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SRC kinase signaling inhibitor 1 (SNAP-25-interacting protein) (SNIP) (p130Cas-associated protein) (p140Cap)

 SRCN1_MOUSE             Reviewed;        1250 AA.
Q9QWI6; O70298;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
25-OCT-2017, entry version 126.
RecName: Full=SRC kinase signaling inhibitor 1;
AltName: Full=SNAP-25-interacting protein;
Short=SNIP;
AltName: Full=p130Cas-associated protein;
AltName: Full=p140Cap;
Name=Srcin1; Synonyms=Kiaa1684, P140;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAC15635.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Croci L., Bossolasco M., Consalez G.G.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-1250 (ISOFORM 3).
TISSUE=Brain {ECO:0000312|EMBL:BAC98232.1};
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3] {ECO:0000305}
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=14657239; DOI=10.1091/mbc.E03-09-0689;
Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
"p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
protein involved in cell spreading.";
Mol. Biol. Cell 15:787-800(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-588; SER-1054
AND SER-1110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND TYR-464, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[8]
TISSUE SPECIFICITY.
PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
"Dynamic microtubules regulate dendritic spine morphology and synaptic
plasticity.";
Neuron 61:85-100(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-52; SER-79;
SER-87; SER-98; SER-211; SER-247; SER-293; TYR-309; SER-366; SER-375;
SER-392; SER-430; SER-432; SER-559; SER-562; SER-566; SER-569;
SER-579; SER-581; SER-583; SER-588; SER-664; SER-688; THR-691;
THR-704; SER-911; SER-933; SER-1054; SER-1110 AND SER-1127, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-397; ARG-404 AND ARG-567,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Acts as a negative regulator of SRC by activating CSK
which inhibits SRC activity and downstream signaling, leading to
impaired cell spreading and migration. Regulates dendritic spine
morphology. Involved in calcium-dependent exocytosis. May play a
role in neurotransmitter release or synapse maintenance (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with the N-terminal coiled-coil region of
SNAP25. Interacts with BCAR1/p130Cas and SRC through its C-
terminal domain. Interacts with CSK, CTTN, SORBS3/vinexin, SYP and
MAPRE3/EB3 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P56945:BCAR1 (xeno); NbExp=3; IntAct=EBI-775592, EBI-702093;
Q61140:Bcar1; NbExp=2; IntAct=EBI-775592, EBI-77088;
Q14247:CTTN (xeno); NbExp=2; IntAct=EBI-775607, EBI-351886;
Q9UPY8:MAPRE3 (xeno); NbExp=5; IntAct=EBI-775607, EBI-726739;
O60504-2:SORBS3 (xeno); NbExp=4; IntAct=EBI-775607, EBI-1222956;
P00523:SRC (xeno); NbExp=2; IntAct=EBI-775607, EBI-848039;
P07825:Syp (xeno); NbExp=2; IntAct=EBI-775607, EBI-976085;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell projection, axon {ECO:0000250}.
Cell projection, dendrite {ECO:0000250}. Cell junction, synapse
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Note=Localized to the
perinuclear region, lamellopodia, cortical actin and actin stress
fibers but not to focal adhesions. Strongly expressed in axons and
dendrites of the CA1 and CA3 hippocampal regions and of the
dentate gyrus. Detected in both presynapses and postsynapses and
in postsynaptic density fractions (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:14657239}; Synonyms=1a
{ECO:0000303|PubMed:14657239};
IsoId=Q9QWI6-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:14657239}; Synonyms=1b
{ECO:0000303|PubMed:14657239};
IsoId=Q9QWI6-2; Sequence=VSP_050631;
Name=3 {ECO:0000305};
IsoId=Q9QWI6-3; Sequence=VSP_050632;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed predominantly in central nervous
system with high levels detected in cortex, cerebellum, midbrain
and spinal cord (at protein level). Also expressed in testis and
epithelial-rich tissues such as mammary gland, lung and kidney.
{ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:19146815}.
-!- PTM: Tyrosine-phosphorylated in response to EGF and to cell
adhesion to integrin ligands. {ECO:0000250|UniProtKB:Q9C0H9}.
-!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC98232.1; Type=Frameshift; Positions=483, 527; Evidence={ECO:0000305};
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EMBL; AF040944; AAC15635.1; -; mRNA.
EMBL; U59873; AAD00087.1; -; mRNA.
EMBL; AK129422; BAC98232.1; ALT_FRAME; mRNA.
PIR; T34101; T34101.
RefSeq; NP_061361.2; NM_018873.2.
UniGene; Mm.342665; -.
ProteinModelPortal; Q9QWI6; -.
SMR; Q9QWI6; -.
BioGrid; 207768; 4.
IntAct; Q9QWI6; 21.
MINT; MINT-4135063; -.
STRING; 10090.ENSMUSP00000103222; -.
iPTMnet; Q9QWI6; -.
PhosphoSitePlus; Q9QWI6; -.
SwissPalm; Q9QWI6; -.
PaxDb; Q9QWI6; -.
PeptideAtlas; Q9QWI6; -.
PRIDE; Q9QWI6; -.
GeneID; 56013; -.
KEGG; mmu:56013; -.
CTD; 80725; -.
MGI; MGI:1933179; Srcin1.
eggNOG; ENOG410IHFG; Eukaryota.
eggNOG; ENOG410XTBA; LUCA.
HOGENOM; HOG000293351; -.
HOVERGEN; HBG019587; -.
InParanoid; Q9QWI6; -.
KO; K19930; -.
PhylomeDB; Q9QWI6; -.
ChiTaRS; Srcin1; mouse.
PRO; PR:Q9QWI6; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
InterPro; IPR022782; AIP3_C.
InterPro; IPR026727; Srcin1.
PANTHER; PTHR22741:SF5; PTHR22741:SF5; 1.
Pfam; PF03915; AIP3; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Exocytosis;
Membrane; Methylation; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Synapse.
CHAIN 1 1250 SRC kinase signaling inhibitor 1.
/FTId=PRO_0000072012.
REGION 681 731 Interaction with SNAP25. {ECO:0000250}.
COILED 627 654 {ECO:0000255}.
COILED 716 741 {ECO:0000255}.
COILED 783 845 {ECO:0000255}.
COMPBIAS 1023 1081 Pro-rich.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXY2}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXY2}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 309 309 Phosphotyrosine.
{ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 397 397 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 404 404 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 464 464 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 567 567 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 691 691 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 704 704 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 933 933 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 951 951 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9C0H9}.
MOD_RES 1054 1054 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 1110 1110 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 1127 1127 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 41 MQPWQCLRRFALAWWERTAEGRARSPREEVGPRDPGGRGEP
-> MGNAPSQ (in isoform 2).
{ECO:0000303|PubMed:14657239,
ECO:0000303|Ref.1}.
/FTId=VSP_050631.
VAR_SEQ 1207 1250 Missing (in isoform 3).
{ECO:0000303|PubMed:14621295}.
/FTId=VSP_050632.
CONFLICT 740 741 NV -> KL (in Ref. 2; BAC98232).
{ECO:0000305}.
CONFLICT 755 755 P -> R (in Ref. 2; BAC98232).
{ECO:0000305}.
CONFLICT 759 760 DV -> EL (in Ref. 2; BAC98232).
{ECO:0000305}.
CONFLICT 821 821 M -> V (in Ref. 2; BAC98232).
{ECO:0000305}.
CONFLICT 960 960 C -> G (in Ref. 2; BAC98232).
{ECO:0000305}.
CONFLICT 1121 1122 KL -> NV (in Ref. 1; AAD00087).
{ECO:0000305}.
SEQUENCE 1250 AA; 134859 MW; 85F394C9523F78C0 CRC64;
MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
EYRTLGGGGG GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
LKSKYPQHAL ALRGQQDRMR EQVGGWTVDP VCLLSSLCSH LHGDSTPSGA GQPAQQPNYW
SFKTRSSRHT QGAQPGLADQ AAKLSYASAE SLETMSEAEL PLGFSRMNRF RQSLPLSRSA
SQTKLRSPGV LFLQFGEETR RVHITHEVSS LDTLHALIAH MFPQKLTMGM LKSPNTAILI
KDEARNVFYE LEDVRDIQDR SIIKIYRKEP LYAAFPGSHL TNGDLRREMV YASRESSPTR
RLNNLSPASH LASSSPPPGL PSGLPSGLPS GSPSRSRLSY AGGRPPSYAG SPVHHAAERL
GGAPTGQGVS PSPSAILERR DVKPDEDLAG KAGGMVLVKG EGLYADPYGL LHEGRLSLAA
AAETHSHTRA RAACTSGVPC ALSAPTPLPR CSPTWRTRCT RRALAALYGD GYGFRLPPSS
PQKLADVSAP SGGPPPPHSP YSGPPSRGSP VRQSFRKDSG SSSVFAESPG GKARSTGSAS
TAGAPPSELF PGPGERSLVG FGPPVPAKDT ETRERMEAME KQIASLTGLV QSALLRGSEP
ETPSEKVEGS NGAATPSAPV CGSGSKSSGA TPVSGPPPPS ASSTPAGQPT AVSRLQMQLH
LRGLQNSASD LRGQLQQLRN VQLQNQESVR ALLKPTEADV SMRVSEAARR QEDPLQRQRT
LVEEERLRYL NDEELITQQL NDLEKSVEKI QRDVAHNHRL MPGPELEEKA LVLKQLGETL
TELKAHFPGL QSKMRVVLRV EVEAVKFLKE EPQRLDGLLK RCRGVTDTLA QIRRQVDEGM
WPPPNNLLNQ SPKKVAAETD FSKGLDFEIP PPSPPLNLHE LSGPAEGTPL TPKSTNPTKC
LDASSKRNTD KAVSVEAAER DWEEKRAALT QYSAKDINRL LEETQAELLK AIPDLDCASK
THPGPAPTPD HKPPKAPHGQ KAAPRTEPSG RRGSDELTVP RYRTEKPSKS PPPPPPRRSF
PSSHGLTTTR TGEVVVTSKK DSVFIKKAES EELEVQKPQV KLRRAVSEVV RPASTPPIMA
SAIKDEDDEE RIIAELESGG SSVPPMKVVT PGASRLKAAQ GPAGSPDKGK HGKQRTEYMR
IQAQQQATKP SKEVSGPNET SSPGSEKPSG SRTSIPVLTS FGARNSSISF


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EIAAB38486 Mapkap1,Mip1,Mitogen-activated protein kinase 2-associated protein 1,Mouse,Mus musculus,SAPK-interacting protein 1,Sin1,Stress-activated map kinase-interacting protein 1,Target of rapamycin complex 2


 

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