BT2A2_HUMAN - dbPTM
BT2A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BT2A2_HUMAN
UniProt AC Q8WVV5
Protein Name Butyrophilin subfamily 2 member A2
Gene Name BTN2A2
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion..
Protein Sequence MEPAAALHFSLPASLLLLLLLLLLSLCALVSAQFTVVGPANPILAMVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQMEEYRGRITFVSKDINRGSVALVIHNVTAQENGIYRCYFQEGRSYDEAILRLVVAGLGSKPLIEIKAQEDGSIWLECISGGWYPEPLTVWRDPYGEVVPALKEVSIADADGLFMVTTAVIIRDKYVRNVSCSVNNTLLGQEKETVIFIPESFMPSASPWMVALAVILTASPWMVSMTVILAVFIIFMAVSICCIKKLQREKKILSGEKKVEQEEKEIAQQLQEELRWRRTFLHAADVVLDPDTAHPELFLSEDRRSVRRGPYRQRVPDNPERFDSQPCVLGWESFASGKHYWEVEVENVMVWTVGVCRHSVERKGEVLLIPQNGFWTLEMFGNQYRALSSPERILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFTVPVRPFFRLGSDDSPIFICPALTGASGVMVPEEGLKLHRVGTHQSL
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 Orthologous
Protein Cluster
50N-linked_GlycosylationILAMVGENTTLRCHL
EEEEECCCCEEEEEC
32.22UniProtKB CARBOHYD
61UbiquitinationRCHLSPEKNAEDMEV
EEECCCCCCHHHCCH
65.91-
83UbiquitinationSPAVFVYKGGRERTE
CCEEEEEECCCCCCH
49.97-
104PhosphorylationRGRITFVSKDINRGS
HCCEEEEECCCCCCC
22.0328674151
105UbiquitinationGRITFVSKDINRGSV
CCEEEEECCCCCCCE
58.2721906983
105 (in isoform 2)Ubiquitination-58.2721906983
105 (in isoform 1)Ubiquitination-58.2721906983
118N-linked_GlycosylationSVALVIHNVTAQENG
CEEEEEEEEEHHHCC
23.01UniProtKB CARBOHYD
151PhosphorylationLVVAGLGSKPLIEIK
HHHCCCCCCCEEEEE
35.8224719451
152 (in isoform 2)Ubiquitination-41.8821906983
152 (in isoform 1)Ubiquitination-41.8821906983
152UbiquitinationVVAGLGSKPLIEIKA
HHCCCCCCCEEEEEE
41.8821906983
166 (in isoform 3)Phosphorylation-6.4425332170
175 (in isoform 3)Phosphorylation-10.8625332170
186PhosphorylationLTVWRDPYGEVVPAL
CEEEECCCCCCCCCC
30.15-
220N-linked_GlycosylationIRDKYVRNVSCSVNN
ECCCCCCCEEEEECC
21.73UniProtKB CARBOHYD
226N-linked_GlycosylationRNVSCSVNNTLLGQE
CCEEEEECCCCCCCC
21.34UniProtKB CARBOHYD
228 (in isoform 3)Phosphorylation-20.3924114839
234 (in isoform 3)Phosphorylation-51.2824114839
294UbiquitinationKKLQREKKILSGEKK
HHHHHHHHHHCCCCH
44.09-
294AcetylationKKLQREKKILSGEKK
HHHHHHHHHHCCCCH
44.0918603609
300AcetylationKKILSGEKKVEQEEK
HHHHCCCCHHHHHHH
66.6918603621
307UbiquitinationKKVEQEEKEIAQQLQ
CHHHHHHHHHHHHHH
54.38-
406UbiquitinationCRHSVERKGEVLLIP
ECCCCCCCCCEEEEC
46.0121906983
406 (in isoform 1)Ubiquitination-46.0121906983
431PhosphorylationGNQYRALSSPERILP
CCEEEECCCHHHHHH
42.7526699800
432PhosphorylationNQYRALSSPERILPL
CEEEECCCHHHHHHC
31.4630576142
440UbiquitinationPERILPLKESLCRVG
HHHHHHCCHHHEEEE
43.23-
466PhosphorylationFYNMRDRSHIYTCPR
EEECCCCCCEEECCC
20.6525072903
469PhosphorylationMRDRSHIYTCPRSAF
CCCCCCEEECCCCCC
9.2525072903
470PhosphorylationRDRSHIYTCPRSAFT
CCCCCEEECCCCCCC
18.5425072903
474PhosphorylationHIYTCPRSAFTVPVR
CEEECCCCCCCCCCC
16.9325072903
477PhosphorylationTCPRSAFTVPVRPFF
ECCCCCCCCCCCCCE
24.5025072903
513UbiquitinationMVPEEGLKLHRVGTH
CCCCCCCEEEECCCC
53.77-
519PhosphorylationLKLHRVGTHQSL---
CEEEECCCCCCC---
17.5530576142
522PhosphorylationHRVGTHQSL------
EECCCCCCC------
28.5728355574

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BT2A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BT2A2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BT2A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FATE1_HUMANFATE1physical
25416956
CREB3_HUMANCREB3physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BT2A2_HUMAN

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Related Literatures of Post-Translational Modification

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