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Q9Y287 (ITM2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integral membrane protein 2B
Alternative name(s):
Immature BRI2
Short name=imBRI2
Protein E25B
Transmembrane protein BRI
Short name=Bri

Cleaved into the following 4 chains:

  1. BRI2, membrane form
    Alternative name(s):
    Mature BRI2
    Short name=mBRI2
  2. BRI2 intracellular domain
    Short name=BRI2 ICD
  3. BRI2C, soluble form
  4. Bri23 peptide
    Short name=Bri2-23
    Alternative name(s):
    ABri23
    C-terminal peptide
    P23 peptide
Gene names
Name:ITM2B
Synonyms:BRI, BRI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a regulatory role in the processing of the beta-amyloid A4 precursor protein (APP) and acts as an inhibitor of the beta-amyloid peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19

Mature BRI2 (mBRI2) functions as a modulator of the beta-amyloid A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed beta-amyloid protein 40 and beta-amyloid protein 42. Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19

Bri23 peptide prevents aggregation of APP beta-amyloid protein 42 peptide into toxic oligomers. Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19

Subunit structure

Homodimer; disulfide-linked. Interacts with SPPL2A and SPPL2B. Interacts with APP. Mature BRI2 (mBRI2) interacts with the APP amyloid beta A4 protein; the interaction occurs at the cell surface and in the endocytic compartments and enable alpha- and beta-secretase-induced APP cleavage inhibition. Mature BRI2 (mBRI2) interacts with the APP C99; the interaction occurs in the endocytic compartments and enable gamma-secretase-induced C99 cleavage inhibition. May form heterodimers with Bri23 peptide and APP beta-amyloid protein 40. Ref.8 Ref.9 Ref.11 Ref.15 Ref.16 Ref.18 Ref.19

Subcellular location

Integral membrane protein 2B: Golgi apparatus membrane; Single-pass type II membrane protein. Note: Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted. Ref.6 Ref.7 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18

BRI2, membrane form: Cell membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Note: Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing. Ref.6 Ref.7 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18

Bri23 peptide: Secreted Ref.6 Ref.7 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18. Note: Detected in the cerebral spinal fluid (CSF). Ref.6 Ref.7 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18

BRI2C, soluble form: Secreted Ref.6 Ref.7 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18.

Tissue specificity

Ubiquitous. Expressed in brain.

Post-translational modification

The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragment (BRI2C, membrane form) is further proteolytically processed by SPPL2A and SPPL2B through regulated intramembrane proteolysis producing a secreted C-peptide and a BRI2 intracellular domain (BRI2 ICD) released in the cytosol. Shedding by ADAM10 facilitates intramembrane cleavage but is not absolutely required for BRI2 ICD generation. Ref.6 Ref.7 Ref.11 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20

Glycosylation at Asn-170 is important for cell surface localization, but doesn't affect furin- and ADAM10-induced proteolytic processing.

Involvement in disease

Cerebral amyloid angiopathy, ITM2B-related 1 (CAA-ITM2B1) [MIM:176500]: A disorder characterized by amyloid deposition in the walls of cerebral blood vessels and neurodegeneration in the central nervous system. Cerebral amyloid angiopathy, non-neuritic and perivascular plaques and neurofibrillary tangles are the predominant pathological lesions. Clinical features include progressive mental deterioration, spasticity and muscular rigidity.
Note: The disease is caused by mutations affecting the gene represented in this entry. A single base substitution at the stop codon of ITM2B generates a 277-residue precursor that is cleaved at the normal furin processing site to generate the ABri amyloidogenic peptide (Ref.1). ABri accumulates in the brain and produces amyloid fibrils responsible for neuronal dysfunction and dementia. ABri peptide variant forms fibrils in vitro (Ref.6). Ref.1 Ref.6 Ref.7

Cerebral amyloid angiopathy, ITM2B-related 2 (CAA-ITM2B2) [MIM:117300]: A disorder characterized by amyloid deposition in the walls of the blood vessels of the cerebrum, choroid plexus, cerebellum, spinal cord and retina. Plaques and neurofibrillary tangles are observed in the hippocampus. Clinical features include progressive ataxia, dementia, cataracts and deafness.
Note: The disease is caused by mutations affecting the gene represented in this entry. A decamer duplication in the 3' region of ITM2B results in the production of the ADan amyloidogenic peptide (Ref.2). ADan is generated by cleavage of the mutated precursor at the normal furin processing site. ADan accumulates in the brain and produces amyloid fibrils responsible for neuronal dysfunction and dementia. Ref.2 Ref.7 Ref.10

Sequence similarities

Belongs to the ITM2 family.

