SSH4_YEAST - dbPTM
SSH4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSH4_YEAST
UniProt AC P32343
Protein Name Protein SSH4
Gene Name SSH4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 579
Subcellular Localization Vacuole membrane
Single-pass type II membrane protein . Endosome membrane
Single-pass type II membrane protein .
Protein Description Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane. Confers leflunomide resistance when overexpressed..
Protein Sequence MYVTFNEALDSSFGNLESPNHDFKVGDPNMVPTPPMDSDSAAISLAFLISLSITFAILMLILVVIAAYVTFCGDDESEYDEENALGTRTSGTLHSLFGKKHSGILLDSSFASPGGFDDEIVLQERELEELPKMSAYEVELYIRAKEFQMMSPPMVKDFGTYLDSDDQQFIKDRGIQSYFLLPSINDNIDEYGNFLPSFIVQDKLDIQFSKFNKSSSTVMNYPLPHNRKDAVYFEVKIFRHIQKSNSIFSIGLTTVPYPYFRVPGMAKYSIAYESTGKLRINNPFTASTLLPKLEEGDTVGFGYRYKTGTIFITHNGKKLMDVTQNIGIDLFIGIGAFNAAYTRTYTRDGLLEDPDNVSFREALSEGKDIEVAKDLQRVHDPHDESDEMTSDEVELHVNLGQVGFVFIEANVKKYAFGSVYGQIGIPPAYNGTEIKKDTILQKGEELPPRYADTDNFFGSMKVKEGSSSRITAQTSKPLWSVGTYERISSNFDRENNVYHDSLETDDNNTDNNVNNNDENAGCNENSPLLEDDGNKRPENSNTPREVSDGAINKNPRNKSTKKRQRNRGKSSKKKNRSRK
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
89PhosphorylationENALGTRTSGTLHSL
HHHCCCCCHHHHHHH		31.2023749301
90PhosphorylationNALGTRTSGTLHSLF
HHCCCCCHHHHHHHH		26.8723749301
92PhosphorylationLGTRTSGTLHSLFGK
CCCCCHHHHHHHHCC		22.5123749301
95PhosphorylationRTSGTLHSLFGKKHS
CCHHHHHHHHCCCCC		28.6223749301
99UbiquitinationTLHSLFGKKHSGILL
HHHHHHCCCCCEEEE		39.7223749301
100UbiquitinationLHSLFGKKHSGILLD
HHHHHCCCCCEEEEE		43.3022817900
145UbiquitinationVELYIRAKEFQMMSP
EEEEEEHHHHHCCCC		49.5723749301
171UbiquitinationSDDQQFIKDRGIQSY
CCCHHHHHHCCCCEE		42.5323749301
212N-linked_GlycosylationDIQFSKFNKSSSTVM
EEEEECCCCCCCEEE		47.22-
356N-linked_GlycosylationGLLEDPDNVSFREAL
CCCCCCCCCCHHHHH		36.40-
358PhosphorylationLEDPDNVSFREALSE
CCCCCCCCHHHHHHC		25.4922369663
364PhosphorylationVSFREALSEGKDIEV
CCHHHHHHCCCCHHH		51.8822369663
367UbiquitinationREALSEGKDIEVAKD
HHHHHCCCCHHHHHH		52.0223749301
373UbiquitinationGKDIEVAKDLQRVHD
CCCHHHHHHHHHHCC		65.2423749301
430N-linked_GlycosylationIGIPPAYNGTEIKKD
CCCCCCCCCCCCCCC		53.68-
435UbiquitinationAYNGTEIKKDTILQK
CCCCCCCCCCCCCCC		38.0623749301
442UbiquitinationKKDTILQKGEELPPR
CCCCCCCCCCCCCCC		65.9223749301
461UbiquitinationDNFFGSMKVKEGSSS
CCCCCCEEECCCCCC		52.4224961812
463UbiquitinationFFGSMKVKEGSSSRI
CCCCEEECCCCCCCE		51.3324961812
476UbiquitinationRITAQTSKPLWSVGT
CEEEECCCCEEECEE		47.7423749301
480PhosphorylationQTSKPLWSVGTYERI
ECCCCEEECEEHHHH		20.5323749301
483PhosphorylationKPLWSVGTYERISSN
CCEEECEEHHHHHCC		21.7623749301
484PhosphorylationPLWSVGTYERISSNF
CEEECEEHHHHHCCC		9.4023749301
507N-linked_GlycosylationDSLETDDNNTDNNVN
CCCCCCCCCCCCCCC		56.99-
547PhosphorylationSNTPREVSDGAINKN
CCCCCCCCCCCCCCC		26.1023749301
553UbiquitinationVSDGAINKNPRNKST
CCCCCCCCCCCCHHH		63.3223749301
557N-linked_GlycosylationAINKNPRNKSTKKRQ
CCCCCCCCHHHHHHH		43.84-
575N-linked_GlycosylationGKSSKKKNRSRK---
CHHHHHHHCCCC---		56.91-
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 SSH4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSH4_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 SSH4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO4_YEASTMYO4physical
16554755
MLC1_YEASTMLC1physical
16554755
MYO2_YEASTMYO2physical
16554755
MET30_YEASTMET30genetic
27708008
NU192_YEASTNUP192genetic
27708008
ARP4_YEASTARP4genetic
27708008
NEP1_YEASTEMG1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
DPOA_YEASTPOL1genetic
27708008
SEC62_YEASTSEC62genetic
27708008
PSB5_YEASTPRE2genetic
27708008
BUR1_YEASTSGV1genetic
27708008
ATG15_YEASTATG15genetic
27708008
RV167_YEASTRVS167genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSH4_YEAST

loading...

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-95 AND SER-358, 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-358, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory