ID PININ_HUMAN Reviewed; 717 AA. AC Q9H307; B4DZX8; O60899; Q53EM7; Q6P5X4; Q7KYL1; Q99738; Q9UHZ9; Q9UQR9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 5. DT 27-MAR-2024, entry version 181. DE RecName: Full=Pinin; DE AltName: Full=140 kDa nuclear and cell adhesion-related phosphoprotein; DE AltName: Full=Desmosome-associated protein; DE AltName: Full=Domain-rich serine protein; DE Short=DRS protein; DE Short=DRSP; DE AltName: Full=Melanoma metastasis clone A protein; DE AltName: Full=Nuclear protein SDK3; DE AltName: Full=SR-like protein; GN Name=PNN; Synonyms=DRS, MEMA; 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], PROTEIN SEQUENCE OF 44-50; 213-228 AND 537-553, RP PUTATIVE FUNCTION IN EPITHELIA MAINTENANCE, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=8922384; DOI=10.1083/jcb.135.4.1027; RA Ouyang P., Sugrue S.P.; RT "Characterization of pinin, a novel protein associated with the desmosome- RT intermediate filament complex."; RL J. Cell Biol. 135:1027-1042(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION. RX PubMed=10645008; DOI=10.1038/sj.onc.1203328; RA Shi Y., Ouyang P., Sugrue S.P.; RT "Characterization of the gene encoding pinin/DRS/memA and evidence for its RT potential tumor suppressor function."; RL Oncogene 19:289-297(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-671. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-717, VARIANT GLY-671, AND TISSUE RP SPECIFICITY. RC TISSUE=Melanoma; RX PubMed=10095061; DOI=10.1016/s0167-4781(99)00012-3; RA Degen W.G.J., Agterbos M.A., Muyrers J.P.P., Bloemers H.P.J., Swart G.W.M.; RT "memA/DRS, a putative mediator of multiprotein complexes, is overexpressed RT in the metastasizing human melanoma cell lines BLM and MV3."; RL Biochim. Biophys. Acta 1444:384-394(1999). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-717, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Keratinocyte; RX PubMed=9447706; DOI=10.1046/j.1432-0436.1997.6230119.x; RA Brandner J., Reidenbach S., Franke W.W.; RT "Evidence that 'pinin', reportedly a differentiation-specific desmosomal RT protein, is actually a widespread nuclear protein."; RL Differentiation 62:119-127(1997). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-717. RC TISSUE=Thymus; 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 [10] RP SUBCELLULAR LOCATION. RX PubMed=10486276; DOI=10.1006/bbrc.1999.1353; RA Ouyang P.; RT "Antibodies differentiate desmosome-form and nucleus-form pinin: evidence RT that pinin is a moonlighting protein with dual location at the desmosome RT and within the nucleus."; RL Biochem. Biophys. Res. Commun. 263:192-200(1999). RN [11] RP INTERACTION WITH KRT8; KRT18 AND KRT19, AND MUTAGENESIS OF LEU-8 AND RP LEU-19. RX PubMed=10809736; DOI=10.1074/jbc.275.20.14910; RA Shi J., Sugrue S.P.; RT "Dissection of protein linkage between keratins and pinin, a protein with RT dual location at desmosome-intermediate filament complex and in the RT nucleus."; RL J. Biol. Chem. 275:14910-14915(2000). RN [12] RP FUNCTION IN PRE-MRNA SPLICING, AND SUBCELLULAR LOCATION. RX PubMed=12051732; DOI=10.1016/s0006-291x(02)00495-3; RA Wang P., Lou P.-J., Leu S., Ouyang P.; RT "Modulation of alternative pre-mRNA splicing in vivo by pinin."; RL Biochem. Biophys. Res. Commun. 294:448-455(2002). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [14] RP INTERACTION WITH PS1D/PNO40. RX PubMed=12893261; DOI=10.1016/s0006-291x(03)01208-7; RA Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.; RT "Molecular characterization of a novel nucleolar protein, pNO40."; RL Biochem. Biophys. Res. Commun. 307:569-577(2003). RN [15] RP IDENTIFICATION IN A COMPLEX WITH SR PROTEINS, INTERACTION WITH PNISR; SFRS4 RP AND SRRM2, AND SUBCELLULAR LOCATION. RX PubMed=14578391; DOI=10.1167/iovs.03-0240; RA Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R., Simmons M.N., RA Shi Y., Sugrue S.P.; RT "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal RT epithelial cells."; RL Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003). RN [16] RP FUNCTION IN PRE-MRNA SPLICING, IDENTIFICATION IN A MRNP COMPLEX WITH RNPS1, RP INTERACTION WITH RNPS1, AND SUBCELLULAR LOCATION. RX PubMed=14517304; DOI=10.1128/mcb.23.20.7363-7376.2003; RA Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.; RT "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA RT processing and export via interaction with RNPS1."; RL Mol. Cell. Biol. 23:7363-7376(2003). RN [17] RP INTERACTION WITH PPIG, AND SUBCELLULAR LOCATION. RX PubMed=15358154; DOI=10.1016/j.bbrc.2004.07.013; RA Lin C.L., Leu S., Lu M.C., Ouyang P.; RT "Over-expression of SR-cyclophilin, an interaction partner of nuclear RT pinin, releases SR family splicing factors from nuclear speckles."; RL Biochem. Biophys. Res. Commun. 