Reviewed, UniProtKB/Swiss-Prot P61769 (B2MG_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-2-microglobulin
Cleaved into the following chain:
    1- Recommended name:
            Beta-2-microglobulin form pI 5.3

Gene names

Name:	B2M
ORF Names:	CDABP0092, HDCMA22P

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	119 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	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. 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	Defects in B2M are the cause of hypercatabolic hypoproteinemia [MIM:241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. Ref.33 Persistent high blood levels of B2M are a cause of hemodialysis-related amyloidosis (HRA) [MIM:109700]. High levels of B2M accumulate in the serum of patients with renal failure, and may lead to amyloid formation. Hemodialysis-related amyloidosis is a form of systemic amyloidosis with a predilection for the synovium and bone that occurs with a disturbingly high frequency among patients on long-term hemodialysis. The clinical features include carpal tunnel syndrome, erosive arthropathy, spondyloarthropathy, lytic bone lesions, and pathologic fractures.
Sequence similarities	Belongs to the beta-2-microglobulin family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Immune response
Cellular component	Amyloid MHC I Secreted
Disease	Amyloidosis Disease mutation
Domain	Immunoglobulin domain Signal
PTM	Disulfide bond Glycation Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	antigen processing and presentation of peptide antigen via MHC class I Inferred from electronic annotation. Source: UniProtKB-KW immune response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi membrane Inferred from Experiment. Source: Reactome MHC class I protein complex Inferred from electronic annotation. Source: UniProtKB-KW early endosome membrane Inferred from Experiment. Source: Reactome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CD1B	P29016	2	EBI-714718,EBI-1033762

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.14 Ref.16 Ref.13 Ref.15

Chain

21 – 119

99

Beta-2-microglobulin

PRO_0000018779

Chain

22 – 119

98

Beta-2-microglobulin form pI 5.3

PRO_0000018780

Regions

Domain

25 – 113

89

Ig-like C1-type

Amino acid modifications

Modified residue

22

1

Pyrrolidone carboxylic acid; in form pI 5.3

Glycosylation

21

1

N-linked (Glc) (glycation); in hemodialysis-associated amyloidosis

Glycosylation

39

1

N-linked (Glc) (glycation); in vitro

Glycosylation

61

1

N-linked (Glc) (glycation); in vitro

Glycosylation

68

1

N-linked (Glc) (glycation); in vitro

Glycosylation

78

1

N-linked (Glc) (glycation); in vitro

Glycosylation

111

1

N-linked (Glc) (glycation); in vitro

Glycosylation

114

1

N-linked (Glc) (glycation); in vitro

Disulfide bond

45 ↔ 100

Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Natural variations

Natural variant

11

1

A → P in hypercatabolic hypoproteinemia; lower levels of B2M, MHC class I and FCGRT proteins. Ref.33

VAR_030660

Experimental info

Mutagenesis

79

1

D → P: Increases tendency towards amyloid formation. Ref.30

Mutagenesis

80

1

W → G: Decreases tendency towards amyloid formation. Ref.31 Ref.32

Mutagenesis

80

1

W → V: Increases tendency towards amyloid formation. Ref.31 Ref.32

Sequence conflict

20

1

A → G in AAA51811. Ref.1

Sequence conflict

52

1

P → Q in AAA51811. Ref.1

Sequence conflict

119

1

M → I in CAG33347. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

119

Helix Strand Turn

Details...

Beta strand

26 – 33

8

Beta strand

41 – 53

13

Beta strand

56 – 61

6

Beta strand

82 – 90

9

Beta strand

98 – 103

6

Beta strand

111 – 114

4

Sequences

	Sequence		Length	Mass (Da)
	P61769-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: AFD2DBEF07DCEF27	FASTA	119	13,715
	10 20 30 40 50 60 MSRSVALAVL ALLSLSGLEA IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL 70 80 90 100 110 KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC RVNHVTLSQP KIVKWDRDM

