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Synaptopodin-2 (Genethonin-2) (Myopodin)

 SYNP2_HUMAN             Reviewed;        1093 AA.
Q9UMS6; B2RWP6; B2Y8J9; C6H0M7; Q9UK89; S5XAM4;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
12-SEP-2018, entry version 144.
RecName: Full=Synaptopodin-2;
AltName: Full=Genethonin-2;
AltName: Full=Myopodin;
Name=SYNPO2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS
1; 2 AND 3), SUBCELLULAR LOCATION, AND VARIANT ALA-573.
PubMed=18371299; DOI=10.1016/j.bbrc.2008.03.086;
De Ganck A., De Corte V., Staes A., Gevaert K., Vandekerckhove J.,
Gettemans J.;
"Multiple isoforms of the tumor suppressor myopodin are simultaneously
transcribed in cancer cells.";
Biochem. Biophys. Res. Commun. 370:269-273(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT ALA-573, FUNCTION
(ISOFORMS 1; 2; 3; 4 AND 5), AND SUBCELLULAR LOCATION (ISOFORMS 1; 2;
3; 4 AND 5).
PubMed=24005909; DOI=10.1096/fj.13-231571;
Kai F., Duncan R.;
"Prostate cancer cell migration induced by myopodin isoforms is
associated with formation of morphologically and biochemically
distinct actin networks.";
FASEB J. 27:5046-5058(2013).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ALA-573, INTERACTION
WITH FLNC AND ACTN2, TISSUE SPECIFICITY (ISOFORM 5), ALTERNATIVE
PROMOTER USAGE, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
TISSUE=Skeletal muscle;
PubMed=20554076; DOI=10.1016/j.ejcb.2010.04.004;
Linnemann A., van der Ven P.F., Vakeel P., Albinus B., Simonis D.,
Bendas G., Schenk J.A., Micheel B., Kley R.A., Fuerst D.O.;
"The sarcomeric Z-disc component myopodin is a multiadapter protein
that interacts with filamin and alpha-actinin.";
Eur. J. Cell Biol. 89:681-692(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-154 AND ALA-573.
TISSUE=Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-573.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-573.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 263-1093 (ISOFORM 1), AND VARIANT
ALA-573.
PubMed=11673475; DOI=10.1083/jcb.200012039;
Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.;
"Differentiation and stress-dependent nuclear-cytoplasmic
redistribution of myopodin, a novel actin bundling protein.";
J. Cell Biol. 155:393-404(2001).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 961-1093, INDUCTION, AND TISSUE
SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=11297942; DOI=10.1016/S0960-8966(00)00198-X;
Tkatchenko A.V., Pietu G., Cros N., Gannoun-Zaki L., Auffray C.,
Leger J.J., Dechesne C.A.;
"Identification of altered gene expression in skeletal muscles from
Duchenne muscular dystrophy patients.";
Neuromuscul. Disord. 11:269-277(2001).
[10]
INTERACTION WITH ZYX, AND FUNCTION.
PubMed=16885336; DOI=10.1158/0008-5472.CAN-06-0227;
Yu Y.P., Luo J.H.;
"Myopodin-mediated suppression of prostate cancer cell migration
involves interaction with zyxin.";
Cancer Res. 66:7414-7419(2006).
[11]
INTERACTION WITH IPO13.
PubMed=17828378; DOI=10.1007/s11010-007-9588-1;
Liang J., Ke G., You W., Peng Z., Lan J., Kalesse M., Tartakoff A.M.,
Kaplan F., Tao T.;
"Interaction between importin 13 and myopodin suggests a nuclear
import pathway for myopodin.";
Mol. Cell. Biochem. 307:93-100(2008).
[12]
INTERACTION WITH ILK, AND PHOSPHORYLATION.
PubMed=21643011; DOI=10.1038/onc.2011.200;
Yu Y.P., Luo J.H.;
"Phosphorylation and interaction of myopodin by integrin-link kinase
lead to suppression of cell growth and motility in prostate cancer
cells.";
Oncogene 30:4855-4863(2011).
[13]
FUNCTION (ISOFORMS 1; 2; 3 AND 5), AND ALTERNATIVE SPLICING (ISOFORMS
1; 2; 3 AND 5).
PubMed=22915763; DOI=10.1093/carcin/bgs268;
Kai F., Tanner K., King C., Duncan R.;
"Myopodin isoforms alter the chemokinetic response of PC3 cells in
response to different migration stimuli via differential effects on
Rho-ROCK signaling pathways.";
Carcinogenesis 33:2100-2107(2012).
