BT2A1_HUMAN - dbPTM
BT2A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BT2A1_HUMAN
UniProt AC Q7KYR7
Protein Name Butyrophilin subfamily 2 member A1
Gene Name BTN2A1
Organism Homo sapiens (Human).
Sequence Length 527
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MESAAALHFSRPASLLLLLLSLCALVSAQFIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQMEEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCYFQEGRSYDEAILHLVVAGLGSKPLISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVAPALKEVSMPDADGLFMVTTAVIIRDKSVRNMSCSINNTLLGQKKESVIFIPESFMPSVSPCAVALPIIVVILMIPIAVCIYWINKLQKEKKILSGEKEFERETREIALKELEKERVQKEEELQVKEKLQEELRWRRTFLHAVDVVLDPDTAHPDLFLSEDRRSVRRCPFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVPVRPFFRLGCEDSPIFICPALTGANGVTVPEEGLTLHRVGTHQSL
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
18UbiquitinationRPASLLLLLLSLCAL
CHHHHHHHHHHHHHH		4.5727667366
46N-linked_GlycosylationILATVGENTTLRCHL
CEEEECCCCEEEEEE		32.22UniProtKB CARBOHYD
57UbiquitinationRCHLSPEKNAEDMEV
EEEECCCCCHHHCCH		65.91-
79UbiquitinationSPAVFVYKGGRERTE
CCEEEEEECCCCCCH		49.9727667366
100PhosphorylationRGRTTFVSKDISRGS
CCCCEEEECCCCCCC		22.03-
101UbiquitinationGRTTFVSKDISRGSV
CCCEEEECCCCCCCE		54.50-
107PhosphorylationSKDISRGSVALVIHN
ECCCCCCCEEEEEEE		11.78-
114N-linked_GlycosylationSVALVIHNITAQENG
CEEEEEEEEECCCCC		23.3719349973
120N-linked_GlycosylationHNITAQENGTYRCYF
EEEECCCCCEEEEEE		35.7119349973
143 (in isoform 3)Ubiquitination-10.4621890473
147PhosphorylationLVVAGLGSKPLISMR
HHHCCCCCCCEEEEC		35.8224719451
173UbiquitinationISRGWYPKPLTVWRD
EECCCCCCCEEEEEC		36.64-
204O-linked_GlycosylationADGLFMVTTAVIIRD
CCCEEEEEEEEEECC		9.39OGP
213PhosphorylationAVIIRDKSVRNMSCS
EEEECCCCHHCCEEE		30.5124260401
216UbiquitinationIRDKSVRNMSCSINN
ECCCCHHCCEEEECC		25.2729967540
222UbiquitinationRNMSCSINNTLLGQK
HCCEEEECCCCCCCC		21.0933845483
230UbiquitinationNTLLGQKKESVIFIP
CCCCCCCCCEEEECC		47.54-
232PhosphorylationLLGQKKESVIFIPES
CCCCCCCEEEECCHH		29.4124248375
234UbiquitinationGQKKESVIFIPESFM
CCCCCEEEECCHHHC		3.4522817900
238UbiquitinationESVIFIPESFMPSVS
CEEEECCHHHCCCCC		52.3629967540
243UbiquitinationIPESFMPSVSPCAVA
CCHHHCCCCCHHHHH		24.3632015554
243PhosphorylationIPESFMPSVSPCAVA
CCHHHCCCCCHHHHH		24.3624248375
267PhosphorylationIPIAVCIYWINKLQK
HHHHHHHHHHHHHHH		8.6324248375
277UbiquitinationNKLQKEKKILSGEKE
HHHHHHHHHHCCCCH		50.3929967540
280 (in isoform 1)Ubiquitination-48.6721890473
281 (in isoform 1)Ubiquitination-46.6921890473
283UbiquitinationKKILSGEKEFERETR
HHHHCCCCHHHHHHH		71.8333845483
289PhosphorylationEKEFERETREIALKE
CCHHHHHHHHHHHHH		39.5624505115
295UbiquitinationETREIALKELEKERV
HHHHHHHHHHHHHHC		51.7521890473
295UbiquitinationETREIALKELEKERV
HHHHHHHHHHHHHHC		51.7522817900
295 (in isoform 2)Ubiquitination-51.7521890473
295UbiquitinationETREIALKELEKERV
HHHHHHHHHHHHHHC		51.7521890473
295UbiquitinationETREIALKELEKERV
HHHHHHHHHHHHHHC		51.7521890473
