CCH1_YEAST - dbPTM
CCH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCH1_YEAST
UniProt AC P50077
Protein Name Calcium-channel protein CCH1
Gene Name CCH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 2039
Subcellular Localization Cell membrane . Membrane
Multi-pass membrane protein .
Protein Description Voltage-gated, high-affinity calcium channel involved in calcium influx in response to some environmental stresses as well as exposure to mating pheromones. Functions together with MID1 to ensure that adequate levels of Ca(2+) are supplied to PMR1 to sustain secretion and growth. Required for growth in low-calcium environments..
Protein Sequence MQGRKRTLTEPFEPNTNPFGDNAAVMTENVEDNSETDGNRLESKPQALVPPALNIVPPESSIHSTEEKKGDEYNGNDKDSSLISNIFRTRVGRSSHENLSRPKLSLKTASFGAAESSRRNVSPSTKSAKSSSQYIDLNDERLRRRSFSSYSRSSSRRVSNSPSSTDRPPRSAKVLSLIAADDMDDFEDLQKGFKSAIDEEGLTWLPQLKSEKSRPVSDVGEDRGEGEQESIPDVHTPNVGASATPGSIHLTPEPAQNGSVSEGLEGSINNSRKKPSPKFFHHLSPQKEDKDQTEVIEYAEDILDFETLQRKLESRPFVLYGHSLGVFSPTNPLRIKIARFLLHRRYSLLYNTLLTFYAILLAIRTYNPHNVVFLYRFSNWTDYFIFILSACFTGNDIAKIIAFGFWDDSEMFKAYGREYKSILQRSGIMKLYIYLREKYGRKLIDFIIPFRIISPGEETKYQRSSLSTSLTKPYGAKENQRPFGTPRAFARSSWNRIDLVSSVSFWLGMFLSIKSYDTKTGIRIFKPLAILRILRLVNVDTGMPSILRGLKYGIPQLVNVSSMLVYFWIFFGILGVQIFQGSFRRQCVWFNPEDPTDTYQYDMQFCGGYLDPVTKRKQNYIYEDGSEGSVSKGFLCPQYSKCVSNANPYNGRISFDNIVNSMELVFVIMSANTFTDLMYYTMDSDEMAACLFFIVCIFVLTIWLLNLLIAVLVSSFEIANEEYKKKKFIYGSRKTGYVARIVTGYWKYFKLKANQTKFPNWSQKGLAIYSHVEFIFVILIICDIGMRASVKVSTSANCNNILLKTDRGISIVLFIESLARLVLYLPNMWKFLTKPSYVYDFIISIITLVISCLAVEGVLGHMYAWLSIFHISRFYRVIISFNLTKKLWKQILSNGVMIWNLSSFYFFFTFLVAIIMAVYFEGVIPPEEMADQPFGMYSLPNSFLSLFIIGSTENWTDILYALQKHSPNISSTFFCSVFFIIWFLLSNSVILNIFIALISESMEVKEEEKRPQQIKHYLKFVYPQKIQEYTHASLVARIRKKFFGGHRNEDTRDFKQFLMRGTAIMNIAQNMGELADEFKEPPSENLFKKGLSKLTIGVPSLKRLRMFANNPFYKNSDVVFTETNDINGRTYILELNEYEDEKLDYLKKYPLFNYSYYFFSPQHRFRRFCQRLVPPSTGKRTDGSRFFEDSTDLYNKRSYFHHIERDVFVFIFALATILLIVCSCYVTPLYRMHHKMGTWNWSSALDCAFIGAFSIEFIVKTVADGFIYSPNAYLRNPWNFIDFCVLISMWINLIAYLKNNGNLSRIFKGLTALRALRCLTISNTARQTFNLVMFDGLNKIFEAGLISLSLLFPFTVWGLSIFKGRLGTCNDGSLGRADCYNEYSNSVFQWDIMSPRVYQQPYLHLDSFASAFSSLYQIISLEGWVDLLENMMNSSGIGTPATVMGSAGNALFLVLFNFLSMVFILNLFVSFIVNNQARTTGSAYFTIEEKAWLESQKLLSQAKPKAIPNLIELSRVRQFFYQLAVEKKNFYYASFLQVVLYLHIIMLLSRSYNPGNLIGYQGVYFMFSTSVFLIQEALHMCGEGPRLYFRQKWNSIRLSIIIIAFIMNAVAFHVPASHYWFHNIKGFFLLVIFLFIIPQNDTLTELLETAMASLPPILSLTYTWGVLFLVYAIALNQIFGLTRLGSNTTDNINFRTVIKSMIVLFRCSFGEGWNYIMADLTVSEPYCSSDDNSTYTDCGSETYAYLLLMSWNIISMYIFVNMFVSLIIGNFSYVYRSGGSRSGINRSEIKKYIEAWSKFDTDGTGELELSYLPRIMHSFDGPLSFKIWEGRLTIKSLVENYMEVNPDDPYDVKIDLIGLNKELNTIDKAKIIQRKLQYRRFVQSIHYTNAYNGCIRFSDLLLQIPLYTAYSARECLGIDQYVHHLYILGKVDKYLENQRNFDVLEMVVTRWKFHCRMKRTIEPEWDVKDPTVSSHISNINVNLEPAPGILEREPIATPRMDYGVNNFMWSPRMNQDSTMEPPEEPIDNNDDSANDLIDR
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
60PhosphorylationLNIVPPESSIHSTEE
CCCCCCHHHCCCCCC		40.1321551504
61PhosphorylationNIVPPESSIHSTEEK
CCCCCHHHCCCCCCC		23.7421551504
64PhosphorylationPPESSIHSTEEKKGD
CCHHHCCCCCCCCCC		35.5221551504
65PhosphorylationPESSIHSTEEKKGDE
CHHHCCCCCCCCCCC		33.7221551504
94PhosphorylationFRTRVGRSSHENLSR
HHHCCCCCCCCCCCC		30.0730377154
95PhosphorylationRTRVGRSSHENLSRP
HHCCCCCCCCCCCCC		33.2028889911
107UbiquitinationSRPKLSLKTASFGAA
CCCCCCCCHHHHCCH		38.3724961812
108PhosphorylationRPKLSLKTASFGAAE
CCCCCCCHHHHCCHH		32.5921440633
110PhosphorylationKLSLKTASFGAAESS
CCCCCHHHHCCHHHH		29.4622369663
116PhosphorylationASFGAAESSRRNVSP
HHHCCHHHHCCCCCC		25.1524961812
117PhosphorylationSFGAAESSRRNVSPS
HHCCHHHHCCCCCCC		27.1124961812
122PhosphorylationESSRRNVSPSTKSAK
HHHCCCCCCCCCCCC		19.3819684113
125PhosphorylationRRNVSPSTKSAKSSS
CCCCCCCCCCCCCCC		32.1930377154
126UbiquitinationRNVSPSTKSAKSSSQ
CCCCCCCCCCCCCCC		53.4023749301
127PhosphorylationNVSPSTKSAKSSSQY
CCCCCCCCCCCCCCC		40.8019684113
146PhosphorylationDERLRRRSFSSYSRS
HHHHHHHHCCCCCCC		27.8923749301
159PhosphorylationRSSSRRVSNSPSSTD
CCCCCCCCCCCCCCC		29.7622369663
161PhosphorylationSSRRVSNSPSSTDRP
CCCCCCCCCCCCCCC		20.7422369663
163PhosphorylationRRVSNSPSSTDRPPR
CCCCCCCCCCCCCCC		45.7722369663
164PhosphorylationRVSNSPSSTDRPPRS
CCCCCCCCCCCCCCH		37.4022369663
165PhosphorylationVSNSPSSTDRPPRSA
CCCCCCCCCCCCCHH		40.1223749301
176PhosphorylationPRSAKVLSLIAADDM
CCHHHHHHHHCCCCC		22.2521440633
194UbiquitinationEDLQKGFKSAIDEEG
HHHHHHHHHHCCCCC		47.8817644757
195PhosphorylationDLQKGFKSAIDEEGL
HHHHHHHHHCCCCCC		28.3521440633
209UbiquitinationLTWLPQLKSEKSRPV
CCCHHHHCCCCCCCC		51.8517644757
210PhosphorylationTWLPQLKSEKSRPVS
CCHHHHCCCCCCCCC		59.8721440633
213PhosphorylationPQLKSEKSRPVSDVG
HHHCCCCCCCCCCCC		37.4528889911
284PhosphorylationPKFFHHLSPQKEDKD
CCCCCCCCCCCCCCC		22.4117287358
460UbiquitinationISPGEETKYQRSSLS
ECCCCCHHHCCCCCC		42.5423749301
472UbiquitinationSLSTSLTKPYGAKEN
CCCCCCCCCCCCCCC		41.3523749301
477UbiquitinationLTKPYGAKENQRPFG
CCCCCCCCCCCCCCC		53.4817644757
641UbiquitinationFLCPQYSKCVSNANP
EECCCHHHHCCCCCC		33.4523749301
745NitrationVARIVTGYWKYFKLK
HHHHHCCCHHHHEEE		6.86-
1055UbiquitinationNEDTRDFKQFLMRGT
CCCCHHHHHHHHHHH		44.4219722269
1977PhosphorylationPTVSSHISNINVNLE
CCCHHHEECEEECCC		26.6628889911
2010PhosphorylationGVNNFMWSPRMNQDS
CCCCCCCCCCCCCCC		7.2828889911
2032PhosphorylationPIDNNDDSANDLIDR
CCCCCCCCHHHHCCC		31.6628152593
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 CCH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCH1_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 CCH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MID1_YEASTMID1physical
10958666
MID1_YEASTMID1genetic
15498550
SPA2_YEASTSPA2genetic
16087740
FIG1_YEASTFIG1genetic
21252230
VPS9_YEASTVPS9genetic
20526336
SLG1_YEASTSLG1genetic
20526336
HKR1_YEASTHKR1genetic
20526336
FAB1_YEASTFAB1genetic
20526336
RV167_YEASTRVS167genetic
20526336
DUR3_YEASTDUR3genetic
20526336
RTG2_YEASTRTG2genetic
20526336
GET1_YEASTGET1genetic
20526336
CSG2_YEASTCSG2genetic
20526336
SRS2_YEASTSRS2genetic
21459050
PIR5_YEASTYJL160Cgenetic
27708008
ATC3_YEASTDRS2genetic
27708008
SLA1_YEASTSLA1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
SIF2_YEASTSIF2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
GPR1_YEASTGPR1genetic
27708008
ACK1_YEASTACK1genetic
27708008
OST4_YEASTOST4genetic
27708008
UME6_YEASTUME6genetic
27708008
YPS7_YEASTYPS7genetic
27708008
RAD4_YEASTRAD4genetic
27708008
HOS2_YEASTHOS2genetic
27708008
SLT2_YEASTSLT2genetic
27708008
MED20_YEASTSRB2genetic
27708008
STB5_YEASTSTB5genetic
27708008
MGA2_YEASTMGA2genetic
27708008
RS21B_YEASTRPS21Bgenetic
27708008
MOG1_YEASTMOG1genetic
27708008
IME1_YEASTIME1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
UTH1_YEASTUTH1genetic
27708008
ALAM_YEASTALT1genetic
27708008
UPS1_YEASTUPS1genetic
27708008
ARV1_YEASTARV1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
ROM2_YEASTROM2genetic
27708008
SST2_YEASTSST2genetic
27708008
GIS4_YEASTGIS4genetic
27708008
OST6_YEASTOST6genetic
27708008
PHO84_YEASTPHO84genetic
27708008
SCS7_YEASTSCS7genetic
27708008
GAS1_YEASTGAS1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
MET22_YEASTMET22genetic
27708008
OST3_YEASTOST3genetic
27708008
RUD3_YEASTRUD3genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
NAA30_YEASTMAK3genetic
27708008
YVC1_YEASTYVC1genetic
27708136
SCS2_YEASTSCS2physical
28742147
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCH1_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-161, AND MASSSPECTROMETRY.
"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 SER-284, AND MASSSPECTROMETRY.

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