dbPTM

YB11A_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YB11A_YEAST
UniProt AC	Q12266
Protein Name	Transposon Ty1-BL Gag polyprotein
Gene Name	TY1A-BL
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	MESQQLSQHSPIFHGSACASVTSKEVQTTQDPLDISASKTEECEKVSTQANSQQPTTPPSSAVPENHHHASPQAAQVPLPQNGPYPQQRMMNTQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFAPSQFLPPWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLATLHYNGSTPADAFEAEVTNILDRLNNNGIPINNKVACQFIMRGLSGEYKFLPYARHRCIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTFNNSPGPDNDLIRGSTTEPIQLKNTHDLHLRPGTY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MESQQLSQHS -----CCCCCHHCCC	23.17	28889911
7	Phosphorylation	-MESQQLSQHSPIFH -CCCCCHHCCCCCCC	22.85	24961812
10	Phosphorylation	SQQLSQHSPIFHGSA CCCHHCCCCCCCCCC	16.44	28889911
16	Phosphorylation	HSPIFHGSACASVTS CCCCCCCCCCCCCCC	16.17	23749301
20	Phosphorylation	FHGSACASVTSKEVQ CCCCCCCCCCCCCCC	26.30	23749301
22	Phosphorylation	GSACASVTSKEVQTT CCCCCCCCCCCCCCC	31.42	24961812
23	Phosphorylation	SACASVTSKEVQTTQ CCCCCCCCCCCCCCC	25.35	23749301
36	Phosphorylation	TQDPLDISASKTEEC CCCCCCCCCCCCHHH	26.59	29688323
38	Phosphorylation	DPLDISASKTEECEK CCCCCCCCCCHHHHH	33.06	21440633
40	Phosphorylation	LDISASKTEECEKVS CCCCCCCCHHHHHHH	34.22	21440633
47	Phosphorylation	TEECEKVSTQANSQQ CHHHHHHHHCCCCCC	26.35	28889911
48	Phosphorylation	EECEKVSTQANSQQP HHHHHHHHCCCCCCC	34.39	28889911
52	Phosphorylation	KVSTQANSQQPTTPP HHHHCCCCCCCCCCC	32.96	21440633
56	Phosphorylation	QANSQQPTTPPSSAV CCCCCCCCCCCHHCC	47.82	28889911
57	Phosphorylation	ANSQQPTTPPSSAVP CCCCCCCCCCHHCCC	39.63	28889911
60	Phosphorylation	QQPTTPPSSAVPENH CCCCCCCHHCCCCCC	31.94	17330950
61	Phosphorylation	QPTTPPSSAVPENHH CCCCCCHHCCCCCCC	38.77	17330950
71	Phosphorylation	PENHHHASPQAAQVP CCCCCCCCCCHHCCC	17.12	17330950
139	Phosphorylation	QYPQYVGTHLNTPSP CCCCCCCCCCCCCCC	17.10	18407956
143	Phosphorylation	YVGTHLNTPSPESGN CCCCCCCCCCCCCCC	31.35	28889911
145	Phosphorylation	GTHLNTPSPESGNSF CCCCCCCCCCCCCCC	38.98	28889911
160	Phosphorylation	PDSSSAKSNMTSTNQ CCCHHCCCCCCCCCC	31.39	21440633
163	Phosphorylation	SSAKSNMTSTNQHVR HHCCCCCCCCCCCCC	36.33	19795423
164	Phosphorylation	SAKSNMTSTNQHVRP HCCCCCCCCCCCCCC	18.00	19795423
165	Phosphorylation	AKSNMTSTNQHVRPP CCCCCCCCCCCCCCC	29.72	19795423
250	Ubiquitination	VDYTDIMKILSKSIN CCHHHHHHHHHHHHH	40.61	24961812
318	Phosphorylation	QFIMRGLSGEYKFLP HHHHCCCCCCCCCHH	32.19	20377248
358	Phosphorylation	QESKRNKSTYRRSPS HHHHHCCCCCCCCCC	33.93	19823750
359	Phosphorylation	ESKRNKSTYRRSPSD HHHHCCCCCCCCCCC	23.74	19823750
360	Phosphorylation	SKRNKSTYRRSPSDE HHHCCCCCCCCCCCC	15.89	19823750
363	Phosphorylation	NKSTYRRSPSDEKKD CCCCCCCCCCCCCCC	21.54	17287358
365	Phosphorylation	STYRRSPSDEKKDSR CCCCCCCCCCCCCCC	60.70	17287358
371	Phosphorylation	PSDEKKDSRTYTNTT CCCCCCCCCCCCCCC	35.09	28889911
377	Phosphorylation	DSRTYTNTTKPKSIT CCCCCCCCCCCCCCC	28.53	28889911
382	Phosphorylation	TNTTKPKSITRNSQK CCCCCCCCCCCCCCC	37.41	21440633
404	Phosphorylation	TARAHNVSTFNNSPG HHHHHCCCCCCCCCC	32.38	29136822
405	Phosphorylation	ARAHNVSTFNNSPGP HHHHCCCCCCCCCCC	26.54	29136822
409	Phosphorylation	NVSTFNNSPGPDNDL CCCCCCCCCCCCCCC	32.13	22369663
420	Phosphorylation	DNDLIRGSTTEPIQL CCCCCCCCCCCCEEC	23.47	22369663
421	Phosphorylation	NDLIRGSTTEPIQLK CCCCCCCCCCCEECC	37.69	24909858
422	Phosphorylation	DLIRGSTTEPIQLKN CCCCCCCCCCEECCC	41.27	22369663
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, ...)

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 YB11A_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YB11A_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 YB11A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YB11A_YEAST !!

Drug and Disease Associations

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

Regulatory Network of YB11A_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-409, AND MASSSPECTROMETRY.	17330950 [Abstract]