Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61769 (B2MG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-2-microglobulin

Cleaved into the following chain:

  1. Beta-2-microglobulin form pI 5.3
Gene names
Name:B2M
ORF Names:CDABP0092, HDCMA22P
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

Subunit structure

Heterodimer of an alpha chain and a beta chain. Beta-2-microglobulin is the beta-chain of major histocompatibility complex class I molecules. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. Ref.14

Subcellular location

Secreted. Note: Detected in serum and urine. Ref.16 Ref.17

Post-translational modification

Glycation of Ile-21 is observed in long-term hemodialysis patients.

Involvement in disease

Hypercatabolic hypoproteinemia (HYCATHYP) [MIM:241600]: Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33

Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Sequence similarities

Belongs to the beta-2-microglobulin family.

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentAmyloid
MHC I
Secreted
   DiseaseAmyloidosis
Disease mutation
   DomainImmunoglobulin domain
Signal
   PTMDisulfide bond
Glycation
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

protein refolding

Inferred from electronic annotation. Source: Ensembl

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

regulation of immune response

Traceable author statement. Source: Reactome

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to molecule of bacterial origin

Inferred from electronic annotation. Source: Ensembl

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

viral process

Traceable author statement. Source: Reactome

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Traceable author statement. Source: Reactome

MHC class I protein complex

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

early endosome lumen

Traceable author statement. Source: Reactome

early endosome membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

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

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 21569201PubMed 22289140PubMed 22575645. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.13 Ref.14 Ref.15 Ref.16
Chain21 – 11999Beta-2-microglobulin
PRO_0000018779
Chain22 – 11998Beta-2-microglobulin form pI 5.3
PRO_0000018780

Regions

Domain25 – 11389Ig-like C1-type

Amino acid modifications

Modified residue221Pyrrolidone carboxylic acid; in form pI 5.3
Glycosylation211N-linked (Glc) (glycation); in hemodialysis-associated amyloidosis Ref.18
Glycosylation391N-linked (Glc) (glycation); in vitro Ref.18
Glycosylation611N-linked (Glc) (glycation); in vitro Ref.18
Glycosylation681N-linked (Glc) (glycation); in vitro Ref.18
Glycosylation781N-linked (Glc) (glycation); in vitro Ref.18
Glycosylation1111N-linked (Glc) (glycation); in vitro Ref.18
Glycosylation1141N-linked (Glc) (glycation); in vitro Ref.18
Disulfide bond45 ↔ 100 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Natural variations

Natural variant111A → P in HYCATHYP; lower levels of B2M, MHC class I and FCGRT proteins. Ref.33
VAR_030660

Experimental info

Mutagenesis791D → P: Increases tendency towards amyloid formation. Ref.30
Mutagenesis801W → G: Decreases tendency towards amyloid formation. Ref.31 Ref.32
Mutagenesis801W → V: Increases tendency towards amyloid formation. Ref.31 Ref.32
Sequence conflict201A → G in AAA51811. Ref.1
Sequence conflict521P → Q in AAA51811. Ref.1
Sequence conflict1191M → I in CAG33347. Ref.7

Secondary structure

....................... 119
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61769 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: AFD2DBEF07DCEF27

FASTA11913,715
        10         20         30         40         50         60 
MSRSVALAVL ALLSLSGLEA IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL 

        70         80         90        100        110 
KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC RVNHVTLSQP KIVKWDRDM 