[14]
INTERACTION WITH BAG3 AND VPS18, ASSOCIATION WITH THE CASA COMPLEX,
AND DOMAIN.
PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
"Cellular mechanotransduction relies on tension-induced and chaperone-
assisted autophagy.";
Curr. Biol. 23:430-435(2013).
[15]
FUNCTION, ACTIN-BINDING, AND SELF-ASSOCIATION.
PubMed=23225103; DOI=10.1007/s10974-012-9334-5;
Linnemann A., Vakeel P., Bezerra E., Orfanos Z., Djinovic-Carugo K.,
van der Ven P.F., Kirfel G., Fuerst D.O.;
"Myopodin is an F-actin bundling protein with multiple independent
actin-binding regions.";
J. Muscle Res. Cell Motil. 34:61-69(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; THR-610; SER-611;
TYR-622; THR-626; SER-729; THR-755; THR-774; SER-777; SER-902; SER-906
AND SER-1056, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138
(ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107
(ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION (ISOFORM 5).
PubMed=25883213; DOI=10.18632/oncotarget.3578;
Kai F., Fawcett J.P., Duncan R.;
"Synaptopodin-2 induces assembly of peripheral actin bundles and
immature focal adhesions to promote lamellipodia formation and
prostate cancer cell migration.";
Oncotarget 6:11162-11174(2015).
-!- FUNCTION: Has an actin-binding and actin-bundling activity. Can
induce the formation of F-actin networks in an isoform-specific
manner (PubMed:24005909, PubMed:23225103). At the sarcomeric Z
lines is proposed to act as adapter protein that links nascent
myofibers to the sarcolemma via ZYX and may play a role in early
assembly and stabilization of the Z lines. Involved in
autophagosome formation. May play a role in chaperone-assisted
selective autophagy (CASA) involved in Z lines maintenance in
striated muscle under mechanical tension; may link the client-
processing CASA chaperone machinery to a membrane-tethering and
fusion complex providing autophagosome membranes (By similarity).
Involved in regulation of cell migration (PubMed:22915763,
PubMed:25883213). May be a tumor suppressor (PubMed:16885336).
{ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q91YE8,
ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:23225103,
ECO:0000269|PubMed:24005909, ECO:0000269|PubMed:25883213,
ECO:0000305|PubMed:16885336, ECO:0000305|PubMed:20554076}.
-!- FUNCTION: Isoform 1: Involved in regulation of cell migration. Can
induce formation of thick, irregular actin bundles in the cell
body. {ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:24005909}.
-!- FUNCTION: Isoform 2: Involved in regulation of cell migration. Can
induce long, well-organized actin bundles frequently orientated in
parallel along the long axis of the cell showing characteristics
of contractile ventral stress fibers.
{ECO:0000269|PubMed:22915763, ECO:0000269|PubMed:24005909}.
-!- FUNCTION: Isoform 3: Involved in regulation of cell migration. Can
induce an amorphous actin meshwork throughout the cell body
containing a mixture of long and short, randomly organized thick
and thin actin bundles. {ECO:0000269|PubMed:22915763,
ECO:0000269|PubMed:24005909}.
-!- FUNCTION: Isoform 4: Can induce long, well-organized actin bundles
frequently orientated in parallel along the long axis of the cell
showing characteristics of contractile ventral stress fibers.
{ECO:0000269|PubMed:24005909}.
-!- FUNCTION: Isoform 5: Involved in regulation of cell migration in
part dependent on the Rho-ROCK cascade; can promote formation of
nascent focal adhesions, actin bundles at the leading cell edge
and lamellipodia (PubMed:22915763, PubMed:25883213). Can induce
formation of thick, irregular actin bundles in the cell body; the
induced actin network is associated with enhanced cell migration
in vitro. {ECO:0000269|PubMed:22915763,
ECO:0000269|PubMed:24005909, ECO:0000269|PubMed:25883213}.
-!- SUBUNIT: May self-associate in muscle cells under oxidative
stress. Binds F-actin (PubMed:23225103). Interacts with ACTN2;
ACTN2 is proposed to anchor SYOP2 at Z lines in mature myocytes
(PubMed:20554076). Interacts with AKAP6, PPP3CA and CAMK2A.
