TCB2_YEAST - dbPTM
TCB2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCB2_YEAST
UniProt AC P48231
Protein Name Tricalbin-2
Gene Name TCB2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1178
Subcellular Localization Cell membrane
Multi-pass membrane protein. Traffics from the cell surface to intracellular vesicles near the vacuole.
Protein Description May play a role in membrane trafficking..
Protein Sequence MSPNSSKTRTDQISSMPGINEATKVESKNVVKDAVPIKSEVETNGTSIVREKQDPSYVGWKQVGGWEEKDELTSEDLLVDVNKDTFLGNLLPDKFYGDWYHEVAILIIAGLCSFVLGYFKFSLASVLIVMLTTGMLYRTSSKKYRESLRDLAQKEQTVEKITSDYESVEWLNTFLDKYWPIIEPSVSQQIVDGTNTALSENVAIPKFIKAIWLDQFTLGVKPPRIDAIKTFQNTKSDVVVMDVCLSFTPHDMSDLDAKQCRNYVNSNVVLKAKIFGMDIPVSVADIFFQVFVRFRFQLMTTLPLVETINIQLLEVPEVDFISRLLGNSVFNWEILAIPGLMRLIQKMAFKYLSPVLLPPFSLQLNIPQLLSKTGLPIGVLEIKVKNAHGLRKLVGMIKKTVDPYLTFELSGKIVGKTKVFKNSANPVWNESIYILLQSFTDPLTIAVYDKRETLSDKKMGTVIFNLNKLHANHYHKNEKVHFLRNSKPVGELTFDLRFFPTIEPKKLLNGDEEPLPDMNTGITKITIRELKGLDELSDKKFVFAELYVNAELVMTTKKEKRTAHLKWNSDYYSVVTDRRKTICRFVLKDQSGKVISSSVQPLNHLIDRTEVNKEWIPLRNGKGELKVTTYWRPVDIDLGLKSVGYTTPIGMLRVFINKAENLRNPDSLGKISPYAKVSVNGVARGRTNERIETLNPIWNQSIYVSVTSPLQKVSIDCFGIDTNGDDHNLGSLNIQTQNIYHKDNDDKYTIFIDNAPRTGNLIGKKGVKGTVTYYLSFYPVVPVLSLEEAKEVDEINEKKDKLEKQKSTLDDKNISKEEKERIKKEEFRLTEKYDMYSYKMKLDLDELLQYNAGVLGVTVLGGELPQPGLYVQTFFDSCGYAAITSAKNAIRTIKTGWSGDFMIKELEWSVTTFRVTKTKDANKAENFICEVNIPTIELVRNCYYKPSVLNLIGKKSAKLLVQVSWFPVTATELPQSDLITNSGDLKITAKSAENLIGVNKNGYSDPYVEFFLNEKSTSPFFKTAVQKKTLNPTWNESKTIEVSNRVNDYLTINVKDYESTNSNRSIGKAVVPLSTIDPESDTTFNIPLVGPKGEDGGVLHLEFEFEPRYTTNVVKREAGLGNFATKGLGTGIKAGSTVFALGTNVVSTGLGTIDKVKAGVFGGKKSTTTGDKKSEEKQ
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
2Phosphorylation------MSPNSSKTR
------CCCCCCCCC		44.0624961812
5Phosphorylation---MSPNSSKTRTDQ
---CCCCCCCCCHHH		36.2724961812
6Phosphorylation--MSPNSSKTRTDQI
--CCCCCCCCCHHHH		44.6924961812
7Ubiquitination-MSPNSSKTRTDQIS
-CCCCCCCCCHHHHH		41.6724961812
8PhosphorylationMSPNSSKTRTDQISS
CCCCCCCCCHHHHHC		40.5224961812
10PhosphorylationPNSSKTRTDQISSMP
CCCCCCCHHHHHCCC		37.1724961812
14PhosphorylationKTRTDQISSMPGINE
CCCHHHHHCCCCCCC		18.2321440633
15PhosphorylationTRTDQISSMPGINEA
CCHHHHHCCCCCCCC		30.5321440633
24UbiquitinationPGINEATKVESKNVV
CCCCCCCCCCCCCCC		51.5624961812
27PhosphorylationNEATKVESKNVVKDA
CCCCCCCCCCCCCCC		32.3021440633
39PhosphorylationKDAVPIKSEVETNGT
CCCCCCCEEEECCCC		47.8219823750
43PhosphorylationPIKSEVETNGTSIVR
CCCEEEECCCCEEEE		44.0919823750
46PhosphorylationSEVETNGTSIVREKQ
EEEECCCCEEEECCC		19.8319823750
47PhosphorylationEVETNGTSIVREKQD
EEECCCCEEEECCCC		22.0821551504
125PhosphorylationYFKFSLASVLIVMLT
HHHHHHHHHHHHHHH		23.8130377154
132PhosphorylationSVLIVMLTTGMLYRT
HHHHHHHHHCCHHHC		11.8330377154
133PhosphorylationVLIVMLTTGMLYRTS
HHHHHHHHCCHHHCC		19.3428889911
137PhosphorylationMLTTGMLYRTSSKKY
HHHHCCHHHCCCHHH		11.7130377154
140PhosphorylationTGMLYRTSSKKYRES
HCCHHHCCCHHHHHH		31.0328889911
141PhosphorylationGMLYRTSSKKYRESL
CCHHHCCCHHHHHHH		32.3330377154
229UbiquitinationPPRIDAIKTFQNTKS
CCCCCHHHHHCCCCC		45.0323749301
399AcetylationKLVGMIKKTVDPYLT
HHHHHHHHCCCCCEE		42.7424489116
613AcetylationIDRTEVNKEWIPLRN
CCCHHCCCCEEECCC		60.6524489116
626UbiquitinationRNGKGELKVTTYWRP
CCCCCEEEEEEEEEE		32.9817644757
641UbiquitinationVDIDLGLKSVGYTTP
EEEEECCCCCCCCCC		41.1017644757
670UbiquitinationRNPDSLGKISPYAKV
CCCCCCCCCCCCCEE		45.3524961812
670AcetylationRNPDSLGKISPYAKV
CCCCCCCCCCCCCEE		45.3524489116
748PhosphorylationHKDNDDKYTIFIDNA
ECCCCCCEEEEEECC		16.4427017623
758PhosphorylationFIDNAPRTGNLIGKK
EEECCCCCCCCCCCC		29.3927017623
832AcetylationEEFRLTEKYDMYSYK
HHHHHHHHCCCCEEE		41.1224489116
911PhosphorylationKELEWSVTTFRVTKT
EEEEEEEEEEEEEEC		18.0719779198
912PhosphorylationELEWSVTTFRVTKTK
EEEEEEEEEEEEECC		13.8019779198
916PhosphorylationSVTTFRVTKTKDANK
EEEEEEEEECCCCCC		28.8319779198
945UbiquitinationLVRNCYYKPSVLNLI
HHHHCCCCHHHHHHC		12.3517644757
954UbiquitinationSVLNLIGKKSAKLLV
HHHHHCCHHCEEEEE		36.2417644757
955UbiquitinationVLNLIGKKSAKLLVQ
HHHHCCHHCEEEEEE		50.8917644757
990AcetylationGDLKITAKSAENLIG
CCEEEEEECHHHHCC		41.3624489116
991PhosphorylationDLKITAKSAENLIGV
CEEEEEECHHHHCCC		38.0523749301
1018PhosphorylationFLNEKSTSPFFKTAV
HCCCCCCCHHHHHHH		27.1427214570
1027UbiquitinationFFKTAVQKKTLNPTW
HHHHHHHHCCCCCCC		40.9217644757
1028UbiquitinationFKTAVQKKTLNPTWN
HHHHHHHCCCCCCCC		40.9517644757
1029PhosphorylationKTAVQKKTLNPTWNE
HHHHHHCCCCCCCCC		38.5127017623
1038UbiquitinationNPTWNESKTIEVSNR
CCCCCCCCCEEEECC		47.5517644757
1068UbiquitinationNSNRSIGKAVVPLST
CCCCCCEEEEEEHHH		36.0223749301
1133UbiquitinationKGLGTGIKAGSTVFA
CCCCCCCCCCCEEEE		48.3017644757
1136PhosphorylationGTGIKAGSTVFALGT
CCCCCCCCEEEEECC		26.6830377154
1137PhosphorylationTGIKAGSTVFALGTN
CCCCCCCEEEEECCC		20.8021440633
1155UbiquitinationTGLGTIDKVKAGVFG
CCCCHHCEEEEEECC		41.6117644757
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 TCB2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCB2_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 TCB2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCB1_YEASTTCB1physical
15141306
TCB3_YEASTTCB3physical
15141306
PDR1_YEASTPDR1physical
15141306
RSP5_YEASTRSP5genetic
15141306
SSB1_YEASTSSB1physical
22940862
EF1A_YEASTTEF2physical
22940862
HSP72_YEASTSSA2physical
22940862
DED1_YEASTDED1physical
22940862
KPYK1_YEASTCDC19physical
22940862
EXO84_YEASTEXO84physical
22940862
PABP_YEASTPAB1physical
22940862
SEC3_YEASTSEC3physical
22940862
HSP71_YEASTSSA1physical
22940862
SEC5_YEASTSEC5physical
22940862
PALH_YEASTRIM21genetic
27803246
GPR1_YEASTGPR1genetic
27708008
STE13_YEASTSTE13genetic
27708008
KIN4_YEASTKIN4genetic
27708008
FLO1_YEASTFLO1genetic
27708008
VPS10_YEASTPEP1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
YRO2_YEASTYRO2genetic
27708008
MSH5_YEASTMSH5genetic
27708008
PAD1_YEASTPAD1genetic
27708008
MED5_YEASTNUT1genetic
27708008
MAL12_YEASTMAL12genetic
27708008
MTHR1_YEASTMET12genetic
27708008
ELOC_YEASTELC1genetic
27708008
PRM4_YEASTPRM4genetic
27708008
CG12_YEASTCLN2genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCB2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-15, AND MASSSPECTROMETRY.

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