PYC2_YEAST - dbPTM
PYC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYC2_YEAST
UniProt AC P32327
Protein Name Pyruvate carboxylase 2
Gene Name PYC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1180
Subcellular Localization Cytoplasm.
Protein Description Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second..
Protein Sequence MSSSKKLAGLRDNFSLLGEKNKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQYTPVGAYLAMDEIIEIAKKHKVDFIHPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATLTQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGNAYAGATISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADLAVNGSSIKGQIGLPKLKSNPSVPHLHDAQGNVINVTKSAPPSGWRQVLLEKGPSEFAKQVRQFNGTLLMDTTWRDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLQPGKKYNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSINALLASLEGNIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPLRSDVLRNKRRKLTCRPGLELEPFDLEKIREDLQNRFGDIDECDVASYNMYPRVYEDFQKIRETYGDLSVLPTKNFLAPAEPDEEIEVTIEQGKTLIIKLQAVGDLNKKTGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIKDGESVDASDLLVVLEEETLPPSQKK
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------MSSSKKLAG
------CCCCHHHHH		55.4022814378
15PhosphorylationAGLRDNFSLLGEKNK
HHCCCCCHHHCCCCE		29.0128889911
20AcetylationNFSLLGEKNKILVAN
CCHHHCCCCEEEEEC		62.8424489116
20SuccinylationNFSLLGEKNKILVAN
CCHHHCCCCEEEEEC		62.8423954790
22UbiquitinationSLLGEKNKILVANRG
HHHCCCCEEEEECCC		48.7823749301
93UbiquitinationEIIEIAKKHKVDFIH
HHHHHHHHCCCCEEC		39.3717644757
95UbiquitinationIEIAKKHKVDFIHPG
HHHHHHCCCCEECCC		52.9917644757
95AcetylationIEIAKKHKVDFIHPG
HHHHHHCCCCEECCC		52.9924489116
115UbiquitinationENSEFADKVVKAGIT
CCHHHHHHHHHCCCE		45.5617644757
228UbiquitinationERFLDKPKHIEVQLL
EECCCCCCEEEEEEE		64.0617644757
258UbiquitinationSVQRRHQKVVEVAPA
CCHHHHHHEEEECCC		41.9723749301
266UbiquitinationVVEVAPAKTLPREVR
EEEECCCCCCCHHHH		49.9223749301
282UbiquitinationAILTDAVKLAKVCGY
HHHHHHHHHHHHCCC		44.4317644757
294PhosphorylationCGYRNAGTAEFLVDN
CCCCCCCEEEEEEEC		22.1728132839
370UbiquitinationITTEDPSKNFQPDTG
EECCCCCCCCCCCCC		68.1423749301
370AcetylationITTEDPSKNFQPDTG
EECCCCCCCCCCCCC		68.1424489116
484UbiquitinationSSQNRAQKLLHYLAD
HCCHHHHHHHHHHHH		52.6217644757
488PhosphorylationRAQKLLHYLADLAVN
HHHHHHHHHHHHHHC		11.9819823750
497PhosphorylationADLAVNGSSIKGQIG
HHHHHCCCCCCCCCC		24.5619823750
498PhosphorylationDLAVNGSSIKGQIGL
HHHHCCCCCCCCCCC		29.7119823750
500UbiquitinationAVNGSSIKGQIGLPK
HHCCCCCCCCCCCCC		46.8717644757
509UbiquitinationQIGLPKLKSNPSVPH
CCCCCCCCCCCCCCC		55.0724961812
510PhosphorylationIGLPKLKSNPSVPHL
CCCCCCCCCCCCCCC		65.4922369663
513PhosphorylationPKLKSNPSVPHLHDA
CCCCCCCCCCCCCCC		53.1622369663
528PhosphorylationQGNVINVTKSAPPSG
CCCEEEECCCCCCCC		18.1322369663
529UbiquitinationGNVINVTKSAPPSGW
CCEEEECCCCCCCCH		40.1017644757
543UbiquitinationWRQVLLEKGPSEFAK
HHHHHHHHCHHHHHH		75.8923749301
543AcetylationWRQVLLEKGPSEFAK
HHHHHHHHCHHHHHH		75.8924489116
659UbiquitinationNAIDHFVKQAKDNGV
HHHHHHHHHHHHCCC		43.5217644757
662UbiquitinationDHFVKQAKDNGVDIF
HHHHHHHHHCCCCHH		49.5923749301
682UbiquitinationLNDLEQLKVGVNAVK
HCCHHHHHCHHHHHH		36.3217644757
682AcetylationLNDLEQLKVGVNAVK
HCCHHHHHCHHHHHH		36.3224489116
711UbiquitinationDMLQPGKKYNLDYYL
CCCCCCCEECHHHHH		45.3317644757
723UbiquitinationYYLEVVEKIVQMGTH
HHHHHHHHHHHHCCH		36.2517644757
735N6-carboxylysineGTHILGIKDMAGTMK
CCHHCCCCCCCCCCC		39.39-
735CarboxylationGTHILGIKDMAGTMK
CCHHCCCCCCCCCCC		39.39-
742UbiquitinationKDMAGTMKPAAAKLL
CCCCCCCCHHHHHHH		31.2023749301
830PhosphorylationHVRELDAYWAEMRLL
HHHHHHHHHHHHHHH		12.5722369663
897UbiquitinationYLLGDIVKVTPTSKV
HHHCCCEECCCCCHH		40.5017644757
901PhosphorylationDIVKVTPTSKVVGDL
CCEECCCCCHHHHHH		31.6423749301
903UbiquitinationVKVTPTSKVVGDLAQ
EECCCCCHHHHHHHH		43.3423749301
967PhosphorylationRNKRRKLTCRPGLEL
HHCCCCCCCCCCCCC		14.9821440633
1013AcetylationRVYEDFQKIRETYGD
HHHHHHHHHHHHHCC		43.6624489116
1013UbiquitinationRVYEDFQKIRETYGD
HHHHHHHHHHHHHCC		43.6617644757
1125UbiquitinationHKGSLVKKGESIAVL
ECCCCEECCCCHHHH		61.5023749301
1128PhosphorylationSLVKKGESIAVLSAM
CCEECCCCHHHHEEC		25.2327017623
1133PhosphorylationGESIAVLSAMKMEMV
CCCHHHHEECEEEEE		21.5123749301
1136BiotinylationIAVLSAMKMEMVVSS
HHHHEECEEEEEEEC		31.27-
1136N6-biotinyllysineIAVLSAMKMEMVVSS
HHHHEECEEEEEEEC		31.27-
1173PhosphorylationLVVLEEETLPPSQKK
EEEEEECCCCCCCCC		48.0922369663
1177PhosphorylationEEETLPPSQKK----
EECCCCCCCCC----		53.3322369663
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 PYC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PYC2_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 PYC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALM_YEASTCMD1physical
16554755
PYC1_YEASTPYC1physical
16554755
MLC1_YEASTMLC1physical
16554755
TPM1_YEASTTPM1physical
16554755
PYC1_YEASTPYC1genetic
18408719
ACEA_YEASTICL1genetic
8543050
MASY_YEASTMLS1genetic
8543050
MTH1_YEASTMTH1genetic
8543050
PYC1_YEASTPYC1genetic
21623372
GPT1_YEASTSCT1genetic
21623372
ASK10_YEASTASK10genetic
27708008
DIT1_YEASTDIT1genetic
27708008
PFA5_YEASTPFA5genetic
27708008
SPI1_YEASTSPI1genetic
27708008
DMC1_YEASTDMC1genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
PYC1_YEASTPYC1genetic
27708008
YG2G_YEASTYGR079Wgenetic
27708008
RL11B_YEASTRPL11Bgenetic
27708008
GTO1_YEASTGTO1genetic
27708008
AZR1_YEASTAZR1genetic
27708008
YHA8_YEASTYHL008Cgenetic
27708008
STB5_YEASTSTB5genetic
27708008
HPM1_YEASTHPM1genetic
27708008
FABG_YEASTOAR1genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
LSM7_YEASTLSM7genetic
27708008
VPH1_YEASTVPH1genetic
27708008
MNE1_YEASTMNE1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
ASNS1_YEASTASN1genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PYC2_YEAST

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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-15 AND SER-513, AND MASSSPECTROMETRY.

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