321:638-647(2004). RN [18] RP INTERACTION WITH RNPS1. RX PubMed=14729963; DOI=10.1128/mcb.24.3.1174-1187.2004; RA Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.; RT "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA RT splicing regulator in vivo."; RL Mol. Cell. Biol. 24:1174-1187(2004). RN [19] RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, INTERACTION WITH CTBP1 RP AND CTBP2, AND MUTAGENESIS OF 502-PRO-GLU-503. RX PubMed=15542832; DOI=10.1128/mcb.24.23.10223-10235.2004; RA Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E., RA Sugrue S.P.; RT "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional RT corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin RT gene."; RL Mol. Cell. Biol. 24:10223-10235(2004). RN [20] RP FUNCTION IN CELL-CELL ADHESION, AND SUBCELLULAR LOCATION. RX PubMed=15735603; RA Joo J.-H., Alpatov R., Munguba G.C., Jackson M.R., Hunt M.E., Sugrue S.P.; RT "Reduction of Pnn by RNAi induces loss of cell-cell adhesion between human RT corneal epithelial cells."; RL Mol. Vis. 11:133-142(2005). RN [21] RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16314458; DOI=10.1261/rna.2155905; RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.; RT "Biochemical analysis of the EJC reveals two new factors and a stable RT tetrameric protein core."; RL RNA 11:1869-1883(2005). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-347 AND SER-381, AND RP IDENTIFICATION BY 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-375 AND RP SER-552, AND 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 [26] 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 [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-96; SER-100; SER-114; RP SER-115; THR-124; SER-347; SER-381; SER-450 AND SER-552, AND IDENTIFICATION RP BY MASS SPECTROMETRY [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 [30] 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 [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-66; SER-100; SER-347; RP SER-450; SER-658; SER-692 AND SER-695, AND IDENTIFICATION BY MASS RP 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 [32] RP IDENTIFICATION IN THE PSAP COMPLEX, AND FUNCTION OF THE PSAP COMPLEX. RX PubMed=22388736; DOI=10.1038/nsmb.2242; RA Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.; RT "The structure of the ASAP core complex reveals the existence of a Pinin- RT containing PSAP complex."; RL Nat. Struct. Mol. Biol. 19:378-386(2012). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-66; SER-100; SER-347; RP SER-381; SER-450 AND SER-552, 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 [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100 AND SER-347, AND 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 [35] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109 AND LYS-157, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [38] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-157; LYS-304; LYS-528 RP AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [39] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-121; LYS-137; LYS-155; RP LYS-157; LYS-228; LYS-280; LYS-304; LYS-311; LYS-359; LYS-365; LYS-528; RP LYS-536 AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Transcriptional activator binding to the E-box 1 core CC sequence of the E-cadherin promoter gene; the core-binding sequence is CC 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription CC repression. Auxiliary component of the splicing-dependent multiprotein CC exon junction complex (EJC) deposited at splice junction on mRNAs. The CC EJC is a dynamic structure consisting of core proteins and several CC peripheral nuclear and cytoplasmic associated factors that join the CC complex only transiently either during EJC assembly or during CC subsequent mRNA metabolism. Participates in the regulation of CC alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt CC upstream of the 5'-splice sites. Component of the PSAP complex which CC binds RNA in a sequence-independent manner and is proposed to be CC recruited to the EJC prior to or during the splicing process and to CC regulate specific excision of introns in specific transcription CC subsets. Involved in the establishment and maintenance of epithelia CC cell-cell adhesion. Potential tumor suppressor for renal cell CC carcinoma. {ECO:0000269|PubMed:12051732, ECO:0000269|PubMed:14517304, CC ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15735603, CC ECO:0000269|PubMed:22388736}. CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex CC (EJC). Found in a complex with SR proteins. Found in a mRNP complex CC with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18 CC and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19, CC PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome CC C complex. {ECO:0000269|PubMed:10809736, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12893261, ECO:0000269|PubMed:14517304, CC ECO:0000269|PubMed:14578391, ECO:0000269|PubMed:14729963, CC ECO:0000269|PubMed:15358154, ECO:0000269|PubMed:15542832, CC ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:22388736}. CC -!