HRD1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HRD1_SCHPO
• UniProt AC: O74757
• Protein Name: ERAD-associated E3 ubiquitin-protein ligase hrd1
• Gene Name: hrd1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 677
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). 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) (By similarity). Together with ubc7, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1..
• Protein Sequence: MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLDMTPKRLPCGHILHFHCLRNWLERQQTCPICRRSVIGNQSSPTGIPASPNVRATQIATQVPNPQNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPRRIALRDGWTMLPIPGTRRIPTYSQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPGWRLVSSNTQSLSTNSAMTSLYQNASSADNNLGSSLPNVVPLSRGLTQSNETSNTFPAASSNISSQLRELHTKIDELRETVSNFRADYNSIRTSLNQLEAASGINERIQTTSADSLLNSNGMSGTEGFENTQTSITTNDNQSSILTSSDQTSPFATDEDRQNSRNVQLETVDENF

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
353	Phosphorylation	TCPICRRSVIGNQSS CCCCCCCCCCCCCCC	9.95	29996109
359	Phosphorylation	RSVIGNQSSPTGIPA CCCCCCCCCCCCCCC	42.14	25720772
360	Phosphorylation	SVIGNQSSPTGIPAS CCCCCCCCCCCCCCC	19.40	25720772
362	Phosphorylation	IGNQSSPTGIPASPN CCCCCCCCCCCCCCC	50.09	25720772
367	Phosphorylation	SPTGIPASPNVRATQ CCCCCCCCCCCCEEE	16.20	28889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HRD1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HRD1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HRD1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YB3C_SCHPO	cay1	genetic	18818364
REC14_SCHPO	rec14	genetic	18818364
SKI3_SCHPO	SPCC1919.05	genetic	18818364
SKI2_SCHPO	SPCC550.03c	genetic	18818364
CAF1_SCHPO	caf1	genetic	18818364
CCR4_SCHPO	ccr4	genetic	18818364
ALG8_SCHPO	alg8	genetic	22681890
MTO1_SCHPO	SPBC30B4.06c	genetic	22681890
YG03_SCHPO	SPBC1604.03c	genetic	22681890
FSV1_SCHPO	fsv1	genetic	22681890
ALG5_SCHPO	alg5	genetic	22681890
FKBP4_SCHPO	fkbp39	genetic	22681890
VPS3_SCHPO	vps3	genetic	22681890
SHR3_SCHPO	psh3	genetic	22681890
MU123_SCHPO	mug123	genetic	22681890
STM1_SCHPO	stm1	genetic	22681890
EMC1_SCHPO	emc1	genetic	22681890
MCL1_SCHPO	mcl1	genetic	22681890
RRP1_SCHPO	nop52	genetic	22681890

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.
PubMed: 18257517