BTN2_YEAST - dbPTM
BTN2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTN2_YEAST
UniProt AC P53286
Protein Name Protein BTN2
Gene Name BTN2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 410
Subcellular Localization Cytoplasm. Late endosome.
Protein Description V-SNARE binding protein that facilitates specific protein retrieval from a late endosome to the Golgi. Modulates the rate of arginine uptake. Involved in pH homeostasis. Required for the correct localization of IST2. May be involved in ion homeostasis together with IST2..
Protein Sequence MFSIFNSPCVFEQLPSFSQPLHSRYFDCSSPVSYYPECKRRKAIKANLRAPKKSDANCSEPLRYALAETPNGYTLSLSKRIPYELFSKYVNEKLGELKENHYRPTYHVVQDFFGNQYYVEDEADEDALLRSALKDLDFRAIGKKIAKDLFQDYEIELNHRGDELSILSKKDKIFKEFSLDQVFEDVFVIGCGVENIDDGSREKYALLKIGLVKHEEEISEGGINEPKMPIIESKIDESHDDVNMSESLKEEEAEKAKEPLTKEDQIKKWIEEERLMQEESRKSEQEKAAKEDEERQKKEKEARLKARKESLINKQKTKRSQQKKLQNSKSLPISEIEASNKNNNSNSGSAESDNESINSDSDTTLDFSVSGNTLKKHASPLLEDVEDEEVDRYNESLSRSPKGNSIIEEI
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
25PhosphorylationSQPLHSRYFDCSSPV
CCCCHHHCCCCCCCC		13.5427017623
29PhosphorylationHSRYFDCSSPVSYYP
HHHCCCCCCCCCCCH		39.2530377154
30PhosphorylationSRYFDCSSPVSYYPE
HHCCCCCCCCCCCHH		35.3327214570
33PhosphorylationFDCSSPVSYYPECKR
CCCCCCCCCCHHHHH		23.4930377154
34PhosphorylationDCSSPVSYYPECKRR
CCCCCCCCCHHHHHH		24.2327017623
35PhosphorylationCSSPVSYYPECKRRK
CCCCCCCCHHHHHHH		5.7627017623
39UbiquitinationVSYYPECKRRKAIKA
CCCCHHHHHHHHHHH		54.2817644757
74PhosphorylationAETPNGYTLSLSKRI
HCCCCCEEEEECCCC		15.9827214570
79UbiquitinationGYTLSLSKRIPYELF
CEEEEECCCCCHHHH		60.6917644757
98UbiquitinationNEKLGELKENHYRPT
HHHHHHHHHHCCCCC		52.7717644757
208UbiquitinationREKYALLKIGLVKHE
HHHHHHEEEECEECH		35.2617644757
213UbiquitinationLLKIGLVKHEEEISE
HEEEECEECHHHHHC		50.7917644757
219PhosphorylationVKHEEEISEGGINEP
EECHHHHHCCCCCCC		33.2127214570
227UbiquitinationEGGINEPKMPIIESK
CCCCCCCCCCEEHHH		51.6417644757
238PhosphorylationIESKIDESHDDVNMS
EHHHCCCCCCCCCCC		28.5928889911
255UbiquitinationLKEEEAEKAKEPLTK
HHHHHHHHHHCCCCH		72.3317644757
257UbiquitinationEEEAEKAKEPLTKED
HHHHHHHHCCCCHHH		71.5717644757
262UbiquitinationKAKEPLTKEDQIKKW
HHHCCCCHHHHHHHH		67.9617644757
267UbiquitinationLTKEDQIKKWIEEER
CCHHHHHHHHHHHHH		36.1017644757
268UbiquitinationTKEDQIKKWIEEERL
CHHHHHHHHHHHHHH		55.8417644757
329UbiquitinationQKKLQNSKSLPISEI
HHHHHHCCCCCHHHH		64.6617644757
341UbiquitinationSEIEASNKNNNSNSG
HHHHHCCCCCCCCCC		59.5617644757
379PhosphorylationNTLKKHASPLLEDVE
HHHHHHCCCHHCCCC		18.7917563356
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 BTN2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTN2_YEAST !!
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 BTN2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YIF1_YEASTYIF1physical
12615067
IST2_YEASTIST2physical
15701790
IST2_YEASTIST2genetic
15701790
TLG2_YEASTTLG2physical
17101785
TLG1_YEASTTLG1physical
17101785
VTI1_YEASTVTI1physical
17101785
SNC1_YEASTSNC1physical
17101785
SNC2_YEASTSNC2physical
17101785
VPS35_YEASTVPS35physical
17101785
PEP8_YEASTPEP8physical
17101785
SNX4_YEASTSNX4physical
17101785
YIF1_YEASTYIF1physical
17101785
RNQ1_YEASTRNQ1physical
18719252
SP382_YEASTSPP382physical
18719252
ADA2_YEASTADA2physical
18719252
MAC1_YEASTMAC1physical
18719252
SSK22_YEASTSSK22physical
18719252
RSF2_YEASTRSF2physical
18719252
MAP2_YEASTMAP2physical
18719252
DPB3_YEASTDPB3genetic
20093466
UBP1_YEASTUBP1genetic
20093466
RSC2_YEASTRSC2genetic
20093466
YMK8_YEASTYML108Wgenetic
20093466
TDA3_YEASTTDA3physical
21441304
SNC1_YEASTSNC1physical
21441304
TDA3_YEASTTDA3genetic
21441304
SNC1_YEASTSNC1genetic
21441304
HS104_YEASTHSP104physical
21441304
SIS1_YEASTSIS1physical
22718905
CUR1_YEASTCUR1genetic
22718905
HSP42_YEASTHSP42physical
22718905
VHL_HUMANVHLphysical
22718905
IST2_YEASTIST2genetic
22808051
GRPE_YEASTMGE1physical
22875988
CUR1_YEASTCUR1genetic
24938787
HSP42_YEASTHSP42genetic
24938787
HSP42_YEASTHSP42genetic
25672362
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
MAF1_YEASTMAF1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
MK07_HUMANMAPK7physical
27107014
UBC9_HUMANUBE2Iphysical
27107014
IHO1_HUMANCCDC36physical
27107014
CA094_HUMANC1orf94physical
27107014
AL2SB_HUMANALS2CR12physical
27107014
UBX11_HUMANUBXN11physical
27107014
SAXO1_HUMANFAM154Aphysical
27107014
SAMD3_HUMANSAMD3physical
27107014
ATRIP_HUMANATRIPphysical
27107014
TRI27_HUMANTRIM27physical
27107014
4ET_HUMANEIF4ENIF1physical
27107014
CEP70_HUMANCEP70physical
27107014
CCD33_HUMANCCDC33physical
27107014
ZBT32_HUMANZBTB32physical
27107014
F208B_HUMANFAM208Bphysical
27107014
IKZF3_HUMANIKZF3physical
27107014
KLH12_HUMANKLHL12physical
27107014
TRI41_HUMANTRIM41physical
27107014
CNDH2_HUMANNCAPH2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BTN2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASSSPECTROMETRY.

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