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Protein

Insulin-induced gene 2 protein

Gene

Insig2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR.2 Publications

GO - Biological processi

  • cholesterol biosynthetic process Source: MGI
  • cholesterol metabolic process Source: MGI
  • cranial suture morphogenesis Source: MGI
  • inner ear morphogenesis Source: MGI
  • middle ear morphogenesis Source: MGI
  • negative regulation of fatty acid biosynthetic process Source: MGI
  • negative regulation of steroid biosynthetic process Source: MGI
  • palate development Source: MGI
  • response to fatty acid Source: Ensembl
  • response to insulin Source: Ensembl
  • response to sterol depletion Source: MGI
  • SREBP signaling pathway Source: MGI
  • sterol biosynthetic process Source: MGI
  • triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-induced gene 2 protein
Short name:
INSIG-2
Gene namesi
Name:Insig2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1920249. Insig2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 4621HelicalSequence analysisAdd
BLAST
Transmembranei71 – 9121HelicalSequence analysisAdd
BLAST
Transmembranei131 – 14818HelicalSequence analysisAdd
BLAST
Transmembranei154 – 17421HelicalSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Insulin-induced gene 2 proteinPRO_0000286798Add
BLAST

Proteomic databases

PaxDbiQ91WG1.
PRIDEiQ91WG1.

PTM databases

PhosphoSiteiQ91WG1.

Expressioni

Tissue specificityi

Expressed in liver, testis, kidney, spleen, intestine, brain and adrenal gland.1 Publication

Gene expression databases

BgeeiQ91WG1.
CleanExiMM_INSIG2.
ExpressionAtlasiQ91WG1. baseline and differential.
GenevisibleiQ91WG1. MM.

Interactioni

Subunit structurei

Binds to the SCAP-SREBF2 complex only in the presence of sterols. Interacts with RNF139 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003818.

Structurei

3D structure databases

ProteinModelPortaliQ91WG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the INSIG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4363. Eukaryota.
ENOG410XQ2M. LUCA.
GeneTreeiENSGT00580000081600.
HOGENOMiHOG000253021.
HOVERGENiHBG058958.
InParanoidiQ91WG1.
OMAiHRFKREW.
OrthoDBiEOG7RNK13.
PhylomeDBiQ91WG1.
TreeFamiTF331013.

Family and domain databases

InterProiIPR025929. INSIG_fam.
[Graphical view]
PfamiPF07281. INSIG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91WG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEGETESPR PKKCGPYISS VTSQSVNVVI RGVVLFFIGV FLALVLNLLQ
60 70 80 90 100
IQRNVTLFPP DVITSIFSSA WWVPPCCGTA SAVIGLLYPC IDRHLGEPHK
110 120 130 140 150
FKREWSSVMR CVAVFVGINH ASAKVDFDNN FQFSLTLAAL SVGLWWTFDR
160 170 180 190 200
SRSGFGLGVG IAFLATVVTQ LLVYNGVYQY TSPDFLYVRS WLPCIFFAGG
210 220
ITMGNIGRQL AMYECKVIAE KSHQE
Length:225
Mass (Da):24,915
Last modified:December 1, 2001 - v1
Checksum:i095F322846DA3CF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981P → H in BAC34233 (PubMed:16141072).Curated
Sequence conflicti106 – 1061S → Y in BAE38307 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527631 mRNA. Translation: AAN28332.1.
AK161256 mRNA. Translation: BAE36273.1.
AK154543 mRNA. Translation: BAE32667.1.
AK152076 mRNA. Translation: BAE30928.1.
AK050394 mRNA. Translation: BAC34233.1.
AK165634 mRNA. Translation: BAE38307.1.
AK040703 mRNA. Translation: BAC30676.1.
BC024411 mRNA. Translation: AAH24411.1.
BC023874 mRNA. Translation: AAH23874.1.
BC023067 mRNA. Translation: AAH23067.1.
BC015288 mRNA. Translation: AAH15288.1.
CCDSiCCDS15236.1.
RefSeqiNP_001258460.1. NM_001271531.1.
NP_598509.1. NM_133748.2.
NP_835183.1. NM_178082.3.
XP_006529952.1. XM_006529889.1.
XP_006529953.1. XM_006529890.2.
XP_006529954.1. XM_006529891.2.
XP_006529955.1. XM_006529892.1.
UniGeneiMm.27136.
Mm.486216.

