SYNPO2
entrez
171024
canonical
uniprot
Q9UMS6
canonical
ensembl
ENSG00000172403
resolver
ensp
ENSP00000306015
resolver
ensp
ENSP00000390965
resolver
ensp
ENSP00000395143
resolver
ensp
ENSP00000412623
resolver
ensp
ENSP00000484885
resolver
ensp
ENSP00000498985
resolver
enst
ENST00000448416
resolver
genesymbol
SYNPO2
resolver
hgnc
HGNC:17732
resolver
uniprot
B2RWP6
resolver
uniprot
B2Y8J9
resolver
uniprot
B4DLE4
resolver
uniprot
B4E258
resolver
uniprot
C6H0M7
resolver
uniprot
F6U138
resolver
uniprot
Q9UK89
resolver
uniprot
S5XAM4
resolver
uniprot_entry
B4DLE4_HUMAN
resolver
uniprot_entry
B4E258_HUMAN
resolver
uniprot_entry
F6U138_HUMAN
resolver
uniprot_entry
SYNP2_HUMAN
resolver
uniprot_sec
B2RWP6
resolver
uniprot_sec
B2Y8J9
resolver
uniprot_sec
C6H0M7
resolver
uniprot_sec
Q9UK89
resolver
uniprot_sec
S5XAM4
resolver
amino_acid_sequence
MGTGDFICISMTGGAPWGFRLQGGKEQKQPLQVAKIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKRPSSGISEALISENENKNLEHLTHGGYVESTTLQIRPATKTQCTEFFLAPVKTEVPLAENQRSGPDCAGSLKEETGPSYQRAPQMPDSQRGRVAEELILREKVEAVQPGPVVELQLSLSQERHKGASGPLVALPGAEKSKSPDPDPNLSHDRIVHINSIPTNEKADPFLRSSKIIQISSGRELRVIQESEAGDAGLPRVEVILDCSDRQKTEGCRLQAGKECVDSPVEGGQSEAPPSLVSFAVSSEGTEQGEDPRSEKDHSRPHKHRARHARLRRSESLSEKQVKEAKSKCKSIALLLTDAPNPNSKGVLMFKKRRRRARKYTLVSYGTGELEREADEEEEGDKEDTCEVAFLGASESEVDEELLSDVDDNTQVVNFDWDSGLVDIEKKLNRGDKMEMLPDTTGKGALMFAKRRERMDQITAQKEEDKVGGTPSREQDAAQTDGLRTTTSYQRKEEESVRTQSSVSKSYIEVSHGLGHVPQQNGFSGTSETANIQRMVPMNRTAKPFPGSVNQPATPFSPTRNMTSPIADFPAPPPYSAVTPPPDAFSRGVSSPIAGPAQPPPWPQPAPWSQPAFYDSSERIASRDERISVPAKRTGILQEAKRRSTTKPMFTFKEPKVSPNPELLSLLQNSEGKRGTGAGGDSGPEEDYLSLGAEACNFMQSSSAKQKTPPPVAPKPAVKSSSSQPVTPVSPVWSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSYPPARPASTLNVAGPFKGPQAAVASQNYTPKPTVSTPTVNAVQPGAVGPSNELPGMSGRGAQLFAKRQSRMEKYVVDSDTVQAHAARAQSPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAALKSQPSAAQPSKMGKKKGKKPLNALDVMKHQPYQLNASLFTFQPPDAKDGLPQKSSVKVNSALAMKQALPPRPVNAASPTNVQASSVYSVPAYTSPPSFFAEASSPVSASPVPVGIPTSPKQESASSSYFVAPRPKFSAKKSGVTIQVWKPSVVEE
uniprot
proteins
function
FUNCTION: Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks in an isoform-specific manner (PubMed:23225103, PubMed:24005909). 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}.
uniprot
proteins
mass_dalton
117514
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
Synaptopodin family
uniprot
proteins
pubmed
11297942
uniprot
proteins
pubmed
11673475
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16885336
uniprot
proteins
pubmed
17828378
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18371299
uniprot
proteins
pubmed
20554076
uniprot
proteins
pubmed
21643011
uniprot
proteins
pubmed
22915763
uniprot
proteins
pubmed
23225103
uniprot
proteins
pubmed
23434281
uniprot
proteins
pubmed
24005909
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25883213
uniprot
proteins
sequence_length
1093
uniprot
proteins
subcellular_location
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}.
uniprot
proteins