SDCB2_HUMAN
ID SDCB2_HUMAN Reviewed; 292 AA.
AC Q9H190; O95892; Q5W0X1; Q9BZ42; Q9H567; Q9NRY8;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Syntenin-2;
DE AltName: Full=Similar to TACIP18 {ECO:0000303|PubMed:11102519};
DE Short=SITAC {ECO:0000303|PubMed:11102519};
DE AltName: Full=Syndecan-binding protein 2;
GN Name=SDCBP2 {ECO:0000312|HGNC:HGNC:15756}; Synonyms=SITAC18;
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).
RC TISSUE=Fetal brain;
RA Fernandez-Larrea J., Borrell-Pages M., Urena J.M., Rojo F.,
RA Merlos-Suarez A., Baselga J., Arribas J.;
RT "SITAC18, a PDZ protein similar to TACIP18/syntenin/mda9 with restricted
RT specificity and expression pattern.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT MET-182, SUBUNIT,
RP AND INTERACTION WITH SDCBP.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-182.
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH TM4SF1.
RX PubMed=11102519; DOI=10.1091/mbc.11.12.4217;
RA Borrell-Pages M., Fernandez-Larrea J., Borroto A., Rojo F., Baselga J.,
RA Arribas J.;
RT "The carboxy-terminal cysteine of the tetraspanin L6 antigen is required
RT for its interaction with SITAC, a novel PDZ protein.";
RL Mol. Biol. Cell 11:4217-4225(2000).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH
RP PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE, AND MUTAGENESIS OF LYS-113; LYS-167;
RP LYS-197 AND LYS-244.
RX PubMed=15961997; DOI=10.1038/sj.emboj.7600722;
RA Mortier E., Wuytens G., Leenaerts I., Hannes F., Heung M.Y., Degeest G.,
RA David G., Zimmermann P.;
RT "Nuclear speckles and nucleoli targeting by PIP2-PDZ domain interactions.";
RL EMBO J. 24:2556-2565(2005).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY HPV8 E6.
RX PubMed=22623796; DOI=10.1128/jvi.00132-12;
RA Lazic D., Hufbauer M., Zigrino P., Buchholz S., Kazem S., Feltkamp M.C.,
RA Mauch C., Steger G., Pfister H., Akguel B.;
RT "Human papillomavirus type 8 E6 oncoprotein inhibits transcription of the
RT PDZ protein syntenin-2.";
RL J. Virol. 86:7943-7952(2012).
RN [9]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23300061; DOI=10.1002/cyto.a.22246;
RA Geeraerts A., Hsiu-Fang F., Zimmermann P., Engelborghs Y.;
RT "The characterization of the nuclear dynamics of syntenin-2, a PIP2 binding
RT PDZ protein.";
RL Cytometry A 83:866-875(2013).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-191.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play
CC a role in the organization of nuclear PIP2, cell division and cell
CC survival (PubMed:15961997). {ECO:0000269|PubMed:15961997}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:11152476, PubMed:23300061).
CC Interacts with SDCBP (PubMed:11152476). Interacts with TM4SF1
CC (PubMed:11102519). {ECO:0000269|PubMed:11102519,
CC ECO:0000269|PubMed:11152476, ECO:0000269|PubMed:23300061}.
CC -!- INTERACTION:
CC Q9H190; O75689: ADAP1; NbExp=3; IntAct=EBI-742426, EBI-714732;
CC Q9H190; Q02040: AKAP17A; NbExp=3; IntAct=EBI-742426, EBI-1042725;
CC Q9H190; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-742426, EBI-541426;
CC Q9H190; P18085: ARF4; NbExp=3; IntAct=EBI-742426, EBI-1237085;
CC Q9H190; Q96BP2: CHCHD1; NbExp=3; IntAct=EBI-742426, EBI-5454898;
CC Q9H190; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-742426, EBI-713677;
CC Q9H190; Q49AN0: CRY2; NbExp=3; IntAct=EBI-742426, EBI-2212355;
CC Q9H190; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-742426, EBI-12051833;
CC Q9H190; P0DMU9: CT45A10; NbExp=3; IntAct=EBI-742426, EBI-12153495;
CC Q9H190; Q8NHU0: CT45A3; NbExp=8; IntAct=EBI-742426, EBI-8643558;
CC Q9H190; Q6NSH3: CT45A5; NbExp=4; IntAct=EBI-742426, EBI-8635816;
CC Q9H190; Q14565: DMC1; NbExp=3; IntAct=EBI-742426, EBI-930865;
CC Q9H190; Q8N9N8: EIF1AD; NbExp=7; IntAct=EBI-742426, EBI-750700;
CC Q9H190; Q8N9E0: FAM133A; NbExp=9; IntAct=EBI-742426, EBI-10268158;
CC Q9H190; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-742426, EBI-751248;
CC Q9H190; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-742426, EBI-10175124;
CC Q9H190; Q9NVF7: FBXO28; NbExp=6; IntAct=EBI-742426, EBI-740282;
CC Q9H190; O75506: HSBP1; NbExp=3; IntAct=EBI-742426, EBI-748664;
CC Q9H190; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-742426, EBI-10274069;
CC Q9H190; P05162: LGALS2; NbExp=7; IntAct=EBI-742426, EBI-7181544;
CC Q9H190; Q9NX58: LYAR; NbExp=8; IntAct=EBI-742426, EBI-713507;
CC Q9H190; Q9BU76: MMTAG2; NbExp=4; IntAct=EBI-742426, EBI-742459;
CC Q9H190; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-742426, EBI-725252;
CC Q9H190; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-742426, EBI-3920396;
CC Q9H190; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-742426, EBI-10180231;
CC Q9H190; O00567: NOP56; NbExp=3; IntAct=EBI-742426, EBI-396034;
CC Q9H190; Q86SE8: NPM2; NbExp=4; IntAct=EBI-742426, EBI-6658150;
CC Q9H190; Q15102: PAFAH1B3; NbExp=5; IntAct=EBI-742426, EBI-711522;
CC Q9H190; P78364: PHC1; NbExp=3; IntAct=EBI-742426, EBI-725403;
CC Q9H190; P04554: PRM2; NbExp=3; IntAct=EBI-742426, EBI-9681663;
CC Q9H190; Q8NAV1: PRPF38A; NbExp=7; IntAct=EBI-742426, EBI-715374;
CC Q9H190; O75400-2: PRPF40A; NbExp=6; IntAct=EBI-742426, EBI-5280197;
CC Q9H190; Q9NZ81: PRR13; NbExp=7; IntAct=EBI-742426, EBI-740924;
CC Q9H190; D3DU92: RNPS1; NbExp=3; IntAct=EBI-742426, EBI-10176640;
CC Q9H190; Q15287: RNPS1; NbExp=4; IntAct=EBI-742426, EBI-395959;
CC Q9H190; P35268: RPL22; NbExp=5; IntAct=EBI-742426, EBI-354533;
CC Q9H190; Q6P5R6: RPL22L1; NbExp=3; IntAct=EBI-742426, EBI-2512545;
CC Q9H190; P62945: RPL41; NbExp=3; IntAct=EBI-742426, EBI-2116899;
CC Q9H190; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-742426, EBI-742426;
CC Q9H190; Q8N9Q2: SREK1IP1; NbExp=6; IntAct=EBI-742426, EBI-10268630;
CC Q9H190; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-742426, EBI-745392;
CC Q9H190; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-742426, EBI-2555179;
CC Q9H190; P48775: TDO2; NbExp=4; IntAct=EBI-742426, EBI-743494;
CC Q9H190; Q96CG3: TIFA; NbExp=6; IntAct=EBI-742426, EBI-740711;
CC Q9H190; P30408: TM4SF1; NbExp=3; IntAct=EBI-742426, EBI-714256;
CC Q9H190; P13805-3: TNNT1; NbExp=3; IntAct=EBI-742426, EBI-12151635;
CC Q9H190; P09430: TNP1; NbExp=4; IntAct=EBI-742426, EBI-10196343;
CC Q9H190; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-742426, EBI-12227803;
CC Q9H190; Q9BRG1: VPS25; NbExp=3; IntAct=EBI-742426, EBI-741945;
CC Q9H190; Q96MU7: YTHDC1; NbExp=7; IntAct=EBI-742426, EBI-2849854;
CC Q9H190; Q8TBK6: ZCCHC10; NbExp=4; IntAct=EBI-742426, EBI-597063;
CC Q9H190; Q9NP64: ZCCHC17; NbExp=8; IntAct=EBI-742426, EBI-746345;
CC Q9H190; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742426, EBI-745520;
CC Q9H190; Q15696: ZRSR2; NbExp=7; IntAct=EBI-742426, EBI-6657923;
CC Q9H190; P01134: Tgfa; Xeno; NbExp=6; IntAct=EBI-742426, EBI-16418721;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15961997}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15961997, ECO:0000269|PubMed:23300061}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:23300061}. Cell membrane
CC {ECO:0000269|PubMed:15961997}. Nucleus speckle
CC {ECO:0000269|PubMed:15961997}. Note=Associates with intracellular
CC membranes and enriched in the apical region of the cell and in
CC intracellular compartments (PubMed:11102519). Colocalizes with TM4SF1
CC in the apical region of the cell (PubMed:11102519). Predominantly
CC targeted to nuclear PIP2 pools. Shuttles between several subcellular
CC compartments (PubMed:15961997). PIP2 plays an important role in the
CC distribution of SDCBP2 (PubMed:23300061). {ECO:0000269|PubMed:11102519,
CC ECO:0000269|PubMed:15961997, ECO:0000269|PubMed:23300061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9H190-1; Sequence=Displayed;
CC Name=3; Synonyms=Beta;
CC IsoId=Q9H190-3; Sequence=VSP_006352;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in cells of the digestive
CC tract (PubMed:11102519). Low expression in skeletal muscle and kidney
CC (PubMed:11102519). Detected in differentiated keratinocytes of normal
CC and malignant epithelium (PubMed:22623796). In healthy skin, expression
CC is localized in suprabasal epidermal layers (PubMed:22623796).