Genome annotation databases

EnsembliENSMUST00000003818; ENSMUSP00000003818; ENSMUSG00000003721.
ENSMUST00000071064; ENSMUSP00000065485; ENSMUSG00000003721.
ENSMUST00000159085; ENSMUSP00000124345; ENSMUSG00000003721.
ENSMUST00000160968; ENSMUSP00000123747; ENSMUSG00000003721.
GeneIDi72999.
KEGGimmu:72999.
UCSCiuc007cjo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527631 mRNA. Translation: AAN28332.1.
AK161256 mRNA. Translation: BAE36273.1.
AK154543 mRNA. Translation: BAE32667.1.
AK152076 mRNA. Translation: BAE30928.1.
AK050394 mRNA. Translation: BAC34233.1.
AK165634 mRNA. Translation: BAE38307.1.
AK040703 mRNA. Translation: BAC30676.1.
BC024411 mRNA. Translation: AAH24411.1.
BC023874 mRNA. Translation: AAH23874.1.
BC023067 mRNA. Translation: AAH23067.1.
BC015288 mRNA. Translation: AAH15288.1.
CCDSiCCDS15236.1.
RefSeqiNP_001258460.1. NM_001271531.1.
NP_598509.1. NM_133748.2.
NP_835183.1. NM_178082.3.
XP_006529952.1. XM_006529889.1.
XP_006529953.1. XM_006529890.2.
XP_006529954.1. XM_006529891.2.
XP_006529955.1. XM_006529892.1.
UniGeneiMm.27136.
Mm.486216.

3D structure databases

ProteinModelPortaliQ91WG1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003818.

PTM databases

PhosphoSiteiQ91WG1.

Proteomic databases

PaxDbiQ91WG1.
PRIDEiQ91WG1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003818; ENSMUSP00000003818; ENSMUSG00000003721.
ENSMUST00000071064; ENSMUSP00000065485; ENSMUSG00000003721.
ENSMUST00000159085; ENSMUSP00000124345; ENSMUSG00000003721.
ENSMUST00000160968; ENSMUSP00000123747; ENSMUSG00000003721.
GeneIDi72999.
KEGGimmu:72999.
UCSCiuc007cjo.1. mouse.

Organism-specific databases

CTDi51141.
MGIiMGI:1920249. Insig2.

Phylogenomic databases

eggNOGiKOG4363. Eukaryota.
ENOG410XQ2M. LUCA.
GeneTreeiENSGT00580000081600.
HOGENOMiHOG000253021.
HOVERGENiHBG058958.
InParanoidiQ91WG1.
OMAiHRFKREW.
OrthoDBiEOG7RNK13.
PhylomeDBiQ91WG1.
TreeFamiTF331013.

Miscellaneous databases

NextBioi337299.
PROiQ91WG1.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WG1.
CleanExiMM_INSIG2.
ExpressionAtlasiQ91WG1. baseline and differential.
GenevisibleiQ91WG1. MM.

Family and domain databases

InterProiIPR025929. INSIG_fam.
[Graphical view]
PfamiPF07281. INSIG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins."
    Yabe D., Brown M.S., Goldstein J.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:12753-12758(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SCAP AND SREBP2 COMPLEX.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C3H/HeJ, C57BL/6J and NOD.
    Tissue: Aorta, Bone marrow, Brain, Dendritic cell, Liver and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Eye, Kidney and Mammary tumor.
  4. "Liver-specific mRNA for Insig-2 down-regulated by insulin: implications for fatty acid synthesis."
    Yabe D., Komuro R., Liang G., Goldstein J.L., Brown M.S.
    Proc. Natl. Acad. Sci. U.S.A. 100:3155-3160(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiINSI2_MOUSE
AccessioniPrimary (citable) accession number: Q91WG1
Secondary accession number(s): Q3TMY2, Q8BWP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 1, 2001
Last modified: December 9, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.