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Protein

Beta-2-microglobulin

Gene

B2M

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation (PubMed:25356553).1 Publication

GO - Molecular functioni

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • antigen processing and presentation of endogenous peptide antigen via MHC class I Source: BHF-UCL
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
  • antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent Source: Ensembl
  • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  • antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • cellular response to iron(III) ion Source: Ensembl
  • cellular response to iron ion Source: BHF-UCL
  • cellular response to lipopolysaccharide Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • ferric iron import Source: Ensembl
  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • iron ion homeostasis Source: BHF-UCL
  • negative regulation of neuron projection development Source: Ensembl
  • negative regulation of receptor binding Source: BHF-UCL
  • neutrophil degranulation Source: Reactome
  • positive regulation of ferrous iron binding Source: BHF-UCL
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of receptor binding Source: BHF-UCL
  • positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  • positive regulation of T cell cytokine production Source: BHF-UCL
  • positive regulation of T cell mediated cytotoxicity Source: Ensembl
  • positive regulation of transferrin receptor binding Source: BHF-UCL
  • protein refolding Source: Ensembl
  • regulation of defense response to virus by virus Source: Reactome
  • regulation of erythrocyte differentiation Source: Ensembl
  • regulation of immune response Source: Reactome
  • regulation of iron ion import Source: BHF-UCL
  • regulation of membrane depolarization Source: UniProtKB
  • response to cadmium ion Source: Ensembl
  • response to drug Source: Ensembl
  • response to molecule of bacterial origin Source: Ensembl
  • retina homeostasis Source: UniProtKB
  • T cell differentiation in thymus Source: Ensembl

Keywordsi

Biological processImmunity

Enzyme and pathway databases

ReactomeiR-HSA-1236974 ER-Phagosome pathway
R-HSA-1236977 Endosomal/Vacuolar pathway
R-HSA-164940 Nef mediated downregulation of MHC class I complex cell surface expression
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-2172127 DAP12 interactions
R-HSA-2424491 DAP12 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-877300 Interferon gamma signaling
R-HSA-977225 Amyloid fiber formation
R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC
SIGNORiP61769

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-2-microglobulin
Cleaved into the following chain:
Gene namesi
Name:B2M
ORF Names:CDABP0092, HDCMA22P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000166710.17
HGNCiHGNC:914 B2M
MIMi109700 gene
neXtProtiNX_P61769

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, MHC I, Secreted

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 43 (IMD43)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by marked reduction in serum concentrations of immunoglobulins and albumin, and hypoproteinemia due to hypercatabolism. Patients may suffer from recurrent respiratory tract infections and severe skin disease.
See also OMIM:241600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03066011A → P in IMD43; lower levels of B2M, MHC class I and FCGRT proteins. 1 PublicationCorresponds to variant dbSNP:rs104894481EnsemblClinVar.1
Amyloidosis 8 (AMYL8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. Apart from the presence of causative mutations, beta-2-microglobulin may adopt the fibrillar configuration of amyloid when its serum levels are persistently high. High beta(2)-microglobulin serum levels result in amyloidosis in patients on long-term hemodialysis (PubMed:7918443). In contrast to patients with dialysis-related amyloidosis, patients with hereditary amyloidosis have normal circulating concentrations of beta2-microglobulin (PubMed:22693999).2 Publications
Disease descriptionA form of hereditary generalized amyloidosis. Clinical features include extensive visceral amyloid deposits, renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. There is no involvement of the nervous system.
See also OMIM:105200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07669196D → N in AMYL8; reduced stability; in contrast to the wild-type, the mutant aggregates into fibrils with classic amyloid-like properties under physiologic solvent conditions. 1 PublicationCorresponds to variant dbSNP:rs398122820EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi79D → P: Increases tendency towards amyloid formation. 1 Publication1
Mutagenesisi80W → G: Decreases tendency towards amyloid formation. 2 Publications1
Mutagenesisi80W → V: Increases tendency towards amyloid formation. 2 Publications1

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNETi567
MalaCardsiB2M
MIMi105200 phenotype
241600 phenotype
OpenTargetsiENSG00000166710
Orphaneti314652 Autosomal dominant beta2-microglobulinic amyloidosis
PharmGKBiPA25207

Chemistry databases

DrugBankiDB02740 3-Indolebutyric Acid
DB00254 Doxycycline
DB04464 N-Formylmethionine

Polymorphism and mutation databases

BioMutaiB2M
DMDMi48428791

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 205 PublicationsAdd BLAST20
ChainiPRO_000001877921 – 119Beta-2-microglobulinAdd BLAST99
ChainiPRO_000001878022 – 119Beta-2-microglobulin form pI 5.3Add BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis1 Publication1
Modified residuei22Pyrrolidone carboxylic acid; in form pI 5.31 Publication1
Glycosylationi39N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Disulfide bondi45 ↔ 100PROSITE-ProRule annotation8 Publications
Glycosylationi61N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi68N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi78N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi111N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi114N-linked (Glc) (glycation) lysine; in vitro1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDiP61769
MaxQBiP61769
PaxDbiP61769
PeptideAtlasiP61769
PRIDEiP61769
TopDownProteomicsiP61769

