SYAP1_HUMAN
ID SYAP1_HUMAN Reviewed; 352 AA.
AC Q96A49; Q68CP1; Q96C60; Q96JQ6; Q96T20;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Synapse-associated protein 1 {ECO:0000305};
DE AltName: Full=BSD domain-containing signal transducer and Akt interactor protein {ECO:0000303|PubMed:23300339};
DE Short=BSTA {ECO:0000303|PubMed:23300339};
GN Name=SYAP1 {ECO:0000312|HGNC:HGNC:16273}; ORFNames=PRO3113;
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].
RA Chang Y., Yu Y., Wang N., Xu Y.;
RT "SYAP1, the human homolog of the SAP47 gene of Drosophila melanogaster.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-352.
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF 198-PHE-TRP-199.
RX PubMed=23300339; DOI=10.1126/scisignal.2003295;
RA Yao Y., Suraokar M., Darnay B.G., Hollier B.G., Shaiken T.E., Asano T.,
RA Chen C.H., Chang B.H., Lu Y., Mills G.B., Sarbassov D., Mani S.A.,
RA Abbruzzese J.L., Reddy S.A.;
RT "BSTA promotes mTORC2-mediated phosphorylation of Akt1 to suppress
RT expression of FoxC2 and stimulate adipocyte differentiation.";
RL Sci. Signal. 6:RA2-RA2(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND IDENTIFICATION BY
RP 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 STRUCTURE BY NMR OF 130-216.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the BSD domain of human synapse associated protein
RT 1.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role in adipocyte differentiation by promoting
CC mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth
CC factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- SUBUNIT: Interacts (via phosphorylated form and BSD domain) with AKT1;
CC this interaction is enhanced in a mTORC2-mediated manner in response to
CC epidermal growth factor (EGF) stimulation and activates AKT1
CC (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- INTERACTION:
CC Q96A49; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-10770179, EBI-10827839;
CC Q96A49; P30301: MIP; NbExp=3; IntAct=EBI-10770179, EBI-8449636;
CC Q96A49; Q99608: NDN; NbExp=6; IntAct=EBI-10770179, EBI-718177;
CC Q96A49; Q9NUX5: POT1; NbExp=2; IntAct=EBI-10770179, EBI-752420;
CC Q96A49; P10827: THRA; NbExp=5; IntAct=EBI-10770179, EBI-286285;
CC Q96A49; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-10770179, EBI-717441;
CC Q96A49; O95159: ZFPL1; NbExp=3; IntAct=EBI-10770179, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9D5V6}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9D5V6}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9D5V6}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9D5V6}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9D5V6}. Membrane {ECO:0000269|PubMed:23300339}.
CC Note=Localizes to cholinergic neuromuscular junctions and in actin-rich
CC growth cone regions (By similarity). Membrane-associated in a epidermal
CC growth factor (EGF)-dependent manner (PubMed:23300339).
CC {ECO:0000250|UniProtKB:Q9D5V6, ECO:0000269|PubMed:23300339}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal
CC muscle, kidney and pancreas (PubMed:23300339).
CC {ECO:0000269|PubMed:23300339}.
CC -!- PTM: Phosphorylated. Phosphorylation increases in a mTORC2-mediated
CC manner in response to epidermal growth factor (EGF) stimulation.
CC {ECO:0000250|UniProtKB:Q9D5V6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK55531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF168955; AAK81893.1; -; mRNA.
DR EMBL; AF338728; AAK69273.1; -; mRNA.
DR EMBL; AK027401; BAB55087.1; -; mRNA.
DR EMBL; CR749849; CAH18697.1; -; mRNA.
DR EMBL; AL445467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98917.1; -; Genomic_DNA.
DR EMBL; BC014657; AAH14657.1; -; mRNA.
DR EMBL; AF305828; AAK55531.1; ALT_INIT; mRNA.
DR CCDS; CCDS14177.1; -.
DR RefSeq; NP_116185.2; NM_032796.3.
DR PDB; 1X3A; NMR; -; A=130-216.
DR PDBsum; 1X3A; -.
DR AlphaFoldDB; Q96A49; -.
DR BMRB; Q96A49; -.
DR SMR; Q96A49; -.
DR BioGRID; 125103; 116.
DR IntAct; Q96A49; 38.
DR MINT; Q96A49; -.
DR STRING; 9606.ENSP00000369500; -.
DR GlyGen; Q96A49; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96A49; -.
DR MetOSite; Q96A49; -.
DR PhosphoSitePlus; Q96A49; -.
DR BioMuta; SYAP1; -.
DR DMDM; 30580522; -.
DR EPD; Q96A49; -.
DR jPOST; Q96A49; -.
DR MassIVE; Q96A49; -.
DR MaxQB; Q96A49; -.
DR PaxDb; Q96A49; -.
DR PeptideAtlas; Q96A49; -.
DR PRIDE; Q96A49; -.
DR ProteomicsDB; 75912; -.
DR Antibodypedia; 395; 130 antibodies from 25 providers.
DR DNASU; 94056; -.
DR Ensembl; ENST00000380155.4; ENSP00000369500.3; ENSG00000169895.6.
DR GeneID; 94056; -.
DR KEGG; hsa:94056; -.
DR MANE-Select; ENST00000380155.4; ENSP00000369500.3; NM_032796.4; NP_116185.2.
DR UCSC; uc004cxp.4; human.
DR CTD; 94056; -.
DR GeneCards; SYAP1; -.
DR HGNC; HGNC:16273; SYAP1.
DR HPA; ENSG00000169895; Low tissue specificity.
DR neXtProt; NX_Q96A49; -.
DR OpenTargets; ENSG00000169895; -.
DR PharmGKB; PA38107; -.
DR VEuPathDB; HostDB:ENSG00000169895; -.
DR eggNOG; KOG4310; Eukaryota.
DR GeneTree; ENSGT00390000007662; -.
DR HOGENOM; CLU_046184_1_1_1; -.
DR InParanoid; Q96A49; -.
DR OMA; FGSYLFN; -.
DR OrthoDB; 782515at2759; -.
DR PhylomeDB; Q96A49; -.
DR TreeFam; TF319666; -.
DR PathwayCommons; Q96A49; -.
DR SignaLink; Q96A49; -.
DR BioGRID-ORCS; 94056; 13 hits in 711 CRISPR screens.
DR ChiTaRS; SYAP1; human.
DR EvolutionaryTrace; Q96A49; -.
DR GeneWiki; SYAP1; -.
DR GenomeRNAi; 94056; -.
DR Pharos; Q96A49; Tbio.
DR PRO; PR:Q96A49; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96A49; protein.
DR Bgee; ENSG00000169895; Expressed in kidney epithelium and 194 other tissues.
DR Genevisible; Q96A49; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:0038203; P:TORC2 signaling; IMP:UniProtKB.
DR Gene3D; 1.10.3970.10; -; 1.
DR InterPro; IPR005607; BSD_dom.
DR InterPro; IPR035925; BSD_dom_sf.
DR Pfam; PF03909; BSD; 1.
DR SMART; SM00751; BSD; 1.
DR SUPFAM; SSF140383; SSF140383; 1.
DR PROSITE; PS50858; BSD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasm; Differentiation;
KW Golgi apparatus; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Synapse.
FT CHAIN 1..352
FT /note="Synapse-associated protein 1"
FT /id="PRO_0000072355"
FT DOMAIN 158..210
FT /note="BSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MUTAGEN 198..199
FT /note="FW->AA: Inhibits interaction with AKT1, mTORC2-
FT mediated phosphorylation of AKT1 at 'Ser-473' and adipocyte
FT differentiation."
FT /evidence="ECO:0000269|PubMed:23300339"
FT CONFLICT 26
FT /note="P -> L (in Ref. 6; AAH14657)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> T (in Ref. 2; BAB55087)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="Q -> H (in Ref. 7; AAK55531)"
FT /evidence="ECO:0000305"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:1X3A"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1X3A"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1X3A"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:1X3A"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1X3A"
FT TURN 188..192
FT /evidence="ECO:0007829|PDB:1X3A"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:1X3A"
SQ SEQUENCE 352 AA; 39933 MW; 2083636CF7CF75AE CRC64;
MFRGLSSWLG LQQPVAGGGQ PNGDAPPEQP SETVAESAEE ELQQAGDQEL LHQAKDFGNY
LFNFASAATK KITESVAETA QTIKKSVEEG KIDGIIDKTI IGDFQKEQKK FVEEQHTKKS
EAAVPPWVDT NDEETIQQQI LALSADKRNF LRDPPAGVQF NFDFDQMYPV ALVMLQEDEL
LSKMRFALVP KLVKEEVFWR NYFYRVSLIK QSAQLTALAA QQQAAGKEEK SNGREQDLPL
AEAVRPKTPP VVIKSQLKTQ EDEEEISTSP GVSEFVSDAF DACNLNQEDL RKEMEQLVLD
KKQEETAVLE EDSADWEKEL QQELQEYEVV TESEKRDENW DKEIEKMLQE EN
