ID PININ_HUMAN Reviewed; 717 AA. AC Q9H307; B4DZX8; O60899; Q53EM7; Q6P5X4; Q7KYL1; Q99738; Q9UHZ9; AC Q9UQR9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 14-MAY-2014, entry version 110. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 44-50; RP 213-228 AND 537-553, PUTATIVE FUNCTION IN EPITHELIA MAINTENANCE, RP SUBCELLULAR LOCATION, AND 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 RT desmosome-intermediate filament complex."; RL J. Cell Biol. 135:1027-1042(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), 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., RA Swart G.W.M.; RT "memA/DRS, a putative mediator of multiprotein complexes, is RT overexpressed in the metastasizing human melanoma cell lines BLM and RT MV3."; RL Biochim. Biophys. Acta 1444:384-394(1999). RN [3] 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 RT its potential tumor suppressor function."; RL Oncogene 19:289-297(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-717 (ISOFORM 1), SUBCELLULAR LOCATION, RP AND TISSUE 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 RT desmosomal protein, is actually a widespread nuclear protein."; RL Differentiation 62:119-127(1997). RN [9] RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT 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 [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: RT evidence that pinin is a moonlighting protein with dual location at RT the desmosome 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 RT with dual location at desmosome-intermediate filament complex and in RT the 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 RP SPLICEOSOMAL 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; RP SFRS4 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., RA Simmons M.N., 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 RP RNPS1, 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 RT mRNA 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- RT mRNA splicing regulator in vivo."; RL Mol. Cell. Biol. 24:1174-1187(2004). RN [19] RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, INTERACTION WITH RP CTBP1 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., RA Hunt M.E., Sugrue S.P.; RT "Nuclear speckle-associated protein Pnn/DRS binds to the RT transcriptional corepressor CtBP and relieves CtBP-mediated repression RT of the E-cadherin gene."; RL Mol. Cell. Biol. 24:10223-10235(2004). RN [20] RP FUNCTION IN CELL-CELL ADHESION, AND SUBCELLULAR LOCATION. RX PubMed=15735603; DOI=1v11/a15; RA Joo J.-H., Alpatov R., Munguba G.C., Jackson M.R., Hunt M.E., RA Sugrue S.P.; RT "Reduction of Pnn by RNAi induces loss of cell-cell adhesion between RT human 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 RP SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION RP BY 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 RT phosphorylation 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, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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; RP SER-443; SER-450 AND SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-443, AND 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 [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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; RP SER-114; SER-115; THR-124; SER-347; SER-381; SER-443; SER-450 AND RP SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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; RP SER-347; SER-381; SER-450; SER-658; SER-692 AND SER-695, 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [32] RP IDENTIFICATION IN THE PSAP COMPLEX, AND FUNCTION OIF 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 RT Pinin-containing PSAP complex."; RL Nat. Struct. Mol. Biol. 19:378-386(2012). CC -!- FUNCTION: Transcriptional activator binding to the E-box 1 core CC sequence of the E-cadherin promoter gene; the core-binding CC sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated CC transcription repression. Auxiliary component of the splicing- CC dependent multiprotein exon junction complex (EJC) deposited at CC splice junction on mRNAs. The EJC is a dynamic structure CC consisting of core proteins and several peripheral nuclear and CC cytoplasmic associated factors that join the complex only CC transiently either during EJC assembly or during subsequent mRNA CC metabolism. Participates in the regulation of alternative pre-mRNA CC splicing. Associates to spliced mRNA within 60 nt upstream of the CC 5'-splice sites. Component of the PSAP complex which binds RNA in CC a sequence-independent manner and is proposed to be recruited to CC the EJC prior to or during the splicing process and to regulate CC specific excision of introns in specific transcription subsets. CC Involved in the establishment and maintenance of epithelia cell- CC cell adhesion. Potential tumor suppressor for renal cell CC carcinoma. CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex CC (EJC). Found in a complex with SR proteins. Found in a mRNP CC complex with RNPS1. Component of the PSAP complex consisting of CC RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, CC KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified CC in the spliceosome C complex. CC -!- INTERACTION: CC Q9UBC1:NFKBIL1; NbExp=1; IntAct=EBI-681904, EBI-1043728; CC Q15287:RNPS1; NbExp=1; IntAct=EBI-681904, EBI-395959; CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Cell junction, desmosome. CC Note=Cell-cell contact area, predominantly desmosome of CC intercellular adherens junction. Not a nucleocytoplasmic shuttling CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H307-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H307-2; Sequence=VSP_015307; CC -!- TISSUE SPECIFICITY: Expressed in placenta, lung, liver, kidney, CC pancreas, spleen, thymus, prostate, testis, ovary, small CC intestine, colon, heart, epidermis, esophagus, brain and smooth CC and skeletal muscle. Expressed strongly in melanoma metastasis CC lesions and advanced primary tumors. CC -!- SIMILARITY: Belongs to the pinin family. 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; Y09703; CAA70874.1; -; mRNA. DR EMBL; AF195139; AAG33941.1; -; Genomic_DNA. DR EMBL; AF112222; AAF17209.1; -; mRNA. DR EMBL; AK303136; BAG64240.1; -; mRNA. DR EMBL; AK223612; BAD97332.1; -; mRNA. DR EMBL; BC062602; AAH62602.1; -; mRNA. DR EMBL; Y10351; CAA71377.1; -; mRNA. DR RefSeq; NP_002678.2; NM_002687.3. [Q9H307-1] DR UniGene; Hs.409965; -. DR ProteinModelPortal; Q9H307; -. DR BioGrid; 111412; 35. DR DIP; DIP-32950N; -. DR IntAct; Q9H307; 25. DR MINT; MINT-1683388; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR PhosphoSite; Q9H307; -. DR DMDM; 73921750; -. DR MaxQB; Q9H307; -. DR PaxDb; Q9H307; -. DR PRIDE; Q9H307; -. DR Ensembl; ENST00000216832; ENSP00000216832; ENSG00000100941. DR GeneID; 5411; -. DR KEGG; hsa:5411; -. DR UCSC; uc001wuw.4; human. [Q9H307-1] DR CTD; 5411; -. DR GeneCards; GC14P039644; -. DR H-InvDB; HIX0037750; -. DR HGNC; HGNC:9162; PNN. DR HPA; HPA001378; -. DR MIM; 603154; gene. DR neXtProt; NX_Q9H307; -. DR PharmGKB; PA33484; -. DR eggNOG; NOG249368; -. DR HOVERGEN; HBG053104; -. DR InParanoid; Q9H307; -. DR KO; K13114; -. DR OrthoDB; EOG7DC25H; -. DR PhylomeDB; Q9H307; -. DR TreeFam; TF331859; -. DR ChiTaRS; PNN; human. DR GeneWiki; Pinin; -. DR GenomeRNAi; 5411; -. DR NextBio; 20949; -. DR PRO; PR:Q9H307; -. DR ArrayExpress; Q9H307; -. DR Bgee; Q9H307; -. DR CleanEx; HS_PNN; -. DR Genevestigator; Q9H307; -. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell. DR GO; GO:0005882; C:intermediate filament; TAS:ProtInc. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR006786; Pinin_SDK_MemA. DR InterPro; IPR006787; Pinin_SDK_N. DR Pfam; PF04696; Pinin_SDK_memA; 1. DR Pfam; PF04697; Pinin_SDK_N; 1. DR ProDom; PD011048; Pinin_SDK_N; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Cell junction; KW Coiled coil; Complete proteome; Direct protein sequencing; KW DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Spliceosome; Transcription; KW Transcription regulation; Tumor suppressor. FT INIT_MET 1 1 Removed. FT CHAIN 2 717 Pinin. FT /FTId=PRO_0000190242. FT REGION 2 284 Necessary for interaction with RNPS1. FT REGION 2 167 Necessary for mediating alternative 5' FT splicing. FT REGION 2 98 Necessary for interactions with KRT8, FT KRT18 and KRT19. FT REGION 221 284 Sufficient for PSAP complex assembly. FT REGION 606 717 Necessary for interaction with PPIG. FT COILED 2 32 Potential. FT COILED 163 234 Potential. FT COILED 287 379 Potential. FT COILED 446 467 Potential. FT COMPBIAS 172 471 Glu-rich. FT COMPBIAS 469 520 Gln-rich. FT COMPBIAS 552 704 Ser-rich. FT COMPBIAS 632 717 Arg-rich. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 58 58 Phosphoserine. FT MOD_RES 66 66 Phosphoserine. FT MOD_RES 96 96 Phosphoserine. FT MOD_RES 100 100 Phosphoserine. FT MOD_RES 114 114 Phosphoserine. FT MOD_RES 115 115 Phosphoserine. FT MOD_RES 124 124 Phosphothreonine. FT MOD_RES 238 238 N6-acetyllysine; alternate. FT MOD_RES 238 238 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 347 347 Phosphoserine. FT MOD_RES 375 375 Phosphoserine. FT MOD_RES 381 381 Phosphoserine. FT MOD_RES 443 443 Phosphoserine. FT MOD_RES 450 450 Phosphoserine. FT MOD_RES 552 552 Phosphoserine. FT MOD_RES 658 658 Phosphoserine. FT MOD_RES 692 692 Phosphoserine. FT MOD_RES 695 695 Phosphoserine. FT VAR_SEQ 1 133 Missing (in isoform 2). FT /FTId=VSP_015307. FT VARIANT 441 441 S -> T (in dbSNP:rs2180792). FT /FTId=VAR_050540. FT VARIANT 671 671 S -> G (in dbSNP:rs13021). FT /FTId=VAR_023368. FT MUTAGEN 8 8 L->P: Abolishes interaction with KRT18. FT MUTAGEN 19 19 L->P: Abolishes interaction with KRT18. FT MUTAGEN 502 503 PE->AA: Abolishes interaction with CTBP1 FT and shows moderate relief of CTBP1- FT mediated repression. FT CONFLICT 69 69 Missing (in Ref. 1; AAB48304). FT CONFLICT 168 168 K -> N (in Ref. 1; AAB48304). FT CONFLICT 268 268 E -> D (in Ref. 1; AAB48304). FT CONFLICT 303 303 Q -> H (in Ref. 1; AAB48304). FT CONFLICT 320 320 E -> V (in Ref. 1; AAB48304). FT CONFLICT 343 343 A -> G (in Ref. 1; AAB48304). FT CONFLICT 402 403 DQ -> EE (in Ref. 3; AAG33941). FT CONFLICT 459 459 E -> D (in Ref. 1; AAB48304). FT CONFLICT 478 478 P -> A (in Ref. 1; AAB48304). FT CONFLICT 491 492 QP -> EPQPQLQPEPAQPQLQSQPQLQLQSQCHA (in FT Ref. 1; AA sequence). FT CONFLICT 497 497 Q -> H (in Ref. 1; AAB48304). FT CONFLICT 520 520 Q -> H (in Ref. 1; AAB48304). FT CONFLICT 523 523 L -> F (in Ref. 1; AAB48304). FT CONFLICT 541 541 P -> T (in Ref. 1; AA sequence). FT CONFLICT 543 543 E -> D (in Ref. 1; AAB48304). FT CONFLICT 547 547 T -> I (in Ref. 1; AA sequence). FT CONFLICT 550 550 P -> S (in Ref. 1; AA sequence). FT CONFLICT 551 551 E -> D (in Ref. 1; AA sequence). FT CONFLICT 553 557 KSKTK -> ESETN (in Ref. 1; AAB48304). FT CONFLICT 566 566 A -> T (in Ref. 1; AAB48304). FT CONFLICT 569 571 KTS -> RTT (in Ref. 1; AAB48304). FT CONFLICT 618 618 S -> G (in Ref. 4; AAF17209 and 8; FT CAA71377). FT CONFLICT 626 626 S -> STS (in Ref. 2; CAA70874). FT CONFLICT 664 664 H -> P (in Ref. 3; AAG33941). SQ SEQUENCE 717 AA; 81614 MW; 1C05E1E12F54299F 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 SLSPGKENVS 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 //