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O15503

- INSI1_HUMAN

UniProt

O15503 - INSI1_HUMAN

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Protein

Insulin-induced gene 1 protein

Gene
INSIG1
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth.5 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. cholesterol biosynthetic process Source: Ensembl
  3. cranial suture morphogenesis Source: Ensembl
  4. inner ear morphogenesis Source: Ensembl
  5. metabolic process Source: ProtInc
  6. middle ear morphogenesis Source: Ensembl
  7. negative regulation of cargo loading into COPII-coated vesicle Source: UniProtKB
  8. negative regulation of fat cell differentiation Source: Ensembl
  9. negative regulation of fatty acid biosynthetic process Source: Ensembl
  10. negative regulation of steroid biosynthetic process Source: Ensembl
  11. palate development Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. SREBP signaling pathway Source: UniProtKB
  14. triglyceride metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

ReactomeiREACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-induced gene 1 protein
Short name:
INSIG-1
Gene namesi
Name:INSIG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6083. INSIG1.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8787Cytoplasmic1 PublicationAdd
BLAST
Transmembranei88 – 10821Helical; Reviewed predictionAdd
BLAST
Topological domaini109 – 12618Lumenal Reviewed predictionAdd
BLAST
Transmembranei127 – 14721Helical; Reviewed predictionAdd
BLAST
Topological domaini148 – 16013Cytoplasmic1 PublicationAdd
BLAST
Transmembranei161 – 17717Helical; Reviewed predictionAdd
BLAST
Topological domaini178 – 1825Lumenal Reviewed prediction
Transmembranei183 – 20321Helical; Reviewed predictionAdd
BLAST
Topological domaini204 – 2096Cytoplasmic1 Publication
Transmembranei210 – 23021Helical; Reviewed predictionAdd
BLAST
Topological domaini231 – 24111Lumenal Reviewed predictionAdd
BLAST
Transmembranei242 – 26221Helical; Reviewed predictionAdd
BLAST
Topological domaini263 – 27715Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. SREBP-SCAP-Insig complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561K → R: Loss of ubiquitination and degradation. 1 Publication
Mutagenesisi158 – 1581K → R: Loss of ubiquitination and degradation. 1 Publication
Mutagenesisi205 – 2051D → A: Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR. 1 Publication

Organism-specific databases

PharmGKBiPA29890.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Insulin-induced gene 1 proteinPRO_0000191675Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki156 – 156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki158 – 158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated. Subsequent to sterol deprivation, the SCAP-SREBF2 complex becomes dissociated from INSIG1, is then ubiquitinated and degraded in proteasomes. Although ubiquitination is required for rapid INSIG1 degradation, it is not required for release of the SCAP-SREBP complex. Ubiquitinated by RNF139.2 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO15503.
PRIDEiO15503.

PTM databases

PhosphoSiteiO15503.

Expressioni

Tissue specificityi

Expressed in all tissues tested with highest expression in the liver.1 Publication

Inductioni

By insulin.

Gene expression databases

ArrayExpressiO15503.
BgeeiO15503.
CleanExiHS_INSIG1.
GenevestigatoriO15503.

Interactioni

Subunit structurei

Binds to the SCAP-SREBF2 complex only in the presence of sterols. Interacts with RNF139. Interacts with HMGCR (via its SSD); the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway. Interacts with AMFR/gp78 (via its membrane domain); the interaction recruits HMCR at the ER membrane for its ubiquitination and degradation by the sterol-mediated ERAD pathway.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CYP2C1P001802EBI-6252425,EBI-6251821From a different organism.
CYP2C2P001813EBI-6252425,EBI-4320576From a different organism.

Protein-protein interaction databases

BioGridi109850. 20 interactions.
IntActiO15503. 5 interactions.
MINTiMINT-4723340.
STRINGi9606.ENSP00000344741.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J81X-ray1.74C/D273-277[»]
ProteinModelPortaliO15503.

Family & Domainsi

Sequence similaritiesi

Belongs to the INSIG family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG263628.
HOGENOMiHOG000253021.
HOVERGENiHBG058958.
OMAiAMSGPEP.
OrthoDBiEOG7RNK13.
PhylomeDBiO15503.
TreeFamiTF331013.

Family and domain databases

InterProiIPR009904. INSIG-1.
IPR025929. INSIG_fam.
[Graphical view]
PANTHERiPTHR15301:SF11. PTHR15301:SF11. 1 hit.
PfamiPF07281. INSIG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15503-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MPRLHDHFWS CSCAHSARRR GPPRASAAGL AAKVGEMINV SVSGPSLLAA    50
HGAPDADPAP RGRSAAMSGP EPGSPYPNTW HHRLLQRSLV LFSVGVVLAL 100
VLNLLQIQRN VTLFPEEVIA TIFSSAWWVP PCCGTAAAVV GLLYPCIDSH 150
LGEPHKFKRE WASVMRCIAV FVGINHASAK LDFANNVQLS LTLAALSLGL 200
WWTFDRSRSG LGLGITIAFL ATLITQFLVY NGVYQYTSPD FLYIRSWLPC 250
IFFSGGVTVG NIGRQLAMGV PEKPHSD 277
Length:277
Mass (Da):29,987
Last modified:October 3, 2006 - v3
Checksum:i198068D53C658A58
GO
Isoform 2 (identifier: O15503-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-164: AVVGLLYPCIDSHLGEPHKFKREWASV → GIHPQISSIFVLGSLVYFSQEASRWGT
     165-277: Missing.

Note: No experimental confirmation available.

Show »
Length:164
Mass (Da):17,530
Checksum:i06076ED6ACE57C04
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271A → T.1 Publication
Corresponds to variant rs1129825 [ dbSNP | Ensembl ].
VAR_027683

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei138 – 16427AVVGL…EWASV → GIHPQISSIFVLGSLVYFSQ EASRWGT in isoform 2. VSP_045084Add
BLAST
Alternative sequencei165 – 277113Missing in isoform 2. VSP_045085Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 322AA → PP in AAB69121. 1 Publication
Sequence conflicti99 – 991A → T in AAB69121. 1 Publication
Sequence conflicti170 – 1723VFV → GFG in AAB69121. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96876 Genomic DNA. Translation: AAB69121.1.
AY112745 mRNA. Translation: AAM44086.1.
BT007227 mRNA. Translation: AAP35891.1.
AK291675 mRNA. Translation: BAF84364.1.
DN996424 mRNA. No translation available.
AC144652 Genomic DNA. No translation available.
AC231970 Genomic DNA. No translation available.
CH236962 Genomic DNA. Translation: EAL23729.1.
CH236962 Genomic DNA. Translation: EAL23730.1.
CH471149 Genomic DNA. Translation: EAX04529.1.
CH471149 Genomic DNA. Translation: EAX04530.1.
BC001880 mRNA. Translation: AAH01880.1.
CCDSiCCDS5938.1. [O15503-1]
CCDS5939.1. [O15503-2]
RefSeqiNP_005533.2. NM_005542.4. [O15503-1]
NP_938150.2. NM_198336.2.
NP_938151.1. NM_198337.2. [O15503-2]
UniGeneiHs.520819.

Genome annotation databases

EnsembliENST00000340368; ENSP00000344741; ENSG00000186480. [O15503-1]
ENST00000342407; ENSP00000344035; ENSG00000186480. [O15503-2]
GeneIDi3638.
KEGGihsa:3638.
UCSCiuc003wly.3. human. [O15503-1]
uc003wlz.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Insig1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96876 Genomic DNA. Translation: AAB69121.1 .
AY112745 mRNA. Translation: AAM44086.1 .
BT007227 mRNA. Translation: AAP35891.1 .
AK291675 mRNA. Translation: BAF84364.1 .
DN996424 mRNA. No translation available.
AC144652 Genomic DNA. No translation available.
AC231970 Genomic DNA. No translation available.
CH236962 Genomic DNA. Translation: EAL23729.1 .
CH236962 Genomic DNA. Translation: EAL23730.1 .
CH471149 Genomic DNA. Translation: EAX04529.1 .
CH471149 Genomic DNA. Translation: EAX04530.1 .
BC001880 mRNA. Translation: AAH01880.1 .
CCDSi CCDS5938.1. [O15503-1 ]
CCDS5939.1. [O15503-2 ]
RefSeqi NP_005533.2. NM_005542.4. [O15503-1 ]
NP_938150.2. NM_198336.2.
NP_938151.1. NM_198337.2. [O15503-2 ]
UniGenei Hs.520819.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4J81 X-ray 1.74 C/D 273-277 [» ]
ProteinModelPortali O15503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109850. 20 interactions.
IntActi O15503. 5 interactions.
MINTi MINT-4723340.
STRINGi 9606.ENSP00000344741.

PTM databases

PhosphoSitei O15503.

Proteomic databases

PaxDbi O15503.
PRIDEi O15503.

Protocols and materials databases

DNASUi 3638.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340368 ; ENSP00000344741 ; ENSG00000186480 . [O15503-1 ]
ENST00000342407 ; ENSP00000344035 ; ENSG00000186480 . [O15503-2 ]
GeneIDi 3638.
KEGGi hsa:3638.
UCSCi uc003wly.3. human. [O15503-1 ]
uc003wlz.3. human.

Organism-specific databases

CTDi 3638.
GeneCardsi GC07P155089.
HGNCi HGNC:6083. INSIG1.
MIMi 602055. gene.
neXtProti NX_O15503.
PharmGKBi PA29890.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263628.
HOGENOMi HOG000253021.
HOVERGENi HBG058958.
OMAi AMSGPEP.
OrthoDBi EOG7RNK13.
PhylomeDBi O15503.
TreeFami TF331013.

Enzyme and pathway databases

Reactomei REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).

Miscellaneous databases

ChiTaRSi INSIG1. human.
GeneWikii INSIG1.
GenomeRNAii 3638.
NextBioi 14239.
PROi O15503.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15503.
Bgeei O15503.
CleanExi HS_INSIG1.
Genevestigatori O15503.

Family and domain databases

InterProi IPR009904. INSIG-1.
IPR025929. INSIG_fam.
[Graphical view ]
PANTHERi PTHR15301:SF11. PTHR15301:SF11. 1 hit.
Pfami PF07281. INSIG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, human chromosomal assignment, and adipose and hepatic expression of the CL-6/INSIG1 gene."
    Peng Y., Schwarz E.J., Lazar M.A., Genin A., Spinner N.B., Taub R.
    Genomics 43:278-284(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-27.
  2. "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER."
    Yang T., Espenshade P.J., Wright M.E., Yabe D., Gong Y., Aebersold R., Goldstein J.L., Brown M.S.
    Cell 110:489-500(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 40-61 AND 64-83, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SCAP AND SREBP2 COMPLEX.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  5. "High-throughput cloning of full-length human cDNAs directly from cDNA libraries optimized for large and rare transcripts."
    Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G., He W.
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mammary tumor.
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Skin.
  9. "Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain."
    Sever N., Yang T., Brown M.S., Goldstein J.L., DeBose-Boyd R.A.
    Mol. Cell 11:25-33(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HMGCR, FUNCTION.
  10. "Membrane topology of human insig-1, a protein regulator of lipid synthesis."
    Feramisco J.D., Goldstein J.L., Brown M.S.
    J. Biol. Chem. 279:8487-8496(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  11. "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase."
    Song B.L., Sever N., DeBose-Boyd R.A.
    Mol. Cell 19:829-840(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMFR, FUNCTION.
  12. "Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake."
    Gong Y., Lee J.N., Lee P.C., Goldstein J.L., Brown M.S., Ye J.
    Cell Metab. 3:15-24(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCAP AND SREBP2 COMPLEX, UBIQUITINATION AT LYS-156 AND LYS-158, MUTAGENESIS OF LYS-156 AND LYS-158.
  13. "Juxtamembranous aspartic acid in Insig-1 and Insig-2 is required for cholesterol homeostasis."
    Gong Y., Lee J.N., Brown M.S., Goldstein J.L., Ye J.
    Proc. Natl. Acad. Sci. U.S.A. 103:6154-6159(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-205.
  14. "The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways."
    Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A., Gemmill R.M.
    Mol. Cancer Res. 8:93-106(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF139, UBIQUITINATION BY RNF139.

Entry informationi

Entry nameiINSI1_HUMAN
AccessioniPrimary (citable) accession number: O15503
Secondary accession number(s): A4D2N1
, A8K6L0, Q53XW8, Q9BUV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Expressed at high levels when nuclear SREBP levels are high as a result of sterol deprivation.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi