YD17A_YEAST - dbPTM
YD17A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD17A_YEAST
UniProt AC Q03964
Protein Name Transposon Ty1-DR2 Gag polyprotein
Gene Name TY1A-DR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 440
Subcellular Localization Cytoplasm.
Protein Description Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity)..
Protein Sequence MESQQLSQHSPISHGSACASVTSKEVQTTQDPLDISASKTEECEKVFTQANSQQPTTPPSAAVPENHHHASPQAAQVPLPQNGPYPQQRMMTPQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFALSQFLPTWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLANLHYNGSTPADAFEAEVTNILDRLKNNGIPINNKVACQFIMRGLSGEYKFLRYARHRYIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTSNNFPGPDNDLIRGSTTEPIQLKNKHDLHLRPGTY
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
3Phosphorylation-----MESQQLSQHS
-----CCCCCHHCCC
23.1722369663
7Phosphorylation-MESQQLSQHSPISH
-CCCCCHHCCCCCCC
22.8522369663
10PhosphorylationSQQLSQHSPISHGSA
CCCHHCCCCCCCHHH
19.1122369663
13PhosphorylationLSQHSPISHGSACAS
HHCCCCCCCHHHCCC
25.7722369663
16PhosphorylationHSPISHGSACASVTS
CCCCCCHHHCCCCCC
18.1022369663
20PhosphorylationSHGSACASVTSKEVQ
CCHHHCCCCCCCCCC
26.3022369663
22PhosphorylationGSACASVTSKEVQTT
HHHCCCCCCCCCCCC
31.4222369663
23PhosphorylationSACASVTSKEVQTTQ
HHCCCCCCCCCCCCC
25.3522369663
24UbiquitinationACASVTSKEVQTTQD
HCCCCCCCCCCCCCC
53.1724961812
36PhosphorylationTQDPLDISASKTEEC
CCCCCCCCCCCHHHH
26.5929688323
38PhosphorylationDPLDISASKTEECEK
CCCCCCCCCHHHHHH
33.0621440633
40PhosphorylationLDISASKTEECEKVF
CCCCCCCHHHHHHHH
34.2221440633
71PhosphorylationPENHHHASPQAAQVP
CCCCCCCCCCHHCCC
17.1217330950
139PhosphorylationQYPQYVGTHLNTPSP
CCCCCCCCCCCCCCC
17.1018407956
143PhosphorylationYVGTHLNTPSPESGN
CCCCCCCCCCCCCCC
31.3528889911
145PhosphorylationGTHLNTPSPESGNSF
CCCCCCCCCCCCCCC
38.9828889911
160PhosphorylationPDSSSAKSNMTSTNQ
CCCHHCCCCCCCCCC
31.3921440633
163PhosphorylationSSAKSNMTSTNQHVR
HHCCCCCCCCCCCCC
36.3319795423
164PhosphorylationSAKSNMTSTNQHVRP
HCCCCCCCCCCCCCC
18.0019795423
165PhosphorylationAKSNMTSTNQHVRPP
CCCCCCCCCCCCCCC
29.7219795423
250UbiquitinationVDYTDIMKILSKSIN
CCHHHHHHHHHHHHH
40.6124961812
318PhosphorylationQFIMRGLSGEYKFLR
HHHHCCCCCHHHHHH
32.1920377248
322AcetylationRGLSGEYKFLRYARH
CCCCCHHHHHHHHHH
33.3525381059
322UbiquitinationRGLSGEYKFLRYARH
CCCCCHHHHHHHHHH
33.3523749301
358PhosphorylationQESKRNKSTYRRSPS
HHHHHCCCCCCCCCC
33.9319823750
359PhosphorylationESKRNKSTYRRSPSD
HHHHCCCCCCCCCCC
23.7419823750
360PhosphorylationSKRNKSTYRRSPSDE
HHHCCCCCCCCCCCC
15.8919823750
363PhosphorylationNKSTYRRSPSDEKKD
CCCCCCCCCCCCCCC
21.5417287358
365PhosphorylationSTYRRSPSDEKKDSR
CCCCCCCCCCCCCCC
60.7017287358
371PhosphorylationPSDEKKDSRTYTNTT
CCCCCCCCCCCCCCC
35.0928889911
377PhosphorylationDSRTYTNTTKPKSIT
CCCCCCCCCCCCCCC
28.5328889911
382PhosphorylationTNTTKPKSITRNSQK
CCCCCCCCCCCCCCC
37.4121440633
404PhosphorylationTARAHNVSTSNNFPG
HHHHCCCCCCCCCCC
31.2828132839
406PhosphorylationRAHNVSTSNNFPGPD
HHCCCCCCCCCCCCC
23.4428889911
420PhosphorylationDNDLIRGSTTEPIQL
CCCCCCCCCCCCEEC
23.4722369663
421PhosphorylationNDLIRGSTTEPIQLK
CCCCCCCCCCCEECC
37.6924909858
422PhosphorylationDLIRGSTTEPIQLKN
CCCCCCCCCCEECCC
41.2722369663
439PhosphorylationDLHLRPGTY------
CCCCCCCCC------
28.8317287358
440PhosphorylationLHLRPGTY-------
CCCCCCCC-------
23.6019779198

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 YD17A_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD17A_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 YD17A_YEAST !!

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

Oops, there are no PPI records of YD17A_YEAST !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD17A_YEAST

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Related Literatures of Post-Translational Modification

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