References

	« Hide 'large scale' referencesShow '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: 3312414] [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: 16108498] [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. , 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: 14702039] [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. , 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: 15489334] [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: 11894933] [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: 6171820] [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: 4586824] [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: 3532124] [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: 8084451] [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: 1336137] [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: 7554280] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-119, SUBCELLULAR LOCATION. 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: 7918443] [Abstract] Cited for: INVOLVEMENT IN AMYLOIDOSIS, GLYCATION AT ILE-21; LYS-39; LYS-61; LYS-68; LYS-78; LYS-111 AND LYS-114, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 3309677] [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: 2038058] [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: 1390678] [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: 7862664] [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: 8624812] [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: 12119416] [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: 12796775] [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: 16901902] [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: 16491088] [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: 17646174] [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: 18835253] [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: 18395224] [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: 19284997] [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: 16549777] [Abstract] Cited for: VARIANT HYPERCATABOLIC HYPOPROTEINEMIA PRO-11, CHARACTERIZATION OF VARIANT HYPERCATABOLIC HYPOPROTEINEMIA PRO-11.
+	Additional computationally mapped references.

Web resources

Wikipedia

Beta-2-microglobulin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00004656.

PIR

MGHUB2. A90976.

RefSeq

NP_004039.1.

UniGene

Hs.534255

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A1M	X-ray	2.30	B	21-119	[»]
1A1N	X-ray	2.00	B	21-119	[»]
1A1O	X-ray	2.30	B	21-119	[»]
1A6Z	X-ray	2.60	B/D	21-119	[»]
1A9B	X-ray	3.20	B/E	21-119	[»]
1A9E	X-ray	2.50	B	21-119	[»]
1AGB	X-ray	2.20	B	21-119	[»]
1AGC	X-ray	2.10	B	21-119	[»]
1AGD	X-ray	2.05	B	21-119	[»]
1AGE	X-ray	2.30	B	21-119	[»]
1AGF	X-ray	2.20	B	21-119	[»]
1AKJ	X-ray	2.65	B	21-119	[»]
1AO7	X-ray	2.60	B	21-119	[»]
1B0G	X-ray	2.50	B/E	21-119	[»]
1B0R	X-ray	2.90	B	21-119	[»]
1BD2	X-ray	2.50	B	21-119	[»]
1C16	X-ray	3.10	B/D/F/H	21-119	[»]
1CE6	X-ray	2.90	B	21-119	[»]
1CG9	X-ray	2.70	B	21-119	[»]
1DE4	X-ray	2.80	B/E/H	21-119	[»]
1DUY	X-ray	2.15	B/E	21-119	[»]
1DUZ	X-ray	1.80	B/E	21-119	[»]
1E27	X-ray	2.20	B	21-119	[»]
1E28	X-ray	3.00	B	21-119	[»]
