CAN1_YEAST - dbPTM
CAN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAN1_YEAST
UniProt AC P04817
Protein Name Arginine permease CAN1
Gene Name CAN1 {ECO:0000303|PubMed:3327612}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 590
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endosome membrane
Multi-pass membrane protein . Recycled via the retromer-mediated pathway (PubMed:21880895). Requires phosphatidyl ethanolamine (PE) for localization and exclusively associated with lip
Protein Description High-affinity permease for arginine. [PubMed: 8436127]
Protein Sequence MTNSKEDADIEEKHMYNEPVTTLFHDVEASQTHHRRGSIPLKDEKSKELYPLRSFPTRVNGEDTFSMEDGIGDEDEGEVQNAEVKRELKQRHIGMIALGGTIGTGLFIGLSTPLTNAGPVGALISYLFMGSLAYSVTQSLGEMATFIPVTSSFTVFSQRFLSPAFGAANGYMYWFSWAITFALELSVVGQVIQFWTYKVPLAAWISIFWVIITIMNLFPVKYYGEFEFWVASIKVLAIIGFLIYCFCMVCGAGVTGPVGFRYWRNPGAWGPGIISKDKNEGRFLGWVSSLINAAFTFQGTELVGITAGEAANPRKSVPRAIKKVVFRILTFYIGSLLFIGLLVPYNDPKLTQSTSYVSTSPFIIAIENSGTKVLPHIFNAVILTTIISAANSNIYVGSRILFGLSKNKLAPKFLSRTTKGGVPYIAVFVTAAFGALAYMETSTGGDKVFEWLLNITGVAGFFAWLFISISHIRFMQALKYRGISRDELPFKAKLMPGLAYYAATFMTIIIIIQGFTAFAPKFNGVSFAAAYISIFLFLAVWILFQCIFRCRFIWKIGDVDIDSDRRDIEAIVWEDHEPKTFWDKFWNVVA
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
2Phosphorylation------MTNSKEDAD
------CCCCHHHCC		48.4719795423
4Phosphorylation----MTNSKEDADIE
----CCCCHHHCCHH		28.4023749301
5Ubiquitination---MTNSKEDADIEE
---CCCCHHHCCHHH		62.7823793018
13UbiquitinationEDADIEEKHMYNEPV
HHCCHHHHHCCCCCC		22.3824961812
21PhosphorylationHMYNEPVTTLFHDVE
HCCCCCCEEEEECHH		28.6224961812
22PhosphorylationMYNEPVTTLFHDVEA
CCCCCCEEEEECHHH		27.8824961812
30PhosphorylationLFHDVEASQTHHRRG
EEECHHHHHHCCCCC		23.3124961812
32PhosphorylationHDVEASQTHHRRGSI
ECHHHHHHCCCCCCC		19.7024961812
38PhosphorylationQTHHRRGSIPLKDEK
HHCCCCCCCCCCCCC		21.1522369663
42UbiquitinationRRGSIPLKDEKSKEL
CCCCCCCCCCCCCCC		59.4923749301
46PhosphorylationIPLKDEKSKELYPLR
CCCCCCCCCCCEECC		29.3424961812
47UbiquitinationPLKDEKSKELYPLRS
CCCCCCCCCCEECCC		63.9123749301
54PhosphorylationKELYPLRSFPTRVNG
CCCEECCCCCCEECC		43.17-
64PhosphorylationTRVNGEDTFSMEDGI
CEECCCCCEECCCCC		17.2024961812
66PhosphorylationVNGEDTFSMEDGIGD
ECCCCCEECCCCCCC		24.2923749301
85UbiquitinationEVQNAEVKRELKQRH
CCCHHHHHHHHHHCC		31.4923749301
480PhosphorylationRFMQALKYRGISRDE
HHHHHHHHCCCCCCC		18.2127017623
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 CAN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAN1_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 CAN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUR7_YEASTSUR7physical
15536122
GAP1_YEASTGAP1genetic
16941010
SHR3_YEASTSHR3physical
16093310
SEC63_YEASTSEC63physical
16093310
ERP2_YEASTERP2physical
16093310
UIP3_YEASTUIP3physical
16093310
ERD2_YEASTERD2physical
16093310
CSG2_YEASTCSG2physical
16093310
PHO88_YEASTPHO88physical
16093310
ALG1_YEASTALG1physical
16093310
MKAR_YEASTIFA38physical
16093310
PBN1_YEASTPBN1physical
16093310
ADY2_YEASTADY2physical
16093310
PMP1_YEASTPMP1physical
16093310
ELO2_YEASTELO2physical
16093310
YCV1_YEASTYCR061Wphysical
16093310
FET5_YEASTFET5physical
16093310
MST27_YEASTMST27physical
16093310
MSB2_YEASTMSB2physical
16093310
ERV29_YEASTERV29physical
16093310
YHE2_YEASTYHL042Wphysical
16093310
NSG1_YEASTNSG1physical
16093310
YHU0_YEASTYHR140Wphysical
16093310
CHS7_YEASTCHS7physical
16093310
SNL1_YEASTSNL1physical
16093310
VDAC2_YEASTPOR2physical
16093310
AXL2_YEASTAXL2physical
16093310
OST1_YEASTOST1physical
16093310
GWT1_YEASTGWT1physical
16093310
PHO86_YEASTPHO86physical
16093310
ELO1_YEASTELO1physical
16093310
SPC1_YEASTSPC1physical
16093310
STE24_YEASTSTE24physical
16093310
YET1_YEASTYET1physical
16093310
SRPB_YEASTSRP102physical
16093310
GAS2_YEASTGAS2physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
CUE1_YEASTCUE1physical
16093310
GOT1_YEASTGOT1physical
16093310
ESBP6_YEASTESBP6physical
16093310
GAS4_YEASTGAS4physical
16093310
ERP4_YEASTERP4physical
16093310
PNS1_YEASTPNS1physical
16093310
GPI2_YEASTGPI2physical
16093310
ALG5_YEASTALG5physical
16093310
VATL2_YEASTVMA11physical
16093310
DPH7_YEASTRRT2physical
21880895
HSP71_YEASTSSA1physical
22940862
HAC1_YEASTHAC1genetic
28228255
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAN1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-38, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.

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