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Entry version 126 (02 Dec 2020)
Sequence version 2 (15 May 2007)
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Protein

Insulin-induced gene 2 protein

Gene

INSIG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR (PubMed:12242332, PubMed:16606821, PubMed:32322062). Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:32322062). Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum (PubMed:26160948, PubMed:17428920, PubMed:32322062). In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi (PubMed:32322062). Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:32322062). Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139 (PubMed:16606821, PubMed:22143767).6 Publications

Caution

A study showed that INSIG2 is not ubiquitinated by AMFR/gp78 (PubMed:17043353). However, another paper showed that it is ubiquitinated on Cys-215, and that ubiquitination takes place in some tissues only and depends on the differentiation state (PubMed:31953408).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei115Required for the recognition of 25-hydroxycholesterol1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism
LigandLipid-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q9Y5U4

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1655829, Regulation of cholesterol biosynthesis by SREBP (SREBF)

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9Y5U4

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Insulin-induced gene 2 protein1 Publication
Short name:
INSIG-21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:INSIG21 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

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EuPathDBi
HostDB:ENSG00000125629.14

Human Gene Nomenclature Database

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HGNCi
HGNC:20452, INSIG2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608660, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9Y5U4

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 28CytoplasmicCuratedAdd BLAST28
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei29 – 51Helical; Name=1By similarityAdd BLAST23
Topological domaini52 – 70LumenalCuratedAdd BLAST19
Transmembranei71 – 88Helical; Name=2By similarityAdd BLAST18
Topological domaini89 – 103CytoplasmicCuratedAdd BLAST15
Transmembranei104 – 126Helical; Name=3By similarityAdd BLAST23
Topological domaini127 – 129LumenalCurated3
Transmembranei130 – 148Helical; Name=4By similarityAdd BLAST19
Topological domaini149 – 153CytoplasmicCurated5
Transmembranei154 – 175Helical; Name=5By similarityAdd BLAST22
Topological domaini176 – 189LumenalCuratedAdd BLAST14
Transmembranei190 – 207Helical; Name=6By similarityAdd BLAST18
Topological domaini208 – 225CytoplasmicCuratedAdd BLAST18

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi39G → F: Decreased binding to 25-hydroxycholesterol, leading to decreased interaction with SCAP. 1 Publication1
Mutagenesisi77C → D: Decreased binding to 25-hydroxycholesterol, leading to decreased interaction with SCAP. 1 Publication1
Mutagenesisi100 – 102KFK → RFR: Does not affect degradation of the protein. 1 Publication3
Mutagenesisi113A → W: Abolished interaction with SCAP even in the presence of 25-hydroxycholesterol. 1 Publication1
Mutagenesisi114V → F: Does not affect interaction with SCAP. 1 Publication1
Mutagenesisi115F → A: Decreased binding to 25-hydroxycholesterol and subsequent interaction with SCAP. 2 Publications1
Mutagenesisi116V → F: Does not affect interaction with SCAP. 1 Publication1
Mutagenesisi117G → F: Abolished interaction with SCAP even in the presence of 25-hydroxycholesterol. 1 Publication1
Mutagenesisi120H → F: Abolished interaction with SCAP even in the presence of 25-hydroxycholesterol. 1 Publication1
Mutagenesisi132Q → A: Abolished interaction with SCAP without affecting binding to 25-hydroxycholesterol. 2 Publications1
Mutagenesisi136T → A: Decreased binding to 25-hydroxycholesterol and subsequent interaction with SCAP. 1 Publication1
Mutagenesisi145W → A: Abolished interaction with SCAP without affecting binding to 25-hydroxycholesterol. 2 Publications1
Mutagenesisi149D → A: Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR. Abolished interaction with SCAP without affecting binding to 25-hydroxycholesterol. 3 Publications1
Mutagenesisi151S → A: Abolished phosphorylation by PCK1, does not affect oxysterol-binding, does not affect the interaction with SCAP. 1 Publication1
Mutagenesisi151S → E: Phosphomimetic mutant, reduced binding to oxysterol. 1 Publication1
Mutagenesisi200G → F: Decreased binding to 25-hydroxycholesterol, leading to decreased interaction with SCAP. 1 Publication1
Mutagenesisi214E → A: Promotes ubiquitination by AMFR/gp78, which does not take place normally. 1 Publication1
Mutagenesisi215C → A: Prevents degradation because of impaired ubiquitination. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
51141

Open Targets

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OpenTargetsi
ENSG00000125629

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134890284

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9Y5U4, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
INSIG2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
147646722

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002867971 – 225Insulin-induced gene 2 proteinAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei151Phosphoserine; by PCK11 Publication1
Modified residuei215Cysteine sulfenic acid (-SOH); alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki215Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-151 by PCK1 reduces binding to oxysterol, disrupting the interaction between INSIG2 and SCAP, thereby promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.1 Publication
Polyubiquitinated by AMFR/gp78 at Cys-215 in some tissues such as adipose tissues, undifferentiated myoblasts and liver, leading to its degradation (PubMed:31953408). In differentiated myotubes, Cys-215 oxidation prevents ubiquitination at the same site, resulting in protein stabilization (PubMed:31953408).1 Publication
Oxidized at Cys-215 in differentiated myotubes, preventing ubiquitination at the same site, and resulting in protein stabilization.1 Publication

Keywords - PTMi

Oxidation, Phosphoprotein, Thioester bond, Ubl conjugation

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y5U4

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9Y5U4

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9Y5U4

PeptideAtlas

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PeptideAtlasi
Q9Y5U4

PRoteomics IDEntifications database

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PRIDEi
Q9Y5U4

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
86507

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Y5U4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9Y5U4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000125629, Expressed in right lobe of liver and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y5U4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y5U4, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000125629, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with SCAP; interaction is direct and only takes place in the presence of sterols; it prevents interaction between SCAP and the coat protein complex II (COPII) (PubMed:12242332, PubMed:17428920, PubMed:26160948, PubMed:32322062). Associates with the SCAP-SREBP complex (composed of SCAP and SREBF1/SREBP1 or SREBF2/SREBP2); association is mediated via its interaction with SCAP and only takes place in the presence of sterols (PubMed:12242332, PubMed:32322062).

Interacts with RNF139 (PubMed:20068067, PubMed:22143767).

Interacts with RNF145 (PubMed:29374057).

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
119325, 74 interactors

Database of interacting proteins

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DIPi
DIP-60913N

Protein interaction database and analysis system

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IntActi
Q9Y5U4, 42 interactors

Molecular INTeraction database

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MINTi
Q9Y5U4

STRING: functional protein association networks

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STRINGi
9606.ENSP00000245787

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9Y5U4, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi219 – 225KxHxx1 Publication7

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Binds oxysterols in a pocket within their transmembrane domains and interacts with SCAP via transmembrane domains 3 and 4.2 Publications
The KxHxx motif mediates association with the coatomer complex.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the INSIG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4363, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00580000081600

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_092922_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y5U4

Database of Orthologous Groups

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OrthoDBi
1342554at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y5U4

TreeFam database of animal gene trees

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TreeFami
TF331013

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR025929, INSIG_fam

The PANTHER Classification System

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PANTHERi
PTHR15301, PTHR15301, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF07281, INSIG, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9Y5U4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEGETESPG PKKCGPYISS VTSQSVNLMI RGVVLFFIGV FLALVLNLLQ
60 70 80 90 100
IQRNVTLFPP DVIASIFSSA WWVPPCCGTA SAVIGLLYPC IDRHLGEPHK
110 120 130 140 150
FKREWSSVMR CVAVFVGINH ASAKVDFDNN IQLSLTLAAL SIGLWWTFDR
160 170 180 190 200
SRSGFGLGVG IAFLATVVTQ LLVYNGVYQY TSPDFLYVRS WLPCIFFAGG
210 220
ITMGNIGRQL AMYECKVIAE KSHQE
Length:225
Mass (Da):24,778
Last modified:May 15, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i13E0392F1B30F08C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0C4DGZ4A0A0C4DGZ4_HUMAN
Insulin-induced gene protein
INSIG2
238Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WCG8F8WCG8_HUMAN
Insulin-induced gene 2 protein
INSIG2
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD43048 differs from that shown. Reason: Frameshift.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF527632 mRNA Translation: AAN28333.1
AF125392 mRNA Translation: AAD43048.1 Frameshift.
AK291433 mRNA Translation: BAF84122.1
AC009303 Genomic DNA Translation: AAX93280.1
CH471103 Genomic DNA Translation: EAW95199.1
BC022475 mRNA Translation: AAH22475.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS2122.1

NCBI Reference Sequences

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RefSeqi
NP_001308258.1, NM_001321329.1
NP_001308259.1, NM_001321330.1
NP_001308260.1, NM_001321331.1
NP_001308261.1, NM_001321332.1
NP_001308262.1, NM_001321333.1
NP_057217.2, NM_016133.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000245787; ENSP00000245787; ENSG00000125629

Database of genes from NCBI RefSeq genomes

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GeneIDi
51141

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:51141

UCSC genome browser

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UCSCi
uc002tlk.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527632 mRNA Translation: AAN28333.1
AF125392 mRNA Translation: AAD43048.1 Frameshift.
AK291433 mRNA Translation: BAF84122.1
AC009303 Genomic DNA Translation: AAX93280.1
CH471103 Genomic DNA Translation: EAW95199.1
BC022475 mRNA Translation: AAH22475.1
CCDSiCCDS2122.1
RefSeqiNP_001308258.1, NM_001321329.1
NP_001308259.1, NM_001321330.1
NP_001308260.1, NM_001321331.1
NP_001308261.1, NM_001321332.1
NP_001308262.1, NM_001321333.1
NP_057217.2, NM_016133.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J82X-ray1.46C/D221-225[»]
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi119325, 74 interactors
DIPiDIP-60913N
IntActiQ9Y5U4, 42 interactors
MINTiQ9Y5U4
STRINGi9606.ENSP00000245787

PTM databases

iPTMnetiQ9Y5U4
PhosphoSitePlusiQ9Y5U4

Polymorphism and mutation databases

BioMutaiINSIG2
DMDMi147646722

Proteomic databases

MassIVEiQ9Y5U4
MaxQBiQ9Y5U4
PaxDbiQ9Y5U4
PeptideAtlasiQ9Y5U4
PRIDEiQ9Y5U4
ProteomicsDBi86507

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
55566, 113 antibodies

Genome annotation databases

EnsembliENST00000245787; ENSP00000245787; ENSG00000125629
GeneIDi51141
KEGGihsa:51141
UCSCiuc002tlk.4, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
51141
DisGeNETi51141
EuPathDBiHostDB:ENSG00000125629.14

GeneCards: human genes, protein and diseases

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GeneCardsi
INSIG2
HGNCiHGNC:20452, INSIG2
HPAiENSG00000125629, Low tissue specificity
MIMi608660, gene
neXtProtiNX_Q9Y5U4
OpenTargetsiENSG00000125629
PharmGKBiPA134890284

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4363, Eukaryota
GeneTreeiENSGT00580000081600
HOGENOMiCLU_092922_0_0_1
InParanoidiQ9Y5U4
OrthoDBi1342554at2759
PhylomeDBiQ9Y5U4
TreeFamiTF331013

Enzyme and pathway databases

PathwayCommonsiQ9Y5U4
ReactomeiR-HSA-1655829, Regulation of cholesterol biosynthesis by SREBP (SREBF)
SIGNORiQ9Y5U4

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
51141, 5 hits in 845 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
INSIG2, human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
INSIG2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
51141
PharosiQ9Y5U4, Tbio

Protein Ontology

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PROi
PR:Q9Y5U4
RNActiQ9Y5U4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000125629, Expressed in right lobe of liver and 238 other tissues
ExpressionAtlasiQ9Y5U4, baseline and differential
GenevisibleiQ9Y5U4, HS

Family and domain databases

InterProiView protein in InterPro
IPR025929, INSIG_fam
PANTHERiPTHR15301, PTHR15301, 1 hit
PfamiView protein in Pfam
PF07281, INSIG, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiINSI2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y5U4
Secondary accession number(s): A8K5W8, Q8TBI8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: December 2, 2020
This is version 126 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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