299UbiquitinationIALKELEKERVQKEE
HHHHHHHHHHCHHHH		64.5429967540
304UbiquitinationLEKERVQKEEELQVK
HHHHHCHHHHHHHHH		65.3232015554
313UbiquitinationEELQVKEKLQEELRW
HHHHHHHHHHHHHHH		50.15-
344PhosphorylationAHPDLFLSEDRRSVR
CCCCCCCCCCCCHHH		30.07-
417 (in isoform 5)Phosphorylation-22.8924719451
436PhosphorylationGQYRAVSSPDRILPL
CCEEECCCCCCEEEC		24.9928555341
439MethylationRAVSSPDRILPLKES
EECCCCCCEEECCHH		35.41-
444UbiquitinationPDRILPLKESLCRVG
CCCEEECCHHHEEEE		43.23-
465 (in isoform 5)Phosphorylation-19.5924719451
478PhosphorylationHIYTCPRSAFSVPVR
CEEECCCHHCCCCCC		20.8624719451
523PhosphorylationLTLHRVGTHQSL---
CEEEECCCCCCC---		17.5530576142
526PhosphorylationHRVGTHQSL------
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 BT2A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BT2A1_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 BT2A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BT2A2_HUMANBTN2A2physical
26186194
GO45_HUMANBLZF1physical
26186194
TYW1_HUMANTYW1physical
26186194
SGPL1_HUMANSGPL1physical
26186194
AT2A3_HUMANATP2A3physical
26186194
OCRL_HUMANOCRLphysical
26186194
RB3GP_HUMANRAB3GAP1physical
26186194
POTEF_HUMANPOTEFphysical
26186194
OSBP1_HUMANOSBPphysical
26186194
PLCB1_HUMANPLCB1physical
26186194
P55G_HUMANPIK3R3physical
26186194
PDZD8_HUMANPDZD8physical
26186194
HMDH_HUMANHMGCRphysical
26186194
UPK3L_HUMANUPK3BLphysical
26186194
TM214_HUMANTMEM214physical
26186194
ESYT1_HUMANESYT1physical
26186194
NU1M_HUMANND1physical
26186194
NCPR_HUMANPORphysical
26186194
TMX4_HUMANTMX4physical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
MARH7_HUMANMARCH7physical
26186194
F1712_HUMANFAM171A2physical
26186194
ITFG2_HUMANITFG2physical
26186194
F189B_HUMANFAM189Bphysical
26186194
DEN6A_HUMANDENND6Aphysical
26186194
DGLB_HUMANDAGLBphysical
26186194
KMCP1_HUMANSLC25A30physical
26186194
UCP5_HUMANSLC25A14physical
26186194
PKHG4_HUMANPLEKHG4physical
26186194
KPTN_HUMANKPTNphysical
26186194
FMN2_HUMANFMN2physical
26186194
BT2A2_HUMANBTN2A2physical
28514442
GO45_HUMANBLZF1physical
28514442
PLCB1_HUMANPLCB1physical
28514442
F1712_HUMANFAM171A2physical
28514442
TMX4_HUMANTMX4physical
28514442
AT2A3_HUMANATP2A3physical
28514442
TYW1_HUMANTYW1physical
28514442
RB3GP_HUMANRAB3GAP1physical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
PDZD8_HUMANPDZD8physical
28514442
OSBP1_HUMANOSBPphysical
28514442
FMN2_HUMANFMN2physical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
KPTN_HUMANKPTNphysical
28514442
NU1M_HUMANND1physical
28514442
ITFG2_HUMANITFG2physical
28514442
KMCP1_HUMANSLC25A30physical
28514442
POTEF_HUMANPOTEFphysical
28514442
SGPL1_HUMANSGPL1physical
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 BT2A1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-114 AND ASN-120, AND MASSSPECTROMETRY.

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