PVH1_YEAST - dbPTM
PVH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PVH1_YEAST
UniProt AC Q02256
Protein Name Tyrosine-protein phosphatase YVH1
Gene Name YVH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 364
Subcellular Localization
Protein Description May be directly involved in signal transduction and/or cell cycle regulation. It is necessary for maintaining growth rate or spore germination. Could show both activity toward tyrosine-protein phosphate as well as with serine-protein phosphate..
Protein Sequence MAGNANSVDEEVTRILGGIYLGGIRPIIDHRPLGAEFNITHILSVIKFQVIPEYLIRKGYTLKNIPIDDDDVTDVLQYFDETNRFIDQCLFPNEVEYSPRLVDFKKKPQRGAVFAHCQAGLSRSVTFIVAYLMYRYGLSLSMAMHAVKRKKPSVEPNENFMEQLHLFEKMGGDFVDFDNPAYKQWKLKQSIKLDPSGSELVSNSGMFKDSESSQDLDKLTEAEKSKVTAVRCKKCRTKLALSTSFIAHDPPSKESSEGHFIKRAANSHRIIDIQESQANCSHFFIEPLKWMQPELQGKQELEGKFSCPGCSSKVGGYNWKGSRCSCGKWVIPAIHLQTSKVDQFPLQSTALPNMVNFESEKVNR
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
7Phosphorylation-MAGNANSVDEEVTR
-CCCCCCCCCHHHHH		28.6521126336
13PhosphorylationNSVDEEVTRILGGIY
CCCCHHHHHHHCCCE		18.4428889911
126PhosphorylationAGLSRSVTFIVAYLM
CCCCHHHHHHHHHHH		14.6427017623
131PhosphorylationSVTFIVAYLMYRYGL
HHHHHHHHHHHHHCC		4.9030377154
134PhosphorylationFIVAYLMYRYGLSLS
HHHHHHHHHHCCHHH		9.7030377154
136PhosphorylationVAYLMYRYGLSLSMA
HHHHHHHHCCHHHHH		12.6330377154
141PhosphorylationYRYGLSLSMAMHAVK
HHHCCHHHHHHHHHH		10.9130377154
190PhosphorylationKQWKLKQSIKLDPSG
HCHHCCCCEEECCCC		21.8022369663
196PhosphorylationQSIKLDPSGSELVSN
CCEEECCCCCCHHCC		55.4022369663
198PhosphorylationIKLDPSGSELVSNSG
EEECCCCCCHHCCCC		31.9022369663
202PhosphorylationPSGSELVSNSGMFKD
CCCCCHHCCCCCCCC		37.5922369663
204PhosphorylationGSELVSNSGMFKDSE
CCCHHCCCCCCCCCC		24.9122369663
210PhosphorylationNSGMFKDSESSQDLD
CCCCCCCCCCCCCHH		39.7122369663
212PhosphorylationGMFKDSESSQDLDKL
CCCCCCCCCCCHHHH		36.9322369663
213PhosphorylationMFKDSESSQDLDKLT
CCCCCCCCCCHHHHH		24.5425521595
242PhosphorylationCRTKLALSTSFIAHD
CCCEEEEEEEEEECC		19.1930377154
243PhosphorylationRTKLALSTSFIAHDP
CCEEEEEEEEEECCC		28.6230377154
361UbiquitinationMVNFESEKVNR----
CCCCCCCCCCC----		54.8323749301
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 PVH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PVH1_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 PVH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PESC_YEASTNOP7physical
11716519
IME1_YEASTIME1genetic
10464190
MCK1_YEASTMCK1genetic
10464190
PESC_YEASTNOP7genetic
11716519
PTP2_YEASTPTP2genetic
8896280
SFK1_YEASTSFK1physical
18467557
GST1_YEASTGTT1physical
18467557
IF6_YEASTTIF6physical
18467557
PEX11_YEASTPEX11physical
18467557
PDR12_YEASTPDR12physical
18467557
DIP5_YEASTDIP5physical
18467557
LSG1_YEASTLSG1physical
19797079
ARX1_YEASTARX1physical
19797079
NMD3_YEASTNMD3physical
19797079
REI1_YEASTREI1physical
19797079
ALB1_YEASTALB1physical
19797079
MEX67_YEASTMEX67physical
19797079
MRT4_YEASTMRT4genetic
19797079
RL5_YEASTRPL5physical
19797079
RL12A_YEASTRPL12Bgenetic
19797078
RL12B_YEASTRPL12Bgenetic
19797078
MRT4_YEASTMRT4genetic
19797078
RL8A_YEASTRPL8Aphysical
19797078
RL12A_YEASTRPL12Bphysical
19797078
RL12B_YEASTRPL12Bphysical
19797078
AP1G1_YEASTAPL4physical
20489023
CDC14_YEASTCDC14physical
20489023
CIC1_YEASTCIC1physical
20489023
CRT10_YEASTCRT10physical
20489023
ERB1_YEASTERB1physical
20489023
LSG1_YEASTLSG1physical
20489023
MMS1_YEASTMMS1physical
20489023
NMD3_YEASTNMD3physical
20489023
RRP5_YEASTRRP5physical
20489023
TAX4_YEASTTAX4physical
20489023
YKC3_YEASTYKL023Wphysical
20489023
RGC1_YEASTRGC1physical
20489023
SRS2_YEASTSRS2genetic
21459050
MRT4_YEASTMRT4genetic
21474464
CTF8_YEASTCTF8genetic
21127252
HEL2_YEASTHEL2genetic
21127252
PACC_YEASTRIM101genetic
21127252
SKN7_YEASTSKN7genetic
21127252
SWI4_YEASTSWI4genetic
21127252
MEX67_YEASTMEX67physical
27775710
MTR2_YEASTMTR2physical
27775710
NMD3_YEASTNMD3physical
27775710
IF6_YEASTTIF6physical
27775710
RLA0_YEASTRPP0physical
27775710
ARX1_YEASTARX1genetic
27775710
NU116_YEASTNUP116genetic
27775710
NMD3_YEASTNMD3genetic
27775710
CGR1_YEASTCGR1genetic
27708008
CDC73_YEASTCDC73genetic
27708008
YL422_YEASTYLR422Wgenetic
27708008
SKY1_YEASTSKY1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
EAF7_YEASTEAF7genetic
27708008
VAM3_YEASTVAM3genetic
27708008
IPYR_YEASTIPP1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
COAD_YEASTCAB4genetic
27708008
UTP13_YEASTUTP13genetic
27708008
RNA1_YEASTRNA1genetic
27708008
SLA1_YEASTSLA1genetic
27708008
ARL1_YEASTARL1genetic
27708008
SOK1_YEASTSOK1genetic
27708008
YD089_YEASTYDR089Wgenetic
27708008
ARO1_YEASTARO1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
PHO86_YEASTPHO86genetic
27708008
OGG1_YEASTOGG1genetic
27708008
ALDH2_YEASTALD2genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
HUB1_YEASTHUB1genetic
27708008
MDM12_YEASTMDM12genetic
27708008
YO036_YEASTYOL036Wgenetic
27708008
HMI1_YEASTHMI1genetic
27708008
YAP4_YEASTCIN5genetic
27708008
SKI7_YEASTSKI7genetic
27708008
SFG1_YEASTSFG1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
MED1_YEASTMED1genetic
27708008
P2R3B_HUMANPPP2R3Bphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PVH1_YEAST

loading...

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-196; SER-202; SER-204AND SER-212, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory