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Protein

Stress-activated map kinase-interacting protein 1

Gene

Sin1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of a multiprotein complex that phosphorylates Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes.1 Publication

GO - Molecular functioni

  1. protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. dendrite morphogenesis Source: FlyBase
  3. regulation of protein phosphorylation Source: FlyBase
  4. synaptic growth at neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_305259. CD28 dependent PI3K/Akt signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_331453. VEGFR2 mediated vascular permeability.
REACT_339689. PIP3 activates AKT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-activated map kinase-interacting protein 1
Short name:
SAPK-interacting protein 1
Short name:
dSin1
Gene namesi
Name:Sin1
ORF Names:CG10105
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033935. Sin1.

Subcellular locationi

GO - Cellular componenti

  1. TORC2 complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 569569Stress-activated map kinase-interacting protein 1PRO_0000218772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei504 – 5041Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V719.
PRIDEiQ9V719.

Expressioni

Gene expression databases

BgeeiQ9V719.

Interactioni

Protein-protein interaction databases

BioGridi62354. 1 interaction.
IntActiQ9V719. 16 interactions.
MINTiMINT-7555994.

Structurei

3D structure databases

ProteinModelPortaliQ9V719.
SMRiQ9V719. Positions 389-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SIN1 family.Curated

Phylogenomic databases

eggNOGiNOG281916.
GeneTreeiENSGT00390000000642.
InParanoidiQ9V719.
OMAiERIEIDQ.
OrthoDBiEOG7GXPBF.
PhylomeDBiQ9V719.

Family and domain databases

InterProiIPR008828. SIN1.
[Graphical view]
PANTHERiPTHR13335. PTHR13335. 1 hit.
PfamiPF05422. SIN1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATYSNQHWL LSHIRNSFIS TDDTGMCETV MLSDDMPKHY LRKFGNSGAG
60 70 80 90 100
GDHYHWRRAH KTPPTGGGTT PERNTRHPDA PLQEVDFICY PGLDLSDDEE
110 120 130 140 150
DMSTHSFDIQ MYPEVGAHRF RSNTAQKLEK LDIAKRRAAR IKSVNYQEEV
160 170 180 190 200
QPPESDDFFK RKELPLSKAE RVKNEPKAND DDLSDEGVQS QLTEQLAKSP
210 220 230 240 250
KQAQNRFIEF ARFDGTSQVG MQTKRINVFL NMLPEPDRNY PLKICVVATA
260 270 280 290 300
KIQEVIGFVC YRTSLQYPDV PLKSLQHYAL YMTEDNDDME DFPPLDNREP
310 320 330 340 350
CSKFGFSQLT LAERRPLAPV TRVDYHSQLG SKSMTSVEDK TALSDAAVKA
360 370 380 390 400
LQNISLNGGT SDPGGGGGGG DSPHDNVKEY EKRLLNHNDM LEAPMHRTFR
410 420 430 440 450
LNIIDKRFFK SDVTLGISGE RIEIDQCKNA KFWPQKKPVS TPIDFVAHCE
460 470 480 490 500
ILERRHLKAL LRIWLKSNSS SPSFSTGCTS APINASVTTL NAGSGSGGIA
510 520 530 540 550
HSPSSPGHSS GLFSSSNIRF KHYDFDTDTH TAEQIHNKLN CILEMRSSDL
560
RREFLLQRDR KQEKRQLKL
Length:569
Mass (Da):64,239
Last modified:May 1, 2000 - v1
Checksum:iBD18DC6186C4E665
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58247.1.
BT003261 mRNA. Translation: AAO25018.1.
RefSeqiNP_610963.1. NM_137119.4.
UniGeneiDm.10957.

Genome annotation databases

EnsemblMetazoaiFBtr0087487; FBpp0086616; FBgn0033935.
GeneIDi36604.
KEGGidme:Dmel_CG10105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58247.1.
BT003261 mRNA. Translation: AAO25018.1.
RefSeqiNP_610963.1. NM_137119.4.
UniGeneiDm.10957.

3D structure databases

ProteinModelPortaliQ9V719.
SMRiQ9V719. Positions 389-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62354. 1 interaction.
IntActiQ9V719. 16 interactions.
MINTiMINT-7555994.

Proteomic databases

PaxDbiQ9V719.
PRIDEiQ9V719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087487; FBpp0086616; FBgn0033935.
GeneIDi36604.
KEGGidme:Dmel_CG10105.

Organism-specific databases

CTDi36604.
FlyBaseiFBgn0033935. Sin1.

Phylogenomic databases

eggNOGiNOG281916.
GeneTreeiENSGT00390000000642.
InParanoidiQ9V719.
OMAiERIEIDQ.
OrthoDBiEOG7GXPBF.
PhylomeDBiQ9V719.

Enzyme and pathway databases

ReactomeiREACT_305259. CD28 dependent PI3K/Akt signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_331453. VEGFR2 mediated vascular permeability.
REACT_339689. PIP3 activates AKT signaling.

Miscellaneous databases

GenomeRNAii36604.
NextBioi799458.
PROiQ9V719.

Gene expression databases

BgeeiQ9V719.

Family and domain databases

InterProiIPR008828. SIN1.
[Graphical view]
PANTHERiPTHR13335. PTHR13335. 1 hit.
PfamiPF05422. SIN1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s."
    Frias M.A., Thoreen C.C., Jaffe J.D., Schroder W., Sculley T., Carr S.A., Sabatini D.M.
    Curr. Biol. 16:1865-1870(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-372 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiSIN1_DROME
AccessioniPrimary (citable) accession number: Q9V719
Secondary accession number(s): Q53YG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.