dbPTM

SYP1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYP1_YEAST
UniProt AC	P25623
Protein Name	Suppressor of yeast profilin deletion
Gene Name	SYP1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	870
Subcellular Localization	Bud neck . Concentrates at the mother-bud neck and at the tip of the forming bud. As the bud grows, abundant in the mother-bud neck and in the bud. At cytokinesis, found predominantly at the junction between the mother cell and the bud. Present at th
Protein Description	Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells..
Protein Sequence	MTEQRTKYADSILTTKSPYEATETIRIRLSQVKLLNKDFYLLFKELANLKRNYAQQLRKIIAENEDITKILNAQMIESNVLTPQEMSAFRFNSLGELRNVWDTVIEELKSDLKSSTEYYNTLDQQVVRELKESVENNTSWRESKDLHSKLSKNAASIEHYSKNNENSSHLEEARRQWDQQSPYLFELFETIDYNRLDTLKNCMLRFQTSFSDYLLNTTKECETVMTKFLAFEPQSEIDRFAKDASQYNFQLSSSSKEVVPNNASPASATGARPVSVSNGAANTEREKKSPQKDKRKSAFGNIGHRLASASSSLTHNDLMNNEFSDSTNNSSLKSKKSSHTLRSKVGSIFGRNKTKNKRQQQSSSNSHIQASITETPNNSSTRVSSTATSSIYQKQRRPTYSSSKSNNWTPGEASDTPPLPPHATPKNVDAPVTADTPPAQTFTPSEVPPSTPQQSSPPTAKEPDSSNLPKTVPISISQPPLQPQSKTKPLPVEPASPSISLPTATVDNQPSGQVDSRPLHIRAPALPPSRKQNFIHNRDSQLYDSLPNHGSGATPTSSSLSSIPQERPVSTLSSQITGELRELNPQATGSSTSLVGQSLFQHSSLDTSQFGLNASIAEVLNASFKDGMLQNSQLIGEIALNYLPNSVMNSPLPIGINLRINNGAKFEKVILNQAFIERVAPEEFKVNPSFIDSRTLGAIKYSIKEPIAPIVIHPVWRFESHQASVVLTVKMSPSLPDEISQIVIEDLVVFVNIDGANATSALSKPQGSFSKEKKRITWRFKEPVVLTRNGEGQRLIARFITDGLAHESAKGVITKFTISETDNVALPHSGAGSGITLTCQELDENNPFGGEWLDVNTKRTLTTGNYHGLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MTEQRTKYADSILTT CCHHHHHHHCCCCCC	18.28	28889911
11	Phosphorylation	QRTKYADSILTTKSP HHHHHHCCCCCCCCC	16.01	21440633
14	Phosphorylation	KYADSILTTKSPYEA HHHCCCCCCCCCCCC	30.43	24961812
15	Phosphorylation	YADSILTTKSPYEAT HHCCCCCCCCCCCCC	26.53	24961812
37	Acetylation	SQVKLLNKDFYLLFK HHHHHHCHHHHHHHH	49.54	24489116
37	Ubiquitination	SQVKLLNKDFYLLFK HHHHHHCHHHHHHHH	49.54	24961812
113	Ubiquitination	EELKSDLKSSTEYYN HHHHHHHHHCHHHHH	47.56	23749301
162	Ubiquitination	ASIEHYSKNNENSSH HHHHHHHHCCCCCHH	57.54	22817900
167	Phosphorylation	YSKNNENSSHLEEAR HHHCCCCCHHHHHHH	16.98	25533186
168	Phosphorylation	SKNNENSSHLEEARR HHCCCCCHHHHHHHH	43.61	25752575
200	Ubiquitination	YNRLDTLKNCMLRFQ CCHHHHHHHHHHHHH	50.63	23749301
208	Phosphorylation	NCMLRFQTSFSDYLL HHHHHHHCCHHHHHC	29.09	30377154
242	Ubiquitination	SEIDRFAKDASQYNF HHHHHHHHHHHHCCE	51.63	23749301
255	Phosphorylation	NFQLSSSSKEVVPNN CEECCCCCCCCCCCC	34.48	28889911
256	Ubiquitination	FQLSSSSKEVVPNNA EECCCCCCCCCCCCC	57.38	23749301
264	Phosphorylation	EVVPNNASPASATGA CCCCCCCCCCCCCCC	24.11	17330950
267	Phosphorylation	PNNASPASATGARPV CCCCCCCCCCCCCCC	29.73	17330950
269	Phosphorylation	NASPASATGARPVSV CCCCCCCCCCCCCCC	28.95	17330950
275	Phosphorylation	ATGARPVSVSNGAAN CCCCCCCCCCCCCCC	23.63	19823750
277	Phosphorylation	GARPVSVSNGAANTE CCCCCCCCCCCCCCH	23.26	19823750
283	Phosphorylation	VSNGAANTEREKKSP CCCCCCCCHHHHCCC	31.52	25005228
289	Phosphorylation	NTEREKKSPQKDKRK CCHHHHCCCCHHHHH	43.56	21440633
292	Ubiquitination	REKKSPQKDKRKSAF HHHCCCCHHHHHHCH	69.47	22817900
294	Ubiquitination	KKSPQKDKRKSAFGN HCCCCHHHHHHCHHH	69.62	22817900
296	Ubiquitination	SPQKDKRKSAFGNIG CCCHHHHHHCHHHHH	52.45	22817900
297	Phosphorylation	PQKDKRKSAFGNIGH CCHHHHHHCHHHHHH	32.63	24930733
308	Phosphorylation	NIGHRLASASSSLTH HHHHHHHHCCCCCCH	33.02	20377248
310	Phosphorylation	GHRLASASSSLTHND HHHHHHCCCCCCHHH	20.26	20377248
311	Phosphorylation	HRLASASSSLTHNDL HHHHHCCCCCCHHHH	29.14	22369663
312	Phosphorylation	RLASASSSLTHNDLM HHHHCCCCCCHHHHH	34.49	22369663
314	Phosphorylation	ASASSSLTHNDLMNN HHCCCCCCHHHHHCC	22.15	22369663
324	Phosphorylation	DLMNNEFSDSTNNSS HHHCCCCCCCCCCCC	25.19	23749301
326	Phosphorylation	MNNEFSDSTNNSSLK HCCCCCCCCCCCCCC	31.66	22369663
327	Phosphorylation	NNEFSDSTNNSSLKS CCCCCCCCCCCCCCC	43.33	21440633
330	Phosphorylation	FSDSTNNSSLKSKKS CCCCCCCCCCCCCCC	38.83	22369663
331	Phosphorylation	SDSTNNSSLKSKKSS CCCCCCCCCCCCCCH	41.77	22369663
334	Phosphorylation	TNNSSLKSKKSSHTL CCCCCCCCCCCHHHH	51.08	28889911
347	Phosphorylation	TLRSKVGSIFGRNKT HHHHHHHHHHCCCCC	20.10	19823750
362	Phosphorylation	KNKRQQQSSSNSHIQ CCHHHHHCCCCCCEE	31.25	30377154
363	Phosphorylation	NKRQQQSSSNSHIQA CHHHHHCCCCCCEEE	29.24	19779198
364	Phosphorylation	KRQQQSSSNSHIQAS HHHHHCCCCCCEEEE	47.82	28889911
366	Phosphorylation	QQQSSSNSHIQASIT HHHCCCCCCEEEEEE	24.74	28889911
371	Phosphorylation	SNSHIQASITETPNN CCCCEEEEEEECCCC	17.42	21440633
373	Phosphorylation	SHIQASITETPNNSS CCEEEEEEECCCCCC	31.17	23749301
375	Phosphorylation	IQASITETPNNSSTR EEEEEEECCCCCCCC	23.75	22369663
379	Phosphorylation	ITETPNNSSTRVSST EEECCCCCCCCEEEC	39.46	22369663
380	Phosphorylation	TETPNNSSTRVSSTA EECCCCCCCCEEECC	23.50	22369663
381	Phosphorylation	ETPNNSSTRVSSTAT ECCCCCCCCEEECCC	34.61	22369663
384	Phosphorylation	NNSSTRVSSTATSSI CCCCCCEEECCCHHH	20.76	22369663
385	Phosphorylation	NSSTRVSSTATSSIY CCCCCEEECCCHHHH	21.14	22369663
386	Phosphorylation	SSTRVSSTATSSIYQ CCCCEEECCCHHHHH	26.84	22369663
388	Phosphorylation	TRVSSTATSSIYQKQ CCEEECCCHHHHHCC	24.09	22369663
389	Phosphorylation	RVSSTATSSIYQKQR CEEECCCHHHHHCCC	16.57	22369663
390	Phosphorylation	VSSTATSSIYQKQRR EEECCCHHHHHCCCC	22.44	22369663
392	Phosphorylation	STATSSIYQKQRRPT ECCCHHHHHCCCCCC	16.17	21440633
394	Ubiquitination	ATSSIYQKQRRPTYS CCHHHHHCCCCCCCC	28.88	23749301
