YD21A_YEAST - dbPTM
YD21A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD21A_YEAST
UniProt AC Q12392
Protein Name Transposon Ty2-DR1 Gag polyprotein
Gene Name TY2A-DR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 438
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 Ty2 RNA and initiation of reverse transcription (By similarity)..
Protein Sequence MESQQLSQNSPNLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDLKNQHSEIPQAKTKVGNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYQRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLRPATERI
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-------MESQQLSQ
-------CCCHHHHC		11.45-
7Phosphorylation-MESQQLSQNSPNLH
-CCCHHHHCCCCCCC		23.9924961812
10PhosphorylationSQQLSQNSPNLHGSA
CHHHHCCCCCCCCCE		13.9215665377
16PhosphorylationNSPNLHGSAYASVTS
CCCCCCCCEEEEECC		13.8324961812
20PhosphorylationLHGSAYASVTSKEVP
CCCCEEEEECCCCCC		17.1624961812
22PhosphorylationGSAYASVTSKEVPSN
CCEEEEECCCCCCCC		31.4224961812
28PhosphorylationVTSKEVPSNQDPLAV
ECCCCCCCCCCCCEE		52.9122369663
36PhosphorylationNQDPLAVSASNLPEF
CCCCCEEECCCCCCC		22.0022369663
38PhosphorylationDPLAVSASNLPEFDR
CCCEEECCCCCCCCC		31.2422369663
47PhosphorylationLPEFDRDSTKVNSQQ
CCCCCCCCCCCCCCC		30.9022369663
48PhosphorylationPEFDRDSTKVNSQQE
CCCCCCCCCCCCCCC		43.2122369663
52PhosphorylationRDSTKVNSQQETTPG
CCCCCCCCCCCCCCC		35.9128889911
57PhosphorylationVNSQQETTPGTSAVP
CCCCCCCCCCCCCCC		20.9718407956
71PhosphorylationPENHHHVSPQPASVP
CCCCCCCCCCCCCCC		17.2918407956
85PhosphorylationPPPQNGQYQQHGMMT
CCCCCCCCCCCCCCC		16.1327738172
92PhosphorylationYQQHGMMTPNKAMAS
CCCCCCCCCCHHHHC		18.1518407956
115PhosphorylationSMMTCSHYQTSPAYY
CCCCCCCCCCCCCCC		9.3718407956
117PhosphorylationMTCSHYQTSPAYYQP
CCCCCCCCCCCCCCC		29.5218407956
118PhosphorylationTCSHYQTSPAYYQPD
CCCCCCCCCCCCCCC		7.6318407956
140PhosphorylationYIPPLSTSSPDPIDL
CCCCCCCCCCCCCCC		36.1818407956
141PhosphorylationIPPLSTSSPDPIDLK
CCCCCCCCCCCCCCC		33.1518407956
152PhosphorylationIDLKNQHSEIPQAKT
CCCCCCCCCCCCCCC		27.7023749301
182UbiquitinationENFSTWVKFYIRFLK
CCHHHHHHHHHHHHH		24.8217644757
189UbiquitinationKFYIRFLKNSNLGDI
HHHHHHHHCCCCCCC		56.4717644757
205UbiquitinationPNDQGEIKRQMTYEE
CCCCCHHHCCCCHHH		32.0717644757
209PhosphorylationGEIKRQMTYEEHAYI
CHHHCCCCHHHHHHH		21.3130377154
210PhosphorylationEIKRQMTYEEHAYIY
HHHCCCCHHHHHHHH		17.6130377154
215PhosphorylationMTYEEHAYIYNTFQA
CCHHHHHHHHHHHHH		13.0730377154
217PhosphorylationYEEHAYIYNTFQAFA
HHHHHHHHHHHHHHC		8.7530377154
219PhosphorylationEHAYIYNTFQAFAPF
HHHHHHHHHHHHCCH		10.5130377154
234UbiquitinationHLLPTWVKQILEINY
HHHHHHHHHHHHCCH		24.1517644757
250UbiquitinationDILTVLCKSVSKMQT
HHHHHHHHHHHHCCC		50.1317644757
294UbiquitinationSTIIQRLKENNINVS
HHHHHHHHHCCCCHH		61.6617644757
311UbiquitinationLACQLILKGLSGDFK
HHHHHHHHHHHCCHH		51.3017644757
331UbiquitinationYRTKTNMKLSQLFAE
HHHHHHHCHHHHHHH		47.2417644757
347UbiquitinationQLIYDENKIMNLNKP
HHHHCCCCCCCCCCH		41.0817644757
353UbiquitinationNKIMNLNKPSQYKQH
CCCCCCCCHHHHCCC		49.5717644757
355PhosphorylationIMNLNKPSQYKQHSE
CCCCCCHHHHCCCCC		47.9921551504
358UbiquitinationLNKPSQYKQHSEYKN
CCCHHHHCCCCCCCC		33.6217644757
367PhosphorylationHSEYKNVSRTSPNTT
CCCCCCCCCCCCCCC		38.9522369663
369PhosphorylationEYKNVSRTSPNTTNT
CCCCCCCCCCCCCCC		40.8222369663
370PhosphorylationYKNVSRTSPNTTNTK
CCCCCCCCCCCCCCC		18.2922369663
373PhosphorylationVSRTSPNTTNTKVTT
CCCCCCCCCCCCEEE		25.4722369663
374PhosphorylationSRTSPNTTNTKVTTR
CCCCCCCCCCCEEEC		47.7522369663
376PhosphorylationTSPNTTNTKVTTRNY
CCCCCCCCCEEECCC		25.4622369663
377UbiquitinationSPNTTNTKVTTRNYQ
CCCCCCCCEEECCCC		39.3922817900
404UbiquitinationHNIATSSKFSRVNND
HCHHCCCCCCCCCCC		47.3123749301
406PhosphorylationIATSSKFSRVNNDHI
HHCCCCCCCCCCCCC		38.7719823750
416PhosphorylationNNDHINESTVSSQYL
CCCCCCCCCCCCCCC		29.6222369663
417PhosphorylationNDHINESTVSSQYLS
CCCCCCCCCCCCCCC		20.4422369663
419PhosphorylationHINESTVSSQYLSDD
CCCCCCCCCCCCCCC		16.2922369663
420PhosphorylationINESTVSSQYLSDDN
CCCCCCCCCCCCCCC		20.6422369663
422PhosphorylationESTVSSQYLSDDNEL
CCCCCCCCCCCCCCC		15.3222369663
424PhosphorylationTVSSQYLSDDNELSL
CCCCCCCCCCCCCCC		37.6722369663
430PhosphorylationLSDDNELSLRPATER
CCCCCCCCCCCCCCC		19.0222369663
435PhosphorylationELSLRPATERI----
CCCCCCCCCCC----		28.6022369663
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 YD21A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD21A_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 YD21A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of YD21A_YEAST !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD21A_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-10 AND SER-424, 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-10 AND SER-424, AND MASS SPECTROMETRY.

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