USA1_YEAST - dbPTM
USA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USA1_YEAST
UniProt AC Q03714
Protein Name U1 SNP1-associating protein 1
Gene Name USA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 838
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1, which is required for ERAD-L, and in HRD1 autoubiquitination and degradation..
Protein Sequence MSEYLAQTPCKFTIWSSEIDLIRTNLLVNAHPLSTVGRLLQYIHYQIYKQLRAIYQPEEQCTNSEIPHTPLNSINTYFLSYEGRELSATCLLKDITSSSHPDSNHFIRLQLEKRTSPSGSAFDLEYDMEGEFNSMNIQFEINTLSSQRIFNSMEPNLPIGTTLARLEKLALERIKDFEKSAGNLCGIKEDHSVSDLQGFIIKGKQTPMFLNYGSDSDYYKDLNLVDLIGIDFAPAHNSFFTFLFKMNHEQNSHIANDEERFVLEFISDATLSITQMNVKPDTTVKQVKDFICSVYTHSLNLRRNDIKLIYKGQLLHENNFAGNSSKISEYIKEPHEVKVHVQINQEYTESGPGFWNEVFNNPNIFQFMPPDTRSQSPVSFAPTQGRSPAAIRGEERGIPYVTESGNDIVPTDELYRKCIINGDEVVFIPVSELNPQSSYLSVIKGDYGEIKIPISSNDYRINGDNILLSPSAIEQLESALNFKIERPRDSTLLHPSGEHVRAADNTSSANDNNTVENDESAWNRRVVRPLRNSFPLLLVLIRTFYLIGYNSLVPFFIILEFGSFLPWKYIILLSLLFIFRTVWNTQEVWNLWRDYLHLNEIDEVKFSQIKEFINSNSLTLNFYKKCKDTQSAIDLLMIPNLHEQRLSVYSKYDIEYDTNTPDVGQLNLLFIKVLSGEIPKDALDELFKEFFELYETTRNMNTLYPQDSLNELLLMIWKESQKKDINTLPKYRRWFQTLCSQIAEHNVLDVVLRYIIPDPVNDRVITAVIKNFVLFWVTLLPYVKEKLDDIVAQRARDREQPAPSAQQQENEDEALIIPDEEEPTATGAQPHLYIPDED
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
11UbiquitinationYLAQTPCKFTIWSSE
HHCCCCCCEEEECCH		46.9017644757
49UbiquitinationYIHYQIYKQLRAIYQ
HHHHHHHHHHHHHHC		44.4817644757
93UbiquitinationLSATCLLKDITSSSH
EEEEEEEEEHHCCCC		33.8517644757
179UbiquitinationERIKDFEKSAGNLCG
HHHHHHHHHHCCCCC		45.6717644757
188UbiquitinationAGNLCGIKEDHSVSD
HCCCCCCCCCCCCCC		42.2317644757
202UbiquitinationDLQGFIIKGKQTPMF
CCCCCEECCCCCCCE		56.0617644757
288UbiquitinationDTTVKQVKDFICSVY
CCCHHHHHHHHHHHH		44.4117644757
311UbiquitinationNDIKLIYKGQLLHEN
CCEEEEEECEECCCC		32.9417644757
326UbiquitinationNFAGNSSKISEYIKE
CCCCCCHHHHHHCCC		50.5017644757
374PhosphorylationFMPPDTRSQSPVSFA
CCCCCCCCCCCCCCC		36.7822369663
376PhosphorylationPPDTRSQSPVSFAPT
CCCCCCCCCCCCCCC		28.6322369663
379PhosphorylationTRSQSPVSFAPTQGR
CCCCCCCCCCCCCCC		21.0522369663
383PhosphorylationSPVSFAPTQGRSPAA
CCCCCCCCCCCCCCH		39.9822369663
387PhosphorylationFAPTQGRSPAAIRGE
CCCCCCCCCCHHCCH		26.2228889911
417UbiquitinationPTDELYRKCIINGDE
CCHHHHHHHEECCCE		19.0717644757
680AcetylationVLSGEIPKDALDELF
HHHCCCCHHHHHHHH		62.3825381059
766PhosphorylationPVNDRVITAVIKNFV
CCCHHHHHHHHHHHH		16.4128889911
778PhosphorylationNFVLFWVTLLPYVKE
HHHHHHHHHHHHHHH		17.1128889911
782PhosphorylationFWVTLLPYVKEKLDD
HHHHHHHHHHHHHHH		24.9128889911
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 USA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USA1_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 USA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDN1_YEASTMDN1physical
11805837
LONM_YEASTPIM1physical
11805837
PEX6_YEASTPEX6physical
11805837
CDC48_YEASTCDC48physical
16873066
UBX2_YEASTUBX2physical
16873066
HRD1_YEASTHRD1physical
16873066
HRD3_YEASTHRD3physical
16873066
OS9_YEASTYOS9physical
16873066
DER1_YEASTDER1physical
16873066
USA1_YEASTUSA1physical
18719252
HRD1_YEASTHRD1physical
19898607
HRD3_YEASTHRD3physical
19898607
CUE1_YEASTCUE1genetic
19325107
DER1_YEASTDER1genetic
19325107
HRD1_YEASTHRD1genetic
19325107
HRD3_YEASTHRD3genetic
19325107
LCL2_YEASTLCL2genetic
19325107
CALX_YEASTCNE1genetic
19325107
CWH41_YEASTCWH41genetic
19325107
FKH1_YEASTFKH1genetic
19325107
INP53_YEASTINP53genetic
19325107
KRE1_YEASTKRE1genetic
19325107
LEM3_YEASTLEM3genetic
19325107
RER1_YEASTRER1genetic
19325107
VPS1_YEASTVPS1genetic
19325107
VPS27_YEASTVPS27genetic
19325107
VPS28_YEASTVPS28genetic
19325107
VPS3_YEASTVPS3genetic
19325107
VPS74_YEASTVPS74genetic
19325107
YUR1_YEASTYUR1genetic
19325107
HRD1_YEASTHRD1genetic
21074049
DER1_YEASTDER1genetic
19940128
HAC1_YEASTHAC1genetic
20005842
HRD1_YEASTHRD1physical
20005842
HRD3_YEASTHRD3physical
20005842
DER1_YEASTDER1physical
20005842
CDC48_YEASTCDC48physical
20005842
DER1_YEASTDER1physical
24292014
RUB1_YEASTRUB1genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
BUD14_YEASTBUD14genetic
27708008
RL23A_YEASTRPL23Agenetic
27708008
RL23B_YEASTRPL23Agenetic
27708008
RTG3_YEASTRTG3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
PCL2_YEASTPCL2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
OPI1_YEASTOPI1genetic
27708008
TOK1_YEASTTOK1genetic
27708008
ALB1_YEASTALB1genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
RAD26_YEASTRAD26genetic
27708008
IME1_YEASTIME1genetic
27708008
MYO3_YEASTMYO3genetic
27708008
JEN1_YEASTJEN1genetic
27708008
SKG1_YEASTSKG1genetic
27708008
ARP6_YEASTARP6genetic
27708008
HRD3_YEASTHRD3genetic
27708008
VAM3_YEASTVAM3genetic
27708008
SFG1_YEASTSFG1genetic
27708008
KASH5_HUMANCCDC155physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USA1_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-374; SER-376 ANDSER-379, AND MASS SPECTROMETRY.
"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-376 AND SER-379, ANDMASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND MASSSPECTROMETRY.

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