399	Phosphorylation	YQKQRRPTYSSSKSN HHCCCCCCCCCCCCC	33.94	28889911
400	Phosphorylation	QKQRRPTYSSSKSNN HCCCCCCCCCCCCCC	14.83	19779198
401	Phosphorylation	KQRRPTYSSSKSNNW CCCCCCCCCCCCCCC	30.52	28889911
402	Phosphorylation	QRRPTYSSSKSNNWT CCCCCCCCCCCCCCC	31.22	21440633
403	Phosphorylation	RRPTYSSSKSNNWTP CCCCCCCCCCCCCCC	33.88	28889911
404	Ubiquitination	RPTYSSSKSNNWTPG CCCCCCCCCCCCCCC	60.18	23749301
405	Phosphorylation	PTYSSSKSNNWTPGE CCCCCCCCCCCCCCC	37.03	22369663
409	Phosphorylation	SSKSNNWTPGEASDT CCCCCCCCCCCCCCC	24.44	29136822
414	Phosphorylation	NWTPGEASDTPPLPP CCCCCCCCCCCCCCC	37.40	25752575
416	Phosphorylation	TPGEASDTPPLPPHA CCCCCCCCCCCCCCC	25.06	21551504
424	Phosphorylation	PPLPPHATPKNVDAP CCCCCCCCCCCCCCC	31.59	29136822
433	Phosphorylation	KNVDAPVTADTPPAQ CCCCCCCCCCCCCCC	20.11	28152593
436	Phosphorylation	DAPVTADTPPAQTFT CCCCCCCCCCCCCCC	28.80	20377248
441	Phosphorylation	ADTPPAQTFTPSEVP CCCCCCCCCCCCCCC	31.42	23749301
443	Phosphorylation	TPPAQTFTPSEVPPS CCCCCCCCCCCCCCC	29.32	23749301
445	Phosphorylation	PAQTFTPSEVPPSTP CCCCCCCCCCCCCCC	48.44	21440633
450	Phosphorylation	TPSEVPPSTPQQSSP CCCCCCCCCCCCCCC	46.80	20377248
451	Phosphorylation	PSEVPPSTPQQSSPP CCCCCCCCCCCCCCC	30.78	20377248
455	Phosphorylation	PPSTPQQSSPPTAKE CCCCCCCCCCCCCCC	39.29	25521595
456	Phosphorylation	PSTPQQSSPPTAKEP CCCCCCCCCCCCCCC	30.47	25521595
459	Phosphorylation	PQQSSPPTAKEPDSS CCCCCCCCCCCCCCC	54.46	20377248
465	Phosphorylation	PTAKEPDSSNLPKTV CCCCCCCCCCCCCCC	31.66	21440633
466	Phosphorylation	TAKEPDSSNLPKTVP CCCCCCCCCCCCCCC	50.17	21440633
470	Ubiquitination	PDSSNLPKTVPISIS CCCCCCCCCCCCEEC	66.38	23749301
485	Phosphorylation	QPPLQPQSKTKPLPV CCCCCCCCCCCCCCC	49.31	27214570
487	Phosphorylation	PLQPQSKTKPLPVEP CCCCCCCCCCCCCCC	43.04	23607784
496	Phosphorylation	PLPVEPASPSISLPT CCCCCCCCCCEECCC	29.87	17330950
498	Phosphorylation	PVEPASPSISLPTAT CCCCCCCCEECCCCE	23.47	25533186
500	Phosphorylation	EPASPSISLPTATVD CCCCCCEECCCCEEC	32.41	17330950
503	Phosphorylation	SPSISLPTATVDNQP CCCEECCCCEECCCC	40.01	23607784
505	Phosphorylation	SISLPTATVDNQPSG CEECCCCEECCCCCC	30.76	21551504
511	Phosphorylation	ATVDNQPSGQVDSRP CEECCCCCCCCCCCC	31.90	29688323
543	Phosphorylation	HNRDSQLYDSLPNHG CCCCCHHHHCCCCCC	8.89	19779198
545	Phosphorylation	RDSQLYDSLPNHGSG CCCHHHHCCCCCCCC	31.97	19779198
551	Phosphorylation	DSLPNHGSGATPTSS HCCCCCCCCCCCCCC	20.08	19779198
554	Phosphorylation	PNHGSGATPTSSSLS CCCCCCCCCCCCCCC	30.53	19779198
556	Phosphorylation	HGSGATPTSSSLSSI CCCCCCCCCCCCCCC	36.57	19779198
557	Phosphorylation	GSGATPTSSSLSSIP CCCCCCCCCCCCCCC	21.09	19779198
558	Phosphorylation	SGATPTSSSLSSIPQ CCCCCCCCCCCCCCC	37.46	21440633
559	Phosphorylation	GATPTSSSLSSIPQE CCCCCCCCCCCCCCC	31.85	21440633
561	Phosphorylation	TPTSSSLSSIPQERP CCCCCCCCCCCCCCC	28.33	19779198
562	Phosphorylation	PTSSSLSSIPQERPV CCCCCCCCCCCCCCC	43.51	23749301
570	Phosphorylation	IPQERPVSTLSSQIT CCCCCCCCCHHHHHH	26.72	23749301
571	Phosphorylation	PQERPVSTLSSQITG CCCCCCCCHHHHHHH	30.78	19779198
573	Phosphorylation	ERPVSTLSSQITGEL CCCCCCHHHHHHHHH	21.93	23607784
574	Phosphorylation	RPVSTLSSQITGELR CCCCCHHHHHHHHHH	28.81	23607784
577	Phosphorylation	STLSSQITGELRELN CCHHHHHHHHHHHHC	19.57	27738172
689	Phosphorylation	EEFKVNPSFIDSRTL HHHCCCHHHCCCCCC	29.63	21440633
810	Ubiquitination	GLAHESAKGVITKFT CCCCCCCCCCEEEEE	64.09	24961812
860	Phosphorylation	LDVNTKRTLTTGNYH EECCCCEEECCCCCC	29.97	21440633
862	Phosphorylation	VNTKRTLTTGNYHGL CCCCEEECCCCCCCC	31.85	21440633

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 SYP1_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYP1_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 SYP1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EDE1_YEAST	EDE1	physical	16554755
EDE1_YEAST	EDE1	physical	16429126
PST2_YEAST	PST2	physical	18467557
HNM1_YEAST	HNM1	physical	18467557
WSC2_YEAST	WSC2	physical	18467557
FLC1_YEAST	FLC1	physical	18467557
SYP1_YEAST	SYP1	physical	18467557
ENT2_YEAST	ENT2	physical	18467557
ATC5_YEAST	DNF1	physical	18467557
PDR12_YEAST	PDR12	physical	18467557
LAS17_YEAST	LAS17	physical	18467557
SHS1_YEAST	SHS1	physical	18467557
MYO5_YEAST	MYO5	physical	18467557
SFK1_YEAST	SFK1	physical	18467557
CDC11_YEAST	CDC11	physical	18467557
GPA2_YEAST	GPA2	physical	18467557
AP18B_YEAST	YAP1802	physical	18467557
YG3A_YEAST	YGR130C	physical	18467557
VRP1_YEAST	VRP1	physical	18467557
MID2_YEAST	MID2	physical	18467557
LSB3_YEAST	LSB3	physical	18467557
EDE1_YEAST	EDE1	physical	19713939
SYP1_YEAST	SYP1	physical	19713939
MID2_YEAST	MID2	physical	19713939
2A5D_YEAST	RTS1	genetic	18791237
PST2_YEAST	PST2	physical	22615397
SLA1_YEAST	SLA1	physical	26179915
FKS1_YEAST	FKS1	physical	26179915
EDE1_YEAST	EDE1	physical	26179915
MID2_YEAST	MID2	physical	28701344
SNC1_YEAST	SNC1	physical	28701344

Drug and Disease Associations

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

Regulatory Network of SYP1_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-267; SER-312;THR-314; SER-331; THR-388; SER-496; SER-500; THR-577; SER-689 ANDTHR-862, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269; SER-311 ANDTHR-314, AND MASS SPECTROMETRY.	17563356 [Abstract]
"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-264; SER-496 ANDSER-500, AND MASS SPECTROMETRY.	17330950 [Abstract]