2D gel databases

DOSAC-COBS-2DPAGEiP61769
OGPiP61769
SWISS-2DPAGEiP61769

PTM databases

iPTMnetiP61769
PhosphoSitePlusiP61769

Expressioni

Gene expression databases

BgeeiENSG00000166710
CleanExiHS_B2M
ExpressionAtlasiP61769 baseline and differential
GenevisibleiP61769 HS

Organism-specific databases

HPAiCAB002572
HPA006361

Interactioni

Subunit structurei

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. B2M alone (not in complex with HLA-I) interacts with M.tuberculosis EsxA (ESAT-6) and an EsxA-EsxB (CFP-10) complex; the tripartite complex can be detected in the host endoplasmic reticulum (PubMed:25356553). The B2M-EsxA complex can be detected in patients with pleural tuberculosis and is stable from pH 4.0 to 8.0 and in the presence of 2M NaCl (PubMed:25356553).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107044, 43 interactors
DIPiDIP-6055N
IntActiP61769, 102 interactors
MINTiP61769
STRINGi9606.ENSP00000452780

Chemistry databases

BindingDBiP61769

Structurei

Secondary structure

1119
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 33Combined sources8
Helixi35 – 37Combined sources3
Beta strandi41 – 53Combined sources13
Beta strandi56 – 61Combined sources6
Beta strandi64 – 66Combined sources3
Beta strandi71 – 78Combined sources8
Beta strandi79 – 82Combined sources4
Beta strandi83 – 88Combined sources6
Turni93 – 95Combined sources3
Beta strandi98 – 103Combined sources6
Beta strandi107 – 109Combined sources3
Beta strandi111 – 114Combined sources4
Helixi117 – 119Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/E20-119[»]
1QRNX-ray2.80B21-119[»]
1QSEX-ray2.80B20-119[»]
1QSFX-ray2.80B20-119[»]
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[»]
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6AVFX-ray2.03M21-119[»]
6AVGX-ray2.60A/H13-119[»]
6BXPX-ray1.45B21-119[»]
6BXQX-ray1.58C21-119[»]
6C09X-ray2.95B21-119[»]
6C15X-ray3.21B21-119[»]
6EI2X-ray1.61B21-119[»]
6ENYelectron microscopy5.80B21-119[»]
ProteinModelPortaliP61769
SMRiP61769
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61769

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 113Ig-like C1-typeAdd BLAST89

Sequence similaritiesi

Belongs to the beta-2-microglobulin family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiENOG410J15A Eukaryota
ENOG410YTDG LUCA
GeneTreeiENSGT00690000102227
HOVERGENiHBG006197
InParanoidiP61769
KOiK08055
OMAiPNFLNCY
OrthoDBiEOG091G0ZOW
PhylomeDBiP61769
TreeFamiTF334167

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR015707 B2Microglobulin
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003006 Ig/MHC_CS
IPR003597 Ig_C1-set
PANTHERiPTHR19944:SF62 PTHR19944:SF62, 1 hit
PfamiView protein in Pfam
PF07654 C1-set, 1 hit
SMARTiView protein in SMART
SM00407 IGc1, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00290 IG_MHC, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSVALAVL ALLSLSGLEA IQRTPKIQVY SRHPAENGKS NFLNCYVSGF
60 70 80 90 100
HPSDIEVDLL KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC
110
RVNHVTLSQP KIVKWDRDM
Length:119
Mass (Da):13,715
Last modified:July 21, 1986 - v1
Checksum:iAFD2DBEF07DCEF27
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20A → G in AAA51811 (PubMed:3312414).Curated1
Sequence conflicti52P → Q in AAA51811 (PubMed:3312414).Curated1
Sequence conflicti119M → I in CAG33347 (Ref. 7) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03066011A → P in IMD43; lower levels of B2M, MHC class I and FCGRT proteins. 1 PublicationCorresponds to variant dbSNP:rs104894481EnsemblClinVar.1
Natural variantiVAR_07669196D → N in AMYL8; reduced stability; in contrast to the wild-type, the mutant aggregates into fibrils with classic amyloid-like properties under physiologic solvent conditions. 1 PublicationCorresponds to variant dbSNP:rs398122820EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS10113.1
PIRiA90976 MGHUB2
RefSeqiNP_004039.1, NM_004048.2
UniGeneiHs.534255

Genome annotation databases

EnsembliENST00000558401; ENSP00000452780; ENSG00000166710
ENST00000559916; ENSP00000453350; ENSG00000166710
ENST00000561424; ENSP00000453191; ENSG00000166710
ENST00000617605; ENSP00000481426; ENSG00000273686
ENST00000631573; ENSP00000488548; ENSG00000273686
ENST00000631728; ENSP00000488321; ENSG00000273686
GeneIDi567
KEGGihsa:567
UCSCiuc001zuc.4 human

Similar proteinsi