ID SYNPO_HUMAN Reviewed; 929 AA. AC Q8N3V7; A5PKZ8; D3DQG8; O15271; Q9UPX1; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=Synaptopodin; GN Name=SYNPO; Synonyms=KIAA1029; 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 3), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=9314539; DOI=10.1083/jcb.139.1.193; RA Mundel P., Heid H.W., Mundel T.M., Krueger M., Reiser J., Kriz W.; RT "Synaptopodin: an actin-associated protein in telencephalic dendrites and RT renal podocytes."; RL J. Cell Biol. 139:193-204(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain, and Kidney; RA Reddy P.H., Gutala R.; RT "Loss of spine apparatus associated protein synaptopodin in Alzheimer's RT disease."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Thalamus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 [8] RP INTERACTION WITH BAIAP1, AND SUBCELLULAR LOCATION. RX PubMed=12042308; DOI=10.1074/jbc.m203072200; RA Patrie K.M., Drescher A.J., Welihinda A., Mundel P., Margolis B.; RT "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin- RT 4, with the tight junction protein MAGI-1."; RL J. Biol. Chem. 277:30183-30190(2002). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-871 (ISOFORM 2), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP INTERACTION WITH WWC1. RX PubMed=18596123; DOI=10.1681/asn.2007080916; RA Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C., Schwab A., RA Schaefer L., Benzing T., Schermer B., Saleem M.A., Huber T.B., Bachmann S., RA Kremerskothen J., Weide T., Pavenstaedt H.; RT "KIBRA modulates directional migration of podocytes."; RL J. Am. Soc. Nephrol. 19:1891-1903(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-871 (ISOFORM 2), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-525; SER-580; RP SER-685; SER-702; THR-746; SER-754 AND SER-833, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-826 AND SER-894 (ISOFORM 2), AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-330. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-580; SER-685; RP THR-746 AND SER-833, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854 AND RP SER-871 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-525; SER-580; RP SER-685; SER-702; SER-754 AND SER-833, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-580; SER-685; RP SER-754; SER-833 AND SER-854, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-738; SER-784; SER-804; SER-812; SER-826; SER-854 AND SER-894 (ISOFORM RP 2), AND IDENTIFICATION BY 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 [19] RP SUBCELLULAR LOCATION. RX PubMed=30661770; DOI=10.1016/j.ajhg.2018.12.016; RA Dorval G., Kuzmuk V., Gribouval O., Welsh G.I., Bierzynska A., Schmitt A., RA Miserey-Lenkei S., Koziell A., Haq S., Benmerah A., Mollet G., Boyer O., RA Saleem M.A., Antignac C.; RT "TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic Syndrome via RT Defective Trafficking Pathways."; RL Am. J. Hum. Genet. 104:348-355(2019). CC -!- FUNCTION: Actin-associated protein that may play a role in modulating CC actin-based shape and motility of dendritic spines and renal podocyte CC foot processes. Seems to be essential for the formation of spine CC apparatuses in spines of telencephalic neurons, which is involved in CC synaptic plasticity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with BAIAP1. Interacts with actin (By similarity). CC Interacts (via PPxY motifs) with WWC1 (via WW domains). {ECO:0000250, CC ECO:0000269|PubMed:12042308, ECO:0000269|PubMed:18596123}. CC -!- INTERACTION: CC Q8N3V7; P12814: ACTN1; NbExp=2; IntAct=EBI-352936, EBI-351710; CC Q8N3V7; Q99459: CDC5L; NbExp=5; IntAct=EBI-352936, EBI-374880; CC Q8N3V7; Q96ES7: SGF29; NbExp=5; IntAct=EBI-352936, EBI-743117; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q8CC35}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:Q8CC35}. Perikaryon CC {ECO:0000250|UniProtKB:Q8CC35}. Cell projection, dendritic spine CC {ECO:0000250|UniProtKB:Q8CC35}. Postsynaptic density CC {ECO:0000250|UniProtKB:Q8CC35}. Synapse {ECO:0000250|UniProtKB:Q8CC35}. CC Cytoplasm, cytosol {ECO:0000269|PubMed:30661770}. Note=Localized at the CC tight junction of cells. In brain, localized to the postsynaptic CC densities and in the perikarya. Associated with dendritic spines of a CC subset of synapses. {ECO:0000250|UniProtKB:Q8CC35}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N3V7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N3V7-2; Sequence=VSP_010476, VSP_010477; CC Name=3; CC IsoId=Q8N3V7-3; Sequence=VSP_010476; CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex. CC {ECO:0000269|PubMed:9314539}. CC -!