Interacts (phosphorylated form) with YWHAB; YWHAB competes with
ACTN2 for interaction with SYNPO2. Interacts with KPNA2; mediating
nuclear import of SYNOP2; dependent on interaction with YWHAB (By
similarity). Interacts with IPO13; may be implicated in SYNOP2
nuclear import (PubMed:17828378). Interacts with ZYX, FLNC, ILK
(PubMed:16885336, PubMed:20554076, PubMed:21643011). Interacts
with BAG3 (via WW 1 domain). May associate with the CASA complex
consisting of HSPA8, HSPB8 and BAG3. Interacts with VPS18
(PubMed:23434281). {ECO:0000250|UniProtKB:D4A702,
ECO:0000250|UniProtKB:Q91YE8, ECO:0000269|PubMed:16885336,
ECO:0000269|PubMed:17828378, ECO:0000269|PubMed:20554076,
ECO:0000269|PubMed:21643011, ECO:0000269|PubMed:23434281}.
-!- INTERACTION:
Q13418:ILK; NbExp=6; IntAct=EBI-3453434, EBI-747644;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91YE8}.
Cytoplasm {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Cytoplasm, myofibril, sarcomere, Z
line {ECO:0000269|PubMed:20554076}. Cell junction, focal adhesion
{ECO:0000269|PubMed:20554076}. Note=Shuttles between the nucleus
and the cytoplasm in a differentiation-dependent and stress-
induced fashion. In undifferentiated myoblasts strongly expressed
in the nucleus, after induction of myotube differentiation is
located to both nucleus and cytoplasm along acting filaments, and
in differentiated myotubes is located at the Z lines. Upon stress
redistributes from cytoplasm of myoblasts and myotubes to the
nucleus. Nuclear import is KPNA2-dependent and promoted by
phosphorylation by PKA and/or CaMK2, and inhibition of
calcineurin. The nuclear export is XPO1-dependent (By similarity).
Localized in a fiber-like pattern, partly overlapping with
filamentous actin (PubMed:18371299).
{ECO:0000250|UniProtKB:Q91YE8, ECO:0000269|PubMed:18371299}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin
bundles with contiguous staining. {ECO:0000269|PubMed:24005909}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin
bundles with punctuate staining. {ECO:0000269|PubMed:24005909}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Note=Localizes to induced irregular
actin bundles with contiguous and punctuated staining.
{ECO:0000269|PubMed:24005909}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin
bundles with punctuate staining. {ECO:0000269|PubMed:24005909}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24005909}. Note=Localizes to induced actin
bundles with contiguous staining. {ECO:0000269|PubMed:24005909}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Myo1, SYNOPb, Synop2A;
IsoId=Q9UMS6-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=Myo3, SYNOPa, Synop2C;
IsoId=Q9UMS6-2; Sequence=VSP_041222;
Note==Produced by alternative splicing of isoform 1. Contains a
phosphoserine at position 1138. {ECO:0000244|PubMed:24275569};
Name=3; Synonyms=Myo2, SYNOPc, Synop2B;
IsoId=Q9UMS6-3; Sequence=VSP_041223;
Note==Produced by alternative splicing of isoform 1.;
Name=4; Synonyms=Myo4, Synop2D;
IsoId=Q9UMS6-4; Sequence=VSP_053771, VSP_041222;
Note==Produced by alternative splicing of isoform 1. Contains a
phosphoserine at position 1107. {ECO:0000244|PubMed:24275569};
Name=5; Synonyms=(delta)N-MYO1, SYNOPd, SYNOP2As;
IsoId=Q9UMS6-5; Sequence=VSP_058887;
Note=Produced by alternative promoter usage.
{ECO:0000269|PubMed:20554076};
-!- TISSUE SPECIFICITY: Expressed in heart muscle. Isoform 5 is
specifically expressed in skeletal muscle.
{ECO:0000269|PubMed:11297942, ECO:0000269|PubMed:20554076}.
-!- DEVELOPMENTAL STAGE: Detected in myoblasts within 24 h after
induction of myogenic differentiation preceeding the expression of
sarcomeric alpha-actinin. Specifically at early stages colocalizes
with ZYX at focal adhesions. {ECO:0000269|PubMed:20554076}.
-!- INDUCTION: Down-regulated in muscle cell lines derived from
patients with Duchenne muscular dystrophy (DMD).
{ECO:0000269|PubMed:11297942}.
-!- DOMAIN: The PPPY motif interacts with the WW domain 1 of BAG3.
{ECO:0000305|PubMed:23434281}.
-!- PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites.
Dephosphorylated by calcineurin; abrogating interaction with YWHAB
and impairing nuclear import (By similarity). Phosphorylated by
ILK. {ECO:0000250|UniProtKB:Q91YE8, ECO:0000269|PubMed:21643011}.
