YB21A_YEAST - dbPTM
YB21A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YB21A_YEAST
UniProt AC Q12260
Protein Name Transposon Ty2-B Gag polyprotein
Gene Name TY2A-B
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 MESQQLHQNPHSLHGSAYASVTSKEVSSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDSQDQHSEVPQAKTKVRNNVLPPHTLTSEENFYTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYHRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLRPATERI
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-----MESQQLHQNP
-----CCCCCHHCCC		23.1724961812
12PhosphorylationQLHQNPHSLHGSAYA
CHHCCCCCCCCCEEE		24.2624961812
16PhosphorylationNPHSLHGSAYASVTS
CCCCCCCCEEEEEEC		13.8324961812
18PhosphorylationHSLHGSAYASVTSKE
CCCCCCEEEEEECCH		10.9124961812
20PhosphorylationLHGSAYASVTSKEVS
CCCCEEEEEECCHHC		17.1624961812
22PhosphorylationGSAYASVTSKEVSSN
CCEEEEEECCHHCCC		31.4224961812
23PhosphorylationSAYASVTSKEVSSNQ
CEEEEEECCHHCCCC		25.3524961812
36PhosphorylationNQDPLAVSASNLPEF
CCCCCEEECCCCCCC		22.0017330950
47PhosphorylationLPEFDRDSTKVNSQQ
CCCCCCCCCCCCCCC		30.9028889911
48PhosphorylationPEFDRDSTKVNSQQE
CCCCCCCCCCCCCCC		43.2128132839
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
140PhosphorylationYIPPLSTSSPDPIDS
CCCCCCCCCCCCCCC		36.1828889911
141PhosphorylationIPPLSTSSPDPIDSQ
CCCCCCCCCCCCCCC		33.1528889911
152PhosphorylationIDSQDQHSEVPQAKT
CCCCCCCCCCCHHHH		34.3628889911
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
377UbiquitinationSPNTTNTKVTTRNYH
CCCCCCCCEEECCCC		39.3922817900
379PhosphorylationNTTNTKVTTRNYHRT
CCCCCCEEECCCCCC		22.9227017623
380PhosphorylationTTNTKVTTRNYHRTN
CCCCCEEECCCCCCC		21.6517287358
383PhosphorylationTKVTTRNYHRTNSSK
CCEEECCCCCCCCCC		6.8727017623
388PhosphorylationRNYHRTNSSKPRAAK
CCCCCCCCCCCCHHH		38.8417287358
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 YB21A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YB21A_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 YB21A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of YB21A_YEAST !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YB21A_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND MASSSPECTROMETRY.

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