YJ11A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YJ11A_YEAST
• UniProt AC: P0CX74
• Protein Name: Transposon Ty1-JR1 Gag polyprotein
• Gene Name: TY1A-JR1
• 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: MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY

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
3	Phosphorylation	-----MESQQLSQHS -----CCCCCHHHCC	23.17	23607784
7	Phosphorylation	-MESQQLSQHSHISH -CCCCCHHHCCCCCC	22.85	23607784
10	Phosphorylation	SQQLSQHSHISHGSA CCCHHHCCCCCCCCC	18.19	24909858
13	Phosphorylation	LSQHSHISHGSACAS HHHCCCCCCCCCCCC	19.17	24909858
16	Phosphorylation	HSHISHGSACASVTS CCCCCCCCCCCCCCC	18.10	23607784
20	Phosphorylation	SHGSACASVTSKEVH CCCCCCCCCCCCCCC	26.30	28889911
22	Phosphorylation	GSACASVTSKEVHTN CCCCCCCCCCCCCCC	31.42	28889911
23	Phosphorylation	SACASVTSKEVHTNQ CCCCCCCCCCCCCCC	25.35	19823750
28	Phosphorylation	VTSKEVHTNQDPLDV CCCCCCCCCCCCCCC	39.49	21440633
36	Phosphorylation	NQDPLDVSASKTEEC CCCCCCCCCCHHHHH	26.88	25533186
38	Phosphorylation	DPLDVSASKTEECEK CCCCCCCCHHHHHHH	32.38	17330950
40	Phosphorylation	LDVSASKTEECEKAS CCCCCCHHHHHHHHH	34.22	21440633
47	Phosphorylation	TEECEKASTKANSQQ HHHHHHHHHHCCCCC	41.32	17330950
48	Phosphorylation	EECEKASTKANSQQT HHHHHHHHHCCCCCC	38.75	25005228
71	Phosphorylation	PENPHHASPQPASVP CCCCCCCCCCCCCCC	21.51	28889911
145	Phosphorylation	GTPLSTPSPESGNTF CCCCCCCCCCCCCCC	41.19	28889911
157	Phosphorylation	NTFTDSSSADSDMTS CCCCCCCCCCCCCCC	39.79	28889911
160	Phosphorylation	TDSSSADSDMTSTKK CCCCCCCCCCCCCCC	29.06	16445868
176	Phosphorylation	VRPPPMLTSPNDFPN CCCCCCCCCCCCCCH	35.57	17330950
177	Phosphorylation	RPPPMLTSPNDFPNW CCCCCCCCCCCCCHH	20.11	17330950
203	Phosphorylation	NLGGIIPTVNGKPVR CCCCEEECCCCEECE	19.05	24909858
255	Phosphorylation	IMKILSKSIEKMQSD HHHHHHHHHHHHHHC	32.38	21440633
261	Phosphorylation	KSIEKMQSDTQEAND HHHHHHHHCCHHHHH	38.84	28132839
263	Phosphorylation	IEKMQSDTQEANDIV HHHHHHCCHHHHHHH	33.29	28132839
280	Phosphorylation	ANLQYNGSTPADAFE HHCEECCCCHHHHHH	27.81	28889911
281	Phosphorylation	NLQYNGSTPADAFET HCEECCCCHHHHHHH	24.72	27214570
318	Phosphorylation	QLIMRGLSGEYKFLR HHHHCCCCCCHHHHH	32.19	21440633
353	Phosphorylation	IYEEQQGSRNSKPNY HHHHHCCCCCCCCCC	24.77	28889911
365	Phosphorylation	PNYRRNLSDEKNDSR CCCCCCCCCCCCCCC	47.47	21082442
371	Phosphorylation	LSDEKNDSRSYTNTT CCCCCCCCCCCCCCC	32.30	17287358
373	Phosphorylation	DEKNDSRSYTNTTKP CCCCCCCCCCCCCCC	40.02	22890988
374	Phosphorylation	EKNDSRSYTNTTKPK CCCCCCCCCCCCCCE	11.69	22890988
375	Phosphorylation	KNDSRSYTNTTKPKV CCCCCCCCCCCCCEE	27.60	21551504
377	Phosphorylation	DSRSYTNTTKPKVIA CCCCCCCCCCCEEEE	28.53	22890988
378	Phosphorylation	SRSYTNTTKPKVIAR CCCCCCCCCCEEEEC	47.63	22890988
397	Phosphorylation	TNNSKSKTARAHNVS CCCCCCCCHHHCCCC	28.59	21551504
404	Phosphorylation	TARAHNVSTSNNSPS CHHHCCCCCCCCCCC	31.28	25533186
405	Phosphorylation	ARAHNVSTSNNSPST HHHCCCCCCCCCCCC	31.06	25533186
406	Phosphorylation	RAHNVSTSNNSPSTD HHCCCCCCCCCCCCC	26.89	21551504
409	Phosphorylation	NVSTSNNSPSTDNDS CCCCCCCCCCCCCCC	25.20	17330950
411	Phosphorylation	STSNNSPSTDNDSIS CCCCCCCCCCCCCCC	48.49	17330950
412	Phosphorylation	TSNNSPSTDNDSISK CCCCCCCCCCCCCCC	42.05	17330950
416	Phosphorylation	SPSTDNDSISKSTTE CCCCCCCCCCCCCCC	34.71	21551504
418	Phosphorylation	STDNDSISKSTTEPI CCCCCCCCCCCCCCE	25.22	25533186
420	Phosphorylation	DNDSISKSTTEPIQL CCCCCCCCCCCCEEC	33.50	24909858
421	Phosphorylation	NDSISKSTTEPIQLN CCCCCCCCCCCEECC	38.63	28889911
422	Phosphorylation	DSISKSTTEPIQLNN CCCCCCCCCCEECCC	47.02	21551504
439	Phosphorylation	DLHLRPGTY------ CCCCCCCCC------	28.83	17287358
440	Phosphorylation	LHLRPGTY------- CCCCCCCC-------	23.60	19779198

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of YJ11A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YJ11A_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of YJ11A_YEAST !!

Protein-Protein Interaction

Oops, there are no PPI records of YJ11A_YEAST !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439, AND MASSSPECTROMETRY.
PubMed: 17287358