-!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SYNPO2ID488.html";
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EMBL; EU481975; ACC93875.1; -; mRNA.
EMBL; KF147165; AGS94404.1; -; mRNA.
EMBL; AL832031; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL833294; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC096745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471229; EAW73659.1; -; Genomic_DNA.
EMBL; FN422000; CAZ66141.1; -; mRNA.
EMBL; BC150629; AAI50630.1; -; mRNA.
EMBL; AJ010482; CAB51856.1; -; mRNA.
EMBL; AF177291; AAD55264.1; -; mRNA.
CCDS; CCDS34054.1; -. [Q9UMS6-2]
CCDS; CCDS47128.1; -. [Q9UMS6-3]
CCDS; CCDS47129.1; -. [Q9UMS6-1]
CCDS; CCDS75185.1; -. [Q9UMS6-4]
RefSeq; NP_001122405.1; NM_001128933.2. [Q9UMS6-1]
RefSeq; NP_001122406.1; NM_001128934.2. [Q9UMS6-3]
RefSeq; NP_001273683.1; NM_001286754.1. [Q9UMS6-4]
RefSeq; NP_597734.2; NM_133477.2. [Q9UMS6-2]
UniGene; Hs.655519; -.
ProteinModelPortal; Q9UMS6; -.
SMR; Q9UMS6; -.
BioGrid; 128105; 20.
DIP; DIP-47311N; -.
IntAct; Q9UMS6; 7.
MINT; Q9UMS6; -.
STRING; 9606.ENSP00000306015; -.
iPTMnet; Q9UMS6; -.
PhosphoSitePlus; Q9UMS6; -.
BioMuta; SYNPO2; -.
DMDM; 51702160; -.
PaxDb; Q9UMS6; -.
PeptideAtlas; Q9UMS6; -.
PRIDE; Q9UMS6; -.
ProteomicsDB; 85210; -.
ProteomicsDB; 85211; -. [Q9UMS6-2]
ProteomicsDB; 85212; -. [Q9UMS6-3]
DNASU; 171024; -.
Ensembl; ENST00000307142; ENSP00000306015; ENSG00000172403. [Q9UMS6-2]
Ensembl; ENST00000429713; ENSP00000395143; ENSG00000172403. [Q9UMS6-1]
Ensembl; ENST00000434046; ENSP00000390965; ENSG00000172403. [Q9UMS6-3]
Ensembl; ENST00000610556; ENSP00000484885; ENSG00000172403. [Q9UMS6-4]
GeneID; 171024; -.
KEGG; hsa:171024; -.
UCSC; uc003icm.6; human. [Q9UMS6-1]
CTD; 171024; -.
DisGeNET; 171024; -.
EuPathDB; HostDB:ENSG00000172403.10; -.
GeneCards; SYNPO2; -.
HGNC; HGNC:17732; SYNPO2.
HPA; CAB037231; -.
HPA; HPA030665; -.
HPA; HPA049707; -.
HPA; HPA068563; -.
neXtProt; NX_Q9UMS6; -.
OpenTargets; ENSG00000172403; -.
PharmGKB; PA38244; -.
eggNOG; ENOG410IIQE; Eukaryota.
eggNOG; ENOG410ZJ02; LUCA.
GeneTree; ENSGT00530000063754; -.
HOGENOM; HOG000261625; -.
HOVERGEN; HBG079226; -.
InParanoid; Q9UMS6; -.
OMA; RERMDQI; -.
OrthoDB; EOG091G01MS; -.
PhylomeDB; Q9UMS6; -.
TreeFam; TF330867; -.
ChiTaRS; SYNPO2; human.
GeneWiki; SYNPO2; -.
GenomeRNAi; 171024; -.
PRO; PR:Q9UMS6; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000172403; Expressed in 208 organ(s), highest expression level in cauda epididymis.
CleanEx; HS_SYNPO2; -.
ExpressionAtlas; Q9UMS6; baseline and differential.
Genevisible; Q9UMS6; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0099023; C:tethering complex; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0003779; F:actin binding; IBA:GO_Central.
GO; GO:0051393; F:alpha-actinin binding; IDA:UniProtKB.
GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
GO; GO:0051371; F:muscle alpha-actinin binding; ISS:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF00595; PDZ; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
Actin-binding; Alternative promoter usage; Alternative splicing;
Cell junction; Complete proteome; Cytoplasm; Cytoskeleton;
Muscle protein; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Tumor suppressor.
CHAIN 1 1093 Synaptopodin-2.
/FTId=PRO_0000187673.
DOMAIN 6 88 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 1 180 Interaction with VPS18.
{ECO:0000269|PubMed:23434281}.
REGION 481 663 Interaction with ACTN2.
{ECO:0000269|PubMed:20554076}.
REGION 534 663 F-actin binding.
{ECO:0000269|PubMed:23225103}.
REGION 607 811 Interaction with YWHAB.
{ECO:0000250|UniProtKB:Q91YE8}.
REGION 615 626 Interaction with BAG3.
{ECO:0000269|PubMed:23434281}.
REGION 664 924 Interaction with ACTN2.
{ECO:0000269|PubMed:20554076}.
REGION 664 916 F-actin bundling activity.
{ECO:0000269|PubMed:23225103}.
REGION 664 803 F-actin binding.
{ECO:0000269|PubMed:23225103}.
REGION 751 900 Actin binding.
{ECO:0000250|UniProtKB:Q91YE8}.
REGION 810 1093 Interaction with FLNC.
{ECO:0000269|PubMed:20554076}.
REGION 901 1093 Interaction with ACTN2.
{ECO:0000269|PubMed:20554076}.
REGION 1000 1019 Interaction with ZYX.
{ECO:0000269|PubMed:16885336}.
MOTIF 398 406 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q91YE8}.
MOTIF 619 622 PPPY motif.
{ECO:0000305|PubMed:23434281}.
COMPBIAS 400 405 Poly-Arg.
COMPBIAS 423 426 Poly-Glu.
COMPBIAS 591 658 Pro-rich.
COMPBIAS 756 818 Pro-rich.
COMPBIAS 767 770 Poly-Ser.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE8}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE8}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE8}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE8}.
MOD_RES 610 610 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 622 622 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 626 626 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 755 755 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 774 774 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 777 777 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE8}.
MOD_RES 902 902 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 906 906 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 910 910 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 1015 1015 Phosphoserine.
{ECO:0000250|UniProtKB:D4A702}.
MOD_RES 1056 1056 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 395 Missing (in isoform 5).
/FTId=VSP_058887.
VAR_SEQ 1 35 MGTGDFICISMTGGAPWGFRLQGGKEQKQPLQVAK -> MV
TQ (in isoform 4).
{ECO:0000303|PubMed:22915763}.
/FTId=VSP_053771.
VAR_SEQ 1085 1093 VWKPSVVEE -> ESGRSLSLPGRSVPPPISTSPWVYQPTY
SYSSKPTDGLEKANKRPTPWEAAAKSPLGLVDDAFQPRNIQ
ESIVANVVSAARRKVLPGPPEDWNERLSYIPQTQKAYMGSC
GRQEYNVTANNNMSTTSQYGSQLPYAYYRQASRNDSAIMSM
ETRSDYCLPVADYNYNPHPRGWRRQT (in isoform 2
and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:22915763}.
/FTId=VSP_041222.
VAR_SEQ 1086 1093 WKPSVVEE -> KCKSGIHSQDIIRTYFPAYLSSST (in
isoform 3).
{ECO:0000303|PubMed:18371299}.
/FTId=VSP_041223.
VARIANT 154 154 G -> A (in dbSNP:rs12645298).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_057256.
VARIANT 174 174 Q -> H (in dbSNP:rs17263971).
/FTId=VAR_057257.
VARIANT 179 179 A -> T (in dbSNP:rs17050152).
/FTId=VAR_057258.
VARIANT 573 573 T -> A (in dbSNP:rs7698598).
{ECO:0000269|PubMed:11673475,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:18371299,
ECO:0000269|PubMed:22915763,
ECO:0000269|Ref.6}.
/FTId=VAR_019670.
CONFLICT 61 61 C -> R (in Ref. 4; AL832031).
{ECO:0000305}.
CONFLICT 147 147 Missing (in Ref. 4; AL832031).
{ECO:0000305}.
CONFLICT 263 266 SSGR -> IRHE (in Ref. 8; CAB51856).
{ECO:0000305}.
CONFLICT 508 508 Q -> P (in Ref. 2; AGS94404).
{ECO:0000305}.
CONFLICT 667 667 I -> M (in Ref. 4; AL832031).
{ECO:0000305}.
CONFLICT 969 969 P -> L (in Ref. 7; AAI50630).
{ECO:0000305}.
CONFLICT 987 987 G -> V (in Ref. 7; AAI50630).
{ECO:0000305}.
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


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