BT3A2_HUMAN - dbPTM
BT3A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BT3A2_HUMAN
UniProt AC P78410
Protein Name Butyrophilin subfamily 3 member A2
Gene Name BTN3A2
Organism Homo sapiens (Human).
Sequence Length 334
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Plays a role in T-cell responses in the adaptive immune response. Inhibits the release of IFNG from activated T-cells..
Protein Sequence MKMASSLAFLLLNFHVSLLLVQLLTPCSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSNLHVEVKGYEDGGIHLECRSTGWYPQPQIQWSNAKGENIPAVEAPVVADGVGLYEVAASVIMRGGSGEGVSCIIRNSLLGLEKTASISIADPFFRSAQPWIAALAGTLPILLLLLAGASYFLWRQQKEITALSSEIESEQEMKEMGYAATEREISLRESLQEELKRKKIQYLTRGEESSSDTNKSA
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
70PhosphorylationMELKWVSSSLRQVVN
HHHHHHHHHHHHHHE
24.6325954137
71PhosphorylationELKWVSSSLRQVVNV
HHHHHHHHHHHHHEE
21.7725954137
83UbiquitinationVNVYADGKEVEDRQS
HEEEECCCCCCCCCC
60.162190698
98PhosphorylationAPYRGRTSILRDGIT
CCCCCCCCHHHCCCC
20.4724719451
108UbiquitinationRDGITAGKAALRIHN
HCCCCCCCHHHEEEE
28.20-
112MethylationTAGKAALRIHNVTAS
CCCCHHHEEEEEECC
24.32-
115N-linked_GlycosylationKAALRIHNVTASDSG
CHHHEEEEEECCCCC
30.39UniProtKB CARBOHYD
123UbiquitinationVTASDSGKYLCYFQD
EECCCCCCEEEEEEC
38.71-
231UbiquitinationNSLLGLEKTASISIA
CCCCCCEECEEEEEC
55.20-
278PhosphorylationWRQQKEITALSSEIE
HHHHHHHHHHHHHCC
23.7228060719
281PhosphorylationQKEITALSSEIESEQ
HHHHHHHHHHCCCHH
24.3828060719
282PhosphorylationKEITALSSEIESEQE
HHHHHHHHHCCCHHH
43.3626657352
286PhosphorylationALSSEIESEQEMKEM
HHHHHCCCHHHHHHH
50.6825159151
295PhosphorylationQEMKEMGYAATEREI
HHHHHHCCHHHHHHH
7.5528796482
313UbiquitinationESLQEELKRKKIQYL
HHHHHHHHHHHCHHH
66.50-
316UbiquitinationQEELKRKKIQYLTRG
HHHHHHHHCHHHHCC
38.79-
319PhosphorylationLKRKKIQYLTRGEES
HHHHHCHHHHCCCCC
17.3226074081
321PhosphorylationRKKIQYLTRGEESSS
HHHCHHHHCCCCCCC
31.5226074081
326PhosphorylationYLTRGEESSSDTNKS
HHHCCCCCCCCCCCC
30.7326074081
327PhosphorylationLTRGEESSSDTNKSA
HHCCCCCCCCCCCCC
35.2026074081
328PhosphorylationTRGEESSSDTNKSA-
HCCCCCCCCCCCCC-
58.7026074081

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 BT3A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BT3A2_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 BT3A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BT3A3_HUMANBTN3A3physical
26186194
BT3A1_HUMANBTN3A1physical
26186194
AT5G1_HUMANATP5G1physical
26186194
PEX13_HUMANPEX13physical
26186194
BT3A3_HUMANBTN3A3physical
28514442
BT3A1_HUMANBTN3A1physical
28514442
PEX13_HUMANPEX13physical
28514442
AT5G1_HUMANATP5G1physical
28514442
TM245_HUMANTMEM245physical
28514442

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 BT3A2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-286, ANDMASS SPECTROMETRY.

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