LAM5_YEAST - dbPTM
LAM5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAM5_YEAST
UniProt AC P43560
Protein Name Membrane-anchored lipid-binding protein LAM5 {ECO:0000303|PubMed:26001273}
Gene Name LAM5 {ECO:0000303|PubMed:26001273}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 674
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Localizes to intracellular puncta representing endoplasmic reticulum (ER)-mitochondrion membrane contact sites, nucleus-vacuole junctions (NVJ) and other non-NVJ ER-vacuole contact sites
Protein Description May be involved in sterol transfer between intracellular membranes..
Protein Sequence MSDVDNWEPVSDNEDSTDSVKQLGPPFEHASNNDNAGDTEAESLQEVPLNTETNDVRKNLVVITNQSAADEHPTEIKHDQSRTSSTSSFFSGMISSFKSNVPSPVSRSTTPTSPVSQPSIISHRREPSMGSKRRSSRRISNATIAEIGSPLQQVEKPDEVKTRLTPSQMKEDNYDHRRFVEERYMDTPYHYASEQRNKDFHETFKSVPKDDRLLDDFNCGLNRELLYQGKLYITETHLCFNSNVLGWIAKVLIAFEDVTFMEKTSAAGLFPSAISIETKMGKTLFNGFISRDAAFGLMKEVWSRTLLQKDMASENINTKAEKSGNGKEIDDAINSIDEENNDKDANDNDTNENDDENISTNETTPNSTSSSPDKEKEKAYKLRADSSYQYDGPIYHHSTSFPAEPMANNEFVLKELPFDCAPGILFEIMFNSEQNEFLLDFLRGQEGSQITTIPNFTSIDGSSMTLKREYSYEKALHFPAGPKSTTCYVAEVIKRKDPDTYYEVISSIRTPNVPSGGSFSTKTRYLIRWNDEITCLLRVSFWVEWTGSSWIKGMVENGCKNGQLEAAQLMERILSKFIKNNVEECQITISKEEEEQDDKEVKNKLKEVDLEQPREAVVTAPAIAEQQGLKVTMETWLFLYLIVVVLLLFNLFYIRSIAVSLHQLVKLQLVELKL
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
2Phosphorylation------MSDVDNWEP
------CCCCCCCCC
28152593
11PhosphorylationVDNWEPVSDNEDSTD
CCCCCCCCCCCCCCH
28152593
16PhosphorylationPVSDNEDSTDSVKQL
CCCCCCCCCHHHHHH
24961812
17PhosphorylationVSDNEDSTDSVKQLG
CCCCCCCCHHHHHHC
24961812
19PhosphorylationDNEDSTDSVKQLGPP
CCCCCCHHHHHHCCC
24961812
31PhosphorylationGPPFEHASNNDNAGD
CCCCCCCCCCCCCCC
19823750
39PhosphorylationNNDNAGDTEAESLQE
CCCCCCCCCCHHHHC
21440633
43PhosphorylationAGDTEAESLQEVPLN
CCCCCCHHHHCCCCC
20377248
51PhosphorylationLQEVPLNTETNDVRK
HHCCCCCCCCCCCHH
19823750
53PhosphorylationEVPLNTETNDVRKNL
CCCCCCCCCCCHHCE
19823750
74PhosphorylationSAADEHPTEIKHDQS
CCCCCCCCCCCCCCC
25704821
84PhosphorylationKHDQSRTSSTSSFFS
CCCCCCCCCCHHHHH
27017623
85PhosphorylationHDQSRTSSTSSFFSG
CCCCCCCCCHHHHHH
27017623
88PhosphorylationSRTSSTSSFFSGMIS
CCCCCCHHHHHHHHH
27017623
99PhosphorylationGMISSFKSNVPSPVS
HHHHHHHHCCCCCCC
22369663
103PhosphorylationSFKSNVPSPVSRSTT
HHHHCCCCCCCCCCC
22369663
106PhosphorylationSNVPSPVSRSTTPTS
HCCCCCCCCCCCCCC
22369663
108PhosphorylationVPSPVSRSTTPTSPV
CCCCCCCCCCCCCCC
22369663
109PhosphorylationPSPVSRSTTPTSPVS
CCCCCCCCCCCCCCC
22369663
110PhosphorylationSPVSRSTTPTSPVSQ
CCCCCCCCCCCCCCC
22369663
112PhosphorylationVSRSTTPTSPVSQPS
CCCCCCCCCCCCCCC
22369663
113PhosphorylationSRSTTPTSPVSQPSI
CCCCCCCCCCCCCCC
22369663
116PhosphorylationTTPTSPVSQPSIISH
CCCCCCCCCCCCCCC
22890988
119PhosphorylationTSPVSQPSIISHRRE
CCCCCCCCCCCCCCC
22890988
122PhosphorylationVSQPSIISHRREPSM
CCCCCCCCCCCCCCC
22890988
128PhosphorylationISHRREPSMGSKRRS
CCCCCCCCCCCCCCC
21551504
131PhosphorylationRREPSMGSKRRSSRR
CCCCCCCCCCCCCHH
21440633
135PhosphorylationSMGSKRRSSRRISNA
CCCCCCCCCHHCCCC
24961812
136PhosphorylationMGSKRRSSRRISNAT
CCCCCCCCHHCCCCC
24961812
140PhosphorylationRRSSRRISNATIAEI
CCCCHHCCCCCHHHC
17330950
143PhosphorylationSRRISNATIAEIGSP
CHHCCCCCHHHCCCC
17330950
149PhosphorylationATIAEIGSPLQQVEK
CCHHHCCCCCHHCCC
17330950
165PhosphorylationDEVKTRLTPSQMKED
CCCCCCCCHHHHHCC
20377248
323PhosphorylationINTKAEKSGNGKEID
CCCHHHHCCCCCHHH
28889911
335PhosphorylationEIDDAINSIDEENND
HHHHHHHHCCCCCCC
22369663
359PhosphorylationENDDENISTNETTPN
CCCCCCCCCCCCCCC
20377248
448PhosphorylationFLRGQEGSQITTIPN
HHCCCCCCCEEECCC
27017623
451PhosphorylationGQEGSQITTIPNFTS
CCCCCCEEECCCCCE
27017623
462PhosphorylationNFTSIDGSSMTLKRE
CCCEECCCCCEEEEE
27017623
506PhosphorylationDTYYEVISSIRTPNV
CCHHHHHHHCCCCCC
27017623
520PhosphorylationVPSGGSFSTKTRYLI
CCCCCCCCCCEEEEE
27017623
521PhosphorylationPSGGSFSTKTRYLIR
CCCCCCCCCEEEEEE
27017623

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 LAM5_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAM5_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 LAM5_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPG_YEASTSEC21physical
22940862
COPD_YEASTRET2physical
22940862
COPA_YEASTCOP1physical
22940862
NCBP2_YEASTCBC2genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
PYC2_YEASTPYC2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
RIM1_YEASTRIM1genetic
27708008
LCMT1_YEASTPPM1genetic
27708008
MED5_YEASTNUT1genetic
27708008
ATC1_YEASTPMR1genetic
27708008
IRE1_YEASTIRE1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
PGM1_YEASTPGM1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ARP6_YEASTARP6genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
ARMT1_YEASTYMR027Wgenetic
27708008
CHMU_YEASTARO7genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAM5_YEAST

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Related Literatures of Post-Translational Modification

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