Q9Y3D2 (MSRB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine-R-sulfoxide reductase B2, mitochondrial
Short name=MsrB2
EC=1.8.4.-

Gene names

Name:	MSRB2
Synonyms:	CBS-1, MSRB
ORF Names:	CGI-131

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	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine By similarity. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance. Ref.8
Catalytic activity	L-methionine + oxidized thioredoxin = L-methionine R-oxide + reduced thioredoxin.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Mitochondrion Ref.8.
Tissue specificity	Ubiquitous. Detected in retina, ocular ciliary body, skeletal muscle, heart, colon, bone marrow, cerebellum, small intestine, fetal brain, fetal liver, kidney, spinal cord, lung, placenta and prostate. Ref.1 Ref.7
Sequence similarities	Belongs to the MsrB Met sulfoxide reductase family.
Sequence caution	The sequence AAD34126.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein repair Inferred from sequence or structural similarity PubMed 14699060. Source: HGNC
Cellular_component	mitochondrion Inferred from sequence or structural similarity PubMed 14699060. Source: HGNC
Molecular_function	peptide-methionine (R)-S-oxide reductase activity Inferred from sequence or structural similarity PubMed 14699060. Source: HGNC sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from sequence or structural similarity PubMed 14699060. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 20	20	Mitochondrion Potential
	Chain	21 – 182	162	Methionine-R-sulfoxide reductase B2, mitochondrial		PRO_0000140324
Sites
	Active site	169	1	Nucleophile By similarity
	Metal binding	90	1	Zinc By similarity
	Metal binding	93	1	Zinc By similarity
	Metal binding	146	1	Zinc By similarity
	Metal binding	149	1	Zinc By similarity
Natural variations
	Natural variant	46	1	E → G. Corresponds to variant rs2296466 [ dbSNP | Ensembl ].		VAR_050448
Experimental info
	Sequence conflict	63	1	F → L in AAH18030. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9Y3D2 [UniParc]. Last modified April 8, 2008. Version 2. Checksum: DFD1D0BF249D45BE	FASTA	182	19,536
	10 20 30 40 50 60 MARLLWLLRG LTLGTAPRRA VRGQAGGGGP GTGPGLGEAG SLATCELPLA KSEWQKKLTP 70 80 90 100 110 120 EQFYVTREKG TEPPFSGIYL NNKEAGMYHC VCCDSPLFSS EKKYCSGTGW PSFSEAHGTS 130 140 150 160 170 180 GSDESHTGIL RRLDTSLGSA RTEVVCKQCE AHLGHVFPDG PGPNGQRFCI NSVALKFKPR KH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases." Huang W., Escribano J., Sarfarazi M., Coca-Prados M. Gene 233:233-240(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Ocular ciliary body.
[2]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Tissue: Brain.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Tissue: Brain.
[6]	"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.
[7]	"Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells." Marchetti M.A., Pizarro G.O., Sagher D., Deamicis C., Brot N., Hejtmancik J.F., Weissbach H., Kantorow M. Invest. Ophthalmol. Vis. Sci. 46:2107-2112(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage." Cabreiro F., Picot C.R., Perichon M., Castel J., Friguet B., Petropoulos I. J. Biol. Chem. 283:16673-16681(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF122004 mRNA. Translation: AAD38899.1. AF151889 mRNA. Translation: AAD34126.1. Frameshift. EF444983 Genomic DNA. Translation: ACA05998.1. AL139281 Genomic DNA. Translation: CAI12665.1. CH471072 Genomic DNA. Translation: EAW86135.1. BC018030 mRNA. Translation: AAH18030.1. BC117471 mRNA. Translation: AAI17472.1. BC130380 mRNA. Translation: AAI30381.1.
IPI	IPI00032871.
RefSeq	NP_036360.3. NM_012228.3.
UniGene	Hs.461420.
3D structure databases
ProteinModelPortal	Q9Y3D2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000365693.
PTM databases
PhosphoSite	Q9Y3D2.
Polymorphism databases
DMDM	182676405.
Proteomic databases
PaxDb	Q9Y3D2.
PRIDE	Q9Y3D2.
Protocols and materials databases
DNASU	22921.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376510; ENSP00000365693; ENSG00000148450.
GeneID	22921.
KEGG	hsa:22921.
UCSC	uc001iro.3. human.
Organism-specific databases
CTD	22921.
GeneCards	GC10P023425.
H-InvDB	HIX0035324.
HGNC	HGNC:17061. MSRB2.
HPA	HPA027933.
MIM	613782. gene.
neXtProt	NX_Q9Y3D2.
PharmGKB	PA134979691.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0229.
HOGENOM	HOG000243424.
HOVERGEN	HBG002192.
KO	K07305.
OMA	EIRCGQC.
OrthoDB	EOG4RFKTW.
Enzyme and pathway databases
BRENDA	1.8.4.12. 2681.
Gene expression databases
Bgee	Q9Y3D2.
CleanEx	HS_MSRB2.
Genevestigator	Q9Y3D2.
GermOnline	ENSG00000148450. Homo sapiens.
Family and domain databases
Gene3D	2.170.150.20. 1 hit.
InterPro	IPR002579. Met_Sox_Rdtase_MsrB. IPR011057. Mss4-like. [Graphical view]
Pfam	PF01641. SelR. 1 hit. [Graphical view]
SUPFAM	SSF51316. Mss4_like. 1 hit.
TIGRFAMs	TIGR00357. TIGR00357. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00134. L-Methionine.
GenomeRNAi	22921.
NextBio	43625.
SOURCE	Search...

Entry information

Entry name

MSRB2_HUMAN

Accession

Primary (citable) accession number: Q9Y3D2
Secondary accession number(s): Q17R44, Q4G1C7, Q9Y5W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	April 8, 2008
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 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.