BT3A3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BT3A3_HUMAN
• UniProt AC: O00478
• Protein Name: Butyrophilin subfamily 3 member A3
• Gene Name: BTN3A3
• Organism: Homo sapiens (Human).
• Sequence Length: 584
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Plays a role in T-cell responses in the adaptive immune response..
• Protein Sequence: MKMASSLAFLLLNFHVSLFLVQLLTPCSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELRWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHIEVKGYEDGGIHLECRSTGWYPQPQIKWSDTKGENIPAVEAPVVADGVGLYAVAASVIMRGSSGGGVSCIIRNSLLGLEKTASISIADPFFRSAQPWIAALAGTLPISLLLLAGASYFLWRQQKEKIALSRETEREREMKEMGYAATEQEISLREKLQEELKWRKIQYMARGEKSLAYHEWKMALFKPADVILDPDTANAILLVSEDQRSVQRAEEPRDLPDNPERFEWRYCVLGCENFTSGRHYWEVEVGDRKEWHIGVCSKNVERKKGWVKMTPENGYWTMGLTDGNKYRALTEPRTNLKLPEPPRKVGIFLDYETGEISFYNATDGSHIYTFPHASFSEPLYPVFRILTLEPTALTICPIPKEVESSPDPDLVPDHSLETPLTPGLANESGEPQAEVTSLLLPAHPGAEVSPSATTNQNHKLQARTEALY

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
70	Phosphorylation	MELRWVSSSLRQVVN HHHHHHHHHHHHHHE	24.63	25954137
71	Phosphorylation	ELRWVSSSLRQVVNV HHHHHHHHHHHHHEE	21.77	25954137
83	Ubiquitination	VNVYADGKEVEDRQS HEEEECCCCCCCCCC	60.16	21906983
98	Phosphorylation	APYRGRTSILRDGIT CCCCCCCCHHHCCCC	20.47	24719451
108	Ubiquitination	RDGITAGKAALRIHN HCCCCCCCHHHEEEE	28.20	-
112	Methylation	TAGKAALRIHNVTAS CCCCHHHEEEEEECC	24.32	-
115	N-linked_Glycosylation	KAALRIHNVTASDSG CHHHEEEEEECCCCC	30.39	19349973
115	N-linked_Glycosylation	KAALRIHNVTASDSG CHHHEEEEEECCCCC	30.39	19349973
123	Ubiquitination	VTASDSGKYLCYFQD EECCCCCCEEEEEEC	38.71	-
168	Phosphorylation	GIHLECRSTGWYPQP CEEEEEECCCCCCCC	42.82	29978859
169	Phosphorylation	IHLECRSTGWYPQPQ EEEEEECCCCCCCCC	16.63	29978859
172	Phosphorylation	ECRSTGWYPQPQIKW EEECCCCCCCCCEEE	8.04	29978859
231	Ubiquitination	NSLLGLEKTASISIA CCCCCCEECEEEEEC	55.20	-
232	Phosphorylation	SLLGLEKTASISIAD CCCCCEECEEEEECC	19.09	22210691
234	Phosphorylation	LGLEKTASISIADPF CCCEECEEEEECCHH	23.31	22210691
281	Phosphorylation	QKEKIALSRETERER HHHHHHHCHHHHHHH	21.03	24719451
295	Phosphorylation	REMKEMGYAATEQEI HHHHHHHCHHHHHHH	7.55	-
303	Phosphorylation	AATEQEISLREKLQE HHHHHHHCHHHHHHH	22.18	-
319	Phosphorylation	LKWRKIQYMARGEKS HHHHHHHHHHCCCCC	9.01	25884760
537	Phosphorylation	HSLETPLTPGLANES CCCCCCCCCCCCCCC	19.26	24275569
584	Phosphorylation	QARTEALY------- HHHHHHHC-------	24.45	-

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

Oops, there are no upstream regulatory protein records of BT3A3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BT3A3_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 BT3A3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CATL1_HUMAN	CTSL	physical	21988832

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115, AND MASSSPECTROMETRY.
PubMed: 19349973