-3]
DR ProteomicsDB; 7183; -.
DR Antibodypedia; 18276; 256 antibodies from 36 providers.
DR DNASU; 9733; -.
DR Ensembl; ENST00000431469.6; ENSP00000414453.2; ENSG00000075856.12. [Q15020-4]
DR Ensembl; ENST00000546611.1; ENSP00000448554.1; ENSG00000075856.12. [Q15020-3]
DR Ensembl; ENST00000546728.5; ENSP00000449743.1; ENSG00000075856.12. [Q15020-2]
DR Ensembl; ENST00000546815.6; ENSP00000449386.2; ENSG00000075856.12. [Q15020-1]
DR GeneID; 9733; -.
DR KEGG; hsa:9733; -.
DR MANE-Select; ENST00000546815.6; ENSP00000449386.2; NM_014706.4; NP_055521.1.
DR UCSC; uc001tmz.2; human. [Q15020-1]
DR CTD; 9733; -.
DR DisGeNET; 9733; -.
DR GeneCards; SART3; -.
DR HGNC; HGNC:16860; SART3.
DR HPA; ENSG00000075856; Low tissue specificity.
DR MIM; 611684; gene.
DR neXtProt; NX_Q15020; -.
DR OpenTargets; ENSG00000075856; -.
DR PharmGKB; PA34948; -.
DR VEuPathDB; HostDB:ENSG00000075856; -.
DR eggNOG; KOG0128; Eukaryota.
DR GeneTree; ENSGT00900000141107; -.
DR HOGENOM; CLU_007172_0_0_1; -.
DR InParanoid; Q15020; -.
DR OrthoDB; 867827at2759; -.
DR PhylomeDB; Q15020; -.
DR TreeFam; TF317554; -.
DR PathwayCommons; Q15020; -.
DR SignaLink; Q15020; -.
DR BioGRID-ORCS; 9733; 770 hits in 1094 CRISPR screens.
DR ChiTaRS; SART3; human.
DR EvolutionaryTrace; Q15020; -.
DR GeneWiki; SART3; -.
DR GenomeRNAi; 9733; -.
DR Pharos; Q15020; Tbio.
DR PRO; PR:Q15020; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15020; protein.
DR Bgee; ENSG00000075856; Expressed in endothelial cell and 211 other tissues.
DR ExpressionAtlas; Q15020; baseline and differential.
DR Genevisible; Q15020; HS.
DR GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR GO; GO:0030624; F:U6atac snRNA binding; IDA:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:1903586; P:positive regulation of histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
DR CDD; cd12391; RRM1_SART3; 1.
DR CDD; cd12392; RRM2_SART3; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR008669; LSM_interact.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034217; SART3_RRM1.
DR InterPro; IPR034218; SART3_RRM2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF05391; Lsm_interact; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..963
FT /note="Squamous cell carcinoma antigen recognized by T-
FT cells 3"
FT /id="PRO_0000223313"
FT REPEAT 126..158
FT /note="HAT 1"
FT REPEAT 164..195
FT /note="HAT 2"
FT REPEAT 201..237
FT /note="HAT 3"
FT REPEAT 242..275
FT /note="HAT 4"
FT REPEAT 324..356
FT /note="HAT 5"
FT REPEAT 359..391
FT /note="HAT 6"
FT REPEAT 394..430
FT /note="HAT 7"
FT REPEAT 487..520
FT /note="HAT 8"
FT DOMAIN 704..782
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 801..878
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..351
FT /note="Mediates interaction with PRPF3"
FT /evidence="ECO:0000269|PubMed:15314151"
FT REGION 50..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..520
FT /note="Required for interaction with USP4"
FT /evidence="ECO:0000269|PubMed:20595234"
FT REGION 537..953
FT /note="Necessary and sufficient for U6 snRNA binding"
FT /evidence="ECO:0000269|PubMed:15314151"
FT REGION 590..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..670
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:11959860"
FT REGION 878..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..46
FT /evidence="ECO:0000255"
FT COILED 82..110
FT /evidence="ECO:0000255"
FT COILED 559..619
FT /evidence="ECO:0000255"
FT MOTIF 601..617
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 906