- PTM: O-glycosylated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA82981.2; 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; Y11072; CAA71955.1; -; mRNA. DR EMBL; AF499136; AAQ07402.1; -; mRNA. DR EMBL; AF499137; AAQ07403.1; -; mRNA. DR EMBL; AB028952; BAA82981.2; ALT_INIT; mRNA. DR EMBL; AK127049; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK290178; BAF82867.1; -; mRNA. DR EMBL; AL831818; CAD38532.1; -; mRNA. DR EMBL; CH471062; EAW61715.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61716.1; -; Genomic_DNA. DR EMBL; BC142683; AAI42684.1; -; mRNA. DR EMBL; BC146665; AAI46666.1; -; mRNA. DR CCDS; CCDS4308.1; -. [Q8N3V7-2] DR CCDS; CCDS54937.1; -. [Q8N3V7-1] DR CCDS; CCDS54938.1; -. [Q8N3V7-3] DR RefSeq; NP_001103444.1; NM_001109974.2. [Q8N3V7-3] DR RefSeq; NP_001159680.1; NM_001166208.1. [Q8N3V7-1] DR RefSeq; NP_001159681.1; NM_001166209.1. [Q8N3V7-1] DR RefSeq; NP_009217.3; NM_007286.5. [Q8N3V7-2] DR RefSeq; XP_005268427.1; XM_005268370.1. DR RefSeq; XP_005268428.1; XM_005268371.1. [Q8N3V7-2] DR RefSeq; XP_011535854.1; XM_011537552.2. DR AlphaFoldDB; Q8N3V7; -. DR BioGRID; 116474; 190. DR IntAct; Q8N3V7; 179. DR MINT; Q8N3V7; -. DR STRING; 9606.ENSP00000377789; -. DR GlyConnect; 2889; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; Q8N3V7; 14 sites, 1 glycan. DR GlyGen; Q8N3V7; 15 sites, 1 O-linked glycan (14 sites). DR iPTMnet; Q8N3V7; -. DR PhosphoSitePlus; Q8N3V7; -. DR BioMuta; SYNPO; -. DR DMDM; 48428650; -. DR EPD; Q8N3V7; -. DR jPOST; Q8N3V7; -. DR MassIVE; Q8N3V7; -. DR MaxQB; Q8N3V7; -. DR PaxDb; 9606-ENSP00000377789; -. DR PeptideAtlas; Q8N3V7; -. DR ProteomicsDB; 71838; -. [Q8N3V7-1] DR ProteomicsDB; 71839; -. [Q8N3V7-2] DR ProteomicsDB; 71840; -. [Q8N3V7-3] DR Pumba; Q8N3V7; -. DR Antibodypedia; 16210; 389 antibodies from 35 providers. DR DNASU; 11346; -. DR Ensembl; ENST00000307662.5; ENSP00000302139.4; ENSG00000171992.13. [Q8N3V7-2] DR Ensembl; ENST00000394243.5; ENSP00000377789.1; ENSG00000171992.13. [Q8N3V7-1] DR Ensembl; ENST00000519664.1; ENSP00000429268.1; ENSG00000171992.13. [Q8N3V7-3] DR Ensembl; ENST00000522122.1; ENSP00000428378.1; ENSG00000171992.13. [Q8N3V7-1] DR GeneID; 11346; -. DR KEGG; hsa:11346; -. DR MANE-Select; ENST00000307662.5; ENSP00000302139.4; NM_007286.6; NP_009217.3. [Q8N3V7-2] DR UCSC; uc003lsn.4; human. [Q8N3V7-1] DR AGR; HGNC:30672; -. DR CTD; 11346; -. DR DisGeNET; 11346; -. DR GeneCards; SYNPO; -. DR HGNC; HGNC:30672; SYNPO. DR HPA; ENSG00000171992; Group enriched (heart muscle, skeletal muscle, tongue). DR MIM; 608155; gene. DR neXtProt; NX_Q8N3V7; -. DR OpenTargets; ENSG00000171992; -. DR PharmGKB; PA134863299; -. DR VEuPathDB; HostDB:ENSG00000171992; -. DR eggNOG; ENOG502R7RM; Eukaryota. DR GeneTree; ENSGT00950000183054; -. DR HOGENOM; CLU_013103_0_0_1; -. DR InParanoid; Q8N3V7; -. DR OMA; KEHMSRK; -. DR OrthoDB; 4841244at2759; -. DR PhylomeDB; Q8N3V7; -. DR TreeFam; TF330867; -. DR PathwayCommons; Q8N3V7; -. DR SignaLink; Q8N3V7; -. DR BioGRID-ORCS; 11346; 16 hits in 1151 CRISPR screens. DR ChiTaRS; SYNPO; human. DR GeneWiki; SYNPO; -. DR GenomeRNAi; 11346; -. DR Pharos; Q8N3V7; Tbio. DR PRO; PR:Q8N3V7; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q8N3V7; Protein. DR Bgee; ENSG00000171992; Expressed in hindlimb stylopod muscle and 203 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043197; C:dendritic spine; TAS:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0097444; C:spine apparatus; IBA:GO_Central. DR GO; GO:0001725; C:stress fiber; IBA:GO_Central. DR GO; GO:0030018; C:Z disc; IBA:GO_Central. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0098886; P:modification of dendritic spine; IDA:SynGO. DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISS:UniProtKB. DR GO; GO:0051492; P:regulation of stress fiber assembly; ISS:UniProtKB. DR GO; GO:1905355; P:spine apparatus assembly; IBA:GO_Central. DR PANTHER; PTHR24217; PUTATIVE-RELATED; 1. DR PANTHER; PTHR24217:SF13; SYNAPTOPODIN; 1. DR Genevisible; Q8N3V7; HS. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Alternative splicing; Cell junction; KW Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein; Phosphoprotein; KW Reference proteome; Synapse; Tight junction. FT CHAIN 1..929 FT /note="Synaptopodin" FT /id="PRO_0000187670" FT REGION 1..260 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 285..389 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 509..558 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 589..