« Hide

References

« Hide 'large scale' references
[1]"The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit."
Guessow D., Rein R., Ginjaar I., Hochstenbach F., Seemann G., Kottman A., Ploegh H.L.
J. Immunol. 139:3132-3138(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning of human beta-microglobulin gene and its high expression in Escherichia coli."
He X.H., Xu L.H., Liu Y., Zeng Y.Y.
Sheng Wu Gong Cheng Xue Bao 20:99-103(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[3]"Human mRNA for beta 2-microglobulin."
Matsumoto K., Minamitani T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[4]"Genetic variation in immune response genes."
Tan J., Ong R., Hibberd M.L., Seielstad M.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"A novel gene from human dendritic cell."
Zhao Z., Huang X., Li N., Zhu X., Cao X.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Dendritic cell.
[6]"Pediatric leukemia cDNA sequencing project."
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Leukemia.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"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. expand/collapse author list , 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].
Tissue: Trachea.
[9]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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: Retina and Skin.
[11]"The beta-2-microglobulin mRNA in human Daudi cells has a mutated initiation codon but is still inducible by interferon."
Rosa F., Berissi H., Weissenbach J., Maroteaux L., Fellous M., Revel M.
EMBO J. 2:239-243(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21.
[12]"Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin."
Suggs S.V., Wallace R.B., Hirose T., Kawashima E.H., Itakura K.
Proc. Natl. Acad. Sci. U.S.A. 78:6613-6617(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-119.
[13]"The complete amino acid sequence of beta 2-microglobulin."
Cunningham B.A., Wang J.L., Berggard I., Peterson P.A.
Biochemistry 12:4811-4822(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-119.
[14]"Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis."
Gorevic P.D., Munoz P.C., Casey T.T., DiRaimondo C.R., Stone W.J., Prelli F.C., Rodrigues M.M., Poulik M.D., Frangione B.
Proc. Natl. Acad. Sci. U.S.A. 83:7908-7912(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-119, SUBUNIT, INVOLVEMENT IN AMYLOIDOSIS.
[15]"Isolation of a granulocyte inhibitory protein from uraemic patients with homology of beta 2-microglobulin."
Haag-Weber M., Mai B., Hoerl W.H.
Nephrol. Dial. Transplant. 9:382-388(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-41.
Tissue: Plasma.
[16]"Biochemical characterization of serum and urinary beta 2 microglobulin in end-stage renal disease patients."
Argiles A., Derancourt J., Jauregui-Adell J., Mion C., Demaille J.G.
Nephrol. Dial. Transplant. 7:1106-1110(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-40, SUBCELLULAR LOCATION.
[17]"Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood."
Momoi T., Suzuki M., Titani K., Hisanaga S., Ogawa H., Saito A.
Clin. Chim. Acta 236:135-144(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-119, SUBCELLULAR LOCATION, PYROGLUTAMATE FORMATION AT GLN-22 (FORM PI 5.3).
Tissue: Urine.
[18]"Glycation of human beta 2-microglobulin in patients with hemodialysis-associated amyloidosis: identification of the glycated sites."
Miyata T., Inagi R., Wada Y., Ueda Y., Iida Y., Takahashi M., Taniguchi N., Maeda K.
Biochemistry 33:12215-12221(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AMYLOIDOSIS, GLYCATION AT ILE-21; LYS-39; LYS-61; LYS-68; LYS-78; LYS-111 AND LYS-114, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Structure of the human class I histocompatibility antigen, HLA-A2."
Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C.
Nature 329:506-512(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[21]"Refined structure of the human histocompatibility antigen HLA-A2 at 2.6-A resolution."
Saper M.A., Bjorkman P.J., Wiley D.C.
J. Mol. Biol. 219:277-319(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[22]"1H NMR assignments and secondary structure of human beta 2-microglobulin in solution."
Okon M., Bray P., Vucelic D.
Biochemistry 31:8906-8915(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[23]"The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain."
Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.
Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[24]"Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53."
Smith K.J., Reid S.W., Harlos K., McMichael A.J., Stuart D.I., Bell J.I., Jones E.Y.
Immunity 4:215-228(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[25]"Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties."
Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., Radford S.E.
Proc. Natl. Acad. Sci. U.S.A. 99:9771-9776(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-119, DISULFIDE BOND.
[26]"A structural basis for immunodominant human T cell receptor recognition."
Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.
Nat. Immunol. 4:657-663(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-119 OF HLA-A/B2M HETERODIMER IN COMPLEX WITH TRAC AND TRBC1, DISULFIDE BOND.
[27]"Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis."
Kihara M., Chatani E., Iwata K., Yamamoto K., Matsuura T., Nakagawa A., Naiki H., Goto Y.
J. Biol. Chem. 281:31061-31069(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-119, AMYLOID FORMATION, DISULFIDE BOND.
[28]"A native to amyloidogenic transition regulated by a backbone trigger."
Eakin C.M., Berman A.J., Miranker A.D.
Nat. Struct. Mol. Biol. 13:202-208(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-119, DISULFIDE BOND.
[29]"High-resolution crystal structure of beta2-microglobulin formed at pH 7.0."
Iwata K., Matsuura T., Sakurai K., Nakagawa A., Goto Y.
J. Biochem. 142:413-419(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) OF 21-119, DISULFIDE BOND.
[30]"DE loop mutations affect beta2-microglobulin stability and amyloid aggregation."
Ricagno S., Colombo M., de Rosa M., Sangiovanni E., Giorgetti S., Raimondi S., Bellotti V., Bolognesi M.
Biochem. Biophys. Res. Commun. 377:146-150(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-119, MUTAGENESIS OF ASP-79, DISULFIDE BOND.
[31]"The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties."
Esposito G., Ricagno S., Corazza A., Rennella E., Guemral D., Mimmi M.C., Betto E., Pucillo C.E., Fogolari F., Viglino P., Raimondi S., Giorgetti S., Bolognesi B., Merlini G., Stoppini M., Bolognesi M., Bellotti V.
J. Mol. Biol. 378:887-897(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-119, MUTAGENESIS OF TRP-80, DISULFIDE BOND.
[32]"Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation."
Ricagno S., Raimondi S., Giorgetti S., Bellotti V., Bolognesi M.
Biochem. Biophys. Res. Commun. 380:543-547(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-119, MUTAGENESIS OF TRP-80, DISULFIDE BOND.
[33]"Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene."
Wani M.A., Haynes L.D., Kim J., Bronson C.L., Chaudhury C., Mohanty S., Waldmann T.A., Robinson J.M., Anderson C.L.
Proc. Natl. Acad. Sci. U.S.A. 103:5084-5089(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYCATHYP PRO-11, CHARACTERIZATION OF VARIANT HYCATHYP PRO-11.
+Additional computationally mapped references.

Web resources

Wikipedia

Beta-2-microglobulin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17987, M17986 Genomic DNA. Translation: AAA51811.1.
AY187687 mRNA. Translation: AAO20842.1.
AB021288 mRNA. Translation: BAA35182.1.
DQ217933 Genomic DNA. Translation: ABB01003.1.
AF072097 mRNA. Translation: AAD48083.1.
AY007153 mRNA. Translation: AAG02006.1.
CR457066 mRNA. Translation: CAG33347.1.
AK315776 mRNA. Translation: BAG38125.1.
CH471082 Genomic DNA. Translation: EAW77277.1.
BC032589 mRNA. Translation: AAH32589.1.
BC064910 mRNA. Translation: AAH64910.1.
V00567 mRNA. Translation: CAA23830.1.
PIRMGHUB2. A90976.
RefSeqNP_004039.1. NM_004048.2.
UniGeneHs.534255.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1MX-ray2.30B21-119[»]
1A1NX-ray2.00B21-119[»]
1A1OX-ray2.30B21-119[»]
1A6ZX-ray2.60B/D21-119[»]
1A9BX-ray3.20B/E21-119[»]
1A9EX-ray2.50B21-119[»]
1AGBX-ray2.20B21-119[»]
1AGCX-ray2.10B21-119[»]
1AGDX-ray2.05B21-119[»]
1AGEX-ray2.30B21-119[»]
1AGFX-ray2.20B21-119[»]
1AKJX-ray2.65B21-119[»]
1AO7X-ray2.60B21-119[»]
1B0GX-ray2.50B/E21-119[»]
1B0RX-ray2.90B21-119[»]
1BD2X-ray2.50B21-119[»]
1C16X-ray3.10B/D/F/H21-119[»]
1CE6X-ray2.90B21-119[»]
1CG9X-ray2.70B21-119[»]
1DE4X-ray2.80B/E/H21-119[»]
1DUYX-ray2.15B/E21-119[»]
1DUZX-ray1.80B/E21-119[»]
1E27X-ray2.20B21-119[»]
1E28X-ray3.00B21-119[»]
1EEYX-ray2.25B/E21-119[»]
1EEZX-ray2.30B/E21-119[»]
1EFXX-ray3.00B21-119[»]
1EXUX-ray2.70B21-119[»]
1GZPX-ray2.80B21-119[»]
1GZQX-ray2.26B21-119[»]
1HHGX-ray2.60B/E21-119[»]
1HHHX-ray3.00B21-119[»]
1HHIX-ray2.50B/E21-119[»]
1HHJX-ray2.50B/E21-119[»]
1HHKX-ray2.50B/E21-119[»]
1HLAX-ray3.50M21-117[»]
1HSAX-ray2.10B/E21-119[»]
1HSBX-ray1.90B21-119[»]
1I1FX-ray2.80B/E21-119[»]
1I1YX-ray2.20B/E21-119[»]
1I4FX-ray1.40B21-119[»]
1I7RX-ray2.20B/E21-119[»]
1I7TX-ray2.80B/E21-119[»]
1I7UX-ray1.80B/E21-119[»]
1IM3X-ray2.20B/F/J/N21-119[»]
1IM9X-ray2.80B/F21-119[»]
1JF1X-ray1.85B21-119[»]
1JGDX-ray1.90B21-119[»]
1JGEX-ray2.10B21-119[»]
1JHTX-ray2.15B21-119[»]
1JNJNMR-A21-119[»]
1K5NX-ray1.09B21-119[»]
1KPRX-ray2.80B/D21-119[»]
1KTLX-ray3.10B/D21-119[»]
1LDSX-ray1.80A21-119[»]
1LP9X-ray2.00B/I21-119[»]
1M05X-ray1.90B/D21-119[»]
1M6OX-ray1.60B21-119[»]
1MHEX-ray2.85B/D21-119[»]
1MI5X-ray2.50B21-119[»]
1N2RX-ray1.70B21-119[»]
1OF2X-ray2.20B21-119[»]
1OGAX-ray1.40B21-119[»]
1OGTX-ray1.47B21-119[»]
1ONQX-ray2.15B/D21-119[»]
1P7QX-ray3.40B21-119[»]
1PY4X-ray2.90A/B/C/D21-119[»]
1Q94X-ray2.40B/E21-119[»]
1QEWX-ray2.20B21-119[»]
1QLFX-ray2.65B21-119[»]
1QQDX-ray2.70B21-118[»]
1QR1X-ray2.40B/E21-119[»]
1QRNX-ray2.80B21-119[»]
1QSEX-ray2.80B21-119[»]
1QSFX-ray2.80B21-119[»]
1QVOX-ray2.22B/E21-119[»]
1R3HX-ray2.50B/D/F/H21-119[»]
1S8DX-ray2.20B21-119[»]
1S9WX-ray2.20B21-119[»]
1S9XX-ray2.50B21-119[»]
1S9YX-ray2.30B21-119[»]
1SYSX-ray2.40B21-119[»]
1SYVX-ray1.70B21-119[»]
1T1WX-ray2.20B21-119[»]
1T1XX-ray2.20B21-119[»]
1T1YX-ray2.00B21-119[»]
1T1ZX-ray1.90B21-119[»]
1T20X-ray2.20B21-119[»]
1T21X-ray2.19B21-119[»]
1T22X-ray2.20B21-119[»]
1TMCX-ray2.30B21-119[»]
1TVBX-ray1.80B/E21-119[»]
1TVHX-ray1.80B/E21-119[»]
1UQSX-ray3.10B21-119[»]
1UR7model-B21-119[»]
1UXSX-ray1.55B21-119[»]
1UXWX-ray1.71B21-119[»]
1VGKX-ray2.06B21-119[»]
1W0VX-ray2.27B21-119[»]
1W0WX-ray2.10B21-119[»]
1W72X-ray2.15B/E21-119[»]
1X7QX-ray1.45B21-119[»]
1XH3X-ray1.48B21-119[»]
1XR8X-ray2.30B21-119[»]
1XR9X-ray1.79B21-119[»]
1XZ0X-ray2.80B/D21-119[»]
1YDPX-ray1.90B21-119[»]
1YPZX-ray3.40B/D21-119[»]
1ZHKX-ray1.60B21-119[»]
1ZHLX-ray1.50B21-119[»]
1ZS8X-ray3.00B/D/F/H/J21-119[»]
1ZSDX-ray1.70B21-119[»]
1ZT4X-ray3.00B/D21-119[»]
1ZVSX-ray2.80B/E21-119[»]
2A83X-ray1.40B21-119[»]
2AK4X-ray2.50B/G/L/R21-119[»]
2AV1X-ray1.95B/E21-119[»]
2AV7X-ray2.05B/E21-119[»]
2AXFX-ray1.80B21-119[»]
2AXGX-ray2.00B21-119[»]
2BCKX-ray2.80B/E21-119[»]
2BNQX-ray1.70B21-119[»]
2BNRX-ray1.90B21-119[»]
2BSRX-ray2.30B21-119[»]
2BSSX-ray2.00B21-119[»]
2BSTX-ray2.10B21-119[»]
2BVOX-ray1.65B21-119[»]
2BVPX-ray1.35B21-119[»]
2BVQX-ray2.00B21-119[»]
2C7UX-ray2.38B/E21-119[»]
2CIIX-ray2.55B21-119[»]
2CIKX-ray1.75B21-119[»]
2CLRX-ray2.00B/E21-119[»]
2D31X-ray3.20B/E21-119[»]
2D4DX-ray2.10A21-119[»]
2D4FX-ray1.70A21-119[»]
2DYPX-ray2.50B21-119[»]
2E8DNMR-A/B/C/D40-61[»]
2ESVX-ray2.60B21-119[»]
2F53X-ray2.10B21-119[»]
2F54X-ray2.70B/G21-119[»]
2F74X-ray2.70B/E21-119[»]
2F8OX-ray1.70A/B21-119[»]
2FYYX-ray1.50B21-119[»]
2FZ3X-ray1.90B21-119[»]
2GITX-ray1.70B/E21-119[»]
2GJ6X-ray2.56B21-119[»]
2GT9X-ray1.75B/E21-119[»]
2GTWX-ray1.55B/E21-119[»]
2GTZX-ray1.70B/E21-119[»]
2GUOX-ray1.90B/E21-119[»]
2H26X-ray1.80B21-119[»]
2H6PX-ray1.90B21-119[»]
2HJKX-ray1.85B21-119[»]
2HJLX-ray1.50B21-119[»]
2HLAX-ray2.60B21-119[»]
2HN7X-ray1.60B21-119[»]
2J8UX-ray2.88B/I21-119[»]
2JCCX-ray2.50B/I21-119[»]
2NW3X-ray1.70B21-119[»]
2NX5X-ray2.70B/G/L/R21-119[»]
2P5EX-ray1.89B21-119[»]
2P5WX-ray2.20B21-119[»]
2PO6X-ray3.20B/F21-119[»]
2PYEX-ray2.30B21-119[»]
2RFXX-ray2.50B21-119[»]
2UWEX-ray2.40B/I21-119[»]
2V2WX-ray1.60B/E21-119[»]
2V2XX-ray1.60B/E21-119[»]
2VB5NMR-A21-119[»]
2VLJX-ray2.40B21-119[»]
2VLKX-ray2.50B21-119[»]
2VLLX-ray1.60B/E21-119[»]
2VLRX-ray2.30B/G21-119[»]
2X4NX-ray2.34B/E21-119[»]
2X4OX-ray2.30B/E21-119[»]
2X4PX-ray2.30B/E21-119[»]
2X4QX-ray1.90B/E21-119[»]
2X4RX-ray2.30B/E21-119[»]
2X4SX-ray2.55B/E21-119[»]
2X4TX-ray2.30B/E21-119[»]
2X4UX-ray2.10B/E21-119[»]
2X70X-ray2.00B/E21-119[»]
2X89X-ray2.16D/E/F/G27-119[»]
2XKSNMR-A21-119[»]
2XKUNMR-A27-119[»]
2XPGX-ray2.60B22-118[»]
2YPKX-ray1.95B21-119[»]
2YPLX-ray2.40B21-119[»]
2YXFX-ray1.13A21-119[»]
2Z9TX-ray1.80A21-119[»]
3AM8X-ray2.80C/D21-119[»]
3B3IX-ray1.86B21-119[»]
3B6SX-ray1.80B21-119[»]
3BGMX-ray1.60B21-119[»]
3BH8X-ray1.65B21-119[»]
3BH9X-ray1.70B21-119[»]
3BHBX-ray2.20B22-119[»]
3BO8X-ray1.80B21-119[»]
3BP4X-ray1.85B21-119[»]
3BP7X-ray1.80B21-119[»]
3BVNX-ray2.55B/E21-119[»]
3BW9X-ray1.75B21-119[»]
3BWAX-ray1.30B21-119[»]
3BXNX-ray1.86B21-119[»]
3BZEX-ray2.50B/D/F/H21-119[»]
3BZFX-ray2.50B/D23-119[»]
3C9NX-ray1.87B21-119[»]
3CDGX-ray3.40B/D21-119[»]
3CIIX-ray4.41B/E21-119[»]
3CIQX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L21-119[»]
3CZFX-ray1.20B21-119[»]
3D18X-ray1.74B21-119[»]
3D25X-ray1.30B22-119[»]
3D2UX-ray2.21B/F21-119[»]
3D39X-ray2.81B21-119[»]
3D3VX-ray2.80B21-119[»]
3DBXX-ray2.00B21-119[»]
3DHJX-ray2.00A21-119[»]
3DHMX-ray1.80A21-119[»]
3DTXX-ray2.10B21-119[»]
3DX6X-ray1.70B21-119[»]
3DX7X-ray1.60B21-119[»]
3DX8X-ray2.10B21-119[»]
3DXAX-ray3.50B/G/L21-119[»]
3EKCX-ray1.80A21-119[»]
3FFCX-ray2.80B/G21-119[»]
3FQNX-ray1.65B22-119[»]
3FQRX-ray1.70B22-119[»]
3FQTX-ray1.80B22-119[»]
3FQUX-ray1.80B22-119[»]
3FQWX-ray1.93B22-119[»]
3FQXX-ray1.70B22-119[»]
3FT2X-ray1.80B21-119[»]
3FT3X-ray1.95B21-119[»]
3FT4X-ray1.90B21-119[»]
3GIVX-ray2.00B/E21-119[»]
3GJFX-ray1.90B/E21-119[»]
3GSNX-ray2.80L21-119[»]
3GSOX-ray1.60B21-119[»]
3GSQX-ray2.12B21-119[»]
3GSRX-ray1.95B21-119[»]
3GSUX-ray1.80B21-119[»]
3GSVX-ray1.90B21-119[»]
3GSWX-ray1.81B21-119[»]
3GSXX-ray2.10B21-119[»]
3H7BX-ray1.88B/E21-119[»]
3H9HX-ray2.00B/E21-119[»]
3H9SX-ray2.70B21-119[»]
3HAEX-ray2.90B/E/K/Q21-119[»]
3HCVX-ray1.95B21-119[»]
3HG1X-ray3.00B21-119[»]
3HLAX-ray2.60B21-119[»]
3HPJX-ray2.00B/E21-119[»]
3HUJX-ray2.50B/D21-119[»]
3I6GX-ray2.20B/E21-119[»]
3I6KX-ray2.80B/F21-119[»]
3I6LX-ray2.40E21-119[»]
3IB4X-ray1.25A21-119[»]
3IXAX-ray2.10B/E21-119[»]
3JTSX-ray2.80B/E/H1-119[»]
3KLAX-ray1.65B/E21-119[»]
3KPLX-ray1.96B21-119[»]
3KPMX-ray1.60B21-119[»]
3KPNX-ray2.00B21-119[»]
3KPOX-ray2.30B21-119[»]
3KPPX-ray1.90B21-119[»]
3KPQX-ray1.84B21-119[»]
3KPRX-ray2.60B/G21-119[»]
3KPSX-ray2.70B21-119[»]
3KWWX-ray2.18B21-119[»]
3KXFX-ray3.10B/F/J/L21-119[»]
3KYNX-ray2.40B21-119[»]
3KYOX-ray1.70B/D21-119[»]
3L3DX-ray1.80B21-119[»]
3L3GX-ray2.10B21-119[»]
3L3IX-ray1.70B21-119[»]
3L3JX-ray2.40B21-119[»]
3L3KX-ray2.60B21-119[»]
3LKNX-ray2.00B21-119[»]
3LKOX-ray1.80B21-119[»]
3LKPX-ray1.80B21-119[»]
3LKQX-ray1.80B21-119[»]
3LKRX-ray2.00B21-119[»]
3LKSX-ray1.90B21-119[»]
3LN4X-ray1.30B21-119[»]
3LN5X-ray1.90B21-119[»]
3LOWX-ray2.30A/B21-119[»]
3LOZX-ray1.80A/B/C/D74-79[»]
3LV3X-ray1.94B21-119[»]
3M17X-ray2.60B/D/F/H21-119[»]
3M1BX-ray3.10B/D/F/H21-119[»]
3MGOX-ray2.30B/E/H/K21-119[»]
3MGTX-ray2.20B/E/H/K21-119[»]
3MR9X-ray1.93B21-119[»]
3MRBX-ray1.40B21-119[»]
3MRCX-ray1.80B21-119[»]
3MRDX-ray1.70B21-119[»]
3MREX-ray1.10B21-119[»]
3MRFX-ray2.30B21-119[»]
3MRGX-ray1.30B21-119[»]
3MRHX-ray2.40B21-119[»]
3MRIX-ray2.10B21-119[»]
3MRJX-ray1.87B21-119[»]
3MRKX-ray1.40B21-119[»]
3MRLX-ray2.41B21-119[»]
3MRMX-ray1.90B21-119[»]
3MRNX-ray2.30B21-119[»]
3MROX-ray2.35B21-119[»]
3MRPX-ray2.10B21-119[»]
3MRQX-ray2.20B21-119[»]
3MRRX-ray1.60B21-119[»]
3MV7X-ray2.00B21-119[»]
3MV8X-ray2.10B21-119[»]
3MV9X-ray2.70B21-119[»]
3MYJX-ray1.89B/E21-119[»]
3MYZX-ray1.60A/B21-119[»]
3MZTX-ray2.70A/B/C/D/E/F21-119[»]
3NA4X-ray1.90A21-119[»]
3NFNX-ray2.39B21-119[»]
3O3AX-ray1.80B/E21-119[»]
3O3BX-ray1.90B/E21-119[»]
3O3DX-ray1.70B/E21-119[»]
3O3EX-ray1.85B/E21-119[»]
3O4LX-ray2.54B21-119[»]
3OV6X-ray2.50A21-119[»]
3OX8X-ray2.16B/E21-119[»]
3OXRX-ray1.70B21-119[»]
3OXSX-ray1.75B21-119[»]
3PWJX-ray1.70B/E21-119[»]
3PWLX-ray1.65B/E21-119[»]
3PWNX-ray1.60B/E21-119[»]
3PWPX-ray2.69B21-119[»]
3QDAX-ray1.57A21-119[»]
3QDGX-ray2.69B21-119[»]
3QDJX-ray2.30B21-119[»]
3QDMX-ray2.80B21-119[»]
3QEQX-ray2.59B21-119[»]
3QFDX-ray1.68B/E21-119[»]
3QFJX-ray2.29B21-119[»]
3QZWX-ray2.80B/E21-119[»]
3REWX-ray1.90B/E21-119[»]
3RL1X-ray2.00B21-119[»]
3RL2X-ray2.39B21-119[»]
3RWJX-ray2.70B21-119[»]
3S6CX-ray2.90A21-119[»]
3SDXX-ray3.12B/D21-119[»]
3SJVX-ray3.10B/G/L/Q21-119[»]
3SKMX-ray1.80B21-119[»]
3SKOX-ray1.60B21-119[»]
3SPVX-ray1.30B21-119[»]
3T8XX-ray1.90B/D21-119[»]
3TIDX-ray1.65B21-119[»]
3TIEX-ray2.25B/E21-119[»]
3TLRX-ray2.45A/B/C/D21-119[»]
3TM6X-ray2.70A/B/C/D/E/F/G/H21-119[»]
3TO2X-ray2.60B21-119[»]
3TZVX-ray3.06D21-119[»]
3U0PX-ray2.80B/D/F21-119[»]
3UPRX-ray2.00B/D21-119[»]
3UTQX-ray1.67B21-119[»]
3UTSX-ray2.71B/G21-119[»]
3UTTX-ray2.60B/G21-119[»]
3V5DX-ray2.00B/E21-119[»]
3V5HX-ray1.63B/E21-119[»]
3V5KX-ray2.31B/E21-119[»]
3VCLX-ray1.70B21-119[»]
3VFMX-ray1.90B21-119[»]
3VFNX-ray1.50B21-119[»]
3VFOX-ray1.70B21-119[»]
3VFPX-ray1.85B21-119[»]
3VFRX-ray1.85B21-119[»]
3VFSX-ray1.85B21-119[»]
3VFTX-ray1.95B21-119[»]
3VFUX-ray1.65B21-119[»]
3VFVX-ray1.55B21-119[»]
3VFWX-ray2.30B21-119[»]
3VH8X-ray1.80B/E21-119[»]
3VRIX-ray1.60B21-119[»]
3VRJX-ray1.90B21-119[»]
3VWJX-ray3.09B21-119[»]
3VWKX-ray2.94B21-119[»]
3VXMX-ray2.50B21-119[»]
3VXNX-ray1.95B21-119[»]
3VXOX-ray2.61B/E21-119[»]
3VXPX-ray2.50B/E21-119[»]
3VXRX-ray2.40B21-119[»]
3VXSX-ray1.80B21-119[»]
3VXUX-ray2.70B/G21-119[»]
3W0WX-ray2.60B21-119[»]
3W39X-ray3.10B/E21-119[»]
4E0KX-ray0.97A/B/C/D78-83[»]
4E0LX-ray1.70A/B/C/D82-88[»]
4E5XX-ray1.95B/E21-119[»]
4EN3X-ray2.57D21-119[»]
4EUPX-ray2.88B/E21-119[»]
4EUQX-ray2.69B/E21-119[»]
4F7MX-ray2.40B/E21-119[»]
4F7PX-ray1.90B21-119[»]
4F7TX-ray1.70B/E21-119[»]
4FTVX-ray2.74B21-119[»]
4FXLX-ray1.40A21-119[»]
4G8GX-ray2.40B21-119[»]
4G8IX-ray1.60B21-119[»]
4G9DX-ray1.60B21-119[»]
4G9FX-ray1.90B21-119[»]
4GKNX-ray2.75B/E21-119[»]
4GKSX-ray2.35B/E21-119[»]
4GUPX-ray3.20B/D21-119[»]
4HKJX-ray3.00B/F/J/N21-119[»]
4HWZX-ray2.40B21-119[»]
4HX1X-ray1.80B21-119[»]
4I48X-ray2.80B21-119[»]
4I4WX-ray1.77B21-119[»]
4JFDX-ray2.46B21-119[»]
4JFEX-ray2.70B21-119[»]
4JFFX-ray2.43B21-119[»]
4JFOX-ray2.11B/E21-119[»]
4JFPX-ray1.91B/E21-119[»]
4JFQX-ray1.90B/E21-119[»]
4JQVX-ray1.50C21-119[»]
4JQXX-ray1.90C21-119[»]
4JRXX-ray2.30B21-119[»]
4JRYX-ray2.80B21-119[»]
4K71X-ray2.40C/F21-119[»]
4K7FX-ray2.00B/E21-119[»]
4KDTX-ray2.60C/D21-119[»]
4L29X-ray3.09B/D/F/H/J/L/N/P/R/T/V/X/Z/b21-119[»]
4L3CX-ray2.64B/D/F/H/J/L/N/P/R/T/V/X/Z/b21-119[»]
4L4TX-ray2.00B/F21-119[»]
4L4VX-ray1.90B/F21-119[»]
4LCWX-ray2.40B/F21-119[»]
4LHUX-ray2.87B21-119[»]
4MNQX-ray2.74B21-119[»]
4N0FX-ray3.02B/F/I/L21-119[»]
4N0UX-ray3.80B21-119[»]
4N8VX-ray2.50B/E21-119[»]
4NQVX-ray2.39B/D/F/H/J/L21-119[»]
4NQXX-ray2.00B/D/F/H/J/L21-119[»]
ProteinModelPortalP61769.
SMRP61769. Positions 21-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107044. 15 interactions.
DIPDIP-6055N.
IntActP61769. 71 interactions.
MINTMINT-85778.
STRING9606.ENSP00000340858.

PTM databases

PhosphoSiteP61769.

Polymorphism databases

DMDM48428791.

2D gel databases

DOSAC-COBS-2DPAGEP61769.
OGPP61769.
SWISS-2DPAGEP61769.

Proteomic databases

PaxDbP61769.
PeptideAtlasP61769.
PRIDEP61769.

Protocols and materials databases

DNASU567.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000558401; ENSP00000452780; ENSG00000166710.
ENST00000559916; ENSP00000453350; ENSG00000166710.
ENST00000561424; ENSP00000453191; ENSG00000166710.
GeneID567.
KEGGhsa:567.
UCSCuc001zuc.3. human.

Organism-specific databases

CTD567.
GeneCardsGC15P045003.
HGNCHGNC:914. B2M.
HPACAB002572.
HPA006361.
MIM109700. gene.
241600. phenotype.
neXtProtNX_P61769.
Orphanet314652. Autosomal dominant beta2-microglobulinic amyloidosis.
PharmGKBPA25207.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40777.
HOVERGENHBG006197.
KOK08055.
OrthoDBEOG7RFTKJ.
PhylomeDBP61769.
TreeFamTF334167.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP61769.
BgeeP61769.
CleanExHS_B2M.
GenevestigatorP61769.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR015707. B2Microglobulin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PANTHERPTHR19944:SF16. PTHR19944:SF16. 1 hit.
PfamPF07654. C1-set. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSB2M. human.
EvolutionaryTraceP61769.
GeneWikiBeta-2_microglobulin.
GenomeRNAi567.
NextBio2313.
PROP61769.
SOURCESearch...

Entry information

Entry nameB2MG_HUMAN
AccessionPrimary (citable) accession number: P61769
Secondary accession number(s): P01884 expand/collapse secondary AC list , Q540F8, Q6IAT8, Q9UCK0, Q9UD48, Q9UDF4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 126 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM