Q9Y287 (ITM2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Amyloid Cell membrane Endosome Golgi apparatus Membrane Secreted
Disease	Amyloidosis Deafness Disease mutation Neurodegeneration
Domain	Signal-anchor Transmembrane Transmembrane helix
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara 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_component	Golgi-associated vesicle membrane Inferred from direct assay Ref.11. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay Ref.12. Source: UniProtKB integral to organelle membrane Inferred from direct assay Ref.6. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay Ref.14Ref.20. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara beta-amyloid binding Inferred from physical interaction PubMed 19849849. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 266	266	Integral membrane protein 2B		PRO_0000045840
	Chain	1 – 243	243	BRI2, membrane form		PRO_0000417464
	Chain	1 – ?		BRI2 intracellular domain		PRO_0000417465
	Chain	? – 243		BRI2C, soluble form		PRO_0000417466
	Peptide	244 – 266	23	Bri23 peptide		PRO_0000016545
Regions
	Topological domain	1 – 54	54	Cytoplasmic Potential
	Transmembrane	55 – 75	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	76 – 266	191	Lumenal Potential
	Domain	137 – 231	95	BRICHOS
	Region	102 – 134	33	Necessary for interaction with APP and inhibitor effects on APP processing
Sites
	Site	243 – 244	2	Cleavage; by furin
Amino acid modifications
	Glycosylation	170	1	N-linked (GlcNAc...) Ref.17
	Disulfide bond	89		Interchain Ref.15 Ref.16
	Disulfide bond	164 ↔ 223		Probable
	Disulfide bond	248 ↔ 265		Interchain (between ADan peptide variants) Ref.15 Ref.16
Natural variations
	Natural variant	266	1	S → 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 variant	266	1	S → SRTVKKNIIEEN in CAA-ITM2B1; amyloid ABri.		VAR_010239
Experimental info
	Mutagenesis	60	1	G → V: Reduces strongly intramembrane cleavage by SPPL2B. Ref.11 Ref.18 Ref.20
	Mutagenesis	170	1	N → A: Accumulates in intracellular compartments. Does not inhibit furin, ADAM10 and SPPL2A extracellular proteolytic processing activity. Ref.11 Ref.17 Ref.18
	Mutagenesis	243 – 244	2	RE → AA: Inhibits cleavage by furin. Does not prevent ADAM10 shedding. Ref.11 Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Q9Y287 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 3A7D8CA259F1F627	FASTA	266	30,338
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, 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, 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

NIEHS-SNPs

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.
IPI	IPI00031821.
RefSeq	NP_068839.1. NM_021999.4.
UniGene	Hs.643683.
3D structure databases
ProteinModelPortal	Q9Y287.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y287. 6 interactions.
STRING	9606.ENSP00000367828.
PTM databases
PhosphoSite	Q9Y287.
Polymorphism databases
DMDM	12643343.
Proteomic databases
PaxDb	Q9Y287.
PeptideAtlas	Q9Y287.
PRIDE	Q9Y287.
Protocols and materials databases
DNASU	9445.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378565; ENSP00000367828; ENSG00000136156.
GeneID	9445.
KEGG	hsa:9445.
UCSC	uc001vbz.3. human.
Organism-specific databases
CTD	9445.
GeneCards	GC13P048807.
HGNC	HGNC:6174. ITM2B.
HPA	HPA029292.
MIM	117300. phenotype. 176500. phenotype. 603904. gene.
neXtProt	NX_Q9Y287.
Orphanet	97345. Familial dementia, British type. 97346. Familial dementia, Danish type.
PharmGKB	PA29971.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG283703.
HOGENOM	HOG000231259.
HOVERGEN	HBG059373.
InParanoid	Q9Y287.
OMA	VDHLGFF.
OrthoDB	EOG48D0WD.
PhylomeDB	Q9Y287.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q9Y287.
Bgee	Q9Y287.
CleanEx	HS_ITM2B.
Genevestigator	Q9Y287.
GermOnline	ENSG00000136156. Homo sapiens.
Family and domain databases
InterPro	IPR007084. BRICHOS_dom. [Graphical view]
Pfam	PF04089. BRICHOS. 1 hit. [Graphical view]
SMART	SM01039. BRICHOS. 1 hit. [Graphical view]
PROSITE	PS50869. BRICHOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ITM2B. human.
GenomeRNAi	9445.
NextBio	35380.
SOURCE	Search...

Entry information

Entry name

ITM2B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.