SIN1_DROME
ID SIN1_DROME Reviewed; 569 AA.
AC Q9V719; Q53YG4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Stress-activated map kinase-interacting protein 1;
DE Short=SAPK-interacting protein 1;
DE Short=dSin1;
GN Name=Sin1; ORFNames=CG10105;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION.
RX PubMed=16919458; DOI=10.1016/j.cub.2006.08.001;
RA Frias M.A., Thoreen C.C., Jaffe J.D., Schroder W., Sculley T., Carr S.A.,
RA Sabatini D.M.;
RT "mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define
RT three distinct mTORC2s.";
RL Curr. Biol. 16:1865-1870(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-372 AND
RP SER-504, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of a multiprotein complex that phosphorylates Akt1,
CC a protein that regulates the balance between cell survival and
CC apoptosis through a cascade that primarily alters the function of
CC transcription factors that regulate pro- and antiapoptotic genes.
CC {ECO:0000269|PubMed:16919458}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58247.1; -; Genomic_DNA.
DR EMBL; BT003261; AAO25018.1; -; mRNA.
DR RefSeq; NP_610963.1; NM_137119.4.
DR AlphaFoldDB; Q9V719; -.
DR SMR; Q9V719; -.
DR BioGRID; 62354; 13.
DR IntAct; Q9V719; 16.
DR MINT; Q9V719; -.
DR STRING; 7227.FBpp0086616; -.
DR iPTMnet; Q9V719; -.
DR PaxDb; Q9V719; -.
DR PRIDE; Q9V719; -.
DR DNASU; 36604; -.
DR EnsemblMetazoa; FBtr0087487; FBpp0086616; FBgn0033935.
DR GeneID; 36604; -.
DR KEGG; dme:Dmel_CG10105; -.
DR CTD; 36604; -.
DR FlyBase; FBgn0033935; Sin1.
DR VEuPathDB; VectorBase:FBgn0033935; -.
DR eggNOG; KOG3739; Eukaryota.
DR GeneTree; ENSGT00390000000642; -.
DR HOGENOM; CLU_514767_0_0_1; -.
DR InParanoid; Q9V719; -.
DR OMA; NAKFWPQ; -.
DR OrthoDB; 1492466at2759; -.
DR PhylomeDB; Q9V719; -.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR BioGRID-ORCS; 36604; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36604; -.
DR PRO; PR:Q9V719; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033935; Expressed in cleaving embryo and 22 other tissues.
DR Genevisible; Q9V719; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IGI:FlyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:FlyBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:FlyBase.
DR GO; GO:0034063; P:stress granule assembly; IMP:FlyBase.
DR GO; GO:0038203; P:TORC2 signaling; IGI:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008828; Sin1/Avo1.
DR InterPro; IPR032679; Sin1_N.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR13335; PTHR13335; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF05422; SIN1; 1.
DR Pfam; PF16979; SIN1_PH; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..569
FT /note="Stress-activated map kinase-interacting protein 1"
FT /id="PRO_0000218772"
FT REGION 52..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 569 AA; 64239 MW; BD18DC6186C4E665 CRC64;
MATYSNQHWL LSHIRNSFIS TDDTGMCETV MLSDDMPKHY LRKFGNSGAG GDHYHWRRAH
KTPPTGGGTT PERNTRHPDA PLQEVDFICY PGLDLSDDEE DMSTHSFDIQ MYPEVGAHRF
RSNTAQKLEK LDIAKRRAAR IKSVNYQEEV QPPESDDFFK RKELPLSKAE RVKNEPKAND
DDLSDEGVQS QLTEQLAKSP KQAQNRFIEF ARFDGTSQVG MQTKRINVFL NMLPEPDRNY
PLKICVVATA KIQEVIGFVC YRTSLQYPDV PLKSLQHYAL YMTEDNDDME DFPPLDNREP
CSKFGFSQLT LAERRPLAPV TRVDYHSQLG SKSMTSVEDK TALSDAAVKA LQNISLNGGT
SDPGGGGGGG DSPHDNVKEY EKRLLNHNDM LEAPMHRTFR LNIIDKRFFK SDVTLGISGE
RIEIDQCKNA KFWPQKKPVS TPIDFVAHCE ILERRHLKAL LRIWLKSNSS SPSFSTGCTS
APINASVTTL NAGSGSGGIA HSPSSPGHSS GLFSSSNIRF KHYDFDTDTH TAEQIHNKLN
CILEMRSSDL RREFLLQRDR KQEKRQLKL