Contains 1 BRICHOS domain.

Ontologies

Keywords
   Cellular componentAmyloid
Cell membrane
Endosome
Golgi apparatus
Membrane
Secreted
   DiseaseAmyloidosis
Deafness
Disease mutation
Neurodegeneration
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processextrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of amyloid precursor protein biosynthetic process

Inferred from direct assay Ref.9Ref.12. Source: UniProtKB

nervous system development

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi-associated vesicle membrane

Inferred from direct assay Ref.11. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.12. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

integral component of organelle membrane

Inferred from direct assay Ref.6. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay Ref.14Ref.20. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: Ensembl

beta-amyloid binding

Inferred from physical interaction PubMed 19849849. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Integral membrane protein 2B
PRO_0000045840
Chain1 – 243243BRI2, membrane form
PRO_0000417464
Chain1 – ?BRI2 intracellular domainPRO_0000417465
Chain? – 243BRI2C, soluble formPRO_0000417466
Peptide244 – 26623Bri23 peptide
PRO_0000016545

Regions

Topological domain1 – 5454Cytoplasmic Potential
Transmembrane55 – 7521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain76 – 266191Lumenal Potential
Domain137 – 23195BRICHOS
Region102 – 13433Necessary for interaction with APP and inhibitor effects on APP processing

Sites

Site243 – 2442Cleavage; by furin

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...) Ref.17
Disulfide bond89Interchain Ref.15 Ref.16
Disulfide bond164 ↔ 223 Probable
Disulfide bond248 ↔ 265Interchain (between ADan peptide variants) Ref.15 Ref.16

Natural variations

Natural variant2661S → FNLFLNSQEKHY in CAA-ITM2B2; amyloid ADan; colocalizes with APP beta-amyloid protein 42 in parenchymal and vascular lesions; interacts with APP beta-amyloid 42; oligomerizes and is subjected to disulfide bond formation; undergoes cyclic pyroglutamate formation on the N-terminus Gln residues and is further proteolytically cleaved in the cerebral cortex. Ref.1 Ref.6 Ref.7
VAR_010240
Natural variant2661S → SRTVKKNIIEEN in CAA-ITM2B1; amyloid ABri.
VAR_010239

Experimental info

Mutagenesis601G → V: Reduces strongly intramembrane cleavage by SPPL2B. Ref.11 Ref.18 Ref.20
Mutagenesis1701N → A: Accumulates in intracellular compartments. Does not inhibit furin, ADAM10 and SPPL2A extracellular proteolytic processing activity. Ref.11 Ref.17 Ref.18
Mutagenesis243 – 2442RE → AA: Inhibits cleavage by furin. Does not prevent ADAM10 shedding. Ref.11 Ref.18

Sequences

Sequence LengthMass (Da)Tools
Q9Y287 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3A7D8CA259F1F627

FASTA26630,338
        10         20         30         40         50         60 
MVKVTFNSAL AQKEAKKDEP KSGEEALIIP PDAVAVDCKD PDDVVPVGQR RAWCWCMCFG 

        70         80         90        100        110        120 
LAFMLAGVIL GGAYLYKYFA LQPDDVYYCG IKYIKDDVIL NEPSADAPAA LYQTIEENIK 

       130        140        150        160        170        180 
IFEEEEVEFI SVPVPEFADS DPANIVHDFN KKLTAYLDLN LDKCYVIPLN TSIVMPPRNL 

       190        200        210        220        230        240 
LELLINIKAG TYLPQSYLIH EHMVITDRIE NIDHLGFFIY RLCHDKETYK LQRRETIKGI 

