UIP4_YEAST - dbPTM
UIP4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UIP4_YEAST
UniProt AC Q08926
Protein Name ULP1-interacting protein 4
Gene Name UIP4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 304
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein . Mitochondrion outer membrane . Nucleus envelope .
Protein Description
Protein Sequence MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDEHSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKERKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTDMSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS
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
46PhosphorylationWEYKFDESSVTKHND
EEEEECHHHCCCCCC
31.7730377154
82PhosphorylationPKEVDEHSNENNVAT
CCCCCCCCCCCCEEE
43.7322369663
89PhosphorylationSNENNVATLNNEEDG
CCCCCEEECCCCCCC
26.2422369663
98PhosphorylationNNEEDGGSAGEEKDE
CCCCCCCCCCCCCCC
38.3322369663
109PhosphorylationEKDEGDKTAHNTNEN
CCCCCCCCCCCCCCC
37.5822369663
113PhosphorylationGDKTAHNTNENGSEL
CCCCCCCCCCCCCEE
33.7622369663
118PhosphorylationHNTNENGSELYYEGP
CCCCCCCCEEEEECC
35.6922369663
121PhosphorylationNENGSELYYEGPETP
CCCCCEEEEECCCCC
8.7422369663
122PhosphorylationENGSELYYEGPETPT
CCCCEEEEECCCCCC
27.3422369663
127PhosphorylationLYYEGPETPTPSLKG
EEEECCCCCCCCCCC
35.2822369663
129PhosphorylationYEGPETPTPSLKGNV
EECCCCCCCCCCCCE
32.6922369663
131PhosphorylationGPETPTPSLKGNVTF
CCCCCCCCCCCCEEC
45.2322369663
137PhosphorylationPSLKGNVTFPSPKTA
CCCCCCEECCCCCCE
33.5522369663
140PhosphorylationKGNVTFPSPKTAISQ
CCCEECCCCCCEECC
34.5322369663
143PhosphorylationVTFPSPKTAISQDGS
EECCCCCCEECCCCC
32.3822369663
146PhosphorylationPSPKTAISQDGSAFA
CCCCCEECCCCCHHH
21.5422369663
150PhosphorylationTAISQDGSAFAKETT
CEECCCCCHHHHHHH
28.6229136822
185PhosphorylationKEENKELSPNFSQEQ
HHHCCCCCCCCCHHH
20.9122369663
189PhosphorylationKELSPNFSQEQTENK
CCCCCCCCHHHHHCC
39.1722369663
193PhosphorylationPNFSQEQTENKQDKG
CCCCHHHHHCCCCCC
40.5522369663
205PhosphorylationDKGLDNLSEGNDNDN
CCCCCCCCCCCCCCC
50.1122369663
213PhosphorylationEGNDNDNTRVNEDTD
CCCCCCCCCCCCCCC
38.5722369663
278AcetylationDYESVLKKLLGALGR
HHHHHHHHHHHHHHH
44.7924489116

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 UIP4_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UIP4_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 UIP4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWA2_YEASTSWA2genetic
21987634
GABAT_YEASTUGA1genetic
21987634

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UIP4_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-140; SER-185 ANDSER-205, AND MASS SPECTROMETRY.
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185 ANDSER-205, AND MASS SPECTROMETRY.

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