HSV2_YEAST - dbPTM
HSV2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSV2_YEAST
UniProt AC P50079
Protein Name SVP1-like protein 2
Gene Name HSV2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 448
Subcellular Localization Endosome membrane
Peripheral membrane protein. Prevacuolar compartment membrane
Peripheral membrane protein. Recruitment to endosomes depends on binding to phosphatidylinositol 3-phosphate.
Protein Description Involved in piecemeal microautophagy of the nucleus (micronucleophagy)..
Protein Sequence MDVRRPIREAVNNRRKPKFLSVSFNQDDSCFSVALENGFRIFNTDPLTSKLSKTFKESATNQSRGTGIGYTRMLYRTNYIALVGGGKRPRHALNKLIIWDDLLQKETITLKFMSSIKDVFLSRIHIVVVLENTIEIFQFQTNPQRICPILDIPPNGSVDYVVCSSKHLQSQASQSQSKILEIIAFPSNKCVGQIQVADLSQIKYNSQNPKESALLPTSIIKAHKNPIKLVRLNRQGTMVATCSVQGTLIRIFSTHNGTLIKEFRRGVDKADIYEMSFSPNGSKLAVLSNKQTLHIFQIFETTNTETNTPDHSRANGSSHPLKNYIPKGLWRPKYLDSVWSICNAHLKNPIFDAHRNDNSGDVTHDNEFYKDRCRIGWCQDSNNREQDDSLVLVWQNSGIWEKFVILEKEQQDSSKTHYSLNESLRNEDTKSAGEPTRWELVRESWREL
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
50UbiquitinationNTDPLTSKLSKTFKE
ECCHHHHHHHHHHHH		52.0923749301
61N-linked_GlycosylationTFKESATNQSRGTGI
HHHHHHCCCCCCCCC		37.23-
63PhosphorylationKESATNQSRGTGIGY
HHHHCCCCCCCCCCH		34.4530377154
155N-linked_GlycosylationPILDIPPNGSVDYVV
EECCCCCCCCCCEEE		50.44-
256N-linked_GlycosylationIRIFSTHNGTLIKEF
EEEEECCCCCHHHHH		45.28-
280N-linked_GlycosylationYEMSFSPNGSKLAVL
EEEEECCCCCEEEEE		67.20-
315N-linked_GlycosylationTPDHSRANGSSHPLK
CCCCCCCCCCCCCHH		50.17-
363PhosphorylationNDNSGDVTHDNEFYK
CCCCCCCCCCCCCCC		28.4027017623
369PhosphorylationVTHDNEFYKDRCRIG
CCCCCCCCCCCEEEE		13.0527017623
419PhosphorylationDSSKTHYSLNESLRN
CCCCCCCCHHHHHCC		19.6724961812
421N-linked_GlycosylationSKTHYSLNESLRNED
CCCCCCHHHHHCCCC		30.76-
423PhosphorylationTHYSLNESLRNEDTK
CCCCHHHHHCCCCCC		31.4024961812
429PhosphorylationESLRNEDTKSAGEPT
HHHCCCCCCCCCCCC		22.2624961812
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 HSV2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSV2_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 HSV2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIL_YEASTERG10physical
11805837
YBY8_YEASTYBR138Cphysical
11536337
ATG21_YEASTATG21genetic
11536337
VPS21_YEASTVPS21physical
11283351
CAPZB_YEASTCAP2physical
18467557
TVP15_YEASTTVP15physical
18719252
SNF1_YEASTSNF1genetic
24586198
REG1_YEASTREG1genetic
24586198
TLG2_YEASTTLG2genetic
24586198
BECN1_YEASTVPS30genetic
24586198
ELO2_YEASTELO2genetic
27708008
PRP11_YEASTPRP11genetic
27708008
FAD1_YEASTFAD1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
SEC7_YEASTSEC7genetic
27708008
SMD1_YEASTSMD1genetic
27708008
TEL2_YEASTTEL2genetic
27708008
SMC4_YEASTSMC4genetic
27708008
MGR1_YEASTMGR1genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
DBF2_YEASTDBF2genetic
27708008
GSH1_YEASTGSH1genetic
27708008
RAV1_YEASTRAV1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
PHD1_YEASTPHD1genetic
27708008
NNK1_YEASTNNK1genetic
27708008
SKY1_YEASTSKY1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
PMA2_YEASTPMA2genetic
27708008
ELP4_YEASTELP4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSV2_YEAST

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Related Literatures of Post-Translational Modification

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