SYNP2_HUMAN
ID SYNP2_HUMAN Reviewed; 1093 AA.
AC Q9UMS6; B2RWP6; B2Y8J9; C6H0M7; Q9UK89; S5XAM4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Synaptopodin-2;
DE AltName: Full=Genethonin-2;
DE AltName: Full=Myopodin;
GN Name=SYNPO2;
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), ALTERNATIVE SPLICING (ISOFORMS 1; 2
RP AND 3), SUBCELLULAR LOCATION, AND VARIANT ALA-573.
RX PubMed=18371299; DOI=10.1016/j.bbrc.2008.03.086;
RA De Ganck A., De Corte V., Staes A., Gevaert K., Vandekerckhove J.,
RA Gettemans J.;
RT "Multiple isoforms of the tumor suppressor myopodin are simultaneously
RT transcribed in cancer cells.";
RL Biochem. Biophys. Res. Commun. 370:269-273(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT ALA-573, FUNCTION (ISOFORMS
RP 1; 2; 3; 4 AND 5), AND SUBCELLULAR LOCATION (ISOFORMS 1; 2; 3; 4 AND 5).
RX PubMed=24005909; DOI=10.1096/fj.13-231571;
RA Kai F., Duncan R.;
RT "Prostate cancer cell migration induced by myopodin isoforms is associated
RT with formation of morphologically and biochemically distinct actin
RT networks.";
RL FASEB J. 27:5046-5058(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ALA-573, INTERACTION WITH
RP FLNC AND ACTN2, TISSUE SPECIFICITY (ISOFORM 5), ALTERNATIVE PROMOTER USAGE,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=20554076; DOI=10.1016/j.ejcb.2010.04.004;
RA Linnemann A., van der Ven P.F., Vakeel P., Albinus B., Simonis D.,
RA Bendas G., Schenk J.A., Micheel B., Kley R.A., Fuerst D.O.;
RT "The sarcomeric Z-disc component myopodin is a multiadapter protein that
RT interacts with filamin and alpha-actinin.";
RL Eur. J. Cell Biol. 89:681-692(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-154
RP AND ALA-573.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-573.
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 2), AND VARIANT ALA-573.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 263-1093 (ISOFORM 1), AND VARIANT ALA-573.
RX PubMed=11673475; DOI=10.1083/jcb.200012039;
RA Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.;
RT "Differentiation and stress-dependent nuclear-cytoplasmic redistribution of
RT myopodin, a novel actin bundling protein.";
RL J. Cell Biol. 155:393-404(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 961-1093, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=11297942; DOI=10.1016/s0960-8966(00)00198-x;
RA Tkatchenko A.V., Pietu G., Cros N., Gannoun-Zaki L., Auffray C.,
RA Leger J.J., Dechesne C.A.;
RT "Identification of altered gene expression in skeletal muscles from
RT Duchenne muscular dystrophy patients.";
RL Neuromuscul. Disord. 11:269-277(2001).
RN [10]
RP INTERACTION WITH ZYX, AND FUNCTION.
RX PubMed=16885336; DOI=10.1158/0008-5472.can-06-0227;
RA Yu Y.P., Luo J.H.;
RT "Myopodin-mediated suppression of prostate cancer cell migration involves
RT interaction with zyxin.";
RL Cancer Res. 66:7414-7419(2006).
RN [11]
RP INTERACTION WITH IPO13.
RX PubMed=17828378; DOI=10.1007/s11010-007-9588-1;
RA Liang J., Ke G., You W., Peng Z., Lan J., Kalesse M., Tartakoff A.M.,
RA Kaplan F., Tao T.;
RT "Interaction between importin 13 and myopodin suggests a nuclear import
RT pathway for myopodin.";
RL Mol. Cell. Biochem. 307:93-100(2008).
RN [12]
RP INTERACTION WITH ILK, AND PHOSPHORYLATION.
RX PubMed=21643011; DOI=10.1038/onc.2011.200;
RA Yu Y.P., Luo J.H.;
RT "Phosphorylation and interaction of myopodin by integrin-link kinase lead
RT to suppression of cell growth and motility in prostate cancer cells.";
RL Oncogene 30:4855-4863(2011).
RN [13]
RP FUNCTION (ISOFORMS 1; 2; 3 AND 5), AND ALTERNATIVE SPLICING (ISOFORMS 1; 2;
RP 3 AND 5).
RX PubMed=22915763; DOI=10.1093/carcin/bgs268;
RA Kai F., Tanner K., King C., Duncan R.;
RT "Myopodin isoforms alter the chemokinetic response of PC3 cells in response
RT to different migration stimuli via differential effects on Rho-ROCK
RT signaling pathways.";
RL Carcinogenesis 33:2100-2107(2012).
RN [14]
RP INTERACTION WITH BAG3 AND VPS18, ASSOCIATION WITH THE CASA COMPLEX, AND
RP DOMAIN.
RX PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
RA Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
RA Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
RA Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
RT "Cellular mechanotransduction relies on tension-induced and chaperone-
RT assisted autophagy.";
RL Curr. Biol. 23:430-435(2013).
RN [15]
RP FUNCTION, ACTIN-BINDING, AND SELF-ASSOCIATION.
RX PubMed=23225103; DOI=10.1007/s10974-012-9334-5;
RA Linnemann A., Vakeel P., Bezerra E., Orfanos Z., Djinovic-Carugo K.,
RA van der Ven P.F., Kirfel G., Fuerst D.O.;
RT "Myopodin is an F-actin bundling protein with multiple independent actin-
RT binding regions.";
RL J. Muscle Res. Cell Motil. 34:61-69(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; THR-610; SER-611;
RP TYR-622; THR-626; SER-729; THR-755; THR-774; SER-777; SER-902; SER-906 AND
RP SER-1056, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 (ISOFORM 4), AND
RP 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 [17]
RP FUNCTION (ISOFORM 5).
RX PubMed=25883213; DOI=10.18632/oncotarget.3578;
RA Kai F., Fawcett J.P., Duncan R.;
RT "Synaptopodin-2 induces assembly of peripheral actin bundles and immature
RT focal adhesions to promote lamellipodia formation and prostate cancer cell
RT migration.";
RL Oncotarget 6:11162-11174(2015).
CC -!- FUNCTION: Has an actin-binding and actin-bundling activity. Can induce
CC the formation of F-actin networks in an isoform-specific manner
CC (PubMed:24005909, PubMed:23225103). At the sarcomeric Z lines is
CC proposed to act as adapter protein that links nascent myofibers to the
CC sarcolemma via ZYX and may play a role in early assembly and
CC stabilization of the Z lines. Involved in autophagosome formation. May
CC play a role in chaperone-assisted selective autophagy (CASA) involved
CC in Z lines maintenance in striated muscle under mechanical tension; may
CC link the client-processing CASA chaperone machinery to a membrane-
CC tethering and fusion complex providing autophagosome membranes (By
CC similarity). Involved in regulation of cell migration (PubMed:22915763,
CC PubMed:25883213). May be a tumor suppressor (PubMed:16885336).
CC {ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q91YE8,
CC ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:23225103,
CC ECO:0000269|PubMed:24005909, ECO:0000269|PubMed:25883213,
CC ECO:0000305|PubMed:16885336, ECO:0000305|PubMed:20554076}.
CC -!- FUNCTION: [Isoform 1]: Involved in regulation of cell migration. Can
CC induce formation of thick, irregular actin bundles in the cell body.
CC {ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:24005909}.
CC -!- FUNCTION: [Isoform 2]: Involved in regulation of cell migration. Can
CC induce long, well-organized actin bundles frequently orientated in
CC parallel along the long axis of the cell showing characteristics of
CC contractile ventral stress fibers. {ECO:0000269|PubMed:22915763,
CC ECO:0000269|PubMed:24005909}.
CC -!- FUNCTION: [Isoform 3]: Involved in regulation of cell migration. Can
CC induce an amorphous actin meshwork throughout the cell body containing
CC a mixture of long and short, randomly organized thick and thin actin
CC bundles. {ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:24005909}.
CC -!- FUNCTION: [Isoform 4]: Can induce long, well-organized actin bundles
CC frequently orientated in parallel along the long axis of the cell
CC showing characteristics of contractile ventral stress fibers.
CC {ECO:0000269|PubMed:24005909}.
CC -!- FUNCTION: [Isoform 5]: Involved in regulation of cell migration in part
CC dependent on the Rho-ROCK cascade; can promote formation of nascent
CC focal adhesions, actin bundles at the leading cell edge and
CC lamellipodia (PubMed:22915763, PubMed:25883213). Can induce formation
CC of thick, irregular actin bundles in the cell body; the induced actin
CC network is associated with enhanced cell migration in vitro.
CC {ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:24005909,
CC ECO:0000269|PubMed:25883213}.
CC -!- SUBUNIT: May self-associate in muscle cells under oxidative stress.
CC Binds F-actin (PubMed:23225103). Interacts with ACTN2; ACTN2 is
CC proposed to anchor SYOP2 at Z lines in mature myocytes
CC (PubMed:20554076). Interacts with AKAP6, PPP3CA and CAMK2A. Interacts
CC (phosphorylated form) with YWHAB; YWHAB competes with ACTN2 for
CC interaction with SYNPO2. Interacts with KPNA2; mediating nuclear import
CC of SYNOP2; dependent on interaction with YWHAB (By similarity).
CC Interacts with IPO13; may be implicated in SYNOP2 nuclear import
CC (PubMed:17828378). Interacts with ZYX, FLNC, ILK (PubMed:16885336,
CC PubMed:20554076, PubMed:21643011). Interacts with BAG3 (via WW 1
CC domain). May associate with the CASA complex consisting of HSPA8, HSPB8
CC and BAG3. Interacts with VPS18 (PubMed:23434281).
CC {ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q91YE8,
CC ECO:0000269|PubMed:16885336, ECO:0000269|PubMed:17828378,
CC ECO:0000269|PubMed:20554076, ECO:0000269|PubMed:21643011,
CC ECO:0000269|PubMed:23434281}.
CC -!- INTERACTION:
CC Q9UMS6; Q13418: ILK; NbExp=6; IntAct=EBI-3453434, EBI-747644;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:20554076}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:20554076}. Note=Shuttles between the nucleus and
CC the cytoplasm in a differentiation-dependent and stress-induced
CC fashion. In undifferentiated myoblasts strongly expressed in the
CC nucleus, after induction of myotube differentiation is located to both
CC nucleus and cytoplasm along acting filaments, and in differentiated
CC myotubes is located at the Z lines. Upon stress redistributes from
CC cytoplasm of myoblasts and myotubes to the nucleus. Nuclear import is
CC KPNA2-dependent and promoted by phosphorylation by PKA and/or CaMK2,
CC and inhibition of calcineurin. The nuclear export is XPO1-dependent (By
CC similarity). Localized in a fiber-like pattern, partly overlapping with
CC filamentous actin (PubMed:18371299). {ECO:0000250|UniProtKB:Q91YE8,
CC ECO:0000269|PubMed:18371299}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin bundles
CC with contiguous staining. {ECO:0000269|PubMed:24005909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin bundles
CC with punctuate staining. {ECO:0000269|PubMed:24005909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Note=Localizes to induced irregular
CC actin bundles with contiguous and punctuated staining.
CC {ECO:0000269|PubMed:24005909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin bundles
CC with punctuate staining. {ECO:0000269|PubMed:24005909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin bundles
CC with contiguous staining. {ECO:0000269|PubMed:24005909}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Myo1, SYNOPb, Synop2A;
CC IsoId=Q9UMS6-1; Sequence=Displayed;
CC Name=2; Synonyms=Myo3, SYNOPa, Synop2C;
CC IsoId=Q9UMS6-2; Sequence=VSP_041222;
CC Name=3; Synonyms=Myo2, SYNOPc, Synop2B;
CC IsoId=Q9UMS6-3; Sequence=VSP_041223;
CC Name=4; Synonyms=Myo4, Synop2D;
CC IsoId=Q9UMS6-4; Sequence=VSP_053771, VSP_041222;
CC Name=5; Synonyms=(delta)N-MYO1, SYNOPd, SYNOP2As;
CC IsoId=Q9UMS6-5; Sequence=VSP_058887;
CC -!- TISSUE SPECIFICITY: Expressed in heart muscle. Isoform 5 is
CC specifically expressed in skeletal muscle.
CC {ECO:0000269|PubMed:11297942, ECO:0000269|PubMed:20554076}.
CC -!- DEVELOPMENTAL STAGE: Detected in myoblasts within 24 h after induction
CC of myogenic differentiation preceeding the expression of sarcomeric
CC alpha-actinin. Specifically at early stages colocalizes with ZYX at
CC focal adhesions. {ECO:0000269|PubMed:20554076}.
CC -!- INDUCTION: Down-regulated in muscle cell lines derived from patients
CC with Duchenne muscular dystrophy (DMD). {ECO:0000269|PubMed:11297942}.
CC -!- DOMAIN: The PPPY motif interacts with the WW domain 1 of BAG3.
CC {ECO:0000305|PubMed:23434281}.
CC -!- PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites.
CC Dephosphorylated by calcineurin; abrogating interaction with YWHAB and
CC impairing nuclear import (By similarity). Phosphorylated by ILK.
CC {ECO:0000250|UniProtKB:Q91YE8, ECO:0000269|PubMed:21643011}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: =Produced by alternative splicing of
CC isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: =Produced by alternative splicing of
CC isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: =Produced by alternative splicing of
CC isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:20554076}.
CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SYNPO2ID488.html";
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DR EMBL; EU481975; ACC93875.1; -; mRNA.
DR EMBL; KF147165; AGS94404.1; -; mRNA.
DR EMBL; AL832031; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL833294; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC096745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471229; EAW73659.1; -; Genomic_DNA.
DR EMBL; FN422000; CAZ66141.1; -; mRNA.
DR EMBL; BC150629; AAI50630.1; -; mRNA.
DR EMBL; AJ010482; CAB51856.1; -; mRNA.
DR EMBL; AF177291; AAD55264.1; -; mRNA.
DR CCDS; CCDS34054.1; -. [Q9UMS6-2]
DR CCDS; CCDS47128.1; -. [Q9UMS6-3]
DR CCDS; CCDS47129.1; -. [Q9UMS6-1]
DR CCDS; CCDS75185.1; -. [Q9UMS6-4]
DR RefSeq; NP_001122405.1; NM_001128933.2. [Q9UMS6-1]
DR RefSeq; NP_001122406.1; NM_001128934.2. [Q9UMS6-3]
DR RefSeq; NP_001273683.1; NM_001286754.1. [Q9UMS6-4]
DR RefSeq; NP_597734.2; NM_133477.2. [Q9UMS6-2]
DR AlphaFoldDB; Q9UMS6; -.
DR SMR; Q9UMS6; -.
DR BioGRID; 128105; 22.
DR DIP; DIP-47311N; -.
DR IntAct; Q9UMS6; 9.
DR MINT; Q9UMS6; -.
DR STRING; 9606.ENSP00000306015; -.
DR iPTMnet; Q9UMS6; -.
DR PhosphoSitePlus; Q9UMS6; -.
DR BioMuta; SYNPO2; -.
DR DMDM; 51702160; -.
DR EPD; Q9UMS6; -.
DR jPOST; Q9UMS6; -.
DR MassIVE; Q9UMS6; -.
DR MaxQB; Q9UMS6; -.
DR PaxDb; Q9UMS6; -.
DR PeptideAtlas; Q9UMS6; -.
DR PRIDE; Q9UMS6; -.
DR ProteomicsDB; 85210; -. [Q9UMS6-1]
DR ProteomicsDB; 85211; -. [Q9UMS6-2]
DR ProteomicsDB; 85212; -. [Q9UMS6-3]
DR Antibodypedia; 48857; 93 antibodies from 25 providers.
DR DNASU; 171024; -.
DR Ensembl; ENST00000307142.9; ENSP00000306015.4; ENSG00000172403.11. [Q9UMS6-2]
DR Ensembl; ENST00000429713.7; ENSP00000395143.2; ENSG00000172403.11. [Q9UMS6-1]
DR Ensembl; ENST00000434046.6; ENSP00000390965.2; ENSG00000172403.11. [Q9UMS6-3]
DR Ensembl; ENST00000610556.4; ENSP00000484885.1; ENSG00000172403.11. [Q9UMS6-4]
DR Ensembl; ENST00000627783.2; ENSP00000498985.1; ENSG00000172403.11. [Q9UMS6-5]
DR GeneID; 171024; -.
DR KEGG; hsa:171024; -.
DR MANE-Select; ENST00000307142.9; ENSP00000306015.4; NM_133477.3; NP_597734.2. [Q9UMS6-2]
DR UCSC; uc003icm.6; human. [Q9UMS6-1]
DR CTD; 171024; -.
DR DisGeNET; 171024; -.
DR GeneCards; SYNPO2; -.
DR HGNC; HGNC:17732; SYNPO2.
DR HPA; ENSG00000172403; Tissue enhanced (skeletal muscle, tongue).
DR neXtProt; NX_Q9UMS6; -.
DR OpenTargets; ENSG00000172403; -.
DR PharmGKB; PA38244; -.
DR VEuPathDB; HostDB:ENSG00000172403; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00950000183054; -.
DR HOGENOM; CLU_007120_0_0_1; -.
DR InParanoid; Q9UMS6; -.
DR OMA; LDCSDRE; -.
DR OrthoDB; 109454at2759; -.
DR PhylomeDB; Q9UMS6; -.
DR TreeFam; TF330867; -.
DR PathwayCommons; Q9UMS6; -.
DR SignaLink; Q9UMS6; -.
DR BioGRID-ORCS; 171024; 4 hits in 1064 CRISPR screens.
DR ChiTaRS; SYNPO2; human.
DR GeneWiki; SYNPO2; -.
DR GenomeRNAi; 171024; -.
DR Pharos; Q9UMS6; Tbio.
DR PRO; PR:Q9UMS6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UMS6; protein.
DR Bgee; ENSG00000172403; Expressed in saphenous vein and 188 other tissues.
DR ExpressionAtlas; Q9UMS6; baseline and differential.
DR Genevisible; Q9UMS6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0099023; C:vesicle tethering complex; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; IDA:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0051371; F:muscle alpha-actinin binding; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative promoter usage; Alternative splicing;
KW Cell junction; Cytoplasm; Cytoskeleton; Muscle protein; Nucleus;
KW Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..1093
FT /note="Synaptopodin-2"
FT /id="PRO_0000187673"
FT DOMAIN 6..88
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..180
FT /note="Interaction with VPS18"
FT /evidence="ECO:0000269|PubMed:23434281"
FT REGION 144..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..663
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000269|PubMed:20554076"
FT REGION 507..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..663
FT /note="F-actin binding"
FT /evidence="ECO:0000269|PubMed:23225103"
FT REGION 607..811
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT REGION 615..626
FT /note="Interaction with BAG3"
FT /evidence="ECO:0000269|PubMed:23434281"
FT REGION 664..924
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000269|PubMed:20554076"
FT REGION 664..916
FT /note="F-actin bundling activity"
FT /evidence="ECO:0000269|PubMed:23225103"
FT REGION 664..803
FT /note="F-actin binding"
FT /evidence="ECO:0000269|PubMed:23225103"
FT REGION 751..900
FT /note="Actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT REGION 810..1093
FT /note="Interaction with FLNC"
FT /evidence="ECO:0000269|PubMed:20554076"
FT REGION 834..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..1093
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000269|PubMed:20554076"
FT REGION 937..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1019
FT /note="Interaction with ZYX"
FT /evidence="ECO:0000269|PubMed:16885336"
FT REGION 1041..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 398..406
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOTIF 619..622
FT /note="PPPY motif"
FT /evidence="ECO:0000305|PubMed:23434281"
FT COMPBIAS 564..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 622
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..395
FT /note="Missing (in isoform 5)"
FT /id="VSP_058887"
FT VAR_SEQ 1..35
FT /note="MGTGDFICISMTGGAPWGFRLQGGKEQKQPLQVAK -> MVTQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:22915763"
FT /id="VSP_053771"
FT VAR_SEQ 1085..1093
FT /note="VWKPSVVEE -> ESGRSLSLPGRSVPPPISTSPWVYQPTYSYSSKPTDGLE
FT KANKRPTPWEAAAKSPLGLVDDAFQPRNIQESIVANVVSAARRKVLPGPPEDWNERLSY
FT IPQTQKAYMGSCGRQEYNVTANNNMSTTSQYGSQLPYAYYRQASRNDSAIMSMETRSDY
FT CLPVADYNYNPHPRGWRRQT (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:22915763"
FT /id="VSP_041222"
FT VAR_SEQ 1086..1093
FT /note="WKPSVVEE -> KCKSGIHSQDIIRTYFPAYLSSST (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18371299"
FT /id="VSP_041223"
FT VARIANT 154
FT /note="G -> A (in dbSNP:rs12645298)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_057256"
FT VARIANT 174
FT /note="Q -> H (in dbSNP:rs17263971)"
FT /id="VAR_057257"
FT VARIANT 179
FT /note="A -> T (in dbSNP:rs17050152)"
FT /id="VAR_057258"
FT VARIANT 573
FT /note="T -> A (in dbSNP:rs7698598)"
FT /evidence="ECO:0000269|PubMed:11673475,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:18371299, ECO:0000269|PubMed:22915763,
FT ECO:0000269|Ref.6"
FT /id="VAR_019670"
FT CONFLICT 61
FT /note="C -> R (in Ref. 4; AL832031)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="Missing (in Ref. 4; AL832031)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..266
FT /note="SSGR -> IRHE (in Ref. 8; CAB51856)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="Q -> P (in Ref. 2; AGS94404)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="I -> M (in Ref. 4; AL832031)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="P -> L (in Ref. 7; AAI50630)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="G -> V (in Ref. 7; AAI50630)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9UMS6-2:1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9UMS6-4:1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1093 AA; 117514 MW; 8DF6F4D2823B444D CRC64;
MGTGDFICIS MTGGAPWGFR LQGGKEQKQP LQVAKIRNQS KASGSGLCEG DEVVSINGNP
CADLTYPEVI KLMESITDSL QMLIKRPSSG ISEALISENE NKNLEHLTHG GYVESTTLQI
RPATKTQCTE FFLAPVKTEV PLAENQRSGP DCAGSLKEET GPSYQRAPQM PDSQRGRVAE
ELILREKVEA VQPGPVVELQ LSLSQERHKG ASGPLVALPG AEKSKSPDPD PNLSHDRIVH
INSIPTNEKA DPFLRSSKII QISSGRELRV IQESEAGDAG LPRVEVILDC SDRQKTEGCR
LQAGKECVDS PVEGGQSEAP PSLVSFAVSS EGTEQGEDPR SEKDHSRPHK HRARHARLRR
SESLSEKQVK EAKSKCKSIA LLLTDAPNPN SKGVLMFKKR RRRARKYTLV SYGTGELERE
ADEEEEGDKE DTCEVAFLGA SESEVDEELL SDVDDNTQVV NFDWDSGLVD IEKKLNRGDK
MEMLPDTTGK GALMFAKRRE RMDQITAQKE EDKVGGTPSR EQDAAQTDGL RTTTSYQRKE
EESVRTQSSV SKSYIEVSHG LGHVPQQNGF SGTSETANIQ RMVPMNRTAK PFPGSVNQPA
TPFSPTRNMT SPIADFPAPP PYSAVTPPPD AFSRGVSSPI AGPAQPPPWP QPAPWSQPAF
YDSSERIASR DERISVPAKR TGILQEAKRR STTKPMFTFK EPKVSPNPEL LSLLQNSEGK
RGTGAGGDSG PEEDYLSLGA EACNFMQSSS AKQKTPPPVA PKPAVKSSSS QPVTPVSPVW
SPGVAPTQPP AFPTSNPSKG TVVSSIKIAQ PSYPPARPAS TLNVAGPFKG PQAAVASQNY
TPKPTVSTPT VNAVQPGAVG PSNELPGMSG RGAQLFAKRQ SRMEKYVVDS DTVQAHAARA
QSPTPSLPAS WKYSSNVRAP PPVAYNPIHS PSYPLAALKS QPSAAQPSKM GKKKGKKPLN
ALDVMKHQPY QLNASLFTFQ PPDAKDGLPQ KSSVKVNSAL AMKQALPPRP VNAASPTNVQ
ASSVYSVPAY TSPPSFFAEA SSPVSASPVP VGIPTSPKQE SASSSYFVAP RPKFSAKKSG
VTIQVWKPSV VEE