- INTERACTION: CC Q9H307; Q9UKV3: ACIN1; NbExp=2; IntAct=EBI-681904, EBI-396258; CC Q9H307; P68400: CSNK2A1; NbExp=2; IntAct=EBI-681904, EBI-347804; CC Q9H307; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-681904, EBI-3044087; CC Q9H307; Q15287-1: RNPS1; NbExp=3; IntAct=EBI-681904, EBI-15972541; CC Q9H307; O00422: SAP18; NbExp=2; IntAct=EBI-681904, EBI-1044156; CC Q9H307; Q13573: SNW1; NbExp=3; IntAct=EBI-681904, EBI-632715; CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Cell junction, desmosome. CC Note=Cell-cell contact area, predominantly desmosome of intercellular CC adherens junction. Not a nucleocytoplasmic shuttling protein. CC -!- TISSUE SPECIFICITY: Expressed in placenta, lung, liver, kidney, CC pancreas, spleen, thymus, prostate, testis, ovary, small intestine, CC colon, heart, epidermis, esophagus, brain and smooth and skeletal CC muscle. Expressed strongly in melanoma metastasis lesions and advanced CC primary tumors. {ECO:0000269|PubMed:10095061, CC ECO:0000269|PubMed:8922384, ECO:0000269|PubMed:9447706}. CC -!- SIMILARITY: Belongs to the pinin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA70874.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U77718; AAB48304.1; -; mRNA. DR EMBL; AF195139; AAG33941.1; -; Genomic_DNA. DR EMBL; AF112222; AAF17209.1; -; mRNA. DR EMBL; AK223612; BAD97332.1; -; mRNA. DR EMBL; BC062602; AAH62602.1; -; mRNA. DR EMBL; Y09703; CAA70874.1; ALT_FRAME; mRNA. DR EMBL; Y10351; CAA71377.1; -; mRNA. DR EMBL; AK303136; BAG64240.1; -; mRNA. DR CCDS; CCDS9671.1; -. DR RefSeq; NP_002678.2; NM_002687.3. DR AlphaFoldDB; Q9H307; -. DR SMR; Q9H307; -. DR BioGRID; 111412; 286. DR ComplexPortal; CPX-2257; PSAP splicing-associated complex. DR ComplexPortal; CPX-2653; SNIP1/SkIP associated RNA-processing complex. DR CORUM; Q9H307; -. DR DIP; DIP-32950N; -. DR IntAct; Q9H307; 125. DR MINT; Q9H307; -. DR STRING; 9606.ENSP00000216832; -. DR MoonProt; Q9H307; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR GlyGen; Q9H307; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H307; -. DR MetOSite; Q9H307; -. DR PhosphoSitePlus; Q9H307; -. DR SwissPalm; Q9H307; -. DR BioMuta; PNN; -. DR DMDM; 73921750; -. DR EPD; Q9H307; -. DR jPOST; Q9H307; -. DR MassIVE; Q9H307; -. DR MaxQB; Q9H307; -. DR PaxDb; 9606-ENSP00000216832; -. DR PeptideAtlas; Q9H307; -. DR Pumba; Q9H307; -. DR Antibodypedia; 55; 303 antibodies from 32 providers. DR DNASU; 5411; -. DR Ensembl; ENST00000216832.9; ENSP00000216832.4; ENSG00000100941.9. DR GeneID; 5411; -. DR KEGG; hsa:5411; -. DR MANE-Select; ENST00000216832.9; ENSP00000216832.4; NM_002687.4; NP_002678.3. DR UCSC; uc001wuw.5; human. DR AGR; HGNC:9162; -. DR CTD; 5411; -. DR DisGeNET; 5411; -. DR GeneCards; PNN; -. DR HGNC; HGNC:9162; PNN. DR HPA; ENSG00000100941; Low tissue specificity. DR MIM; 603154; gene. DR neXtProt; NX_Q9H307; -. DR OpenTargets; ENSG00000100941; -. DR PharmGKB; PA33484; -. DR VEuPathDB; HostDB:ENSG00000100941; -. DR eggNOG; KOG3756; Eukaryota. DR GeneTree; ENSGT00730000111160; -. DR HOGENOM; CLU_025370_0_0_1; -. DR InParanoid; Q9H307; -. DR OMA; DEQKHEM; -. DR OrthoDB; 57304at2759; -. DR PhylomeDB; Q9H307; -. DR TreeFam; TF331859; -. DR PathwayCommons; Q9H307; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9H307; -. DR SIGNOR; Q9H307; -. DR BioGRID-ORCS; 5411; 673 hits in 1160 CRISPR screens. DR ChiTaRS; PNN; human. DR GeneWiki; Pinin; -. DR GenomeRNAi; 5411; -. DR Pharos; Q9H307; Tbio. DR PRO; PR:Q9H307; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9H307; Protein. DR Bgee; ENSG00000100941; Expressed in tendon of biceps brachii and 210 other cell types or tissues. DR ExpressionAtlas; Q9H307; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc. DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell. DR GO; GO:0005882; C:intermediate filament; TAS:ProtInc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR InterPro; IPR039853; Pinin. DR InterPro; IPR006786; Pinin_SDK_MemA. DR InterPro; IPR006787; Pinin_SDK_N. DR PANTHER; PTHR12707:SF0; PININ; 1. DR PANTHER; PTHR12707; PINN; 1. DR Pfam; PF04696; Pinin_SDK_memA; 1. DR Pfam; PF04697; Pinin_SDK_N; 1. DR Genevisible; Q9H307; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Cell junction; Coiled coil; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Spliceosome; Transcription; Transcription regulation; KW Tumor suppressor; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330" FT CHAIN 2..717 FT /note="Pinin" FT /id="PRO_0000190242" FT REGION 2..284 FT /note="Necessary for interaction with RNPS1" FT REGION 2..167 FT /note="Necessary for mediating alternative 5' splicing" FT REGION 2..98 FT /note="Necessary for interactions with KRT8, KRT18 and FT KRT19" FT REGION 46..