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 105..129
FT /note="LSINVYDYNCHVDLIRLLRLEGELT -> VGPGVGSGHLPVFQVLGSPCPGP
FT PP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017248"
FT VAR_SEQ 130..963
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017249"
FT VAR_SEQ 351..364
FT /note="SQYLDRQLKVKDLV -> RSTTESKGFGFICT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11959860"
FT /id="VSP_017250"
FT VAR_SEQ 365..963
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11959860"
FT /id="VSP_017251"
FT VAR_SEQ 401..436
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057284"
FT VARIANT 23
FT /note="D -> E (in dbSNP:rs2072579)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_038802"
FT VARIANT 591
FT /note="V -> M (found in a patient with disseminated
FT superficial actinic porokeratosis; unknown pathological
FT significance; dbSNP:rs118203954)"
FT /evidence="ECO:0000269|PubMed:15840095"
FT /id="VAR_038683"
FT VARIANT 621
FT /note="E -> D (in dbSNP:rs2287546)"
FT /id="VAR_038684"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:5JJX"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:5JJX"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:5JJX"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 279..304
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:5JJX"
FT HELIX 396..409
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 414..429
FT /evidence="ECO:0007829|PDB:5CTQ"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5JJW"
FT HELIX 440..457
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 473..484
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 489..501
FT /evidence="ECO:0007829|PDB:5CTQ"
FT TURN 502..506
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 508..521
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 524..537
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 542..556
FT /evidence="ECO:0007829|PDB:5CTQ"
FT HELIX 559..603
FT /evidence="ECO:0007829|PDB:5CTQ"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:2DO4"
FT HELIX 814..821
FT /evidence="ECO:0007829|PDB:2DO4"
FT TURN 822..824
FT /evidence="ECO:0007829|PDB:2DO4"
FT STRAND 827..834
FT /evidence="ECO:0007829|PDB:2DO4"
FT STRAND 840..850
FT /evidence="ECO:0007829|PDB:2DO4"
FT HELIX 851..861
FT /evidence="ECO:0007829|PDB:2DO4"
FT STRAND 864..868
FT /evidence="ECO:0007829|PDB:2DO4"
FT STRAND 870..875
FT /evidence="ECO:0007829|PDB:2DO4"
SQ SEQUENCE 963 AA; 109935 MW; 06B26CEB8B19102A CRC64;
MATAAETSAS EPEAESKAGP KADGEEDEVK AARTRRKVLS RAVAAATYKT MGPAWDQQEE
GVSESDGDEY AMASSAESSP GEYEWEYDEE EEKNQLEIER LEEQLSINVY DYNCHVDLIR
LLRLEGELTK VRMARQKMSE IFPLTEELWL EWLHDEISMA QDGLDREHVY DLFEKAVKDY
ICPNIWLEYG QYSVGGIGQK GGLEKVRSVF ERALSSVGLH MTKGLALWEA YREFESAIVE
AARLEKVHSL FRRQLAIPLY DMEATFAEYE EWSEDPIPES VIQNYNKALQ QLEKYKPYEE
ALLQAEAPRL AEYQAYIDFE MKIGDPARIQ LIFERALVEN CLVPDLWIRY SQYLDRQLKV
KDLVLSVHNR AIRNCPWTVA LWSRYLLAME RHGVDHQVIS VTFEKALNAG FIQATDYVEI
WQAYLDYLRR RVDFKQDSSK ELEELRAAFT RALEYLKQEV EERFNESGDP SCVIMQNWAR
IEARLCNNMQ KARELWDSIM TRGNAKYANM WLEYYNLERA HGDTQHCRKA LHRAVQCTSD
YPEHVCEVLL TMERTEGSLE DWDIAVQKTE TRLARVNEQR MKAAEKEAAL VQQEEEKAEQ
RKRARAEKKA LKKKKKIRGP EKRGADEDDE KEWGDDEEEQ PSKRRRVENS IPAAGETQNV
EVAAGPAGKC AAVDVEPPSK QKEKAASLKR DMPKVLHDSS KDSITVFVSN LPYSMQEPDT
KLRPLFEACG EVVQIRPIFS NRGDFRGYCY VEFKEEKSAL QALEMDRKSV EGRPMFVSPC
VDKSKNPDFK VFRYSTSLEK HKLFISGLPF SCTKEELEEI CKAHGTVKDL RLVTNRAGKP
KGLAYVEYEN ESQASQAVMK MDGMTIKENI IKVAISNPPQ RKVPEKPETR KAPGGPMLLP
QTYGARGKGR TQLSLLPRAL QRPSAAAPQA ENGPAAAPAV AAPAATEAPK MSNADFAKLF
LRK
