BT1A1_HUMAN - dbPTM
BT1A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BT1A1_HUMAN
UniProt AC Q13410
Protein Name Butyrophilin subfamily 1 member A1
Gene Name BTN1A1
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization Membrane
Single-pass type I membrane protein. Secreted.
Protein Description May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity)..
Protein Sequence MAVFPSSGLPRCLLTLILLQLPKLDSAPFDVIGPPEPILAVVGEDAELPCRLSPNASAEHLELRWFRKKVSPAVLVHRDGREQEAEQMPEYRGRATLVQDGIAKGRVALRIRGVRVSDDGEYTCFFREDGSYEEALVHLKVAALGSDPHISMQVQENGEICLECTSVGWYPEPQVQWRTSKGEKFPSTSESRNPDEEGLFTVAASVIIRDTSAKNVSCYIQNLLLGQEKKVEISIPASSLPRLTPWIVAVAVILMVLGLLTIGSIFFTWRLYNERPRERRNEFSSKERLLEELKWKKATLHAVDVTLDPDTAHPHLFLYEDSKSVRLEDSRQKLPEKTERFDSWPCVLGRETFTSGRHYWEVEVGDRTDWAIGVCRENVMKKGFDPMTPENGFWAVELYGNGYWALTPLRTPLPLAGPPRRVGIFLDYESGDISFYNMNDGSDIYTFSNVTFSGPLRPFFCLWSSGKKPLTICPIADGPERVTVIANAQDLSKEIPLSPMGEDSAPRDADTLHSKLIPTQPSQGAP
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
6Phosphorylation--MAVFPSSGLPRCL
--CCCCCCCCHHHHH
26.1023403867
7Phosphorylation-MAVFPSSGLPRCLL
-CCCCCCCCHHHHHH
44.5823403867
55N-linked_GlycosylationLPCRLSPNASAEHLE
CCCCCCCCCCHHHEE
43.0518780401
55N-linked_GlycosylationLPCRLSPNASAEHLE
CCCCCCCCCCHHHEE
43.0518780401
71PhosphorylationRWFRKKVSPAVLVHR
HHHHHCCCCEEEECC
18.93-
215N-linked_GlycosylationIRDTSAKNVSCYIQN
EECCCCCCCEEEEEH
30.5618780401
215N-linked_GlycosylationIRDTSAKNVSCYIQN
EECCCCCCCEEEEEH
30.5618780401
238PhosphorylationVEISIPASSLPRLTP
EEEEEEHHHCCCCHH
27.3629262532
239PhosphorylationEISIPASSLPRLTPW
EEEEEHHHCCCCHHH
44.4924719451
498PhosphorylationLSKEIPLSPMGEDSA
HHCCCCCCCCCCCCC
13.9030576142

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 BT1A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BT1A1_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 BT1A1_HUMAN !!

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

Oops, there are no PPI records of BT1A1_HUMAN !!

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 BT1A1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55 AND ASN-215, AND MASSSPECTROMETRY.

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