SMF1_YEAST - dbPTM
SMF1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMF1_YEAST
UniProt AC P38925
Protein Name Manganese transporter SMF1
Gene Name SMF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 575
Subcellular Localization Cell membrane
Multi-pass membrane protein . Targeted to the vacuolar lumen in presence of excess manganese, where it is degraded.
Protein Description High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel..
Protein Sequence MVNVGPSHAAVAVDASEARKRNISEEVFELRDKKDSTVVIEGEAPVRTFTSSSSNHEREDTYVSKRQVMRDIFAKYLKFIGPGLMVSVAYIDPGNYSTAVDAGASNQFSLLCIILLSNFIAIFLQCLCIKLGSVTGLDLSRACREYLPRWLNWTLYFFAECAVIATDIAEVIGTAIALNILIKVPLPAGVAITVVDVFLIMFTYKPGASSIRFIRIFECFVAVLVVGVCICFAIELAYIPKSTSVKQVFRGFVPSAQMFDHNGIYTAISILGATVMPHSLFLGSALVQPRLLDYDVKHGNYTVSEEQDKVKKSKSTEEIMEEKYFNYRPTNAAIKYCMKYSMVELSITLFTLALFVNCAILVVAGSTLYNSPEADGADLFTIHELLSRNLAPAAGTIFMLALLLSGQSAGVVCTMSGQIVSEGHINWKLQPWQRRLATRCISIIPCLVISICIGREALSKALNASQVVLSIVLPFLVAPLIFFTCKKSIMKTEITVDHTEEDSHNHQNNNDRSAGSVIEQDGSSGMEIENGKDVKIVYMANNWIITVIAIIVWLFLSLLNVYAIVQLGMSHGDIS
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
7Phosphorylation-MVNVGPSHAAVAVD
-CCCCCCCCCEEECC		21.6030377154
16PhosphorylationAAVAVDASEARKRNI
CEEECCHHHHHHCCC		27.5930377154
24PhosphorylationEARKRNISEEVFELR
HHHHCCCCHHHHHHH		31.1124961812
33UbiquitinationEVFELRDKKDSTVVI
HHHHHHCCCCCEEEE		52.6324961812
34UbiquitinationVFELRDKKDSTVVIE
HHHHHCCCCCEEEEE		62.2923749301
51PhosphorylationAPVRTFTSSSSNHER
CCEEEECCCCCCCCC		24.8330377154
52PhosphorylationPVRTFTSSSSNHERE
CEEEECCCCCCCCCC		34.4327017623
53PhosphorylationVRTFTSSSSNHERED
EEEECCCCCCCCCCC		34.6228889911
54PhosphorylationRTFTSSSSNHEREDT
EEECCCCCCCCCCCC		44.1230377154
140PhosphorylationSVTGLDLSRACREYL
CCCCCCHHHHHHHHH		19.9427017623
297UbiquitinationRLLDYDVKHGNYTVS
CCCCCCCCCCCEECC		42.7823749301
309UbiquitinationTVSEEQDKVKKSKST
ECCHHHHHHHCCCCH		56.5023793018
311UbiquitinationSEEQDKVKKSKSTEE
CHHHHHHHCCCCHHH		58.0022817900
312UbiquitinationEEQDKVKKSKSTEEI
HHHHHHHCCCCHHHH		67.1322817900
313PhosphorylationEQDKVKKSKSTEEIM
HHHHHHCCCCHHHHH		26.5627717283
314UbiquitinationQDKVKKSKSTEEIME
HHHHHCCCCHHHHHH		70.9923749301
315PhosphorylationDKVKKSKSTEEIMEE
HHHHCCCCHHHHHHH		48.4123749301
316PhosphorylationKVKKSKSTEEIMEEK
HHHCCCCHHHHHHHH		41.1827214570
323UbiquitinationTEEIMEEKYFNYRPT
HHHHHHHHHHCCCCC		41.6623749301
513PhosphorylationHQNNNDRSAGSVIEQ
CCCCCCCCCCCEEEE		39.5823749301
516PhosphorylationNNDRSAGSVIEQDGS
CCCCCCCCEEEECCC		21.4623749301
523PhosphorylationSVIEQDGSSGMEIEN
CEEEECCCCCCEEEC		31.8223749301
524PhosphorylationVIEQDGSSGMEIENG
EEEECCCCCCEEECC		47.9223749301
532UbiquitinationGMEIENGKDVKIVYM
CCEEECCCEEEEEEE		71.5723749301
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMF1_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 SMF1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMF2_YEASTSMF2genetic
1447206
PER1_YEASTPER1genetic
9560393
SMF2_YEASTSMF2genetic
17932044
ECM21_YEASTECM21physical
18953286
CDC1_YEASTCDC1genetic
9560392
SMF3_YEASTSMF3genetic
17932044
BUD31_YEASTBUD31genetic
27708008
MTU1_YEASTSLM3genetic
27708008
ENV10_YEASTENV10genetic
27708008
RAD1_YEASTRAD1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
PP2C3_YEASTPTC3genetic
27708008
FLR1_YEASTFLR1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
VAC17_YEASTVAC17genetic
27708008
UBP3_YEASTUBP3genetic
27708008
MED20_YEASTSRB2genetic
27708008
MMR1_YEASTMMR1genetic
27708008
SPH1_YEASTSPH1genetic
27708008
ELP6_YEASTELP6genetic
27708008
ELOC_YEASTELC1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMF1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASSSPECTROMETRY.

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