1EEY	X-ray	2.25	B/E	21-119	[»]
1EEZ	X-ray	2.30	B/E	21-119	[»]
1EFX	X-ray	3.00	B	21-119	[»]
1EXU	X-ray	2.70	B	21-119	[»]
1GZP	X-ray	2.80	B	21-119	[»]
1GZQ	X-ray	2.26	B	21-119	[»]
1HHG	X-ray	2.60	B/E	21-119	[»]
1HHH	X-ray	3.00	B	21-119	[»]
1HHI	X-ray	2.50	B/E	21-119	[»]
1HHJ	X-ray	2.50	B/E	21-119	[»]
1HHK	X-ray	2.50	B/E	21-119	[»]
1HLA	X-ray	3.50	M	21-117	[»]
1HSA	X-ray	2.10	B/E	21-119	[»]
1HSB	X-ray	1.90	B	21-119	[»]
1I1F	X-ray	2.80	B/E	21-119	[»]
1I1Y	X-ray	2.20	B/E	21-119	[»]
1I4F	X-ray	1.40	B	21-119	[»]
1I7R	X-ray	2.20	B/E	21-119	[»]
1I7T	X-ray	2.80	B/E	21-119	[»]
1I7U	X-ray	1.80	B/E	21-119	[»]
1IM3	X-ray	2.20	B/F/J/N	21-119	[»]
1IM9	X-ray	2.80	B/F	21-119	[»]
1JF1	X-ray	1.85	B	21-119	[»]
1JGD	X-ray	1.90	B	21-119	[»]
1JGE	X-ray	2.10	B	21-119	[»]
1JHT	X-ray	2.15	B	21-119	[»]
1JNJ	NMR	-	A	21-119	[»]
1K5N	X-ray	1.09	B	21-119	[»]
1KPR	X-ray	2.80	B/D	21-119	[»]
1KTL	X-ray	3.10	B/D	21-119	[»]
1LDS	X-ray	1.80	A	21-119	[»]
1LP9	X-ray	2.00	B/I	21-119	[»]
1M05	X-ray	1.90	B/D	21-119	[»]
1M6O	X-ray	1.60	B	21-119	[»]
1MHE	X-ray	2.85	B/D	21-119	[»]
1MI5	X-ray	2.50	B	21-119	[»]
1N2R	X-ray	1.70	B	21-119	[»]
1OF2	X-ray	2.20	B	21-119	[»]
1OGA	X-ray	1.40	B	21-119	[»]
1OGT	X-ray	1.47	B	21-119	[»]
1ONQ	X-ray	2.15	B/D	21-119	[»]
1P7Q	X-ray	3.40	B	21-119	[»]
1PY4	X-ray	2.90	A/B/C/D	21-119	[»]
1Q94	X-ray	2.40	B/E	21-119	[»]
1QEW	X-ray	2.20	B	21-119	[»]
1QLF	X-ray	2.65	B	21-119	[»]
1QQD	X-ray	2.70	B	21-118	[»]
1QR1	X-ray	2.40	B/E	21-119	[»]
1QRN	X-ray	2.80	B	21-119	[»]
1QSE	X-ray	2.80	B	21-119	[»]
1QSF	X-ray	2.80	B	21-119	[»]
1QVO	X-ray	2.22	B/E	21-119	[»]
1R3H	X-ray	2.50	B/D/F/H	21-119	[»]
1S8D	X-ray	2.20	B	21-119	[»]
1S9W	X-ray	2.20	B	21-119	[»]
1S9X	X-ray	2.50	B	21-119	[»]
1S9Y	X-ray	2.30	B	21-119	[»]
1SYS	X-ray	2.40	B	21-119	[»]
1SYV	X-ray	1.70	B	21-119	[»]
1T1W	X-ray	2.20	B	21-119	[»]
1T1X	X-ray	2.20	B	21-119	[»]
1T1Y	X-ray	2.00	B	21-119	[»]
1T1Z	X-ray	1.90	B	21-119	[»]
1T20	X-ray	2.20	B	21-119	[»]
1T21	X-ray	2.19	B	21-119	[»]
1T22	X-ray	2.20	B	21-119	[»]
1TMC	X-ray	2.30	B	21-119	[»]
1TVB	X-ray	1.80	B/E	21-119	[»]
1TVH	X-ray	1.80	B/E	21-119	[»]
1UQS	X-ray	3.10	B	21-119	[»]
1UR7	model	-	B	21-119	[»]
1UXS	X-ray	1.55	B	21-119	[»]
1UXW	X-ray	1.71	B	21-119	[»]
1VGK	X-ray	2.06	B	21-119	[»]
1W0V	X-ray	2.27	B	21-119	[»]
1W0W	X-ray	2.10	B	21-119	[»]
1W72	X-ray	2.15	B/E	21-119	[»]
1X7Q	X-ray	1.45	B	21-119	[»]
1XH3	X-ray	1.48	B	21-119	[»]
1XR8	X-ray	2.30	B	21-119	[»]
1XR9	X-ray	1.79	B	21-119	[»]
1XZ0	X-ray	2.80	B/D	21-119	[»]
1YDP	X-ray	1.90	B	21-119	[»]
1YPZ	X-ray	3.40	B/D	21-119	[»]
1ZHK	X-ray	1.60	B	21-119	[»]
1ZHL	X-ray	1.50	B	21-119	[»]
1ZS8	X-ray	3.00	B/D/F/H/J	21-119	[»]
1ZSD	X-ray	1.70	B	21-119	[»]
1ZT4	X-ray	3.00	B/D	21-119	[»]
1ZVS	X-ray	2.80	B/E	21-119	[»]
2A83	X-ray	1.40	B	21-119	[»]
2AK4	X-ray	2.50	B/G/L/R	21-119	[»]
2AV1	X-ray	1.95	B/E	21-119	[»]
2AV7	X-ray	2.05	B/E	21-119	[»]
2AXF	X-ray	1.80	B	21-119	[»]
2AXG	X-ray	2.00	B	21-119	[»]
2BCK	X-ray	2.80	B/E	21-119	[»]
2BNQ	X-ray	1.70	B	21-119	[»]
2BNR	X-ray	1.90	B	21-119	[»]
2BSR	X-ray	2.30	B	21-119	[»]
2BSS	X-ray	2.00	B	21-119	[»]
2BST	X-ray	2.10	B	21-119	[»]
2BVO	X-ray	1.65	B	21-119	[»]
2BVP	X-ray	1.35	B	21-119	[»]
2BVQ	X-ray	2.00	B	21-119	[»]
2C7U	X-ray	2.38	B/E	21-119	[»]
