BT3A1_HUMAN - dbPTM
BT3A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BT3A1_HUMAN
UniProt AC O00481
Protein Name Butyrophilin subfamily 3 member A1
Gene Name BTN3A1
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate..
Protein Sequence MKMASFLAFLLLNFRVCLLLLQLLMPHSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAYNEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALTICPA
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
60.16-
83 (in isoform 2)Ubiquitination-60.1621906983
83 (in isoform 1)Ubiquitination-60.1621906983
98PhosphorylationAPYRGRTSILRDGIT
CCCCCCCCHHHCCCC
20.4724719451
108UbiquitinationRDGITAGKAALRIHN
HCCCCCCCHHHEEEE
28.20-
112MethylationTAGKAALRIHNVTAS
CCCCHHHEEEEEECC
24.32-
115N-linked_GlycosylationKAALRIHNVTASDSG
CHHHEEEEEECCCCC
30.3922846996
123UbiquitinationVTASDSGKYLCYFQD
EECCCCCCEEEEEEC
38.71-
155UbiquitinationSDLHVDVKGYKDGGI
CCEEEEECEEECCCE
52.65-
244O-linked_GlycosylationIADPFFRSAQRWIAA
ECCHHHHHHHHHHHH
24.4829351928
255O-linked_GlycosylationWIAALAGTLPVLLLL
HHHHHHCHHHHHHHH
23.4529351928
299UbiquitinationEMAWSTMKQEQSTRV
HHHHHHHHHHHHHHH
51.26-
316PhosphorylationLEELRWRSIQYASRG
HHHHHHHHHHHHHCC
13.69-
327PhosphorylationASRGERHSAYNEWKK
HHCCCCCHHHHHHHH
38.3728857561
334UbiquitinationSAYNEWKKALFKPAD
HHHHHHHHHHCCCCC
51.93-
338UbiquitinationEWKKALFKPADVILD
HHHHHHCCCCCEEEC
39.90-
347UbiquitinationADVILDPKTANPILL
CCEEECCCCCCCEEE
60.99-
392PhosphorylationLGCESFISGRHYWEV
EECCCEECCCCEEEE
27.9724719451
441PhosphorylationGLTDGNKYRTLTEPR
CCCCCCCEECCCCCC
16.90-

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 BT3A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BT3A1_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 BT3A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFF1_HUMANTFF1physical
21982860

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BT3A1_HUMAN

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Related Literatures of Post-Translational Modification

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