GRH1_YEAST - dbPTM
GRH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRH1_YEAST
UniProt AC Q04410
Protein Name GRASP65 homolog protein 1
Gene Name GRH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 372
Subcellular Localization Cytoplasm. Golgi apparatus, cis-Golgi network membrane
Peripheral membrane protein. Localizes to cytoplasm in a punctate pattern. Association with the cis-Golgi requires N-terminal acetylation and is probably mediated via an N-terminal amphipathic h
Protein Description Involved in the spindle assembly checkpoint. Involved in ER to Golgi vesicle-mediated transport by either facilitating USO1-dependent and -independent tethering or increasing target accuracy of fusion events of COPII-coated vesicles..
Protein Sequence MFRIAKNLVRTFEQSVQDTLALSQDSSNLDAFFQSIPPNLLSAQLESPVDAVSEGVKHTNVNETLSGLRIVWVDEMQFQLQSFFDYIVGFNDDPVPVVSNQHGFSYPDYRRITSIFNEHCGRTLKVNIWSAKGGTFRDEYISIISKESDDLDDVSLNHDERRPSSGEAHQFQALGFKVQWTPLIASTFTYHILNVNIPDGPAQSAGLIPDEDYIIGCQDGLLATGGETLLQDIVRSRANYDLVLYVYNKVSDCVRPITVHIGPDGRLGCNVGYGFLHRIPTVKHCPQQAQQQGQDDNPVPVPVPVESETAFVPSAFTAPPVPTKKKSKNKKGTQPLAMDDYFNEGRDKSSTAAKSAESDILAPPPQKQSSSD
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-------MFRIAKNL
-------CCHHHHHH		4.6117261844
6Acetylation--MFRIAKNLVRTFE
--CCHHHHHHHHHHH		48.7425381059
47PhosphorylationLLSAQLESPVDAVSE
HHHHHCCCHHHHHHH		38.5228889911
64PhosphorylationKHTNVNETLSGLRIV
CCCCHHHHHCCCEEE		22.4828889911
66PhosphorylationTNVNETLSGLRIVWV
CCHHHHHCCCEEEEE		43.1128889911
148PhosphorylationISIISKESDDLDDVS
EEEEECCCCCCCCCC		39.9122890988
155PhosphorylationSDDLDDVSLNHDERR
CCCCCCCCCCCCCCC		30.3722369663
164PhosphorylationNHDERRPSSGEAHQF
CCCCCCCCCCCCHHH		49.5222369663
165PhosphorylationHDERRPSSGEAHQFQ
CCCCCCCCCCCHHHH		43.2522369663
349PhosphorylationFNEGRDKSSTAAKSA
CCCCCCCCCHHHHHH		36.8924961812
350PhosphorylationNEGRDKSSTAAKSAE
CCCCCCCCHHHHHHC		28.0124961812
351PhosphorylationEGRDKSSTAAKSAES
CCCCCCCHHHHHHCC		37.4124961812
355PhosphorylationKSSTAAKSAESDILA
CCCHHHHHHCCCCCC		32.3222369663
358PhosphorylationTAAKSAESDILAPPP
HHHHHHCCCCCCCCC		29.6622369663
369PhosphorylationAPPPQKQSSSD----
CCCCCCCCCCC----		38.5529136822
370PhosphorylationPPPQKQSSSD-----
CCCCCCCCCC-----		35.7128889911
371PhosphorylationPPQKQSSSD------
CCCCCCCCC------		53.2229136822
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 GRH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRH1_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 GRH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUG1_YEASTBUG1physical
16554755
SEC24_YEASTSEC24physical
16554755
SEC23_YEASTSEC23physical
16554755
ADH1_YEASTADH1physical
16429126
ERV14_YEASTERV14genetic
16269340
CHO2_YEASTCHO2genetic
16269340
ALG3_YEASTALG3genetic
16269340
BUG1_YEASTBUG1physical
17261844
SEC24_YEASTSEC24physical
17261844
SEC23_YEASTSEC23physical
17261844
SFB2_YEASTSFB2physical
17261844
SFB3_YEASTSFB3physical
17261844
RBD2_YEASTRBD2physical
18467557
URE2_YEASTURE2physical
18467557
SEC24_YEASTSEC24physical
18467557
STP22_YEASTSTP22physical
22144692
HSP78_YEASTHSP78physical
22940862
PSD1_YEASTPSD1genetic
23891562
GLO3_YEASTGLO3genetic
23891562
COPD_YEASTRET2genetic
23891562
ERV14_YEASTERV14genetic
23891562
TRS20_YEASTTRS20genetic
23891562
YPT1_YEASTYPT1genetic
23891562
RGP1_YEASTRGP1genetic
23891562
RIC1_YEASTRIC1genetic
23891562
RL13A_YEASTRPL13Agenetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
SEI1_YEASTFLD1genetic
27708008
ELG1_YEASTELG1genetic
27708008
DGK1_YEASTDGK1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
QOR_YEASTZTA1genetic
27708008
YBY7_YEASTYBR137Wgenetic
27708008
MTC4_YEASTMTC4genetic
27708008
VBA2_YEASTVBA2genetic
27708008
PER1_YEASTPER1genetic
27708008
TREA_YEASTNTH1genetic
27708008
TRS85_YEASTTRS85genetic
27708008
ERV14_YEASTERV14genetic
27708008
MED5_YEASTNUT1genetic
27708008
RT13_YEASTMRP13genetic
27708008
TRS65_YEASTTRS65genetic
27708008
ATG32_YEASTATG32genetic
27708008
YIV5_YEASTYIR035Cgenetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
YKH7_YEASTYKL077Wgenetic
27708008
CTK1_YEASTCTK1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
YL036_YEASTYLR036Cgenetic
27708008
UPS1_YEASTUPS1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
CTL1_YEASTCTL1genetic
27708008
YM54_YEASTYMR196Wgenetic
27708008
HFA1_YEASTHFA1genetic
27708008
ELP6_YEASTELP6genetic
27708008
ADE_YEASTAAH1genetic
27708008
NTH2_YEASTNTG2genetic
27708008
MSH2_YEASTMSH2genetic
27708008
SGF11_YEASTSGF11genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
THP3_YEASTTHP3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRH1_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-47; SER-155; SER-164 ANDSER-355, AND MASS SPECTROMETRY.
"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 SER-155; SER-164 ANDSER-165, AND MASS SPECTROMETRY.

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