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Synapse-associated protein 1 (BSD domain-containing signal transducer and Akt interactor protein) (BSTA)

 SYAP1_MOUSE             Reviewed;         365 AA.
Q9D5V6; Q3UI67; Q9D870;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 108.
RecName: Full=Synapse-associated protein 1 {ECO:0000305};
AltName: Full=BSD domain-containing signal transducer and Akt interactor protein {ECO:0000250|UniProtKB:Q96A49};
Short=BSTA {ECO:0000250|UniProtKB:Q96A49};
Name=Syap1 {ECO:0000312|MGI:MGI:1914293};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Heart, Small intestine, Spinal ganglion, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262; SER-283 AND
SER-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[5]
FUNCTION, INTERACTION WITH AKT1, PHOSPHORYLATION, TISSUE SPECIFICITY,
AND INDUCTION.
PubMed=23300339; DOI=10.1126/scisignal.2003295;
Yao Y., Suraokar M., Darnay B.G., Hollier B.G., Shaiken T.E.,
Asano T., Chen C.H., Chang B.H., Lu Y., Mills G.B., Sarbassov D.,
Mani S.A., Abbruzzese J.L., Reddy S.A.;
"BSTA promotes mTORC2-mediated phosphorylation of Akt1 to suppress
expression of FoxC2 and stimulate adipocyte differentiation.";
Sci. Signal. 6:RA2-RA2(2013).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=27344443; DOI=10.1007/s00418-016-1457-0;
Schmitt D., Funk N., Blum R., Asan E., Andersen L., Ruelicke T.,
Sendtner M., Buchner E.;
"Initial characterization of a Syap1 knock-out mouse and distribution
of Syap1 in mouse brain and cultured motoneurons.";
Histochem. Cell Biol. 146:489-512(2016).
-!- FUNCTION: Plays a role in adipocyte differentiation by promoting
mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth
factor stimulation (PubMed:23300339).
{ECO:0000269|PubMed:23300339}.
-!- SUBUNIT: Interacts (via phosphorylated form and BSD domain) with
AKT1; this interaction is enhanced in a mTORC2-mediated manner in
response to epidermal growth factor (EGF) stimulation and
activates AKT1 (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:27344443}. Golgi apparatus
{ECO:0000269|PubMed:27344443}. Perikaryon
{ECO:0000269|PubMed:27344443}. Cell projection, axon
{ECO:0000269|PubMed:27344443}. Cell projection, dendrite
{ECO:0000269|PubMed:27344443}. Cell projection, growth cone
{ECO:0000269|PubMed:27344443}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:27344443}. Cell junction,
synapse, postsynaptic cell membrane {ECO:0000269|PubMed:27344443}.
Membrane {ECO:0000250|UniProtKB:Q96A49}. Note=Localizes to
cholinergic neuromuscular junctions and in actin-rich growth cone
regions (PubMed:27344443). Membrane-associated in a epidermal
growth factor (EGF)-dependent manner (By similarity).
{ECO:0000250|UniProtKB:Q96A49, ECO:0000269|PubMed:27344443}.
-!- TISSUE SPECIFICITY: Expressed in the liver, kidney, skeletal
muscle and in white and brown adipose tissues (PubMed:23300339,
PubMed:27344443). Expressed in the cortex, cerebellum, thalamus,
hippocampus, braistem, olfactory bulb, spinal cord and striatum of
the brain (PubMed:27344443). Expressed in most neuropil regions
containing glutamatergic synaptic terminals (PubMed:27344443).
Expressed in the CA1, CA2 and CA3 perikarya of the hippocampus
(PubMed:27344443). Expressed in neurons and Purkinje cells (at the
protein level) (PubMed:27344443). {ECO:0000269|PubMed:23300339,
ECO:0000269|PubMed:27344443}.
-!- INDUCTION: Up-regulated during adipocyte differentiation (at
protein level) (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
-!- PTM: Phosphorylated (PubMed:23300339). Phosphorylation increases
in a mTORC2-mediated manner in response to epidermal growth factor
(EGF) stimulation (PubMed:23300339).
{ECO:0000269|PubMed:23300339}.
-!- DISRUPTION PHENOTYPE: Mice appear normal and healthy
(PubMed:27344443). Display no alteration on the survival or axonal
elongation in primary embryonic motoneurons (PubMed:27344443).
Show no alteration in total AKT phosphorylation in primary
embryonic motoneurons (PubMed:27344443).
{ECO:0000269|PubMed:27344443}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK008390; BAB25643.1; -; mRNA.
EMBL; AK014893; BAB29608.1; -; mRNA.
EMBL; AK051251; BAC34575.1; -; mRNA.
EMBL; AK147055; BAE27639.1; -; mRNA.
EMBL; BC021373; AAH21373.1; -; mRNA.
CCDS; CCDS30511.1; -.
RefSeq; NP_080208.2; NM_025932.2.
UniGene; Mm.44207; -.
ProteinModelPortal; Q9D5V6; -.
SMR; Q9D5V6; -.
STRING; 10090.ENSMUSP00000033723; -.
iPTMnet; Q9D5V6; -.
PhosphoSitePlus; Q9D5V6; -.
REPRODUCTION-2DPAGE; IPI00317599; -.
EPD; Q9D5V6; -.
MaxQB; Q9D5V6; -.
PaxDb; Q9D5V6; -.
PeptideAtlas; Q9D5V6; -.
PRIDE; Q9D5V6; -.
Ensembl; ENSMUST00000033723; ENSMUSP00000033723; ENSMUSG00000031357.
GeneID; 67043; -.
KEGG; mmu:67043; -.
UCSC; uc009uun.2; mouse.
CTD; 94056; -.
MGI; MGI:1914293; Syap1.
eggNOG; KOG4310; Eukaryota.
eggNOG; ENOG410ZPSV; LUCA.
GeneTree; ENSGT00390000007662; -.
HOGENOM; HOG000231677; -.
HOVERGEN; HBG057553; -.
InParanoid; Q9D5V6; -.
OMA; ETADWEK; -.
OrthoDB; EOG091G0HAT; -.
PhylomeDB; Q9D5V6; -.
TreeFam; TF319666; -.
PRO; PR:Q9D5V6; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031357; -.
CleanEx; MM_SYAP1; -.
Genevisible; Q9D5V6; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISS:UniProtKB.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; ISS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0038203; P:TORC2 signaling; IMP:UniProtKB.
Gene3D; 1.10.3970.10; -; 1.
InterPro; IPR005607; BSD_dom.
InterPro; IPR035925; BSD_dom_sf.
Pfam; PF03909; BSD; 1.
SMART; SM00751; BSD; 1.
PROSITE; PS50858; BSD; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Differentiation; Golgi apparatus; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Synapse.
CHAIN 1 365 Synapse-associated protein 1.
/FTId=PRO_0000072356.
DOMAIN 172 224 BSD. {ECO:0000255|PROSITE-
ProRule:PRU00036}.
MOD_RES 262 262 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q96A49}.
CONFLICT 243 243 E -> K (in Ref. 1; BAB25643).
{ECO:0000305}.
SEQUENCE 365 AA; 41350 MW; 7553E79C0C50E96B CRC64;
MFGGLSSWLG LKPPEGAAAE GEEPPSRDGD KLSAGAAPSE ESPERPVEPT EEQQQQPPTE
DPQFLHQAKG LGNYLYNFAS AATKKITESV TETAQTIKKS VEEGKIDDIL DKTILGDFQK
EQKKFVEEQN TKKSEAAVPP WVESHDEETI QQQILALSAD KRNFLRDPPA GVQFNFDFDQ
MYPVALVMLQ EDELLSKMRF ALVPKLVKEE VFWRNYFYRI SLIKQSAQLT ALAAQQQASG
KEEKSSNRDD NLPLTEAVRP KTPPVVIKSQ LKSQEDEEEI STSPGVSEFV SDAFDTCSLN
QEDLRKEMEQ LVLDKKQEEA TALEEDSTDW EKELQQELQE YEVVAESEKR DENWDKEIEK
MLQES


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