YH11A_YEAST - dbPTM
YH11A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YH11A_YEAST
UniProt AC P0C2I4
Protein Name Transposon Ty1-H Gag polyprotein
Gene Name TY1A-H
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 478
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 MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENLHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPETY
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
1Acetylation-------MESQQLSN
-------CCCCCHHC		11.45-
13PhosphorylationLSNYPHISHGSACAS
HHCCCCCCCCCCCCC		20.8215665377
16PhosphorylationYPHISHGSACASVTS
CCCCCCCCCCCCCCC		18.1028889911
20PhosphorylationSHGSACASVTSKEVH
CCCCCCCCCCCCCCC		26.3028889911
22PhosphorylationGSACASVTSKEVHTN
CCCCCCCCCCCCCCC		31.4228889911
23PhosphorylationSACASVTSKEVHTNQ
CCCCCCCCCCCCCCC		25.3519823750
24UbiquitinationACASVTSKEVHTNQD
CCCCCCCCCCCCCCC		55.1617644757
28PhosphorylationVTSKEVHTNQDPLDV
CCCCCCCCCCCCCCC		39.4928889911
36PhosphorylationNQDPLDVSASKIQEY
CCCCCCCCHHHHHHH		26.8825521595
38PhosphorylationDPLDVSASKIQEYDK
CCCCCCHHHHHHHHH		23.8425521595
39UbiquitinationPLDVSASKIQEYDKA
CCCCCHHHHHHHHHH		48.3924961812
43PhosphorylationSASKIQEYDKASTKA
CHHHHHHHHHHHCCC		13.3322890988
45UbiquitinationSKIQEYDKASTKANS
HHHHHHHHHHCCCCC		43.2515699485
47PhosphorylationIQEYDKASTKANSQQ
HHHHHHHHCCCCCCC		35.8625533186
48PhosphorylationQEYDKASTKANSQQT
HHHHHHHCCCCCCCC		38.7522890988
71PhosphorylationPENLHHASPQPASVP
CCCCCCCCCCCCCCC		21.5128889911
145PhosphorylationGTPLSTPSPESGNTF
CCCCCCCCCCCCCCC		41.1928889911
157PhosphorylationNTFTDSSSADSDMTS
CCCCCCCCCCCCCCC		39.7928889911
160PhosphorylationTDSSSADSDMTSTKK
CCCCCCCCCCCCCCC		29.0616445868
166UbiquitinationDSDMTSTKKYVRPPP
CCCCCCCCCCCCCCC		41.7015699485
167UbiquitinationSDMTSTKKYVRPPPM
CCCCCCCCCCCCCCC		49.4117644757
176PhosphorylationVRPPPMLTSPNDFPN
CCCCCCCCCCCCCCH		35.5717330950
177PhosphorylationRPPPMLTSPNDFPNW
CCCCCCCCCCCCCHH		20.1117330950
186UbiquitinationNDFPNWVKTYIKFLQ
CCCCHHHHHHHHHHH		27.5017644757
203PhosphorylationNLGGIIPTVNGKPVP
CCCCCCCCCCCEECC		19.0524909858
228UbiquitinationNWVKTYIKFLQNSNL
HHHHHHHHHHHHCCC		29.6117644757
241PhosphorylationNLGGIIPTVNGKPVR
CCCCEEECCCCEECE		19.0524909858
245UbiquitinationIIPTVNGKPVRQITD
EEECCCCEECEECCH		34.8323749301
276UbiquitinationQFLPTWVKDILSVDY
HHCCHHHHHHHCCCH		30.5215699485
288UbiquitinationVDYTDIMKILSKSIE
CCHHHHHHHHHHHHH		40.6124961812
293PhosphorylationIMKILSKSIEKMQSD
HHHHHHHHHHHHHHC		32.3821440633
299PhosphorylationKSIEKMQSDTQEAND
HHHHHHHHCCHHHHH		38.8428132839
301PhosphorylationIEKMQSDTQEANDIV
HHHHHHCCHHHHHHH		33.2928132839
318PhosphorylationANLQYNGSTPADAFE
HHCEECCCCHHHHHH		27.8128889911
319PhosphorylationNLQYNGSTPADAFET
HCEECCCCHHHHHHH		24.7227214570
327UbiquitinationPADAFETKVTNIIDR
HHHHHHHHHHHHHHH		39.6017644757
345UbiquitinationNGIHINNKVACQLIM
CCCCCCHHHHHHHHH		27.0717644757
356PhosphorylationQLIMRGLSGEYKFLR
HHHHCCCCCCHHHHH		32.1921440633
360UbiquitinationRGLSGEYKFLRYTRH
CCCCCCHHHHHHHHH		33.3523749301
391PhosphorylationIYEEQQGSRNSKPNY
HHHHHCCCCCCCCCC		24.7728889911
395UbiquitinationQQGSRNSKPNYRRNP
HCCCCCCCCCCCCCC		40.6122817900
403PhosphorylationPNYRRNPSDEKNDSR
CCCCCCCCCCCCCCC		63.0528889911
409PhosphorylationPSDEKNDSRSYTNTT
CCCCCCCCCCCCCCC		32.3017287358
411PhosphorylationDEKNDSRSYTNTTKP
CCCCCCCCCCCCCCC		40.0225521595
412PhosphorylationEKNDSRSYTNTTKPK
CCCCCCCCCCCCCCE		11.6922890988
413PhosphorylationKNDSRSYTNTTKPKV
CCCCCCCCCCCCCEE		27.6021551504
415PhosphorylationDSRSYTNTTKPKVIA
CCCCCCCCCCCEEEE		28.5322890988
416PhosphorylationSRSYTNTTKPKVIAR
CCCCCCCCCCEEEEC		47.6322890988
417UbiquitinationRSYTNTTKPKVIARN
CCCCCCCCCEEEECC		40.5822817900
419UbiquitinationYTNTTKPKVIARNPQ
CCCCCCCEEEECCCC		48.0722817900
435PhosphorylationTNNSKSKTARAHNVS
CCCCCCCCHHHCCCC		28.5921551504
442PhosphorylationTARAHNVSTSNNSPS
CHHHCCCCCCCCCCC		31.2825533186
443PhosphorylationARAHNVSTSNNSPST
HHHCCCCCCCCCCCC		31.0625533186
444PhosphorylationRAHNVSTSNNSPSTD
HHCCCCCCCCCCCCC		26.8921551504
447PhosphorylationNVSTSNNSPSTDNDS
CCCCCCCCCCCCCCC		25.2017330950
449PhosphorylationSTSNNSPSTDNDSIS
CCCCCCCCCCCCCCC		48.4917330950
450PhosphorylationTSNNSPSTDNDSISK
CCCCCCCCCCCCCCC		42.0517330950
454PhosphorylationSPSTDNDSISKSTTE
CCCCCCCCCCCCCCC		34.7121551504
456PhosphorylationSTDNDSISKSTTEPI
CCCCCCCCCCCCCCE		25.2225533186
457UbiquitinationTDNDSISKSTTEPIQ
CCCCCCCCCCCCCEE		50.5923749301
458PhosphorylationDNDSISKSTTEPIQL
CCCCCCCCCCCCEEC		33.5024909858
459PhosphorylationNDSISKSTTEPIQLN
CCCCCCCCCCCEECC		38.6328889911
460PhosphorylationDSISKSTTEPIQLNN
CCCCCCCCCCEECCC		47.0221551504
468UbiquitinationEPIQLNNKHDLHLRP
CCEECCCCCCCCCCC		37.1124961812
477PhosphorylationDLHLRPETY------
CCCCCCCCC------		36.8928889911
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 YH11A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YH11A_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 YH11A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of YH11A_YEAST !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YH11A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.

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