YD180_YEAST - dbPTM
YD180_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD180_YEAST
UniProt AC Q12301
Protein Name Uncharacterized membrane protein YDL180W
Gene Name YDL180W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 547
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MVRLNHAASYFMPIFCSTRPHIVILSALFSISLFSLFYASSELLLHQYDDPLMFKPNSQDYFRTFLLGLFSPFLYYFLKTFLFNINQRFLILNLIVDFPINDVFMLLILIGLAYPQVQDHEGGTIKHKECSWHIIPRQAYIFGISWALGEFTICIIGNLFNYQEIADPNINSGFTHQESANTYCNNNDMSHNDDCGCSTEYRPNVVDRSDITLSKCIEVRNDSSSISNNVYSSEYHPIKPLRSSSSTYGSIRQQPHENKKQLHVPDNSQDDTIIMMNPIDNSLKLTTLDTGDLSFPIDEEQPILKKSFGYTWAVPNENTQNTTKSFTPIKRFIAFSTAYQLVTGLLLMILVVGSNIMLTIGESLILSMYFVYVRGHEGLFTPVVNYFGSRTISNFILCVIIPFISLNFLINTSIYLRRELDDWFNNSQGEFEDDDENTISKRVATNQEYQHPLSANYISMDSPDVINSSPGHFGMNSGQLLGNTTLYYGSLNGDDDDMTNDSALLRFCKKLVKNWRALARNDSFVLGVMVSWSLLVFVTGILSTVYI
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
10PhosphorylationRLNHAASYFMPIFCS
CCCCHHHHHHHHHCC		10.1228132839
223PhosphorylationCIEVRNDSSSISNNV
EEEECCCCCCCCCCC		29.5428889911
224PhosphorylationIEVRNDSSSISNNVY
EEECCCCCCCCCCCC		34.2619779198
225PhosphorylationEVRNDSSSISNNVYS
EECCCCCCCCCCCCC		33.7121440633
227PhosphorylationRNDSSSISNNVYSSE
CCCCCCCCCCCCCCC		25.0521440633
235PhosphorylationNNVYSSEYHPIKPLR
CCCCCCCCCCCCCCC		18.1619779198
243PhosphorylationHPIKPLRSSSSTYGS
CCCCCCCCCCCCCCC		42.1022369663
244PhosphorylationPIKPLRSSSSTYGSI
CCCCCCCCCCCCCCC		23.1322369663
245PhosphorylationIKPLRSSSSTYGSIR
CCCCCCCCCCCCCCC		28.1322369663
246PhosphorylationKPLRSSSSTYGSIRQ
CCCCCCCCCCCCCCC		27.8322369663
247PhosphorylationPLRSSSSTYGSIRQQ
CCCCCCCCCCCCCCC		33.5722369663
248PhosphorylationLRSSSSTYGSIRQQP
CCCCCCCCCCCCCCC		15.7222369663
250PhosphorylationSSSSTYGSIRQQPHE
CCCCCCCCCCCCCCC		12.2722369663
290PhosphorylationLKLTTLDTGDLSFPI
EEEEECCCCCCCCCC		35.3917563356
294PhosphorylationTLDTGDLSFPIDEEQ
ECCCCCCCCCCCCCC		33.4424961812
427PhosphorylationLDDWFNNSQGEFEDD
HHHHHHCCCCCCCCC		40.4419684113
438PhosphorylationFEDDDENTISKRVAT
CCCCCCCCCHHHHHC		25.2827017623
523PhosphorylationRALARNDSFVLGVMV
HHHHCCCCHHHHHHH		22.3227017623
533PhosphorylationLGVMVSWSLLVFVTG
HHHHHHHHHHHHHHH		12.3427017623
539PhosphorylationWSLLVFVTGILSTVY
HHHHHHHHHHHHHCC		13.6727017623
543PhosphorylationVFVTGILSTVYI---
HHHHHHHHHCCC---		17.5727017623
544PhosphorylationFVTGILSTVYI----
HHHHHHHHCCC----		17.5527017623
546PhosphorylationTGILSTVYI------
HHHHHHCCC------		10.8727017623
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 YD180_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD180_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 YD180_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YIA6_YEASTYIA6genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
INO4_YEASTINO4genetic
27708008
TAF12_YEASTTAF12genetic
27708008
VPS8_YEASTVPS8genetic
27708008
HPH2_YEASTFRT2genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
MIX23_YEASTMIX23genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
YMC2_YEASTYMC2genetic
27708008
EF1A_YEASTTEF2genetic
27708008
PEX34_YEASTPEX34genetic
27708008
RV161_YEASTRVS161genetic
27708008
NRG1_YEASTNRG1genetic
27708008
DOS2_YEASTDOS2genetic
27708008
PAA1_YEASTPAA1genetic
27708008
DOT1_YEASTDOT1genetic
27708008
PP2C2_YEASTPTC2genetic
27708008
BUD27_YEASTBUD27genetic
27708008
MIC19_YEASTMIC19genetic
27708008
YG1O_YEASTYGR035Cgenetic
27708008
ELP2_YEASTELP2genetic
27708008
DAP2_YEASTDAP2genetic
27708008
PUT2_YEASTPUT2genetic
27708008
IGO2_YEASTIGO2genetic
27708008
PEX28_YEASTPEX28genetic
27708008
ATG7_YEASTATG7genetic
27708008
AIM20_YEASTAIM20genetic
27708008
IME2_YEASTIME2genetic
27708008
KAPC_YEASTTPK3genetic
27708008
MEH1_YEASTMEH1genetic
27708008
RIC1_YEASTRIC1genetic
27708008
PNPH_YEASTPNP1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
YL281_YEASTYLR281Cgenetic
27708008
IMH1_YEASTIMH1genetic
27708008
ASND1_YEASTYML096Wgenetic
27708008
AIM34_YEASTAIM34genetic
27708008
MPIP_YEASTMIH1genetic
27708008
MSN2_YEASTMSN2genetic
27708008
YET2_YEASTYET2genetic
27708008
JLP2_YEASTJLP2genetic
27708008
RE114_YEASTREC114genetic
27708008
YM22_YEASTYMR144Wgenetic
27708008
SIW14_YEASTSIW14genetic
27708008
LKHA4_YEASTLAP2genetic
27708008
ARE2_YEASTARE2genetic
27708008
HUB1_YEASTHUB1genetic
27708008
MAM3_YEASTMAM3genetic
27708008
RRP6_YEASTRRP6genetic
27708008
SWT1_YEASTSWT1genetic
27708008
BUD7_YEASTBUD7genetic
27708008
LCF1_YEASTFAA1genetic
27708008
YP014_YEASTYPL014Wgenetic
27708008
ELP3_YEASTELP3genetic
27708008
ELP4_YEASTELP4genetic
27708008
AIM44_YEASTAIM44genetic
27708008
CISY3_YEASTCIT3genetic
27708008
MED1_YEASTMED1genetic
27708008
AXL1_YEASTAXL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD180_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-246, AND MASSSPECTROMETRY.
"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-290, AND MASSSPECTROMETRY.

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