ALY1_YEAST - dbPTM
ALY1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALY1_YEAST
UniProt AC P36117
Protein Name Arrestin-related trafficking adapter 6
Gene Name ALY1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 915
Subcellular Localization Cytoplasm .
Protein Description May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli..
Protein Sequence MLQFNTENDTVAPVFPMEQDINAAPDAVPLVQTTTLQVFVKLAEPIVFLKGFETNGLSEIAPSILRGSLIVRVLKPNKLKSISITFKGISRTEWPEGIPPKREEFSDVETVVNHTWPFYQADDGMNSFTLEHHSSNNSSNRPSMSDEDYLLEKSGASVYIPPTAEPPKDNSNLSLDAYERNSLSSDNLSNKPVSSDVSHDDSKLLAIQKTPLPSSSRRGSVPANFHGNSLSPHTFISDLFTKTFSNSGATPSPEQEDNYLTPSKDSKEVFIFRPGDYIYTFEQPISQSYPESIKANFGSVEYKLSIDIERFGAFKSTIHTQLPIKVVRLPSDGSVEETEAIAISKDWKDLLHYDVVIFSKEIVLNAFLPIDFHFAPLDKVTLHRIRIYLTESMEYTCNSNGNHEKARRLEPTKKFLLAEHNGPKLPHIPAGSNPLKAKNRGNILLDEKSGDLVNKDFQFEVFVPSKFTNSIRLHPDTNYDKIKAHHWIKICLRLSKKYGDNRKHFEISIDSPIHILNQLCSHANTLLPSYESHFQYCDEDGNFAPAADQQNYASHHDSNIFFPKEVLSSPVLSPNVQKMNIRIPSDLPVVRNRAESVKKSKSDNTSKKNDQSSNVFASKQLVANIYKPNQIPRELTSPQALPLSPITSPILNYQPLSNSPPPDFDFDLAKRGAADSHAIPVDPPSYFDVLKADGIELPYYDTSSSKIPELKLNKSRETLASIEEDSFNGWSQIDDLSDEDDNDGDIASGFNFKLSTSAPSENVNSHTPILQSLNMSLDGRKKNRASLHATSVLPSTIRQNNQHFNDINQMLGSSDEDAFPKSQSLNFNKKLPILKINDNVIQSNSNSNNRVDNPEDTVDSSVDITAFYDPRMSSDSKFDWEVSKNHVDPAAYSVNVASENRVLDDFKKAFREKRK
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
81PhosphorylationLKPNKLKSISITFKG
CCCCCCEEEEEEEEC		31.8227017623
163PhosphorylationASVYIPPTAEPPKDN
CCEECCCCCCCCCCC		37.9922369663
171PhosphorylationAEPPKDNSNLSLDAY
CCCCCCCCCCCCCHH		49.6422369663
174PhosphorylationPKDNSNLSLDAYERN
CCCCCCCCCCHHHHC		28.5822369663
178PhosphorylationSNLSLDAYERNSLSS
CCCCCCHHHHCCCCC		18.3223749301
182PhosphorylationLDAYERNSLSSDNLS
CCHHHHCCCCCCCCC		35.5322369663
184PhosphorylationAYERNSLSSDNLSNK
HHHHCCCCCCCCCCC		35.1522369663
185PhosphorylationYERNSLSSDNLSNKP
HHHCCCCCCCCCCCC		35.4922369663
189PhosphorylationSLSSDNLSNKPVSSD
CCCCCCCCCCCCCCC		49.4120377248
194PhosphorylationNLSNKPVSSDVSHDD
CCCCCCCCCCCCCCC		29.3722369663
195PhosphorylationLSNKPVSSDVSHDDS
CCCCCCCCCCCCCCH		42.1222369663
198PhosphorylationKPVSSDVSHDDSKLL
CCCCCCCCCCCHHEE		26.6222369663
202PhosphorylationSDVSHDDSKLLAIQK
CCCCCCCHHEEEEEE		31.1222369663
214PhosphorylationIQKTPLPSSSRRGSV
EEECCCCCCCCCCCC		48.9424961812
215PhosphorylationQKTPLPSSSRRGSVP
EECCCCCCCCCCCCC		26.4024961812
216PhosphorylationKTPLPSSSRRGSVPA
ECCCCCCCCCCCCCC		30.2724961812
220PhosphorylationPSSSRRGSVPANFHG
CCCCCCCCCCCCCCC		24.1021440633
229PhosphorylationPANFHGNSLSPHTFI
CCCCCCCCCCCCCHH		34.5119779198
231PhosphorylationNFHGNSLSPHTFISD
CCCCCCCCCCCHHHH		17.9223749301
242UbiquitinationFISDLFTKTFSNSGA
HHHHHHHHHCCCCCC		39.9924961812
245PhosphorylationDLFTKTFSNSGATPS
HHHHHHCCCCCCCCC		35.0027017623
247PhosphorylationFTKTFSNSGATPSPE
HHHHCCCCCCCCCHH		28.7127017623
252PhosphorylationSNSGATPSPEQEDNY
CCCCCCCCHHHCCCC		36.3923749301
325AcetylationIHTQLPIKVVRLPSD
EECCCCEEEEECCCC		32.5124489116
379UbiquitinationFHFAPLDKVTLHRIR
EEECCCCCEEEEEEE		44.8123749301
413UbiquitinationARRLEPTKKFLLAEH
HHHCCCCHHHHHHCC		52.8522817900
414UbiquitinationRRLEPTKKFLLAEHN
HHCCCCHHHHHHCCC		43.6623749301
481UbiquitinationHPDTNYDKIKAHHWI
CCCCCHHHHHHHHHH		35.4323749301
564UbiquitinationDSNIFFPKEVLSSPV
CCCCCCCHHHHCCCC		56.1317644757
568PhosphorylationFFPKEVLSSPVLSPN
CCCHHHHCCCCCCCC		37.4629136822
569PhosphorylationFPKEVLSSPVLSPNV
CCHHHHCCCCCCCCC		18.1822369663
573PhosphorylationVLSSPVLSPNVQKMN
HHCCCCCCCCCEECC		18.0521082442
578UbiquitinationVLSPNVQKMNIRIPS
CCCCCCEECCEECCC		29.6324961812
585PhosphorylationKMNIRIPSDLPVVRN
ECCEECCCCCHHHHH		49.7821440633
596PhosphorylationVVRNRAESVKKSKSD
HHHHHHHHHHHCCCC		37.9524961812
607UbiquitinationSKSDNTSKKNDQSSN
CCCCCCCCCCCCCCC		54.2617644757
608UbiquitinationKSDNTSKKNDQSSNV
CCCCCCCCCCCCCCC		66.5717644757
619UbiquitinationSSNVFASKQLVANIY
CCCCHHHHHHHHHCC		44.1917644757
627UbiquitinationQLVANIYKPNQIPRE
HHHHHCCCCCCCCCC		33.4223749301
644PhosphorylationSPQALPLSPITSPIL
CCCCCCCCCCCCCCC		16.5923749301
647PhosphorylationALPLSPITSPILNYQ
CCCCCCCCCCCCCCC		31.6628889911
648PhosphorylationLPLSPITSPILNYQP
CCCCCCCCCCCCCCC		15.6328889911
653PhosphorylationITSPILNYQPLSNSP
CCCCCCCCCCCCCCC		14.2023749301
657PhosphorylationILNYQPLSNSPPPDF
CCCCCCCCCCCCCCC		41.7823749301
659PhosphorylationNYQPLSNSPPPDFDF
CCCCCCCCCCCCCCC		35.0923749301
685PhosphorylationAIPVDPPSYFDVLKA
CCCCCCCCHHHHEEC		43.7624961812
686PhosphorylationIPVDPPSYFDVLKAD
CCCCCCCHHHHEECC		15.0124961812
706UbiquitinationYYDTSSSKIPELKLN
EECCCCCCCCCCCCC		65.3123749301
757PhosphorylationFNFKLSTSAPSENVN
EEEEECCCCCCCCCC		34.5028889911
767PhosphorylationSENVNSHTPILQSLN
CCCCCCCCHHHHHHH		16.3123749301
786PhosphorylationGRKKNRASLHATSVL
CCCCCCHHHHHHHCC		19.9023749301
813PhosphorylationDINQMLGSSDEDAFP
HHHHHCCCCCCCCCC		30.5622369663
814PhosphorylationINQMLGSSDEDAFPK
HHHHCCCCCCCCCCH		43.1322369663
822PhosphorylationDEDAFPKSQSLNFNK
CCCCCCHHHCCCCCC		25.8222369663
824PhosphorylationDAFPKSQSLNFNKKL
CCCCHHHCCCCCCCC		32.1622369663
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALY1_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 ALY1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
20489023
SEC7_YEASTSEC7physical
20489023
ALY2_YEASTALY2genetic
20739461
GAP1_YEASTGAP1physical
20739461
LST4_YEASTLST4genetic
20739461
CLH_YEASTCHC1physical
20739461
AP1B1_YEASTAPL2physical
20739461
ALY2_YEASTALY2genetic
20956561
PP2B1_YEASTCNA1physical
23824189
RSP5_YEASTRSP5physical
23824189
BMH1_YEASTBMH1physical
23824189
BMH2_YEASTBMH2physical
23824189
RHO1_YEASTRHO1physical
26459639
ALY2_YEASTALY2genetic
26459639
LDB19_YEASTLDB19genetic
26459639
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALY1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-189; SER-569; SER-573;SER-585 AND SER-657, AND MASS SPECTROMETRY.

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