Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Beta-2-microglobulin  

UniProtKB / Swiss-Prot ID :  B2MG_HUMAN

Gene Name (Synonyms) : 
B2M CDABP0092, HDCMA22P  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. Note=Detected in serum and urine. 

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

Protein Sequence MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVE...
Predicted Secondary Structure CCCHHHEEEEEEEEECCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEEEECCCCEEEEEECCEECCCEE...
Protein Variant
LocationDescription
11A -> P (in HYCATHYP; lower levels of B2M,MHC class I and FCGRT proteins).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
21N-linked (Glc) (glycation); inGLEAIQRTP
CCCCCCCCC
1.76UniProtKB
Link
22Pyrrolidone carboxylic acid; in form pI5.3.LEAIQRTPK
CCCCCCCCC
50.68UniProtKB
Link
39N-linked (Glc) (glycation); in vitro.AENGKSNFL
CCCCCCEEE
54.53UniProtKB
Link
61N-linked (Glc) (glycation); in vitro.VDLLKNGER
EEEEECCEE
70.92UniProtKB
Link
68N-linked (Glc) (glycation); in vitro.ERIEKVEHS
EECCCEEEC
51.02UniProtKB
Link
78N-linked (Glc) (glycation); in vitro.LSFSKDWSF
CEECCCCCE
62.29UniProtKB
Link
111N-linked (Glc) (glycation); in vitro.LSQPKIVKW
CCCCEEEEE
53.12UniProtKB
Link
114N-linked (Glc) (glycation); in vitro.PKIVKWDRD
CEEEEEECC
47.02UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PRS23_HUMANphysical interactionMINT-63248MINT16169070
1B51_HUMANphysical interactionMINT-24943MINT10975842
CD1B_HUMANphysical interactionMINT-24761MINT12118248
1B08_HUMANphysical interactionMINT-24861MINTmissing_pmid
1B53_HUMANphysical interactionMINT-24786MINT8624812
1B35_HUMANphysical interactionMINT-24887MINT8624811
BAT3_HUMANphysical interactionMINT-63948MINT16169070
1A02_HUMANphysical interactionDIP:10967EDIP8906788
O19691_HUMANphysical interactionDIP:10960EDIP8976183
FCGRN_HUMANphysical interactionDIP:11022EDIP10933786
1B27_HUMANphysical interactionDIP:11038EDIP1525820
BAT3_HUMANphysical interactionEBI-731371
intact16169070
HFE_HUMANphysical interactionEBI-1028931
intact10638746
TFR1_HUMANphysical interactionEBI-1028931
intact10638746
CD1B_HUMANdirect interaction
direct interaction
direct interaction
EBI-1033789
EBI-1033800
EBI-1
intact12118248
12118248
14764708
CD1A_HUMANdirect interaction
direct interaction
EBI-1036784
EBI-1041868
intact12833155
15723809
A2MG_HUMANin vitroHPRD:00189HPRD10731476
CALR_HUMANin vivoHPRD:00189HPRD8769474
B2MG_HUMANin vitro
in vivo
HPRD:00189HPRD12023961
CD8A_HUMANin vitroHPRD:00189HPRD11914379
BAT3_HUMANyeast 2-hybridHPRD:00189HPRD16169070
PRS23_HUMANyeast 2-hybridHPRD:00189HPRD16169070
CD4_HUMANENSP00000340858STRING
FCGRN_HUMANENSP00000340858STRING
CD79A_HUMANENSP00000340858STRING
CD79A_HUMANENSP00000340858STRING
IFNG_HUMANENSP00000340858STRING
CALX_HUMANENSP00000340858STRING
CD8A_HUMANENSP00000340858STRING
PDIA3_HUMANENSP00000340858STRING
HFE_HUMANENSP00000340858STRING
CALR_HUMANENSP00000340858STRING
A2MG_HUMANENSP00000340858STRING
1B27_HUMANENSP00000340858STRING
1B58_HUMANENSP00000340858STRING
1B37_HUMANENSP00000340858STRING
1B51_HUMANENSP00000340858STRING
1B57_HUMANENSP00000340858STRING
1B13_HUMANENSP00000340858STRING
1B15_HUMANENSP00000340858STRING
1B18_HUMANENSP00000340858STRING
1B44_HUMANENSP00000340858STRING
1B45_HUMANENSP00000340858STRING
1B47_HUMANENSP00000340858STRING
1B49_HUMANENSP00000340858STRING
1B50_HUMANENSP00000340858STRING
1B52_HUMANENSP00000340858STRING
1B53_HUMANENSP00000340858STRING
1B54_HUMANENSP00000340858STRING
1B55_HUMANENSP00000340858STRING
1B56_HUMANENSP00000340858STRING
1B78_HUMANENSP00000340858STRING
1B35_HUMANENSP00000340858STRING
1B40_HUMANENSP00000340858STRING
1B82_HUMANENSP00000340858STRING
1B59_HUMANENSP00000340858STRING
HLAG_HUMANENSP00000340858STRING
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Disease Reference
Kegg disease
OMIM disease
241600Hypercatabolic hypoproteinemia (HYCATHYP)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycation of human beta 2-microglobulin in patients withhemodialysis-associated amyloidosis: identification of the glycatedsites.";
Miyata T., Inagi R., Wada Y., Ueda Y., Iida Y., Takahashi M.,Taniguchi N., Maeda K.;
Biochemistry 33:12215-12221(1994).
Cited for: INVOLVEMENT IN AMYLOIDOSIS, GLYCATION AT ILE-21; LYS-39; LYS-61;LYS-68; LYS-78; LYS-111 AND LYS-114, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures