ADD37_YEAST - dbPTM
ADD37_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADD37_YEAST
UniProt AC Q03233
Protein Name Alpha1-proteinase inhibitor-degradation deficient protein 37
Gene Name ADD37
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 198
Subcellular Localization Cytoplasm .
Protein Description Involved in ER-associated protein degradation (ERAD)..
Protein Sequence MAIKPTKSFQNCLEAEVPGYNDCPTVLFSIDPNSGPRSKSKQRTKSKRCVSGRLATEVLDLYGNTKTATTPPPVLRRPSVTAAQQESACEGVLVKDQGDRQLQPILCSKEELVAKINDLCVCGSKLSSKELEFYKKKLDSNITKILQNEHTKTVLSQIFNEKDKNMAVKTIKHWMVTDTTISNWCPAFLKIFENAMPN
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
8PhosphorylationMAIKPTKSFQNCLEA
CCCCCCHHHHCHHHC
34.2520377248
34PhosphorylationLFSIDPNSGPRSKSK
EEEECCCCCCCCCCC
56.4121440633
67PhosphorylationDLYGNTKTATTPPPV
HHHCCCCCCCCCCCC
27.4822369663
69PhosphorylationYGNTKTATTPPPVLR
HCCCCCCCCCCCCCC
45.1021440633
70PhosphorylationGNTKTATTPPPVLRR
CCCCCCCCCCCCCCC
31.1922369663
79PhosphorylationPPVLRRPSVTAAQQE
CCCCCCCCCCHHHHH
30.2317330950
81PhosphorylationVLRRPSVTAAQQESA
CCCCCCCCHHHHHHH
22.1817330950
129AcetylationCGSKLSSKELEFYKK
CCCCCCHHHHHHHHH
64.0424489116
143PhosphorylationKKLDSNITKILQNEH
HHHHHHHHHHHHCHH
19.1130377154
151PhosphorylationKILQNEHTKTVLSQI
HHHHCHHHHHHHHHH
23.4129136822
153PhosphorylationLQNEHTKTVLSQIFN
HHCHHHHHHHHHHHC
28.0329136822
156PhosphorylationEHTKTVLSQIFNEKD
HHHHHHHHHHHCHHC
19.5229136822
162AcetylationLSQIFNEKDKNMAVK
HHHHHCHHCCCHHHE
75.1024489116

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 ADD37_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADD37_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 ADD37_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERD2_YEASTERD2genetic
27708008
CDC10_YEASTCDC10genetic
27708008
SEC7_YEASTSEC7genetic
27708008
SPC19_YEASTSPC19genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ALG2_YEASTALG2genetic
27708008
IF2A_YEASTSUI2genetic
27708008
SEC12_YEASTSEC12genetic
27708008
OSH6_YEASTOSH6genetic
27708008
CDC27_YEASTCDC27genetic
27708008
CALM_YEASTCMD1genetic
27708008
TRS20_YEASTTRS20genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC48_YEASTCDC48genetic
27708008
RPB1_YEASTRPO21genetic
27708008
DBF4_YEASTDBF4genetic
27708008
SC61G_YEASTSSS1genetic
27708008
COG3_YEASTCOG3genetic
27708008
ERG26_YEASTERG26genetic
27708008
GPI1_YEASTGPI1genetic
27708008
SEC24_YEASTSEC24genetic
27708008
NEP1_YEASTEMG1genetic
27708008
SEC13_YEASTSEC13genetic
27708008
SEC39_YEASTSEC39genetic
27708008
TRM6_YEASTGCD10genetic
27708008
TIM23_YEASTTIM23genetic
27708008
SMC5_YEASTSMC5genetic
27708008
HRP1_YEASTHRP1genetic
27708008
RPB2_YEASTRPB2genetic
27708008
SYA_YEASTALA1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
STE50_YEASTSTE50genetic
27708008
MGR1_YEASTMGR1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
PHB2_YEASTPHB2genetic
27708008
SNF6_YEASTSNF6genetic
27708008
SNX4_YEASTSNX4genetic
27708008
CSF1_YEASTCSF1genetic
27708008
YNO3_YEASTYNL143Cgenetic
27708008
YME1_YEASTYME1genetic
27708008
IKZF1_HUMANIKZF1physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADD37_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-79, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASSSPECTROMETRY.
"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 THR-70, AND MASSSPECTROMETRY.

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