SYNPO_HUMAN
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 03-AUG-2022, entry version 169.
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};
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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. [Q8N3V7-2]
DR RefSeq; XP_005268428.1; XM_005268371.1. [Q8N3V7-2]
DR RefSeq; XP_011535854.1; XM_011537552.2. [Q8N3V7-1]
DR AlphaFoldDB; Q8N3V7; -.
DR BioGRID; 116474; 184.
DR IntAct; Q8N3V7; 177.
DR MINT; Q8N3V7; -.
DR STRING; 9606.ENSP00000377789; -.
DR GlyConnect; 2889; 1 O-Linked glycan (1 site).
DR GlyGen; Q8N3V7; 14 sites, 1 O-linked glycan (13 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; Q8N3V7; -.
DR PeptideAtlas; Q8N3V7; -.
DR PRIDE; Q8N3V7; -.
DR ProteomicsDB; 71838; -. [Q8N3V7-1]
DR ProteomicsDB; 71839; -. [Q8N3V7-2]
DR ProteomicsDB; 71840; -. [Q8N3V7-3]
DR Antibodypedia; 16210; 313 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 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; QPPYQMR; -.
DR OrthoDB; 691538at2759; -.
DR PhylomeDB; Q8N3V7; -.
DR TreeFam; TF330867; -.
DR PathwayCommons; Q8N3V7; -.
DR SignaLink; Q8N3V7; -.
DR BioGRID-ORCS; 11346; 14 hits in 1073 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 201 other tissues.
DR Genevisible; Q8N3V7; HS.
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:UniProtKB.
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 InterPro; IPR028753; Synpo.
DR PANTHER; PTHR24217:SF13; PTHR24217:SF13; 1.
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
