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 27-MAR-2024, entry version 182. 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}; 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; 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; 79. DR IntAct; Q9H190; 72. 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; 9606-ENSP00000371233; -. DR PeptideAtlas; Q9H190; -. DR ProteomicsDB; 80379; -. [Q9H190-1] DR ProteomicsDB; 80380; -. [Q9H190-3] DR Antibodypedia; 23059; 256 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 AGR; HGNC:15756; -. 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; 5395964at2759; -. DR PhylomeDB; Q9H190; -. DR TreeFam; TF327131; -. DR PathwayCommons; Q9H190; -. DR SignaLink; Q9H190; -. DR SIGNOR; Q9H190; -. DR BioGRID-ORCS; 27111; 24 hits in 1154 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 131 other cell types or tissues. 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: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 CDD; cd00136; PDZ; 1. DR CDD; cd00992; PDZ_signaling; 1. 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:SF13; SYNTENIN-2; 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; Q9H190; HS. 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 FT 4,5-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 FT 4,5-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 FT 4,5-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 FT 4,5-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 //