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 221..284 FT /note="Sufficient for PSAP complex assembly" FT REGION 279..717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 606..717 FT /note="Necessary for interaction with PPIG" FT /evidence="ECO:0000269|PubMed:15358154" FT COILED 2..32 FT /evidence="ECO:0000255" FT COILED 163..234 FT /evidence="ECO:0000255" FT COILED 287..379 FT /evidence="ECO:0000255" FT COILED 446..467 FT /evidence="ECO:0000255" FT COMPBIAS 82..110 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..139 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 279..330 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..443 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 450..469 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 478..520 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 558..572 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..632 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..652 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 653..717 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.6, ECO:0007744|PubMed:19413330" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 54 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O35691" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 124 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 238 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 238 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:O35691" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35691" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 552 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 658 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 692 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 109 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 155 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 157 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 157 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 228 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 280 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 304 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 311 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 359 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 365 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 528 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 536 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 553 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VARIANT 671 FT /note="S -> G (in dbSNP:rs13021)" FT /evidence="ECO:0000269|PubMed:10095061, ECO:0000269|Ref.4" FT /id="VAR_023368" FT MUTAGEN 8 FT /note="L->P: Abolishes interaction with KRT18." FT /evidence="ECO:0000269|PubMed:10809736" FT MUTAGEN 19 FT /note="L->P: Abolishes interaction with KRT18." FT /evidence="ECO:0000269|PubMed:10809736" FT MUTAGEN 502..503 FT /note="PE->AA: Abolishes interaction with CTBP1 and shows FT moderate relief of CTBP1-mediated repression." FT /evidence="ECO:0000269|PubMed:15542832" FT CONFLICT 69 FT /note="Missing (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="K -> N (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="E -> D (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="Q -> H (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 320 FT /note="E -> V (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="A -> G (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 402..403 FT /note="DQ -> EE (in Ref. 2; AAG33941)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="T -> S (in Ref. 9; BAG64240 and 7; CAA70874)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="E -> D (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="P -> A (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 491..492 FT /note="QP -> EPQPQLQPEPAQPQLQSQPQLQLQSQCHA (in Ref. 1; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 497 FT /note="Q -> H (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="Q -> H (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 523 FT /note="L -> F (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="P -> T (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 543 FT /note="E -> D (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 547 FT /note="T -> I (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 550 FT /note="P -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="E -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 553..557 FT /note="KSKTK -> ESETN (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="A -> T (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 569..571 FT /note="KTS -> RTT (in Ref. 1; AAB48304)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="S -> G (in Ref. 3; AAF17209 and 8; CAA71377)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="S -> SST (in Ref. 7; CAA70874)" FT /evidence="ECO:0000305" FT CONFLICT 664 FT /note="H -> P (in Ref. 2; AAG33941)" FT /evidence="ECO:0000305" SQ SEQUENCE 717 AA; 81628 MW; 1F24D3F12E053C8F CRC64; MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE ASKELEPEME FEIEPDKECK TLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR //