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Q9V719

- SIN1_DROME

UniProt

Q9V719 - SIN1_DROME

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Protein

Stress-activated map kinase-interacting protein 1

Gene

Sin1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 - 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_184384. Constitutive PI3K/AKT Signaling in Cancer.

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: 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. 12 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF58247.1 .
BT003261 mRNA. Translation: AAO25018.1 .
RefSeqi NP_610963.1. NM_137119.4.
UniGenei Dm.10957.

3D structure databases

ProteinModelPortali Q9V719.
SMRi Q9V719. Positions 389-547.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62354. 1 interaction.
IntActi Q9V719. 12 interactions.
MINTi MINT-7555994.

Proteomic databases

PaxDbi Q9V719.
PRIDEi Q9V719.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087487 ; FBpp0086616 ; FBgn0033935 .
GeneIDi 36604.
KEGGi dme:Dmel_CG10105.

Organism-specific databases

CTDi 36604.
FlyBasei FBgn0033935. Sin1.

Phylogenomic databases

eggNOGi NOG281916.
GeneTreei ENSGT00390000000642.
InParanoidi Q9V719.
OMAi ERIEIDQ.
OrthoDBi EOG7GXPBF.
PhylomeDBi Q9V719.

Enzyme and pathway databases

Reactomei REACT_184384. Constitutive PI3K/AKT Signaling in Cancer.

Miscellaneous databases

GenomeRNAii 36604.
NextBioi 799458.
PROi Q9V719.

Gene expression databases

Bgeei Q9V719.

Family and domain databases

InterProi IPR008828. SIN1.
[Graphical view ]
PANTHERi PTHR13335. PTHR13335. 1 hit.
Pfami PF05422. SIN1. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 88 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