P5CR_YEAST - dbPTM
P5CR_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P5CR_YEAST
UniProt AC P32263
Protein Name Pyrroline-5-carboxylate reductase
Gene Name PRO3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 286
Subcellular Localization
Protein Description
Protein Sequence MTYTLAILGCGVMGQALLSAIYNAPKAADETAAAFYPSKIITCNHDEPSAQQVTDLVETFDESPNGIKVESTYGHNVSAVEEASVVLLGTKPFLAEEVLNGVKSVIGGKLLISLAAGWTIDQLSQYTSTVCRVMTNTPAKYGYGCAVVSYSADVSKEQKPLVNELISQVGKYVELPEKNMDAATALVGSGPAFVLLMLESLMESGLKLGIPLQESKECAMKVLEGTVKMVEKSGAHPSVLKHQVCTPGGTTIAGLCVMEEKGVKSGIINGVEEAARVASQLGQKKK
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------MTYTLAILG
------CCEEEEHHC
25.8030377154
3Phosphorylation-----MTYTLAILGC
-----CCEEEEHHCC
9.8430377154
22PhosphorylationQALLSAIYNAPKAAD
HHHHHHHHCCCHHCC
12.6528132839
140UbiquitinationVMTNTPAKYGYGCAV
HHCCCCCCCCCCEEE
40.1723749301
151PhosphorylationGCAVVSYSADVSKEQ
CEEEEEEECCCCHHH
15.5327017623
159AcetylationADVSKEQKPLVNELI
CCCCHHHHHHHHHHH
41.2224489116
171AcetylationELISQVGKYVELPEK
HHHHHHHHHCCCCCC
47.4624489116
171UbiquitinationELISQVGKYVELPEK
HHHHHHHHHCCCCCC
47.4623749301
216UbiquitinationGIPLQESKECAMKVL
CCCHHHCHHHHHHHH
56.9423749301
216SuccinylationGIPLQESKECAMKVL
CCCHHHCHHHHHHHH
56.9423954790
216AcetylationGIPLQESKECAMKVL
CCCHHHCHHHHHHHH
56.9424489116
221UbiquitinationESKECAMKVLEGTVK
HCHHHHHHHHHHHHH
25.7423749301
228UbiquitinationKVLEGTVKMVEKSGA
HHHHHHHHHHHHCCC
36.7523749301
228AcetylationKVLEGTVKMVEKSGA
HHHHHHHHHHHHCCC
36.7524489116
232AcetylationGTVKMVEKSGAHPSV
HHHHHHHHCCCCHHH
42.6622865919
232UbiquitinationGTVKMVEKSGAHPSV
HHHHHHHHCCCCHHH
42.6623749301
233PhosphorylationTVKMVEKSGAHPSVL
HHHHHHHCCCCHHHH
27.9228889911
246PhosphorylationVLKHQVCTPGGTTIA
HHCEEEECCCCCEEE
26.5521440633
250PhosphorylationQVCTPGGTTIAGLCV
EEECCCCCEEEEEEE
22.4228889911
251PhosphorylationVCTPGGTTIAGLCVM
EECCCCCEEEEEEEE
16.4729734811
261UbiquitinationGLCVMEEKGVKSGII
EEEEECCCCCCCCCC
56.5522817900
264UbiquitinationVMEEKGVKSGIINGV
EECCCCCCCCCCCHH
52.1923749301
265PhosphorylationMEEKGVKSGIINGVE
ECCCCCCCCCCCHHH
32.5821440633
279PhosphorylationEEAARVASQLGQKKK
HHHHHHHHHHCCCCC
24.0722369663
284SuccinylationVASQLGQKKK-----
HHHHHCCCCC-----
61.8123954790

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 P5CR_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P5CR_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 P5CR_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P5CR_YEASTPRO3physical
10688190
URE2_YEASTURE2genetic
12620851
MAM33_YEASTMAM33physical
16554755
NAP1_YEASTNAP1physical
16554755
COPB2_YEASTSEC27physical
18467557
P5CR_YEASTPRO3physical
18467557
ATX1_YEASTATX1physical
18467557
P5CR_YEASTPRO3physical
18719252
PUT4_YEASTPUT4genetic
16941010
UBR1_YEASTUBR1genetic
22670231
SAN1_YEASTSAN1genetic
22670231
COPB2_YEASTSEC27physical
22615397
PUT1_YEASTPUT1genetic
25112878

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P5CR_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 THR-246 AND SER-279, ANDMASS SPECTROMETRY.

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