PRA1_YEAST - dbPTM
PRA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRA1_YEAST
UniProt AC P53633
Protein Name Prenylated Rab acceptor 1
Gene Name YIP3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 176
Subcellular Localization Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MNQLGALAQVSRFTQNFSMENIKSEFQSLQSKLATLRTPQEFFNFKKISKPQNFGEVQSRVAYNLKYFSSNYGLIIGCLSIYTLLTNLLLLFVIVLVVAGIVGINKLKGEELVTPFGSFKTNQLYTGLVCVAVPIGFLASPISTLLWLIGASAVSVFGHASLMEKPIETVFDEETV
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
1Acetylation-------MNQLGALA
-------CCHHHHHH
6.9522814378
11PhosphorylationLGALAQVSRFTQNFS
HHHHHHHHHHHHCCC
15.0324909858
14PhosphorylationLAQVSRFTQNFSMEN
HHHHHHHHHCCCHHH
22.8422369663
18PhosphorylationSRFTQNFSMENIKSE
HHHHHCCCHHHHHHH
32.5122369663
23UbiquitinationNFSMENIKSEFQSLQ
CCCHHHHHHHHHHHH
56.3623749301
23AcetylationNFSMENIKSEFQSLQ
CCCHHHHHHHHHHHH
56.3624489116
32UbiquitinationEFQSLQSKLATLRTP
HHHHHHHHHHHCCCH
29.2224961812
32AcetylationEFQSLQSKLATLRTP
HHHHHHHHHHHCCCH
29.2224489116
46UbiquitinationPQEFFNFKKISKPQN
HHHHHCCCCCCCCCC
50.7517644757
46AcetylationPQEFFNFKKISKPQN
HHHHHCCCCCCCCCC
50.7524489116
46SuccinylationPQEFFNFKKISKPQN
HHHHHCCCCCCCCCC
50.7523954790
47UbiquitinationQEFFNFKKISKPQNF
HHHHCCCCCCCCCCH
48.3417644757
50UbiquitinationFNFKKISKPQNFGEV
HCCCCCCCCCCHHHH
54.8423749301
59PhosphorylationQNFGEVQSRVAYNLK
CCHHHHHHHHHHHHH
33.6230377154
108UbiquitinationIVGINKLKGEELVTP
HHCHHHCCCCCCCCC
66.9224961812

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 PRA1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRA1_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 PRA1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC4_YEASTSEC4physical
11785952
YPT1_YEASTYPT1physical
11785952
YPT10_YEASTYPT10physical
11785952
YPT11_YEASTYPT11physical
11785952
YPT31_YEASTYPT31physical
11785952
YPT32_YEASTYPT32physical
11785952
YPT52_YEASTYPT52physical
11785952
YPT6_YEASTYPT6physical
11785952
RTN1_YEASTRTN1physical
16002643
ERG2_YEASTERG2genetic
16269340
ATC3_YEASTDRS2genetic
16269340
ATC1_YEASTPMR1genetic
16269340
BFR1_YEASTBFR1genetic
16269340
PLMT_YEASTOPI3genetic
16269340
SWA2_YEASTSWA2genetic
16269340
GYP1_YEASTGYP1genetic
16269340
TLG2_YEASTTLG2genetic
16269340
NEM1_YEASTNEM1genetic
16269340
HIP1_YEASTHIP1genetic
16269340
RGP1_YEASTRGP1genetic
16269340
ASI3_YEASTASI3genetic
16269340
RIC1_YEASTRIC1genetic
16269340
TRS85_YEASTTRS85genetic
16269340
ARF1_YEASTARF1genetic
16269340
MON2_YEASTMON2genetic
16269340
TRS33_YEASTTRS33genetic
16269340
PRA1_YEASTYIP3physical
11283351
PEX14_YEASTPEX14physical
18719252
PRA1_YEASTYIP3physical
18719252
PEX5_YEASTPEX5physical
18719252
GET2_YEASTGET2genetic
19325107
ARL1_YEASTARL1genetic
19325107
CDC1_YEASTCDC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
YIP1_YEASTYIP1genetic
27708008
ORC6_YEASTORC6genetic
27708008
TAD3_YEASTTAD3genetic
27708008
APC5_YEASTAPC5genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRA1_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-18, AND MASSSPECTROMETRY.

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