SDCB1_HUMAN
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 03-AUG-2022, entry version 215.
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; 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; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-727004, EBI-8643161;
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; Q6ZMK1-3: CYHR1; NbExp=3; IntAct=EBI-727004, EBI-11997340;
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; 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="http://atlasgeneticsoncology.org/Genes/SDCBPID44377ch8q12.html";
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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 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 AlphaFoldDB; O00560; -.
DR SMR; O00560; -.
DR BioGRID; 112287; 418.
DR ComplexPortal; CPX-3282; Syndecan-1-syntenin-1-ALIX complex.
DR DIP; DIP-42705N; -.
DR IntAct; O00560; 403.
DR MINT; O00560; -.
DR STRING; 9606.ENSP00000260130; -.
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; O00560; -.
DR PeptideAtlas; O00560; -.
DR PRIDE; O00560; -.
DR ProteomicsDB; 47974; -. [O00560-1]
DR ProteomicsDB; 47975; -. [O00560-2]
DR ProteomicsDB; 47976; -. [O00560-3]
DR TopDownProteomics; O00560-1; -. [O00560-1]
DR Antibodypedia; 3216; 535 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 CTD; 6386; -.
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; QFAQSTA; -.
DR OrthoDB; 1035679at2759; -.
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; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; SDCBP; human.
DR EvolutionaryTrace; O00560; -.
DR GeneWiki; SDCBP; -.
DR GenomeRNAi; 6386; -.
DR Pharos; O00560; Tbio.
DR PRO; PR:O00560; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O00560; protein.
DR Bgee; ENSG00000137575; Expressed in pigmented layer of retina and 208 other tissues.
DR ExpressionAtlas; O00560; baseline and differential.
DR Genevisible; O00560; HS.
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:0045202; C:synapse; IEA:GOC.
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:0042043; F:neurexin family protein binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI: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:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP: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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
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 Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030528; SDCBP.
DR PANTHER; PTHR12345:SF10; PTHR12345:SF10; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
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 C-
FT terminal peptides from FZD7 and phosphatidylinositol-4,5-
FT bisphosphate. Impaired interaction with FZD7 and disruption
FT of the cooperative binding of C-terminal peptides from FZD7
FT and phosphatidylinositol-4,5-bisphosphate; when associated
FT with A-250."
FT /evidence="ECO:0000269|PubMed:27386966"
FT MUTAGEN 215
FT /note="N->D: Disruption of the cooperative binding of C-
FT terminal peptides from FZD7 and phosphatidylinositol-4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:27386966"
FT MUTAGEN 250
FT /note="K->A: Disruption of the cooperative binding of C-
FT terminal peptides from FZD7 and phosphatidylinositol-4,5-
FT bisphosphate. Impaired interaction with FZD7 and disruption
FT of the cooperative binding of C-terminal peptides from FZD7
FT and phosphatidylinositol-4,5-bisphosphate; when associated
FT with 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 113..118
FT /evidence="ECO:0007829|PDB:1W9E"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1W9O"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1W9E"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1W9E"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1W9E"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1W9E"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1W9E"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:1W9E"
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..274
FT /evidence="ECO:0007829|PDB:4Z33"
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