2CII	X-ray	2.55	B	21-119	[»]
2CIK	X-ray	1.75	B	21-119	[»]
2CLR	X-ray	2.00	B/E	21-119	[»]
2D31	X-ray	3.20	B/E	21-119	[»]
2D4D	X-ray	2.10	A	21-119	[»]
2D4F	X-ray	1.70	A	21-119	[»]
2DYP	X-ray	2.50	B	21-119	[»]
2E8D	NMR	-	A/B/C/D	40-61	[»]
2ESV	X-ray	2.60	B	21-119	[»]
2F53	X-ray	2.10	B	21-119	[»]
2F54	X-ray	2.70	B/G	21-119	[»]
2F74	X-ray	2.70	B/E	21-119	[»]
2F8O	X-ray	1.70	A/B	21-119	[»]
2FYY	X-ray	1.50	B	21-119	[»]
2FZ3	X-ray	1.90	B	21-119	[»]
2GIT	X-ray	1.70	B/E	21-119	[»]
2GJ6	X-ray	2.56	B	21-119	[»]
2GT9	X-ray	1.75	B/E	21-119	[»]
2GTW	X-ray	1.55	B/E	21-119	[»]
2GTZ	X-ray	1.70	B/E	21-119	[»]
2GUO	X-ray	1.90	B/E	21-119	[»]
2H26	X-ray	1.80	B	21-119	[»]
2H6P	X-ray	1.90	B	21-119	[»]
2HJK	X-ray	1.85	B	21-119	[»]
2HJL	X-ray	1.50	B	21-119	[»]
2HLA	X-ray	2.60	B	21-119	[»]
2HN7	X-ray	1.60	B	21-119	[»]
2J8U	X-ray	2.88	B/I	21-119	[»]
2JCC	X-ray	2.50	B/I	21-119	[»]
2NW3	X-ray	1.70	B	21-119	[»]
2NX5	X-ray	2.70	B/G/L/R	21-119	[»]
2P5E	X-ray	1.89	B	22-119	[»]
2P5W	X-ray	2.20	B	22-119	[»]
2PO6	X-ray	3.20	B/F	21-119	[»]
2PYE	X-ray	2.30	B	21-119	[»]
2RFX	X-ray	2.50	B	21-119	[»]
2UWE	X-ray	2.40	B/I	21-119	[»]
2V2W	X-ray	1.60	B/E	21-119	[»]
2V2X	X-ray	1.60	B/E	21-119	[»]
2VB5	NMR	-	A	21-119	[»]
2VLJ	X-ray	2.40	B	21-119	[»]
2VLK	X-ray	2.50	B	21-119	[»]
2VLL	X-ray	1.60	B/E	21-119	[»]
2VLR	X-ray	2.30	B/G	21-119	[»]
2YXF	X-ray	1.13	A	21-119	[»]
2Z9T	X-ray	1.80	A	21-119	[»]
3B3I	X-ray	1.86	B	21-119	[»]
3B6S	X-ray	1.80	B	21-119	[»]
3BGM	X-ray	1.60	B	21-119	[»]
3BH8	X-ray	1.65	B	21-119	[»]
3BH9	X-ray	1.70	B	21-119	[»]
3BHB	X-ray	2.20	B	22-119	[»]
3BO8	X-ray	1.80	B	21-119	[»]
3BP4	X-ray	1.85	B	21-119	[»]
3BP7	X-ray	1.80	B	21-119	[»]
3BVN	X-ray	2.55	B/E	21-119	[»]
3BW9	X-ray	1.75	B	21-119	[»]
3BWA	X-ray	1.30	B	21-119	[»]
3BXN	X-ray	1.86	B	21-119	[»]
3BZE	X-ray	2.50	B/D/F/H	21-119	[»]
3BZF	X-ray	2.50	B/D	23-119	[»]
3C9N	X-ray	1.87	B	21-119	[»]
3CDG	X-ray	3.40	B/D	21-119	[»]
3CII	X-ray	4.41	B/E	21-119	[»]
3CIQ	X-ray	2.90	A/B/C/D/E/F/G/H/I/J/K/L	21-119	[»]
3CZF	X-ray	1.20	B	21-119	[»]
3D18	X-ray	1.74	B	21-119	[»]
3D25	X-ray	1.30	B	22-119	[»]
3D2U	X-ray	2.21	B/F	21-119	[»]
3D39	X-ray	2.81	B	21-119	[»]
3D3V	X-ray	2.80	B	21-119	[»]
3DBX	X-ray	2.00	B	21-119	[»]
3DHJ	X-ray	2.00	A	21-119	[»]
3DHM	X-ray	1.80	A	21-119	[»]
3DTX	X-ray	2.10	B	21-119	[»]
3DX6	X-ray	1.70	B	21-119	[»]
3DX7	X-ray	1.60	B	21-119	[»]
3DX8	X-ray	2.10	B	21-119	[»]
3DXA	X-ray	3.50	B/G/L	21-119	[»]
3EKC	X-ray	1.80	A	21-119	[»]
3FFC	X-ray	2.80	B/G	21-119	[»]
3FQN	X-ray	1.65	B	22-119	[»]
3FQR	X-ray	1.70	B	22-119	[»]
3FQT	X-ray	1.80	B	22-119	[»]
3FQU	X-ray	1.80	B	22-119	[»]
3FQW	X-ray	1.93	B	22-119	[»]
3FQX	X-ray	1.70	B	22-119	[»]
3FT2	X-ray	1.80	B	21-119	[»]
3FT3	X-ray	1.95	B	21-119	[»]
3FT4	X-ray	1.90	B	21-119	[»]
3GIV	X-ray	2.00	B/E	21-119	[»]
3GJF	X-ray	1.90	B/E	21-119	[»]
3GSN	X-ray	2.80	L	21-119	[»]
3GSO	X-ray	1.60	B	21-119	[»]
3GSQ	X-ray	2.12	B	21-119	[»]
3GSR	X-ray	1.95	B	21-119	[»]
3GSU	X-ray	1.80	B	21-119	[»]
3GSV	X-ray	1.90	B	21-119	[»]
3GSW	X-ray	1.81	B	21-119	[»]
3GSX	X-ray	2.10	B	21-119	[»]
3HAE	X-ray	2.90	B/E/K/Q	21-119	[»]
3HCV	X-ray	1.95	B	21-119	[»]
3HG1	X-ray	3.00	B	21-119	[»]
3HLA	X-ray	2.60	B	21-119	[»]
3HUJ	X-ray	2.50	B/D	21-119	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6055N.

IntAct

P61769. 14 interactions.

STRING

P61769.

2-D gel databases

SWISS-2DPAGE

P61769.

DOSAC-COBS-2DPAGE

P61769.

OGP

P61769.

Siena-2DPAGE

P61769.

Proteomic databases

PeptideAtlas

P61769.

PRIDE

P61769.

Genome annotation databases

Ensembl

ENST00000349264; ENSP00000340858; ENSG00000166710; Homo sapiens. [Genome view]
ENST00000396754; ENSP00000379978; ENSG00000166710; Homo sapiens. [Genome view]

GeneID

567.

KEGG

hsa:567.

UCSC

uc001zuc.1. human.

Organism-specific databases

CTD

567.

GeneCards

GC15P042790.

H-InvDB

HIX0012200.

HGNC

HGNC:914. B2M.

HPA

CAB002572.
HPA006361.

MIM

109700. gene.
241600. phenotype.

Orphanet

85446. Amyloidosis beta2-microglobulinic.

PharmGKB

PA25207.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P61769.

Enzyme and pathway databases

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
il12_2pathway. IL12-mediated signaling events.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.

Reactome

REACT_6185. HIV Infection.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P61769.

Bgee

P61769.

CleanEx

HS_B2M.

Genevestigator

P61769.

GermOnline

ENSG00000166710. Homo sapiens.

Family and domain databases

InterPro

IPR015707. B2Microglobulin.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

PANTHER

PTHR19944:SF16. B2Microglobulin. 1 hit.

Pfam

PF07654. C1-set. 1 hit.
[Graphical view]

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

2313.

SOURCE

Search...

Entry information

Entry name

B2MG_HUMAN

Accession

Primary (citable) accession number: P61769
Secondary accession number(s): P01884 , Q540F8, Q6IAT8, Q9UCK0, Q9UD48, Q9UDF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 15, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.