MPCP_YEAST - dbPTM
MPCP_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPCP_YEAST
UniProt AC P23641
Protein Name Mitochondrial phosphate carrier protein
Gene Name MIR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 311
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description Transport of phosphate groups from the cytosol to the mitochondrial matrix..
Protein Sequence MSVSAAPAIPQYSVSDYMKFALAGAIGCGSTHSSMVPIDVVKTRIQLEPTVYNKGMVGSFKQIIAGEGAGALLTGFGPTLLGYSIQGAFKFGGYEVFKKFFIDNLGYDTASRYKNSVYMGSAAMAEFLADIALCPLEATRIRLVSQPQFANGLVGGFSRILKEEGIGSFYSGFTPILFKQIPYNIAKFLVFERASEFYYGFAGPKEKLSSTSTTLLNLLSGLTAGLAAAIVSQPADTLLSKVNKTKKAPGQSTVGLLAQLAKQLGFFGSFAGLPTRLVMVGTLTSLQFGIYGSLKSTLGCPPTIEIGGGGH
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
2Acetylation------MSVSAAPAI
------CCCCCCCCC		25.4417761666
2Phosphorylation------MSVSAAPAI
------CCCCCCCCC		25.4428152593
4Phosphorylation----MSVSAAPAIPQ
----CCCCCCCCCCC		16.0628889911
12PhosphorylationAAPAIPQYSVSDYMK
CCCCCCCCCHHHHHH		12.9928889911
19UbiquitinationYSVSDYMKFALAGAI
CCHHHHHHHHHHHHC		22.6617644757
42AcetylationMVPIDVVKTRIQLEP
CCCCHHEECEEEECC		31.7524489116
42UbiquitinationMVPIDVVKTRIQLEP
CCCCHHEECEEEECC		31.7517644757
54AcetylationLEPTVYNKGMVGSFK
ECCCCCCCCCCCCHH		30.6024489116
54UbiquitinationLEPTVYNKGMVGSFK
ECCCCCCCCCCCCHH		30.6024961812
90UbiquitinationYSIQGAFKFGGYEVF
EECCCCHHHCCHHHH		42.4317644757
982-HydroxyisobutyrylationFGGYEVFKKFFIDNL
HCCHHHHHHHHHHHC		54.57-
98UbiquitinationFGGYEVFKKFFIDNL
HCCHHHHHHHHHHHC		54.5717644757
98SuccinylationFGGYEVFKKFFIDNL
HCCHHHHHHHHHHHC		54.5723954790
98AcetylationFGGYEVFKKFFIDNL
HCCHHHHHHHHHHHC		54.5724489116
99UbiquitinationGGYEVFKKFFIDNLG
CCHHHHHHHHHHHCC		33.7617644757
145PhosphorylationATRIRLVSQPQFANG
HHHEEEECCHHHHCC		40.5128889911
162UbiquitinationGGFSRILKEEGIGSF
CHHHHHHHHHCCCCC		51.8817644757
179UbiquitinationGFTPILFKQIPYNIA
CCHHHHHHHCCHHHH		43.8217644757
187AcetylationQIPYNIAKFLVFERA
HCCHHHHHHHHHHCH		35.1224489116
205UbiquitinationYYGFAGPKEKLSSTS
HCCCCCCHHHCCHHH		67.5717644757
205AcetylationYYGFAGPKEKLSSTS
HCCCCCCHHHCCHHH		67.5724489116
2052-HydroxyisobutyrylationYYGFAGPKEKLSSTS
HCCCCCCHHHCCHHH		67.57-
207UbiquitinationGFAGPKEKLSSTSTT
CCCCCHHHCCHHHHH		60.8517644757
241UbiquitinationPADTLLSKVNKTKKA
CHHHHHHHHCCCCCC		50.2017644757
246UbiquitinationLSKVNKTKKAPGQST
HHHHCCCCCCCCCCH		48.8517644757
247UbiquitinationSKVNKTKKAPGQSTV
HHHCCCCCCCCCCHH		66.1117644757
252PhosphorylationTKKAPGQSTVGLLAQ
CCCCCCCCHHHHHHH		30.8621126336
262UbiquitinationGLLAQLAKQLGFFGS
HHHHHHHHHHCCCHH		55.4317644757
297PhosphorylationIYGSLKSTLGCPPTI
ECCCHHHHCCCCCEE		26.1128889911
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 MPCP_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPCP_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 MPCP_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM29_YEASTECM29physical
16429126
IMB2_YEASTKAP104physical
16429126
GEA2_YEASTGEA2physical
16429126
TBA1_YEASTTUB1physical
16429126
XPO1_YEASTCRM1physical
16429126
HSC82_YEASTHSC82physical
16429126
PYR1_YEASTURA2physical
16429126
FAS1_YEASTFAS1physical
16429126
GDE_YEASTGDB1physical
16429126
HSP60_YEASTHSP60physical
16429126
NU192_YEASTNUP192physical
16429126
PPZ1_YEASTPPZ1physical
16429126
CBS_YEASTCYS4genetic
21623372
ADH3_YEASTADH3genetic
21623372
GLRX3_YEASTGRX3genetic
21623372
CEM1_YEASTCEM1genetic
21623372
PHSG_YEASTGPH1genetic
21623372
PPT2_YEASTPPT2genetic
21623372
CSG2_YEASTCSG2genetic
21623372
SUR2_YEASTSUR2genetic
21623372
ALDH6_YEASTALD6genetic
21623372
COQ2_YEASTCOQ2genetic
21623372
FUMH_YEASTFUM1genetic
21623372
ELO2_YEASTELO2genetic
21623372
FHP_YEASTYHB1genetic
27708008
INO4_YEASTINO4genetic
27708008
FTH1_YEASTFTH1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
RIM1_YEASTRIM1genetic
27708008
SAN1_YEASTSAN1genetic
27708008
PIC2_YEASTPIC2genetic
27708008
MIG1_YEASTMIG1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
SODM_YEASTSOD2genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
ECM12_YEASTECM12genetic
27708008
ORN_YEASTREX2genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
ATP10_YEASTATP10genetic
27708008
PHO23_YEASTPHO23genetic
27708008
TOM70_YEASTTOM70genetic
27708008
ATG3_YEASTATG3genetic
27708008
CY1_YEASTCYT1genetic
27708008
ALDH6_YEASTALD6genetic
27708008
ISU1_YEASTISU1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPCP_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-145 AND THR-297,AND MASS SPECTROMETRY.

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