B2MG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: B2MG_HUMAN
• UniProt AC: P61769
• Protein Name: Beta-2-microglobulin
• Gene Name: B2M
• Organism: Homo sapiens (Human).
• Sequence Length: 119
• Subcellular Localization: Secreted . Cell surface . Detected in serum and urine (PubMed:1336137, PubMed:7554280).; (Microbial infection) In the presence of M.tuberculosis EsxA-EsxB complex decreased amounts of B2M are found on the cell surface (PubMed:25356553).
• Protein Description: 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]
• Protein Sequence: MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MSRSVALAVLA ----CCHHHHHHHHH	12.39	-
14	Phosphorylation	LAVLALLSLSGLEAI HHHHHHHHHCCHHHH	22.72	-
21	N-linked_Glycosylation	SLSGLEAIQRTPKIQ HHCCHHHHHCCCCEE	1.76	7918443
22	Pyrrolidone_carboxylic_acid	LSGLEAIQRTPKIQV HCCHHHHHCCCCEEE	50.68	7554280
22	Pyrrolidone_carboxylic_acid	LSGLEAIQRTPKIQV HCCHHHHHCCCCEEE	50.68	7554280
22	Pyrrolidone_carboxylic_acid	LSGLEAIQRTPKIQV HCCHHHHHCCCCEEE	50.68	-
24	Phosphorylation	GLEAIQRTPKIQVYS CHHHHHCCCCEEEEE	16.74	-
26	Ubiquitination	EAIQRTPKIQVYSRH HHHHCCCCEEEEECC	45.20	25015289
26	Glycation	EAIQRTPKIQVYSRH HHHHCCCCEEEEECC	45.20	-
30	Phosphorylation	RTPKIQVYSRHPAEN CCCCEEEEECCCCCC	5.43	-
31	Phosphorylation	TPKIQVYSRHPAENG CCCEEEEECCCCCCC	25.84	-
39	Ubiquitination	RHPAENGKSNFLNCY CCCCCCCCCCEEEEE	54.53	21963094
39	N-linked_Glycosylation	RHPAENGKSNFLNCY CCCCCCCCCCEEEEE	54.53	7918443
39	Glycation	RHPAENGKSNFLNCY CCCCCCCCCCEEEEE	54.53	-
45	S-palmitoylation	GKSNFLNCYVSGFHP CCCCEEEEEECCCCH	3.74	29575903
45	S-nitrosylation	GKSNFLNCYVSGFHP CCCCEEEEEECCCCH	3.74	25040305
48	O-linked_Glycosylation	NFLNCYVSGFHPSDI CEEEEEECCCCHHHC	14.85	OGP
61	N-linked_Glycosylation	DIEVDLLKNGERIEK HCEEEEECCCCEEEE	70.92	7918443
61	Ubiquitination	DIEVDLLKNGERIEK HCEEEEECCCCEEEE	70.92	21963094
61	Glycation	DIEVDLLKNGERIEK HCEEEEECCCCEEEE	70.92	-
61	Acetylation	DIEVDLLKNGERIEK HCEEEEECCCCEEEE	70.92	25038526
68	Ubiquitination	KNGERIEKVEHSDLS CCCCEEEEEECCCCC	51.02	29967540
68	Glycation	KNGERIEKVEHSDLS CCCCEEEEEECCCCC	51.02	-
68	2-Hydroxyisobutyrylation	KNGERIEKVEHSDLS CCCCEEEEEECCCCC	51.02	-
68	N-linked_Glycosylation	KNGERIEKVEHSDLS CCCCEEEEEECCCCC	51.02	7918443
68	Acetylation	KNGERIEKVEHSDLS CCCCEEEEEECCCCC	51.02	26051181
72	Phosphorylation	RIEKVEHSDLSFSKD EEEEEECCCCCCCCC	27.09	23911959
75	Phosphorylation	KVEHSDLSFSKDWSF EEECCCCCCCCCCEE	32.25	25159151
77	Phosphorylation	EHSDLSFSKDWSFYL ECCCCCCCCCCEEEE	26.74	23911959
78	N-linked_Glycosylation	HSDLSFSKDWSFYLL CCCCCCCCCCEEEEE	62.29	7918443
78	Glycation	HSDLSFSKDWSFYLL CCCCCCCCCCEEEEE	62.29	-
78	Methylation	HSDLSFSKDWSFYLL CCCCCCCCCCEEEEE	62.29	-
88	O-linked_Glycosylation	SFYLLYYTEFTPTEK EEEEEEEEECCCCCC	15.86	OGP
106	Phosphorylation	ACRVNHVTLSQPKIV EEEECEEEECCCEEE	17.09	28270605
106	O-linked_Glycosylation	ACRVNHVTLSQPKIV EEEECEEEECCCEEE	17.09	55825743
108	Phosphorylation	RVNHVTLSQPKIVKW EECEEEECCCEEEEC	34.76	23911959
111	Glycation	HVTLSQPKIVKWDRD EEEECCCEEEECCCC	53.12	-
111	Ubiquitination	HVTLSQPKIVKWDRD EEEECCCEEEECCCC	53.12	29967540
111	N-linked_Glycosylation	HVTLSQPKIVKWDRD EEEECCCEEEECCCC	53.12	7918443
114	N-linked_Glycosylation	LSQPKIVKWDRDM-- ECCCEEEECCCCC--	47.02	7918443
114	Ubiquitination	LSQPKIVKWDRDM-- ECCCEEEECCCCC--	47.02	-
114	Glycation	LSQPKIVKWDRDM-- ECCCEEEECCCCC--	47.02	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of B2MG_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of B2MG_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of B2MG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAG6_HUMAN	BAG6	physical	16169070
A2MG_HUMAN	A2M	physical	10731476
TAP1_HUMAN	TAP1	physical	17055437
TPSN_HUMAN	TAPBP	physical	17055437
B2MG_HUMAN	B2M	physical	18543331
HFE_HUMAN	HFE	physical	20618438
B2MG_HUMAN	B2M	physical	23645685
CRYAB_HUMAN	CRYAB	physical	23645685
RGPD2_HUMAN	RGPD2	physical	28514442
FCGRN_HUMAN	FCGRT	physical	28514442
RGPD5_HUMAN	RGPD5	physical	28514442
DLGP5_HUMAN	DLGAP5	physical	28514442
TPST1_HUMAN	TPST1	physical	28514442
RBP2_HUMAN	RANBP2	physical	28514442
RAGP1_HUMAN	RANGAP1	physical	28514442
IMA3_HUMAN	KPNA4	physical	28514442
CDCA2_HUMAN	CDCA2	physical	28514442
UBC9_HUMAN	UBE2I	physical	28514442
NUSAP_HUMAN	NUSAP1	physical	28514442
IMB1_HUMAN	KPNB1	physical	28514442
NEMP1_HUMAN	TMEM194A	physical	28514442
PUR1_HUMAN	PPAT	physical	28514442
MOG1_HUMAN	RANGRF	physical	28514442
IMA4_HUMAN	KPNA3	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 241600: Hypercatabolic hypoproteinemia (HYCATHYP)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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.
PubMed: 7918443