ID SDCB1_HUMAN Reviewed; 298 AA. AC O00560; B2R5Q7; B4DUH3; B7ZLN2; O00173; O43391; Q14CP2; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 224. DE RecName: Full=Syntenin-1; DE AltName: Full=Melanoma differentiation-associated protein 9; DE Short=MDA-9; DE AltName: Full=Pro-TGF-alpha cytoplasmic domain-interacting protein 18; DE Short=TACIP18; DE AltName: Full=Scaffold protein Pbp1; DE AltName: Full=Syndecan-binding protein 1; GN Name=SDCBP; Synonyms=MDA9, SYCL; 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). RA Lin J.J., Jiang H., Fisher P.B.; RT "Characterization of a novel melanoma differentiation associated gene, mda- RT 9, that is down-regulated during terminal cell differentiation."; RL Mol. Cell. Differ. 4:317-333(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SDC2, AND VARIANT RP SER-69. RX PubMed=9391086; DOI=10.1073/pnas.94.25.13683; RA Grootjans J.J., Zimmermann P., Reekmans G., Smets A., Degeest G., Duerr J., RA David G.; RT "Syntenin, a PDZ protein that binds syndecan cytoplasmic domains."; RL Proc. Natl. Acad. Sci. U.S.A. 94:13683-13688(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Burbelo P.D.; RT "A new family of scaffold proteins."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9511750; DOI=10.1016/s0378-1119(97)00562-3; RA Lin J.J., Jiang H., Fisher P.B.; RT "Melanoma differentiation associated gene-9, mda-9, is a human gamma RT interferon responsive gene."; RL Gene 207:105-110(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Rectum, and Urinary bladder; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 [9] RP PROTEIN SEQUENCE OF 2-14; 218-229 AND 289-298, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Pre-B cell; RA Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W.; RL Submitted (FEB-2009) to UniProtKB. RN [10] RP INTERACTION WITH EPHB1 AND EPHA7. RX PubMed=9883737; DOI=10.1016/s0896-6273(00)80663-7; RA Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., RA Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.; RT "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors RT and their ephrin ligands."; RL Neuron 21:1453-1463(1998). RN [11] RP FUNCTION, AND INTERACTION WITH TGFA. RX PubMed=10230395; DOI=10.1016/s1097-2765(00)80470-0; RA Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.; RT "A role for a PDZ protein in the early secretory pathway for the targeting RT of proTGF-alpha to the cell surface."; RL Mol. Cell 3:423-433(1999). RN [12] RP INTERACTION WITH SYNDECANS; NRXN2 AND EPHB1. RX PubMed=10770943; DOI=10.1074/jbc.m002459200; RA Grootjans J.J., Reekmans G., Ceulemans H., David G.; RT "Syntenin-syndecan binding requires syndecan-synteny and the co-operation RT of both PDZ domains of syntenin."; RL J. Biol. Chem. 275:19933-19941(2000). RN [13] RP INTERACTION WITH SDCBP2. RC TISSUE=Fetal brain; RX PubMed=11152476; DOI=10.1074/jbc.m010647200; RA Koroll M., Rathjen F.G., Volkmer H.; RT "The neural cell recognition molecule neurofascin interacts with syntenin-1 RT but not with syntenin-2, both of which reveal self-associating activity."; RL J. Biol. Chem. 276:10646-10654(2001). RN [14] RP INTERACTION WITH NF2. RX PubMed=11432873; DOI=10.1074/jbc.m105792200; RA Jannatipour M., Dion P., Khan S., Jindal H., Fan X., Laganiere J., RA Chishti A.H., Rouleau G.A.; RT "Schwannomin isoform-1 interacts with syntenin via PDZ domains."; RL J. Biol. Chem. 276:33093-33100(2001). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11179419; DOI=10.1091/mbc.12.2.339; RA Zimmermann P., Tomatis D., Rosas M., Grootjans J.J., Leenaerts I., RA Degeest G., Reekmans G., Coomans C., David G.; RT "Characterization of syntenin, a syndecan-binding PDZ protein, as a RT component of cell adhesion sites and microfilaments."; RL Mol. Biol. Cell 12:339-350(2001). RN [16] RP FUNCTION, AND INTERACTION WITH IL5RA. RX PubMed=11498591; DOI=10.1126/science.1059157; RA Geijsen N., Uings I.J., Pals C., Armstrong J., McKinnon M., RA Raaijmakers J.A.M., Lammers J.-W., Koenderman L., Coffer P.J.; RT "Cytokine-specific transcriptional regulation through an IL-5Ralpha RT interacting protein."; RL Science 293:1136-1138(2001). RN [17] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., RA Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [18] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6IP. RX PubMed=22660413; DOI=10.1038/ncb2502; RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A., RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P., RA David G.; RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes."; RL Nat. Cell Biol. 14:677-685(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-46, AND IDENTIFICATION BY RP 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 [24] RP REVIEW. RX PubMed=26032692; DOI=10.1111/boc.201500010; RA Friand V., David G., Zimmermann P.; RT "Syntenin and syndecan in the biogenesis of exosomes."; RL Biol. Cell 107:331-341(2015). RN [25] RP REVIEW. RX PubMed=25219541; DOI=10.1517/14728222.2014.959495; RA Kegelman T.P., Das S.K., Emdad L., Hu B., Menezes M.E., Bhoopathi P., RA Wang X.Y., Pellecchia M., Sarkar D., Fisher P.B.; RT "Targeting tumor invasion: the roles of MDA-9/Syntenin."; RL Expert Opin. Ther. Targets 19:97-112(2015). RN [26] RP FUNCTION. RX PubMed=26539120; DOI=10.3389/fphar.2015.00241; RA Kashyap R., Roucourt B., Lembo F., Fares J., Carcavilla A.M., Restouin A., RA Zimmermann P., Ghossoub R.; RT "Syntenin controls migration, growth, proliferation, and cell cycle RT progression in cancer cells."; RL Front. Pharmacol. 6:241-241(2015). RN [27] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFBR1, AND TISSUE RP SPECIFICITY. RX PubMed=25893292; DOI=10.1038/onc.2015.100; RA Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.; RT "Syntenin regulates TGF-beta1-induced Smad activation and the epithelial- RT to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I RT receptor internalization."; RL Oncogene 35:389-401(2016). RN [28] RP REVIEW, AND FUNCTION. RX PubMed=26291527; DOI=10.1002/jcp.25136; RA Philley J.V., Kannan A., Dasgupta S.; RT "MDA-9/syntenin control."; RL J. Cell. Physiol. 231:545-550(2016). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 113-273. RX PubMed=12679023; DOI=10.1016/s0969-2126(03)00052-2; RA Kang B.S., Cooper D.R., Jelen F., Devedjiev Y., Derewenda U., Dauter Z., RA Otlewski J., Derewenda Z.S.; RT "PDZ tandem of human syntenin: crystal structure and functional RT properties."; RL Structure 11:459-468(2003). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 197-270 IN COMPLEXES WITH IL5RA RP AND SDC4. RX PubMed=12842047; DOI=10.1016/s0969-2126(03)00125-4; RA Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.; RT "Molecular roots of degenerate specificity in syntenin's PDZ2 domain: RT reassessment of the PDZ recognition paradigm."; RL Structure 11:845-853(2003). RN [31] RP X-RAY CRYSTALLOGRAPHY (0.73 ANGSTROMS) OF 197-273. RX PubMed=15081807; DOI=10.1016/j.jmb.2004.02.057; RA Kang B.S., Devedjiev Y., Derewenda U., Derewenda Z.S.; RT "The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap RT between macromolecular and small molecule crystallography."; RL J. Mol. Biol. 338:483-493(2004). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 113-273 IN COMPLEXES WITH RP C-TERMINAL PEPTIDES FROM NEUREXIN; EPHB1 AND SDC4. RX PubMed=16533050; DOI=10.1021/bi052225y; RA Grembecka J., Cierpicki T., Devedjiev Y., Derewenda U., Kang B.S., RA Bushweller J.H., Derewenda Z.S.; RT "The binding of the PDZ tandem of syntenin to target proteins."; RL Biochemistry 45:3674-3683(2006). RN [33] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 111-275 IN COMPLEXES WITH RP C-TERMINAL PEPTIDES FROM FZD7 AND INOSITOL BISPHOSPHATE, INTERACTION WITH RP FZD7, MUTAGENESIS OF LYS-214; ASN-215 AND LYS-250, AND SUBCELLULAR RP LOCATION. RX PubMed=27386966; DOI=10.1038/ncomms12101; RA Egea-Jimenez A.L., Gallardo R., Garcia-Pino A., Ivarsson Y., RA Wawrzyniak A.M., Kashyap R., Loris R., Schymkowitz J., Rousseau F., RA Zimmermann P.; RT "Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 RT trafficking and signalling."; RL Nat. Commun. 7:12101-12101(2016). CC -!- FUNCTION: Multifunctional adapter protein involved in diverse array of CC functions including trafficking of transmembrane proteins, neuro and CC immunomodulation, exosome biogenesis, and tumorigenesis CC (PubMed:26291527). Positively regulates TGFB1-mediated SMAD2/3 CC activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) CC and cell migration in various cell types. May increase TGFB1 signaling CC by enhancing cell-surface expression of TGFR1 by preventing the CC interaction between TGFR1 and CAV1 and subsequent CAV1-dependent CC internalization and degradation of TGFR1 (PubMed:25893292). In concert CC with SDC1/4 and PDCD6IP, regulates exosome biogenesis CC (PubMed:22660413). Regulates migration, growth, proliferation, and cell CC cycle progression in a variety of cancer types (PubMed:26539120). In CC adherens junctions may function to couple syndecans to cytoskeletal CC proteins or signaling components. Seems to couple transcription factor CC SOX4 to the IL-5 receptor (IL5RA) (PubMed:11498591). May also play a CC role in vesicular trafficking (PubMed:11179419). Seems to be required CC for the targeting of TGFA to the cell surface in the early secretory CC pathway (PubMed:10230395). {ECO:0000269|PubMed:10230395, CC ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:11498591, CC ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:25893292, CC ECO:0000269|PubMed:26539120, ECO:0000303|PubMed:26291527}. CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with SDC1, CC SDC2, SDC3, SDC4, NRXN2, EPHA7, EPHB1, NF2 isoform 1, TGFA and IL5RA. CC Interacts with NFASC and PTPRJ (By similarity). Interacts with SDCBP2 CC (PubMed:11152476). Interacts with PDCD6IP (PubMed:22660413). Forms a CC complex with PDCD6IP and SDC2 (PubMed:22660413). Interacts (via C- CC terminus) with TGFBR1 (PubMed:25893292). Binds to FZD7; this CC interaction is increased by inositol trisphosphate (IP3) CC (PubMed:27386966). Interacts with SMO (By similarity). CC {ECO:0000250|UniProtKB:O08992, ECO:0000250|UniProtKB:Q9JI92, CC ECO:0000269|PubMed:11152476, ECO:0000269|PubMed:22660413, CC ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:27386966}. CC -!- INTERACTION: CC O00560; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-727004, EBI-743598; CC O00560; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-727004, EBI-8643161; CC O00560; Q7Z3H0-1: ANKRD33; NbExp=3; IntAct=EBI-727004, EBI-16746154; CC O00560; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-727004, EBI-12170453; CC O00560; Q6AI12: ANKRD40; NbExp=3; IntAct=EBI-727004, EBI-2838246; CC O00560; Q92688: ANP32B; NbExp=6; IntAct=EBI-727004, EBI-762428; CC O00560; Q96GX9: APIP; NbExp=5; IntAct=EBI-727004, EBI-359248; CC O00560; P53365: ARFIP2; NbExp=3; IntAct=EBI-727004, EBI-638194; CC O00560; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-727004, EBI-714543; CC O00560; P54253: ATXN1; NbExp=6; IntAct=EBI-727004, EBI-930964; CC O00560; Q5TBC7: BCL2L15; NbExp=3; IntAct=EBI-727004, EBI-10247136; CC O00560; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-727004, EBI-10181188; CC O00560; Q9H3H3: C11orf68; NbExp=3; IntAct=EBI-727004, EBI-721765; CC O00560; Q9H3H3-3: C11orf68; NbExp=3; IntAct=EBI-727004, EBI-12002214; CC O00560; O14523: C2CD2L; NbExp=3; IntAct=EBI-727004, EBI-12822627; CC O00560; Q9NP86: CABP5; NbExp=3; IntAct=EBI-727004, EBI-10311131; CC O00560; A2RRN7: CADPS; NbExp=3; IntAct=EBI-727004, EBI-10179719; CC O00560; Q9ULU8-4: CADPS; NbExp=3; IntAct=EBI-727004, EBI-10180690; CC O00560; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-727004, EBI-739580; CC O00560; P51636: CAV2; NbExp=3; IntAct=EBI-727004, EBI-603607; CC O00560; O75828: CBR3; NbExp=8; IntAct=EBI-727004, EBI-714504; CC O00560; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-727004, EBI-10171570; CC O00560; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-727004, EBI-711501; CC O00560; P32320: CDA; NbExp=6; IntAct=EBI-727004, EBI-9250559; CC O00560; P49427: CDC34; NbExp=6; IntAct=EBI-727004, EBI-975634; CC O00560; Q9H5V8: CDCP1; NbExp=6; IntAct=EBI-727004, EBI-1019736; CC O00560; O14735: CDIPT; NbExp=3; IntAct=EBI-727004, EBI-358858; CC O00560; P55273: CDKN2D; NbExp=3; IntAct=EBI-727004, EBI-745859; CC O00560; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-727004, EBI-747776; CC O00560; Q6P2H3-3: CEP85; NbExp=3; IntAct=EBI-727004, EBI-12368239; CC O00560; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-727004, EBI-723153; CC O00560; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-727004, EBI-741528; CC O00560; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-727004, EBI-1057156; CC O00560; P49760: CLK2; NbExp=3; IntAct=EBI-727004, EBI-750020; CC O00560; P49761: CLK3; NbExp=6; IntAct=EBI-727004, EBI-745579; CC O00560; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-727004, EBI-2548702; CC O00560; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-727004, EBI-11522780; CC O00560; P13073: COX4I1; NbExp=4; IntAct=EBI-727004, EBI-1056574; CC O00560; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-727004, EBI-10260134; CC O00560; O43186: CRX; NbExp=3; IntAct=EBI-727004, EBI-748171; CC O00560; P02489: CRYAA; NbExp=7; IntAct=EBI-727004, EBI-6875961; CC O00560; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-727004, EBI-12051833; CC O00560; P0DMU9: CT45A10; NbExp=6; IntAct=EBI-727004, EBI-12153495; CC O00560; Q8NHU0: CT45A3; NbExp=9; IntAct=EBI-727004, EBI-8643558; CC O00560; Q6NSH3: CT45A5; NbExp=3; IntAct=EBI-727004, EBI-8635816; CC O00560; P56545-3: CTBP2; NbExp=3; IntAct=EBI-727004, EBI-10171902; CC O00560; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-727004, EBI-751587; CC O00560; Q9NTM9: CUTC; NbExp=6; IntAct=EBI-727004, EBI-714918; CC O00560; P32321: DCTD; NbExp=6; IntAct=EBI-727004, EBI-739870; CC O00560; Q9H773: DCTPP1; NbExp=3; IntAct=EBI-727004, EBI-723569; CC O00560; Q13838: DDX39B; NbExp=3; IntAct=EBI-727004, EBI-348622; CC O00560; Q96Q80: DERL3; NbExp=3; IntAct=EBI-727004, EBI-12831318; CC O00560; Q14565: DMC1; NbExp=7; IntAct=EBI-727004, EBI-930865; CC O00560; G5E9A7: DMWD; NbExp=3; IntAct=EBI-727004, EBI-10976677; CC O00560; P50570: DNM2; NbExp=3; IntAct=EBI-727004, EBI-346547; CC O00560; Q14919: DRAP1; NbExp=5; IntAct=EBI-727004, EBI-712941; CC O00560; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-727004, EBI-465804; CC O00560; P63172: DYNLT1; NbExp=3; IntAct=EBI-727004, EBI-1176455; CC O00560; Q96JC9: EAF1; NbExp=3; IntAct=EBI-727004, EBI-769261; CC O00560; Q8WWZ3: EDARADD; NbExp=3; IntAct=EBI-727004, EBI-2949647; CC O00560; Q8N9N8: EIF1AD; NbExp=6; IntAct=EBI-727004, EBI-750700; CC O00560; P63241: EIF5A; NbExp=3; IntAct=EBI-727004, EBI-373150; CC O00560; Q9GZV4: EIF5A2; NbExp=6; IntAct=EBI-727004, EBI-748028; CC O00560; Q15717: ELAVL1; NbExp=3; IntAct=EBI-727004, EBI-374260; CC O00560; Q9NT22: EMILIN3; NbExp=3; IntAct=EBI-727004, EBI-3197883; CC O00560; Q8TC92: ENOX1; NbExp=3; IntAct=EBI-727004, EBI-713221; CC O00560; Q96C92-2: ENTR1; NbExp=3; IntAct=EBI-727004, EBI-10178036; CC O00560; A1L162: ERICH2; NbExp=3; IntAct=EBI-727004, EBI-2682520; CC O00560; Q9NPD3: EXOSC4; NbExp=3; IntAct=EBI-727004, EBI-371823; CC O00560; Q13158: FADD; NbExp=6; IntAct=EBI-727004, EBI-494804; CC O00560; Q9NWS6: FAM118A; NbExp=3; IntAct=EBI-727004, EBI-8638992; CC O00560; Q9BPY3: FAM118B; NbExp=3; IntAct=EBI-727004, EBI-726822; CC O00560; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-727004, EBI-8468186; CC O00560; Q8IZU0: FAM9B; NbExp=6; IntAct=EBI-727004, EBI-10175124; CC O00560; Q13643: FHL3; NbExp=3; IntAct=EBI-727004, EBI-741101; CC O00560; Q5TD97: FHL5; NbExp=3; IntAct=EBI-727004, EBI-750641; CC O00560; Q8NFF5: FLAD1; NbExp=4; IntAct=EBI-727004, EBI-742815; CC O00560; O15409: FOXP2; NbExp=3; IntAct=EBI-727004, EBI-983612; CC O00560; Q6NZ44: FTH1; NbExp=3; IntAct=EBI-727004, EBI-10180219; CC O00560; P02792: FTL; NbExp=6; IntAct=EBI-727004, EBI-713279; CC O00560; O75084: FZD7; NbExp=4; IntAct=EBI-727004, EBI-746917; CC O00560; Q7L5D6: GET4; NbExp=3; IntAct=EBI-727004, EBI-711823; CC O00560; O95749: GGPS1; NbExp=3; IntAct=EBI-727004, EBI-10179283; CC O00560; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-727004, EBI-743722; CC O00560; Q9Y3E0: GOLT1B; NbExp=3; IntAct=EBI-727004, EBI-4402607; CC O00560; Q8N954: GPATCH11; NbExp=3; IntAct=EBI-727004, EBI-2555378; CC O00560; Q8N954-2: GPATCH11; NbExp=3; IntAct=EBI-727004, EBI-12178961; CC O00560; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-727004, EBI-5235612; CC O00560; O15499: GSC2; NbExp=3; IntAct=EBI-727004, EBI-19954058; CC O00560; Q2KHT4-3: GSG1; NbExp=3; IntAct=EBI-727004, EBI-12951679; CC O00560; A0A024RA76: hCG_1744368; NbExp=5; IntAct=EBI-727004, EBI-10180729; CC O00560; V9HW60: HEL-S-182mP; NbExp=3; IntAct=EBI-727004, EBI-10180762; CC O00560; V9HW40: HEL-S-25; NbExp=3; IntAct=EBI-727004, EBI-10330099; CC O00560; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-727004, EBI-5460660; CC O00560; Q5VTY9: HHAT; NbExp=3; IntAct=EBI-727004, EBI-12951255; CC O00560; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-727004, EBI-2549423; CC O00560; O15347: HMGB3; NbExp=7; IntAct=EBI-727004, EBI-2214136; CC O00560; P07910: HNRNPC; NbExp=6; IntAct=EBI-727004, EBI-357966; CC O00560; Q9NSC5: HOMER3; NbExp=5; IntAct=EBI-727004, EBI-748420; CC O00560; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-727004, EBI-10172004; CC O00560; P49639: HOXA1; NbExp=6; IntAct=EBI-727004, EBI-740785; CC O00560; P31268: HOXA7; NbExp=3; IntAct=EBI-727004, EBI-3910421; CC O00560; P00492: HPRT1; NbExp=7; IntAct=EBI-727004, EBI-748210; CC O00560; O75506: HSBP1; NbExp=8; IntAct=EBI-727004, EBI-748664; CC O00560; O75031: HSF2BP; NbExp=3; IntAct=EBI-727004, EBI-7116203; CC O00560; P42858: HTT; NbExp=12; IntAct=EBI-727004, EBI-466029; CC O00560; O60921: HUS1; NbExp=3; IntAct=EBI-727004, EBI-1056174; CC O00560; Q02535: ID3; NbExp=3; IntAct=EBI-727004, EBI-1387094; CC O00560; P24592: IGFBP6; NbExp=3; IntAct=EBI-727004, EBI-947015; CC O00560; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-727004, EBI-8638439; CC O00560; Q13422: IKZF1; NbExp=3; IntAct=EBI-727004, EBI-745305; CC O00560; Q01344: IL5RA; NbExp=2; IntAct=EBI-727004, EBI-1759442; CC O00560; Q8NBZ0: INO80E; NbExp=6; IntAct=EBI-727004, EBI-769401; CC O00560; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-727004, EBI-715394; CC O00560; O95259: KCNH1; NbExp=3; IntAct=EBI-727004, EBI-2909270; CC O00560; P63252: KCNJ2; NbExp=3; IntAct=EBI-727004, EBI-703457; CC O00560; Q719H9: KCTD1; NbExp=6; IntAct=EBI-727004, EBI-9027502; CC O00560; Q8NC69: KCTD6; NbExp=6; IntAct=EBI-727004, EBI-2511344; CC O00560; Q7L273: KCTD9; NbExp=6; IntAct=EBI-727004, EBI-4397613; CC O00560; Q5VWX1: KHDRBS2; NbExp=6; IntAct=EBI-727004, EBI-742808; CC O00560; O60333-2: KIF1B; NbExp=3; IntAct=EBI-727004, EBI-10975473; CC O00560; Q53G59: KLHL12; NbExp=8; IntAct=EBI-727004, EBI-740929; CC O00560; O95198: KLHL2; NbExp=3; IntAct=EBI-727004, EBI-746999; CC O00560; P02533: KRT14; NbExp=3; IntAct=EBI-727004, EBI-702178; CC O00560; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-727004, EBI-11749135; CC O00560; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-727004, EBI-11741292; CC O00560; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-727004, EBI-10172290; CC O00560; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-727004, EBI-3958099; CC O00560; O43679: LDB2; NbExp=3; IntAct=EBI-727004, EBI-2865580; CC O00560; P07195: LDHB; NbExp=3; IntAct=EBI-727004, EBI-358748; CC O00560; O95751: LDOC1; NbExp=6; IntAct=EBI-727004, EBI-740738; CC O00560; O95214: LEPROTL1; NbExp=3; IntAct=EBI-727004, EBI-750776; CC O00560; P05162: LGALS2; NbExp=9; IntAct=EBI-727004, EBI-7181544; CC O00560; P62312: LSM6; NbExp=6; IntAct=EBI-727004, EBI-373310; CC O00560; Q8IV03: LURAP1L; NbExp=3; IntAct=EBI-727004, EBI-12898559; CC O00560; Q9NQ48: LZTFL1; NbExp=6; IntAct=EBI-727004, EBI-2824799; CC O00560; Q13257: MAD2L1; NbExp=3; IntAct=EBI-727004, EBI-78203; CC O00560; P45984: MAPK9; NbExp=3; IntAct=EBI-727004, EBI-713568; CC O00560; Q9UPY8: MAPRE3; NbExp=6; IntAct=EBI-727004, EBI-726739; CC O00560; O95460-2: MATN4; NbExp=3; IntAct=EBI-727004, EBI-12072296; CC O00560; O95983: MBD3; NbExp=3; IntAct=EBI-727004, EBI-1783068; CC O00560; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-727004, EBI-394607; CC O00560; P50221: MEOX1; NbExp=3; IntAct=EBI-727004, EBI-2864512; CC O00560; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-727004, EBI-16439278; CC O00560; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-727004, EBI-12866138; CC O00560; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-727004, EBI-10172526; CC O00560; Q9H8M7: MINDY3; NbExp=3; IntAct=EBI-727004, EBI-724928; CC O00560; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-727004, EBI-373524; CC O00560; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-727004, EBI-742459; CC O00560; Q13875-3: MOBP; NbExp=3; IntAct=EBI-727004, EBI-12013470; CC O00560; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-727004, EBI-995714; CC O00560; Q96HT8: MRFAP1L1; NbExp=8; IntAct=EBI-727004, EBI-748896; CC O00560; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-727004, EBI-742948; CC O00560; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-727004, EBI-11522433; CC O00560; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-727004, EBI-6952711; CC O00560; O15049: N4BP3; NbExp=3; IntAct=EBI-727004, EBI-2512055; CC O00560; O95544: NADK; NbExp=7; IntAct=EBI-727004, EBI-743949; CC O00560; Q9UJ70: NAGK; NbExp=5; IntAct=EBI-727004, EBI-372578; CC O00560; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-727004, EBI-11526455; CC O00560; Q9H115: NAPB; NbExp=3; IntAct=EBI-727004, EBI-3921185; CC O00560; Q7Z6G3-2: NECAB2; NbExp=5; IntAct=EBI-727004, EBI-10172876; CC O00560; Q15223: NECTIN1; NbExp=8; IntAct=EBI-727004, EBI-1771314; CC O00560; Q6ZUT1: NKAPD1; NbExp=8; IntAct=EBI-727004, EBI-3920396; CC O00560; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-727004, EBI-10180231; CC O00560; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-727004, EBI-945833; CC O00560; P49902: NT5C2; NbExp=3; IntAct=EBI-727004, EBI-742084; CC O00560; P0CE72: OCM; NbExp=3; IntAct=EBI-727004, EBI-11955379; CC O00560; A1E959: ODAM; NbExp=3; IntAct=EBI-727004, EBI-5774125; CC O00560; Q96CV9: OPTN; NbExp=3; IntAct=EBI-727004, EBI-748974; CC O00560; Q92882: OSTF1; NbExp=3; IntAct=EBI-727004, EBI-1051152; CC O00560; P61457: PCBD1; NbExp=3; IntAct=EBI-727004, EBI-740475; CC O00560; P49585: PCYT1A; NbExp=3; IntAct=EBI-727004, EBI-2563309; CC O00560; Q5VU43: PDE4DIP; NbExp=4; IntAct=EBI-727004, EBI-1105124; CC O00560; Q5VU43-2: PDE4DIP; NbExp=4; IntAct=EBI-727004, EBI-9640281; CC O00560; O76083-2: PDE9A; NbExp=3; IntAct=EBI-727004, EBI-11524542; CC O00560; P50479: PDLIM4; NbExp=3; IntAct=EBI-727004, EBI-372861; CC O00560; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-727004, EBI-716063; CC O00560; Q99471: PFDN5; NbExp=3; IntAct=EBI-727004, EBI-357275; CC O00560; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-727004, EBI-713786; CC O00560; Q9UIL8: PHF11; NbExp=3; IntAct=EBI-727004, EBI-2861403; CC O00560; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-727004, EBI-10232538; CC O00560; Q8ND90: PNMA1; NbExp=8; IntAct=EBI-727004, EBI-302345; CC O00560; Q9UL42: PNMA2; NbExp=7; IntAct=EBI-727004, EBI-302355; CC O00560; P52435: POLR2J; NbExp=3; IntAct=EBI-727004, EBI-394753; CC O00560; Q9Y2Y1: POLR3K; NbExp=3; IntAct=EBI-727004, EBI-11023785; CC O00560; Q8NAV1: PRPF38A; NbExp=3; IntAct=EBI-727004, EBI-715374; CC O00560; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-727004, EBI-5280197; CC O00560; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-727004, EBI-740924; CC O00560; P49720: PSMB3; NbExp=3; IntAct=EBI-727004, EBI-603340; CC O00560; P62333: PSMC6; NbExp=6; IntAct=EBI-727004, EBI-357669; CC O00560; Q9UL46: PSME2; NbExp=3; IntAct=EBI-727004, EBI-741630; CC O00560; O43586: PSTPIP1; NbExp=3; IntAct=EBI-727004, EBI-1050964; CC O00560; Q03393: PTS; NbExp=4; IntAct=EBI-727004, EBI-712344; CC O00560; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-727004, EBI-1053259; CC O00560; Q53H96: PYCR3; NbExp=8; IntAct=EBI-727004, EBI-2959680; CC O00560; Q53GL6: RALY; NbExp=3; IntAct=EBI-727004, EBI-9512693; CC O00560; Q14498: RBM39; NbExp=3; IntAct=EBI-727004, EBI-395290; CC O00560; Q96HR9: REEP6; NbExp=3; IntAct=EBI-727004, EBI-750345; CC O00560; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-727004, EBI-14065960; CC O00560; Q04864: REL; NbExp=3; IntAct=EBI-727004, EBI-307352; CC O00560; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-727004, EBI-9091816; CC O00560; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-727004, EBI-396669; CC O00560; P13489: RNH1; NbExp=8; IntAct=EBI-727004, EBI-1237106; CC O00560; Q9HAT0: ROPN1; NbExp=6; IntAct=EBI-727004, EBI-1378139; CC O00560; Q8TA86: RP9; NbExp=5; IntAct=EBI-727004, EBI-630339; CC O00560; P49247: RPIA; NbExp=3; IntAct=EBI-727004, EBI-744831; CC O00560; P35268: RPL22; NbExp=5; IntAct=EBI-727004, EBI-354533; CC O00560; Q96P16-3: RPRD1A; NbExp=3; IntAct=EBI-727004, EBI-12840198; CC O00560; Q9NS64: RPRM; NbExp=3; IntAct=EBI-727004, EBI-1052363; CC O00560; P62854: RPS26; NbExp=3; IntAct=EBI-727004, EBI-353438; CC O00560; P31350: RRM2; NbExp=3; IntAct=EBI-727004, EBI-2339245; CC O00560; Q15050: RRS1; NbExp=3; IntAct=EBI-727004, EBI-749186; CC O00560; Q17RB0: RTL8B; NbExp=3; IntAct=EBI-727004, EBI-10238588; CC O00560; Q16799-3: RTN1; NbExp=3; IntAct=EBI-727004, EBI-10180131; CC O00560; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-727004, EBI-747225; CC O00560; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-727004, EBI-11957366; CC O00560; P04271: S100B; NbExp=3; IntAct=EBI-727004, EBI-458391; CC O00560; Q8WXD2: SCG3; NbExp=3; IntAct=EBI-727004, EBI-12162999; CC O00560; Q9UN30-2: SCML1; NbExp=3; IntAct=EBI-727004, EBI-12137487; CC O00560; O00560: SDCBP; NbExp=7; IntAct=EBI-727004, EBI-727004; CC O00560; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-727004, EBI-693002; CC O00560; Q9UH03: SEPTIN3; NbExp=6; IntAct=EBI-727004, EBI-727037; CC O00560; Q01105: SET; NbExp=3; IntAct=EBI-727004, EBI-1053182; CC O00560; Q01105-2: SET; NbExp=3; IntAct=EBI-727004, EBI-7481343; CC O00560; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-727004, EBI-2854842; CC O00560; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-727004, EBI-747107; CC O00560; Q9BRV3: SLC50A1; NbExp=3; IntAct=EBI-727004, EBI-8634123; CC O00560; P51531: SMARCA2; NbExp=2; IntAct=EBI-727004, EBI-679562; CC O00560; P51531-2: SMARCA2; NbExp=3; IntAct=EBI-727004, EBI-10212306; CC O00560; P37840: SNCA; NbExp=3; IntAct=EBI-727004, EBI-985879; CC O00560; P09012: SNRPA; NbExp=3; IntAct=EBI-727004, EBI-607085; CC O00560; Q13596: SNX1; NbExp=3; IntAct=EBI-727004, EBI-2822329; CC O00560; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-727004, EBI-12037215; CC O00560; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-727004, EBI-5235340; CC O00560; P12931: SRC; NbExp=2; IntAct=EBI-727004, EBI-621482; CC O00560; Q8N9Q2: SREK1IP1; NbExp=6; IntAct=EBI-727004, EBI-10268630; CC O00560; Q05519: SRSF11; NbExp=3; IntAct=EBI-727004, EBI-1051785; CC O00560; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-727004, EBI-11975029; CC O00560; P84103: SRSF3; NbExp=3; IntAct=EBI-727004, EBI-372557; CC O00560; Q16629: SRSF7; NbExp=6; IntAct=EBI-727004, EBI-398885; CC O00560; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-727004, EBI-10172867; CC O00560; O43805: SSNA1; NbExp=6; IntAct=EBI-727004, EBI-2515299; CC O00560; P53999: SUB1; NbExp=3; IntAct=EBI-727004, EBI-998260; CC O00560; O43704: SULT1B1; NbExp=3; IntAct=EBI-727004, EBI-10179062; CC O00560; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-727004, EBI-12187159; CC O00560; Q16563: SYPL1; NbExp=3; IntAct=EBI-727004, EBI-2800683; CC O00560; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-727004, EBI-13075176; CC O00560; O43680: TCF21; NbExp=3; IntAct=EBI-727004, EBI-723267; CC O00560; P15884-3: TCF4; NbExp=3; IntAct=EBI-727004, EBI-13636688; CC O00560; P48775: TDO2; NbExp=7; IntAct=EBI-727004, EBI-743494; CC O00560; Q969V4: TEKT1; NbExp=3; IntAct=EBI-727004, EBI-10180409; CC O00560; Q12800: TFCP2; NbExp=3; IntAct=EBI-727004, EBI-717422; CC O00560; Q9NWX6: THG1L; NbExp=3; IntAct=EBI-727004, EBI-746510; CC O00560; Q96CG3: TIFA; NbExp=8; IntAct=EBI-727004, EBI-740711; CC O00560; Q3LXA3: TKFC; NbExp=3; IntAct=EBI-727004, EBI-4291069; CC O00560; Q08117: TLE5; NbExp=3; IntAct=EBI-727004, EBI-717810; CC O00560; Q7Z6W1: TMCO2; NbExp=3; IntAct=EBI-727004, EBI-12807858; CC O00560; Q86X19: TMEM17; NbExp=3; IntAct=EBI-727004, EBI-11343485; CC O00560; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-727004, EBI-9675724; CC O00560; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-727004, EBI-11528917; CC O00560; P0DTL5: TMEM276; NbExp=3; IntAct=EBI-727004, EBI-11997340; CC O00560; O95379: TNFAIP8; NbExp=6; IntAct=EBI-727004, EBI-1049336; CC O00560; Q5GJ75: TNFAIP8L3; NbExp=3; IntAct=EBI-727004, EBI-14222571; CC O00560; O95271: TNKS; NbExp=5; IntAct=EBI-727004, EBI-1105254; CC O00560; O00463: TRAF5; NbExp=8; IntAct=EBI-727004, EBI-523498; CC O00560; P14373: TRIM27; NbExp=3; IntAct=EBI-727004, EBI-719493; CC O00560; Q13049: TRIM32; NbExp=7; IntAct=EBI-727004, EBI-742790; CC O00560; O00635: TRIM38; NbExp=3; IntAct=EBI-727004, EBI-2130415; CC O00560; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-727004, EBI-2130429; CC O00560; Q15645: TRIP13; NbExp=3; IntAct=EBI-727004, EBI-358993; CC O00560; Q86WV8: TSC1; NbExp=3; IntAct=EBI-727004, EBI-12806590; CC O00560; Q15631: TSN; NbExp=3; IntAct=EBI-727004, EBI-1044160; CC O00560; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-727004, EBI-11988865; CC O00560; P0CG47: UBB; NbExp=3; IntAct=EBI-727004, EBI-413034; CC O00560; P49459: UBE2A; NbExp=9; IntAct=EBI-727004, EBI-2339348; CC O00560; P61086: UBE2K; NbExp=3; IntAct=EBI-727004, EBI-473850; CC O00560; Q712K3: UBE2R2; NbExp=3; IntAct=EBI-727004, EBI-2340879; CC O00560; O95292: VAPB; NbExp=3; IntAct=EBI-727004, EBI-1188298; CC O00560; Q9Y3C0: WASHC3; NbExp=6; IntAct=EBI-727004, EBI-712969; CC O00560; O00401: WASL; NbExp=6; IntAct=EBI-727004, EBI-957615; CC O00560; O76024: WFS1; NbExp=3; IntAct=EBI-727004, EBI-720609; CC O00560; O95070: YIF1A; NbExp=3; IntAct=EBI-727004, EBI-2799703; CC O00560; O43829: ZBTB14; NbExp=3; IntAct=EBI-727004, EBI-10176632; CC O00560; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-727004, EBI-742740; CC O00560; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-727004, EBI-597063; CC O00560; Q9NP64: ZCCHC17; NbExp=8; IntAct=EBI-727004, EBI-746345; CC O00560; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-727004, EBI-12030590; CC O00560; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-727004, EBI-10252492; CC O00560; Q8NCK3: ZNF485; NbExp=3; IntAct=EBI-727004, EBI-12901093; CC O00560; Q6AZW8: ZNF660; NbExp=3; IntAct=EBI-727004, EBI-12376497; CC O00560; Q9H5H4: ZNF768; NbExp=3; IntAct=EBI-727004, EBI-1210580; CC O00560; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-727004, EBI-527853; CC O00560; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-727004, EBI-5667532; CC O00560-1; P59637: E; Xeno; NbExp=4; IntAct=EBI-9640690, EBI-25487741; CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion CC {ECO:0000269|PubMed:11179419}. Cell junction, adherens junction CC {ECO:0000269|PubMed:11179419}. Cell membrane CC {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:25893292, CC ECO:0000269|PubMed:27386966}; Peripheral membrane protein CC {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:27386966}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:17081065}; Peripheral membrane CC protein {ECO:0000269|PubMed:17081065}. Nucleus CC {ECO:0000269|PubMed:11179419}. Melanosome {ECO:0000269|PubMed:12643545, CC ECO:0000269|PubMed:17081065}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:11179419}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11179419}. Secreted, extracellular exosome CC {ECO:0000269|PubMed:22660413}. Membrane raft CC {ECO:0000269|PubMed:25893292}. Note=Mainly membrane-associated. CC Localized to adherens junctions, focal adhesions and endoplasmic CC reticulum. Colocalized with actin stress fibers. Also found in the CC nucleus. Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. Associated to the plasma membrane in the presence CC of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) CC (PubMed:27386966). {ECO:0000269|PubMed:11179419, CC ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:27386966}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O00560-1; Sequence=Displayed; CC Name=2; CC IsoId=O00560-2; Sequence=VSP_038375; CC Name=3; CC IsoId=O00560-3; Sequence=VSP_038374; CC -!- TISSUE SPECIFICITY: Expressed in lung cancers, including CC adenocarcinoma, squamous cell carcinoma and small-cell carcinoma (at CC protein level) (PubMed:25893292). Widely expressed. Expressed in fetal CC kidney, liver, lung and brain. In adult highest expression in heart and CC placenta. {ECO:0000269|PubMed:25893292}. CC -!- INDUCTION: By IFNG/IFN-gamma in melanoma cells. CC -!- PTM: Phosphorylated on tyrosine residues. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44377/SDCBP"; 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; AF006636; AAC52050.1; -; mRNA. DR EMBL; AF000652; AAB97144.1; -; mRNA. DR EMBL; U83463; AAB51246.1; -; mRNA. DR EMBL; AK300647; BAG62335.1; -; mRNA. DR EMBL; AK312274; BAG35204.1; -; mRNA. DR EMBL; AC068522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471068; EAW86814.1; -; Genomic_DNA. DR EMBL; BC113674; AAI13675.1; -; mRNA. DR EMBL; BC113676; AAI13677.1; -; mRNA. DR EMBL; BC143915; AAI43916.1; -; mRNA. DR EMBL; BC143916; AAI43917.1; -; mRNA. DR CCDS; CCDS47862.1; -. [O00560-2] DR CCDS; CCDS47863.1; -. [O00560-3] DR CCDS; CCDS6172.1; -. [O00560-1] DR PIR; JC6537; JC6537. DR RefSeq; NP_001007068.1; NM_001007067.1. [O00560-1] DR RefSeq; NP_001007069.1; NM_001007068.1. [O00560-3] DR RefSeq; NP_001007070.1; NM_001007069.1. [O00560-2] DR RefSeq; NP_001007071.1; NM_001007070.1. [O00560-2] DR RefSeq; NP_005616.2; NM_005625.3. [O00560-1] DR PDB; 1N99; X-ray; 1.94 A; A/B=113-273. DR PDB; 1NTE; X-ray; 1.24 A; A=197-273. DR PDB; 1OBX; X-ray; 1.35 A; A=197-270. DR PDB; 1OBY; X-ray; 1.85 A; A/B=197-270. DR PDB; 1OBZ; X-ray; 1.69 A; A/B=113-273. DR PDB; 1R6J; X-ray; 0.73 A; A=197-273. DR PDB; 1V1T; X-ray; 1.80 A; A/B=113-273. DR PDB; 1W9E; X-ray; 1.56 A; A/B=113-273. DR PDB; 1W9O; X-ray; 2.25 A; A/B=113-273. DR