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 630..726 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 740..763 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 826..916 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 562..565 FT /note="PPxY motif" FT MOTIF 581..584 FT /note="PPxY motif" FT COMPBIAS 1..16 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 154..179 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..204 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 312..383 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 643..660 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..763 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 863..880 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CC35" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CC35" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CC35" FT MOD_RES 525 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 560 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Z327" FT MOD_RES 580 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 685 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 746 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 754 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 758 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CC35" FT MOD_RES 779 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z327" FT MOD_RES 783 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8CC35" FT MOD_RES 833 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 854 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 1..244 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10470851, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9314539, ECO:0000303|Ref.2" FT /id="VSP_010476" FT VAR_SEQ 921..929 FT /note="VWKPSFCFK -> DRRESLPTSPPWTPGASRPPSSLDGWVSPGPWEPGRGSS FT MSSPPPLPPPPPMSPSWSERSVSPLRPETEARPPSRQLQALLARNIINAARRKSASPRS FT AGAENPRPFSPPRAPPPPPPPPPPPPRMRSPQPARPGSAAVPGAAFAPIPRSPLPAGPS FT SCTSPRSPLPAPPRPFLYRRSPTDSDVSLDSEDSGAKSPGILGYNICPRGWNGSLRLKR FT GSLPAEASCTT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10470851, ECO:0000303|Ref.2" FT /id="VSP_010477" FT CONFLICT 95 FT /note="Q -> R (in Ref. 5; CAD38532)" FT /evidence="ECO:0000305" FT CONFLICT 417 FT /note="E -> G (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 428 FT /note="A -> V (in Ref. 1; CAA71955)" FT /evidence="ECO:0000305" FT CONFLICT 744 FT /note="S -> G (in Ref. 1; CAA71955)" FT /evidence="ECO:0000305" FT CONFLICT 836 FT /note="K -> R (in Ref. 4)" FT /evidence="ECO:0000305" FT MOD_RES Q8N3V7-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES Q8N3V7-2:738 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:784 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:804 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:812 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:826 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:854 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-2:871 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231" FT MOD_RES Q8N3V7-2:894 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES Q8N3V7-3:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 929 AA; 99463 MW; 38723B6FDD046F15 CRC64; MLGPHLPPPP LAPSEGRPTP CAFQIPDGSY RCLALEAEES SGEEGLQGEV GPTDLEEDEG VSRSGDDSAC RVTQGTPQLP KALGIQPPSC SREEQGASQH DDRASQDWDV VKAGQMMTAS PSPGPGPRVA QKPALGRSTS LTEKDLKEAK ARSQQIAAQL TTPPSSNSRG VQLFNRRRQR VNEFTLESHG QRGQKPSQES LRVLPSSLPG HAPGLSLSST SLPEPGPPRH PSPQSPDRGV PGHSMEGYSE EASLLRHLEK VASEEEEVPL VVYLKENAAL LTANGLHLSQ NREAQQSSPA PPPAEVHSPA ADVNQNLASP SATLTTPTSN SSHNPPATDV NQNPPATVVP QSLPLSSIQQ NSSEAQLPSN GTGPASKPST LCADGQPQAP AEEVRCSTLL IDKVSTPATT TSTFSREATL IPSSRPPASD FMSSSLLIDI QPNTLVVSAD QEMSGRAAAT TPTKVYSEVH FTLAKPPSVV NRTARPFGIQ APGGTSQMER SPMLERRHFG EKAPAPQPPS LPDRSPRPQR HIMSRSPMVE RRMMGQRSPA SERRPLGNFT APPTYTETLS TAPLASWVRS PPSYSVLYPS SDPKSSHLKG QAVPASKTGI LEESMARRGS RKSMFTFVEK PKVTPNPDLL DLVQTADEKR RQRDQGEVGV EEEPFALGAE ASNFQQEPAP RDRASPAAAE EVVPEWASCL KSPRIQAKPK PKPNQNLSEA SGKGAELYAR RQSRMEKYVI ESSSHTPELA RCPSPTMSLP SSWKYPTNAP GAFRVASRSP ARTPPASLYH GYLPENGVLR PEPTKQPPYQ LRPSLFVLSP IKEPAKVSPR AASPAKPSSL DLVPNLPKGA LPPSPALPRP SRSSPGLYTS PGQDSLQPTA VSPPYGGDIS PVSPSRAWSP RAKQAPRPSF STRNAGIEAQ VWKPSFCFK //