CMC1_YEAST - dbPTM
CMC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMC1_YEAST
UniProt AC D6W196
Protein Name Truncated non-functional calcium-binding mitochondrial carrier SAL1-1
Gene Name SAL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 494
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Calcium-dependent mitochondrial solute carrier..
Protein Sequence MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKVNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESSIKFGSFEVTKKIMTKLEGCRDTKDLSKFSTYIAGGLAGMAAQFSVYPIDTLKFRVQCAPLDTKLKGNNLLFQTAKDMFREGGGQIILQRCHSRYSGHISLCCIRFGDFFCLKKMVYCQTGKDPEPTTRSGHSKQPGCTSNGCIQWNCRSFCCLSNQSFKNKTTSPRNICTSLCV
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
75AcetylationVVDLSDFKKYASNAE
CCCHHHHHHHHHCHH		50.2825381059
156PhosphorylationIALRGQASHKKNTDN
EECCCHHHCCCCCCC		28.1417287358
161PhosphorylationQASHKKNTDNDRSKK
HHHCCCCCCCCCCCC		45.0917287358
268PhosphorylationLSSILLNSKTDLLAK
HHHHHHCCCHHHHHC		36.5827017623
330AcetylationFGSFEVTKKIMTKLE
ECCHHHHHHHHHHCC		45.5424489116
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 CMC1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMC1_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 CMC1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADT2_YEASTPET9genetic
18431598
SHY1_YEASTSHY1genetic
18431598
MTG1_YEASTMTG1genetic
18431598
ADT1_YEASTAAC1genetic
18431598
RIC1_YEASTRIC1genetic
20093466
MDM12_YEASTMDM12genetic
20093466
RAS1_YEASTRAS1genetic
20093466
VPS17_YEASTVPS17genetic
20093466
ASI3_YEASTASI3physical
16093310
SLA1_YEASTSLA1genetic
21987634
RS8A_YEASTRPS8Agenetic
21987634
RS8B_YEASTRPS8Agenetic
21987634
DOP1_YEASTDOP1genetic
21987634
ISC1_YEASTISC1genetic
21987634
PEP12_YEASTPEP12genetic
21987634
GEP3_YEASTGEP3genetic
21987634
INO2_YEASTINO2genetic
27708008
ASF1_YEASTASF1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CMC1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND THR-161, ANDMASS SPECTROMETRY.

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