PDB; 1W9Q; X-ray; 1.70 A; A/B=113-273. DR PDB; 1YBO; X-ray; 2.30 A; A/B=113-273. DR PDB; 4Z33; X-ray; 2.45 A; A/B=111-275. DR PDB; 6R9H; X-ray; 2.00 A; A/B/C/D=113-273. DR PDB; 6RLC; X-ray; 2.20 A; A/B/C/D=113-273. DR PDB; 7FSG; X-ray; 2.02 A; A/B/C/D=106-298. DR PDB; 7FSH; X-ray; 2.11 A; A/B/C/D=106-298. DR PDB; 7FSI; X-ray; 2.31 A; A/B/C/D=106-298. DR PDB; 7FSJ; X-ray; 1.97 A; A/B/C/D=106-298. DR PDB; 7FSK; X-ray; 2.40 A; A/B/C/D=106-298. DR PDB; 7FSL; X-ray; 2.38 A; A/B/C/D=106-298. DR PDB; 7FSM; X-ray; 2.10 A; A/B/C/D=106-298. DR PDB; 7FSN; X-ray; 2.40 A; A/B/C/D=106-298. DR PDB; 7FSO; X-ray; 1.90 A; A/B/C/D=106-298. DR PDB; 7FSP; X-ray; 1.86 A; A/B/C/D=106-298. DR PDB; 7FSQ; X-ray; 2.07 A; A/B/C/D=106-298. DR PDB; 7FSR; X-ray; 2.29 A; A/B/C/D=106-298. DR PDB; 7FSS; X-ray; 2.11 A; A/B/C/D=106-298. DR PDB; 7FST; X-ray; 1.98 A; A/B/C/D=106-298. DR PDB; 7FSU; X-ray; 1.97 A; A/B/C/D=106-298. DR PDB; 7FSV; X-ray; 2.25 A; A/B/C/D=106-298. DR PDB; 7FSW; X-ray; 2.14 A; A/B/C/D=106-298. DR PDB; 7FSX; X-ray; 1.91 A; A/B/C/D=106-298. DR PDB; 7FSY; X-ray; 2.80 A; A/B/C/D=106-298. DR PDB; 7FSZ; X-ray; 2.05 A; A/B/C/D=106-298. DR PDB; 7FT0; X-ray; 2.45 A; A/B/C/D=106-298. DR PDB; 7FT1; X-ray; 2.11 A; A/B/C/D=106-298. DR PDB; 7FT2; X-ray; 2.04 A; A/B/C/D=106-298. DR PDB; 7FT3; X-ray; 2.05 A; A/B/C/D=106-298. DR PDB; 7FT4; X-ray; 2.17 A; A/B/C/D=106-298. DR PDB; 7FT5; X-ray; 1.77 A; A/B/C/D=106-298. DR PDB; 7FT6; X-ray; 1.85 A; A/B/C/D=106-298. DR PDB; 7FT7; X-ray; 1.78 A; A/B/C/D=106-298. DR PDB; 7FT8; X-ray; 2.40 A; A/B/C/D=106-298. DR PDB; 7FT9; X-ray; 1.77 A; A/B/C/D=106-298. DR PDB; 7FTA; X-ray; 2.03 A; A/B/C/D=106-298. DR PDB; 7FTB; X-ray; 2.22 A; A/B/C/D=106-298. DR PDB; 7FTC; X-ray; 1.87 A; A/B/C/D=106-298. DR PDB; 7FTD; X-ray; 1.80 A; A/B/C/D=106-298. DR PDB; 8AAI; X-ray; 2.76 A; A/B/C/D=113-273. DR PDB; 8AAK; X-ray; 2.55 A; A/B=113-273. DR PDB; 8AAO; X-ray; 2.47 A; A/B=113-273. DR PDB; 8AAP; X-ray; 2.17 A; A/B=113-273. DR PDB; 8BLU; X-ray; 1.50 A; A/B/C/D=106-298. DR PDB; 8BLV; X-ray; 1.50 A; A/B=106-298. DR PDB; 8HCK; X-ray; 2.00 A; A=113-191. DR PDBsum; 1N99; -. DR PDBsum; 1NTE; -. DR PDBsum; 1OBX; -. DR PDBsum; 1OBY; -. DR PDBsum; 1OBZ; -. DR PDBsum; 1R6J; -. DR PDBsum; 1V1T; -. DR PDBsum; 1W9E; -. DR PDBsum; 1W9O; -. DR PDBsum; 1W9Q; -. DR PDBsum; 1YBO; -. DR PDBsum; 4Z33; -. DR PDBsum; 6R9H; -. DR PDBsum; 6RLC; -. DR PDBsum; 7FSG; -. DR PDBsum; 7FSH; -. DR PDBsum; 7FSI; -. DR PDBsum; 7FSJ; -. DR PDBsum; 7FSK; -. DR PDBsum; 7FSL; -. DR PDBsum; 7FSM; -. DR PDBsum; 7FSN; -. DR PDBsum; 7FSO; -. DR PDBsum; 7FSP; -. DR PDBsum; 7FSQ; -. DR PDBsum; 7FSR; -. DR PDBsum; 7FSS; -. DR PDBsum; 7FST; -. DR PDBsum; 7FSU; -. DR PDBsum; 7FSV; -. DR PDBsum; 7FSW; -. DR PDBsum; 7FSX; -. DR PDBsum; 7FSY; -. DR PDBsum; 7FSZ; -. DR PDBsum; 7FT0; -. DR PDBsum; 7FT1; -. DR PDBsum; 7FT2; -. DR PDBsum; 7FT3; -. DR PDBsum; 7FT4; -. DR PDBsum; 7FT5; -. DR PDBsum; 7FT6; -. DR PDBsum; 7FT7; -. DR PDBsum; 7FT8; -. DR PDBsum; 7FT9; -. DR PDBsum; 7FTA; -. DR PDBsum; 7FTB; -. DR PDBsum; 7FTC; -. DR PDBsum; 7FTD; -. DR PDBsum; 8AAI; -. DR PDBsum; 8AAK; -. DR PDBsum; 8AAO; -. DR PDBsum; 8AAP; -. DR PDBsum; 8BLU; -. DR PDBsum; 8BLV; -. DR PDBsum; 8HCK; -. DR AlphaFoldDB; O00560; -. DR SMR; O00560; -. DR BioGRID; 112287; 433. DR ComplexPortal; CPX-3282; Syndecan-1-syntenin-1-ALIX complex. DR DIP; DIP-42705N; -. DR IntAct; O00560; 408. DR MINT; O00560; -. DR STRING; 9606.ENSP00000428184; -. DR BindingDB; O00560; -. DR ChEMBL; CHEMBL4739667; -. DR MoonDB; O00560; Predicted. DR TCDB; 8.A.24.2.1; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family. DR GlyGen; O00560; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O00560; -. DR PhosphoSitePlus; O00560; -. DR SwissPalm; O00560; -. DR BioMuta; SDCBP; -. DR EPD; O00560; -. DR jPOST; O00560; -. DR MassIVE; O00560; -. DR MaxQB; O00560; -. DR PaxDb; 9606-ENSP00000260130; -. DR PeptideAtlas; O00560; -. DR ProteomicsDB; 47974; -. [O00560-1] DR ProteomicsDB; 47975; -. [O00560-2] DR ProteomicsDB; 47976; -. [O00560-3] DR Pumba; O00560; -. DR TopDownProteomics; O00560-1; -. [O00560-1] DR Antibodypedia; 3216; 589 antibodies from 38 providers. DR DNASU; 6386; -. DR Ensembl; ENST00000260130.9; ENSP00000260130.4; ENSG00000137575.12. [O00560-1] DR Ensembl; ENST00000413219.6; ENSP00000411771.2; ENSG00000137575.12. [O00560-1] DR Ensembl; ENST00000424270.6; ENSP00000395351.2; ENSG00000137575.12. [O00560-3] DR Ensembl; ENST00000447182.6; ENSP00000409288.2; ENSG00000137575.12. [O00560-2] DR GeneID; 6386; -. DR KEGG; hsa:6386; -. DR MANE-Select; ENST00000260130.9; ENSP00000260130.4; NM_005625.4; NP_005616.2. DR UCSC; uc003xtn.3; human. [O00560-1] DR AGR; HGNC:10662; -. DR DisGeNET; 6386; -. DR GeneCards; SDCBP; -. DR HGNC; HGNC:10662; SDCBP. DR HPA; ENSG00000137575; Low tissue specificity. DR MIM; 602217; gene. DR neXtProt; NX_O00560; -. DR OpenTargets; ENSG00000137575; -. DR PharmGKB; PA35592; -. DR VEuPathDB; HostDB:ENSG00000137575; -. DR eggNOG; KOG0849; Eukaryota. DR GeneTree; ENSGT00940000154502; -. DR InParanoid; O00560; -. DR OMA; RSSMDHS; -. DR OrthoDB; 5395964at2759; -. DR PhylomeDB; O00560; -. DR TreeFam; TF327131; -. DR PathwayCommons; O00560; -. DR Reactome; R-HSA-3928664; Ephrin signaling. DR Reactome; R-HSA-447043; Neurofascin interactions. DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis. DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O00560; -. DR SIGNOR; O00560; -. DR BioGRID-ORCS; 6386; 21 hits in 1157 CRISPR screens. DR ChiTaRS; SDCBP; human. DR EvolutionaryTrace; O00560; -. DR GeneWiki; SDCBP; -. DR GenomeRNAi; 6386; -. DR Pharos; O00560; Tchem. DR PRO; PR:O00560; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; O00560; Protein. DR Bgee; ENSG00000137575; Expressed in pigmented layer of retina and 210 other cell types or tissues. DR ExpressionAtlas; O00560; baseline and differential. DR GO; GO:0005912; C:adherens junction; NAS:UniProtKB. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0005895; C:interleukin-5 receptor complex; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl. DR GO; GO:0008093; F:cytoskeletal anchor activity; NAS:UniProtKB. DR GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl. DR GO; GO:0005109; F:frizzled binding; IPI:BHF-UCL. DR GO; GO:0019838; F:growth factor binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005137; F:interleukin-5 receptor binding; ISS:UniProtKB. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl. DR GO; GO:0042043; F:neurexin family protein binding; IEA:Ensembl. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0140311; F:protein sequestering activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0045545; F:syndecan binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; NAS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0002091; P:negative regulation of receptor internalization; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB. DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB. DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB. DR GO; GO:0046330; P:positive regulation of JNK cascade; IC:BHF-UCL. DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0099054; P:presynapse assembly; IEA:Ensembl. DR GO; GO:0006612; P:protein targeting to membrane; NAS:UniProtKB. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; NAS:UniProtKB. DR CDD; cd00992; PDZ_signaling; 2. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR12345; SYNTENIN RELATED; 1. DR PANTHER; PTHR12345:SF10; SYNTENIN-1; 1. DR Pfam; PF00595; PDZ; 2. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; PDZ domain-like; 2. DR PROSITE; PS50106; PDZ; 2. DR Genevisible; O00560; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell junction; KW Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Endoplasmic reticulum; Lipid-binding; Membrane; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Secreted. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330" FT CHAIN 2..298 FT /note="Syntenin-1" FT /id="PRO_0000184001" FT DOMAIN 114..193 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 198..273 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 2..60 FT /note="Interaction with PDCD6IP" FT /evidence="ECO:0000269|PubMed:22660413" FT MOTIF 3..7 FT /note="LYPX(n)L motif 1" FT /evidence="ECO:0000250|UniProtKB:O08992" FT MOTIF 45..49 FT /note="LYPX(n)L motif 2" FT /evidence="ECO:0000250|UniProtKB:O08992" FT MOTIF 49..53 FT /note="LYPX(n)L motif 3" FT /evidence="ECO:0000250|UniProtKB:O08992" FT BINDING 215 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000269|PubMed:27386966, FT ECO:0007744|PDB:4Z33" FT BINDING 250..251 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000269|PubMed:27386966, FT ECO:0007744|PDB:4Z33" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 46 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 12..17 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038374" FT VAR_SEQ 81 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_038375" FT VARIANT 69 FT /note="N -> S (in dbSNP:rs1127509)" FT /evidence="ECO:0000269|PubMed:9391086" FT /id="VAR_013160" FT MUTAGEN 214 FT /note="K->A: Disruption of the cooperative binding of FT C-terminal peptides from FZD7 and FT phosphatidylinositol-4,5-bisphosphate. Impaired interaction FT with FZD7 and disruption of the cooperative binding of FT C-terminal peptides from FZD7 and FT phosphatidylinositol-4,5-bisphosphate; when associated with FT A-250." FT /evidence="ECO:0000269|PubMed:27386966" FT MUTAGEN 215 FT /note="N->D: Disruption of the cooperative binding of FT C-terminal peptides from FZD7 and FT phosphatidylinositol-4,5-bisphosphate." FT /evidence="ECO:0000269|PubMed:27386966" FT MUTAGEN 250 FT /note="K->A: Disruption of the cooperative binding of FT C-terminal peptides from FZD7 and FT phosphatidylinositol-4,5-bisphosphate. Impaired interaction FT with FZD7 and disruption of the cooperative binding of FT C-terminal peptides from FZD7 and FT phosphatidylinositol-4,5-bisphosphate; when associated with FT A-214." FT /evidence="ECO:0000269|PubMed:27386966" FT CONFLICT 62 FT /note="N -> S (in Ref. 2; AAB51246)" FT /evidence="ECO:0000305" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:8BLU" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:1W9O" FT STRAND 127..132 FT /evidence="ECO:0007829|PDB:8BLU" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:8BLU" FT HELIX 146..149 FT /evidence="ECO:0007829|PDB:8BLU" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:8BLU" FT HELIX 171..180 FT /evidence="ECO:0007829|PDB:8BLU" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:8BLU" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:1R6J" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:1N99" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:1R6J" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:1R6J" FT HELIX 226..230 FT /evidence="ECO:0007829|PDB:1R6J" FT STRAND 234..241 FT /evidence="ECO:0007829|PDB:1R6J" FT HELIX 251..260 FT /evidence="ECO:0007829|PDB:1R6J" FT STRAND 263..271 FT /evidence="ECO:0007829|PDB:1R6J" FT HELIX 272..279 FT /evidence="ECO:0007829|PDB:8BLU" FT HELIX 284..290 FT /evidence="ECO:0007829|PDB:8BLU" SQ SEQUENCE 298 AA; 32444 MW; 574E1349F86F949F CRC64; MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY PELSQYMGLS LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND VGIRRAEIKQ GIREVILCKD QDGKIGLRLK SIDNGIFVQL VQANSPASLV GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ AFGEKITMTI RDRPFERTIT MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE INGQNVIGLK DSQIADILST SGTVVTITIM PAFIFEHIIK RMAPSIMKSL MDHTIPEV //