CC {ECO:0000269|PubMed:11102519, ECO:0000269|PubMed:22623796}.
CC -!- INDUCTION: Down-regulated by HPV8 E6 papillomavirus (HPV) oncoprotein
CC (at protein level). {ECO:0000269|PubMed:22623796}.
CC -!- DOMAIN: Binds phosphatidylinositol 4,5-bisphosphate (PIP2) via its two
CC PDZ domains. These domains target SDCBP2 to the plasma membranes and
CC nucleoli, two PIP2-rich regions. {ECO:0000269|PubMed:15961997}.
CC -!- CAUTION: The nuclear speckles location of SDCBP2 is under debate. One
CC study shows that in paraformaldehyde fixed cells, SDCBP2 is highly
CC enriched in nuclear speckles (PubMed:15961997). The same authors
CC investigate subcellular location in living cells and fail to detect
CC SDCBP2 in nuclear speckles, and propose that enrichment in nuclear
CC speckles is fixation-dependent (PubMed:23300061).
CC {ECO:0000269|PubMed:15961997, ECO:0000269|PubMed:23300061}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02727.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF159228; AAF80369.1; -; mRNA.
DR EMBL; AJ292245; CAC21573.1; -; mRNA.
DR EMBL; AJ292244; CAC21716.1; -; mRNA.
DR EMBL; AF131809; AAD20049.1; -; mRNA.
DR EMBL; AL136531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002727; AAH02727.2; ALT_INIT; mRNA.
DR CCDS; CCDS13013.1; -. [Q9H190-3]
DR CCDS; CCDS42848.1; -. [Q9H190-1]
DR RefSeq; NP_001186713.1; NM_001199784.1. [Q9H190-1]
DR RefSeq; NP_056500.2; NM_015685.5. [Q9H190-3]
DR RefSeq; NP_536737.3; NM_080489.4. [Q9H190-1]
DR AlphaFoldDB; Q9H190; -.
DR SMR; Q9H190; -.
DR BioGRID; 118007; 77.
DR IntAct; Q9H190; 71.
DR MINT; Q9H190; -.
DR STRING; 9606.ENSP00000371233; -.
DR MoonDB; Q9H190; Predicted.
DR iPTMnet; Q9H190; -.
DR PhosphoSitePlus; Q9H190; -.
DR SwissPalm; Q9H190; -.
DR BioMuta; SDCBP2; -.
DR DMDM; 20455288; -.
DR EPD; Q9H190; -.
DR jPOST; Q9H190; -.
DR MassIVE; Q9H190; -.
DR MaxQB; Q9H190; -.
DR PaxDb; Q9H190; -.
DR PeptideAtlas; Q9H190; -.
DR PRIDE; Q9H190; -.
DR ProteomicsDB; 80379; -. [Q9H190-1]
DR ProteomicsDB; 80380; -. [Q9H190-3]
DR Antibodypedia; 23059; 244 antibodies from 30 providers.
DR DNASU; 27111; -.
DR Ensembl; ENST00000339987.7; ENSP00000342935.3; ENSG00000125775.15. [Q9H190-1]
DR Ensembl; ENST00000360779.4; ENSP00000354013.3; ENSG00000125775.15. [Q9H190-1]
DR Ensembl; ENST00000381808.7; ENSP00000371229.3; ENSG00000125775.15. [Q9H190-3]
DR Ensembl; ENST00000381812.5; ENSP00000371233.1; ENSG00000125775.15. [Q9H190-1]
DR GeneID; 27111; -.
DR KEGG; hsa:27111; -.
DR MANE-Select; ENST00000360779.4; ENSP00000354013.3; NM_080489.5; NP_536737.3.
DR UCSC; uc002weu.5; human. [Q9H190-1]
DR CTD; 27111; -.
DR DisGeNET; 27111; -.
DR GeneCards; SDCBP2; -.
DR HGNC; HGNC:15756; SDCBP2.
DR HPA; ENSG00000125775; Tissue enhanced (esophagus, intestine, stomach).
DR MIM; 617358; gene.
DR neXtProt; NX_Q9H190; -.
DR OpenTargets; ENSG00000125775; -.
DR PharmGKB; PA38033; -.
DR VEuPathDB; HostDB:ENSG00000125775; -.
DR eggNOG; ENOG502S0HE; Eukaryota.
DR GeneTree; ENSGT00940000161179; -.
DR HOGENOM; CLU_059870_0_0_1; -.
DR InParanoid; Q9H190; -.
DR OMA; AVCEVNG; -.
DR OrthoDB; 1035679at2759; -.
DR PhylomeDB; Q9H190; -.
DR TreeFam; TF327131; -.
DR PathwayCommons; Q9H190; -.
DR SignaLink; Q9H190; -.
DR BioGRID-ORCS; 27111; 22 hits in 1078 CRISPR screens.
DR GeneWiki; SDCBP2; -.
DR GenomeRNAi; 27111; -.
DR Pharos; Q9H190; Tbio.
DR PRO; PR:Q9H190; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H190; protein.
DR Bgee; ENSG00000125775; Expressed in ileal mucosa and 129 other tissues.
DR Genevisible; Q9H190; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; NAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Lipid-binding; Membrane;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..292
FT /note="Syntenin-2"
FT /id="PRO_0000184004"
FT DOMAIN 108..187
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 192..267
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11152476, ECO:0000303|Ref.3"
FT /id="VSP_006352"
FT VARIANT 182
FT /note="V -> M (in dbSNP:rs2273959)"
FT /evidence="ECO:0000269|PubMed:11152476, ECO:0000269|Ref.3"
FT /id="VAR_053700"
FT VARIANT 191
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs35367003)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036544"
FT VARIANT 223
FT /note="R -> C (in dbSNP:rs1048621)"
FT /id="VAR_053701"
FT VARIANT 242
FT /note="G -> R (in dbSNP:rs4814111)"
FT /id="VAR_053702"
FT MUTAGEN 113
FT /note="K->A: Abolishes phosphatidylinositol 4,5-
FT bisphosphate binding and targeting to plasma membrane,
FT speckles and nucleoli; when associated with A-167; A-197
FT and A-244. Reduces phosphatidylinositol 4,5-bisphosphate
FT binding and does not change subcellular localization; when
FT associated with A-167."
FT /evidence="ECO:0000269|PubMed:15961997"
FT MUTAGEN 167
FT /note="K->A: Abolishes phosphatidylinositol 4,5-
FT bisphosphate binding and targeting to plasma membrane,
FT speckles and nucleoli; when associated with A-113; A-197
FT and A-244. Reduces phosphatidylinositol 4,5-bisphosphate
FT binding and does not change subcellular localization; when
FT associated with A-113."
FT /evidence="ECO:0000269|PubMed:15961997"
FT MUTAGEN 197
FT /note="K->A: Abolishes phosphatidylinositol 4,5-
FT bisphosphate binding and targeting to plasma membrane,
FT speckles and nucleoli; when associated with A-113; A-167
FT and A-244. Reduces phosphatidylinositol 4,5-bisphosphate
FT binding and does not change subcellular localization; when
FT associated with A-244."
FT /evidence="ECO:0000269|PubMed:15961997"
FT MUTAGEN 244
FT /note="K->A: Abolishes phosphatidylinositol 4,5-
FT bisphosphate binding and targeting to plasma membrane,
FT speckles and nucleoli; when associated with A-113; A-167
FT and A-197. Reduces phosphatidylinositol 4,5-bisphosphate
FT binding and does not change subcellular localization; when
FT associated with A-197."
FT /evidence="ECO:0000269|PubMed:15961997"
FT CONFLICT 69
FT /note="Q -> H (in Ref. 2; CAC21716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 31594 MW; E12536839E1CD91C CRC64;
MSSLYPSLED LKVDQAIQAQ VRASPKMPAL PVQATAISPP PVLYPNLAEL ENYMGLSLSS
QEVQESLLQI PEGDSTAVSG PGPGQMVAPV TGYSLGVRRA EIKPGVREIH LCKDERGKTG
LRLRKVDQGL FVQLVQANTP ASLVGLRFGD QLLQIDGRDC AGWSSHKAHQ VVKKASGDKI
VVVVRDRPFQ RTVTMHKDSM GHVGFVIKKG KIVSLVKGSS AARNGLLTNH YVCEVDGQNV
IGLKDKKIME ILATAGNVVT LTIIPSVIYE HMVKKLPPVL LHHTMDHSIP DA