       250        260 
QKREASNCFA IRHFENKFAV ETLICS 

« Hide

References

« Hide 'large scale' references
[1]"A stop-codon mutation in the BRI gene associated with familial British dementia."
Vidal R., Frangione B., Rostagno A., Mead S., Revesz T., Plant G., Ghiso J.
Nature 399:776-781(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CAA-ITM2B1 ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS.
Tissue: Pituitary.
[2]"A decamer duplication in the 3' region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred."
Vidal R., Revesz T., Rostagno A., Kim E., Holton J.L., Bek T., Bojsen-Moeller M., Braendgaard H., Plant G., Ghiso J., Frangione B.
Proc. Natl. Acad. Sci. U.S.A. 97:4920-4925(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CAA-ITM2B2 SER-266 DELINS PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR.
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[4]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
Tissue: Brain.
[6]"Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia."
Kim S.H., Wang R., Gordon D.J., Bass J., Steiner D.F., Lynn D.G., Thinakaran G., Meredith S.C., Sisodia S.S.
Nat. Neurosci. 2:984-988(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CAA-ITM2B1 ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS, TOPOLOGY, CLEAVAGE BY FURIN, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Axonal transport of British and Danish amyloid peptides via secretory vesicles."
Choi S.I., Vidal R., Frangione B., Levy E.
FASEB J. 18:373-375(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOPOLOGY, PROTEOLYTIC CLEAVAGE, CHARACTERIZATION OF VARIANTS CAA-ITM2B1 ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS AND CAA-ITM2B2 SER-266 DELINS PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR, SUBCELLULAR LOCATION.
[8]"The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production."
Matsuda S., Giliberto L., Matsuda Y., Davies P., McGowan E., Pickford F., Ghiso J., Frangione B., D'Adamio L.
J. Biol. Chem. 280:28912-28916(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APP.
[9]"BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) production."
Fotinopoulou A., Tsachaki M., Vlavaki M., Poulopoulos A., Rostagno A., Frangione B., Ghiso J., Efthimiopoulos S.
J. Biol. Chem. 280:30768-30772(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APP.
[10]"Familial Danish dementia: co-existence of Danish and Alzheimer amyloid subunits (ADan AND A{beta}) in the absence of compact plaques."
Tomidokoro Y., Lashley T., Rostagno A., Neubert T.A., Bojsen-Moller M., Braendgaard H., Plant G., Holton J., Frangione B., Revesz T., Ghiso J.
J. Biol. Chem. 280:36883-36894(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CAA-ITM2B2 SER-266 DELINS PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR.
[11]"Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b."
Martin L., Fluhrer R., Reiss K., Kremmer E., Saftig P., Haass C.
J. Biol. Chem. 283:1644-1652(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, CLEAVAGE BY ADAM10; FURIN; SPPL2A AND SPPL2B, INTERACTION WITH SPPL2A AND SPPL2B, MUTAGENESIS OF 243-ARG-GLU-244.
[12]"BRI2 (ITM2b) inhibits Abeta deposition in vivo."
Kim J., Miller V.M., Levites Y., West K.J., Zwizinski C.W., Moore B.D., Troendle F.J., Bann M., Verbeeck C., Price R.W., Smithson L., Sonoda L., Wagg K., Rangachari V., Zou F., Younkin S.G., Graff-Radford N., Dickson D., Rosenberry T., Golde T.E.
J. Neurosci. 28:6030-6036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SECRETED BRI23 PEPTIDE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate."
Matsuda S., Giliberto L., Matsuda Y., McGowan E.M., D'Adamio L.
J. Neurosci. 28:8668-8676(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis."
Martin L., Fluhrer R., Haass C.
J. Biol. Chem. 284:5662-5670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ADAM10; FURIN AND SPPL2B, SUBCELLULAR LOCATION.
[15]"The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-23) and amyloid beta-peptide (Abeta1-40): Implications for Bri2 effects on processing of amyloid precursor protein and Abeta aggregation."
Peng S., Fitzen M., Jornvall H., Johansson J.
Biochem. Biophys. Res. Commun. 393:356-361(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SECRETED BRI23 PEPTIDE, SUBUNIT, INTERACTION WITH APP BETA-AMYLOID PROTEIN 40, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"BRI2 homodimerizes with the involvement of intermolecular disulfide bonds."
Tsachaki M., Ghiso J., Rostagno A., Efthimiopoulos S.
Neurobiol. Aging 31:88-98(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BONDS.
[17]"Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10."
Tsachaki M., Serlidaki D., Fetani A., Zarkou V., Rozani I., Ghiso J., Efthimiopoulos S.
Glycobiology 21:1382-1388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ADAM10; FURIN AND SPPL2B, GLYCOSYLATION AT ASN-170, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-170.
[18]"Maturation of BRI2 generates a specific inhibitor that reduces APP processing at the plasma membrane and in endocytic vesicles."
Matsuda S., Matsuda Y., Snapp E.L., D'Adamio L.
Neurobiol. Aging 32:1400-1408(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF MBRI2 IN APP PROCESSING INHIBITION, INTERACTION WITH APP AMYLOID BETA A4 AND APP C99, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, MUTAGENESIS OF 243-ARG-GLU-244.
[19]"beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia."
Tamayev R., Matsuda S., Arancio O., D'Adamio L.
EMBO Mol. Med. 4:171-179(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF MBRI2 IN APP PROCESSING INHIBITION, INTERACTION WITH APP AMYLOID BETA A4 AND APP C99.
[20]"The alpha-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)."
Fluhrer R., Martin L., Klier B., Haug-Kroper M., Grammer G., Nuscher B., Haass C.
J. Biol. Chem. 287:5156-5163(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY SPPL2A AND SPPL2B, MUTAGENESIS OF GLY-60.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152462 mRNA. Translation: AAD45280.1.
AF246221 mRNA. Translation: AAF66130.1.
AF092128 mRNA. Translation: AAD40370.1.
AY341247 Genomic DNA. Translation: AAP88930.1.
BC000554 mRNA. Translation: AAH00554.1.
RefSeqNP_068839.1. NM_021999.4.
UniGeneHs.643683.

3D structure databases

ProteinModelPortalQ9Y287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114835. 4 interactions.
IntActQ9Y287. 7 interactions.
STRING9606.ENSP00000367828.

PTM databases

PhosphoSiteQ9Y287.

Polymorphism databases

DMDM12643343.

Proteomic databases

PaxDbQ9Y287.
PeptideAtlasQ9Y287.
PRIDEQ9Y287.

Protocols and materials databases

DNASU9445.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378565; ENSP00000367828; ENSG00000136156.
GeneID9445.
KEGGhsa:9445.
UCSCuc001vbz.3. human.

Organism-specific databases

CTD9445.
GeneCardsGC13P048807.
HGNCHGNC:6174. ITM2B.
HPAHPA029292.
MIM117300. phenotype.
176500. phenotype.
603904. gene.
neXtProtNX_Q9Y287.
Orphanet97345. Familial dementia, British type.
97346. Familial dementia, Danish type.
PharmGKBPA29971.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283703.
HOGENOMHOG000231259.
HOVERGENHBG059373.
InParanoidQ9Y287.
OMAVTIRHFE.
OrthoDBEOG70KGQD.
PhylomeDBQ9Y287.
TreeFamTF317770.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressQ9Y287.
BgeeQ9Y287.
CleanExHS_ITM2B.
GenevestigatorQ9Y287.

Family and domain databases

InterProIPR007084. BRICHOS_dom.
[Graphical view]
PfamPF04089. BRICHOS. 1 hit.
[Graphical view]
SMARTSM01039. BRICHOS. 1 hit.
[Graphical view]
PROSITEPS50869. BRICHOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITM2B. human.
GeneWikiITM2B.
GenomeRNAi9445.
NextBio35380.
PROQ9Y287.
SOURCESearch...

Entry information

Entry nameITM2B_HUMAN
AccessionPrimary (citable) accession number: Q9Y287
Secondary accession number(s): Q9NYH1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM