P5CR3_HUMAN - dbPTM
P5CR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P5CR3_HUMAN
UniProt AC Q53H96
Protein Name Pyrroline-5-carboxylate reductase 3 {ECO:0000312|HGNC:HGNC:25846}
Gene Name PYCR3 {ECO:0000312|HGNC:HGNC:25846}
Organism Homo sapiens (Human).
Sequence Length 274
Subcellular Localization Cytoplasm .
Protein Description Enzyme that catalyzes the last step in proline biosynthesis. Proline is synthesized from either glutamate or ornithine; both are converted to pyrroline-5-carboxylate (P5C), and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked to the conversion of ornithine to proline..
Protein Sequence MAAAEPSPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLCHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETKLLQHLLEACGRCEEVPEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHALEQGGLRAATMSAVEAATCRAKELSRK
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------MAAAEPSPR
------CCCCCCCCC		18.5122814378
7Phosphorylation-MAAAEPSPRRVGFV
-CCCCCCCCCCCCCC		23.6529255136
32MalonylationQGLIRAGKVEAQHIL
HHHHHCCCCCHHHHH		35.6026320211
32UbiquitinationQGLIRAGKVEAQHIL
HHHHHCCCCCHHHHH		35.60-
39UbiquitinationKVEAQHILASAPTDR
CCCHHHHHHCCCCCC		2.64-
44UbiquitinationHILASAPTDRNLCHF
HHHHCCCCCCCCCCH		47.51-
129GlutathionylationRVLPNLPCVVQEGAI
EECCCCCEEEECCEE		5.4422555962
146PhosphorylationARGRHVGSSETKLLQ
ECCCCCCCHHHHHHH		24.7429083192
147PhosphorylationRGRHVGSSETKLLQH
CCCCCCCHHHHHHHH		42.3820071362
149PhosphorylationRHVGSSETKLLQHLL
CCCCCHHHHHHHHHH		32.8729083192
159PhosphorylationLQHLLEACGRCEEVP
HHHHHHHCCCCCCCC		2.29-
202PhosphorylationAVKMGMPSSLAHRIA
HHHCCCCHHHHHHHH		29.1423403867
203PhosphorylationVKMGMPSSLAHRIAA
HHCCCCHHHHHHHHH		24.5723403867
212PhosphorylationAHRIAAQTLLGTAKM
HHHHHHHHHHHHHHH		21.1520068231
216PhosphorylationAAQTLLGTAKMLLHE
HHHHHHHHHHHHHHC		24.0720068231
218UbiquitinationQTLLGTAKMLLHEGQ
HHHHHHHHHHHHCCC		29.8921906983
228PhosphorylationLHEGQHPAQLRSDVC
HHCCCCHHHHCCCEE		20.9320068231
230UbiquitinationEGQHPAQLRSDVCTP
CCCCHHHHCCCEECC		6.51-
232PhosphorylationQHPAQLRSDVCTPGG
CCHHHHCCCEECCCC		42.8823312004
235GlutathionylationAQLRSDVCTPGGTTI
HHHCCCEECCCCCEE		4.5722555962
236PhosphorylationQLRSDVCTPGGTTIY
HHCCCEECCCCCEEE		25.4723312004
240PhosphorylationDVCTPGGTTIYGLHA
CEECCCCCEEECHHH		18.8820071362
241PhosphorylationVCTPGGTTIYGLHAL
EECCCCCEEECHHHH		18.5720071362
243PhosphorylationTPGGTTIYGLHALEQ
CCCCCEEECHHHHHH		16.1423312004
248PhosphorylationTIYGLHALEQGGLRA
EEECHHHHHHCCCCH		3.3424719451
257PhosphorylationQGGLRAATMSAVEAA
HCCCCHHHHHHHHHH		15.6328857561
266GlutathionylationSAVEAATCRAKELSR
HHHHHHHHHHHHHHC		3.2322555962
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 P5CR3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P5CR3_HUMAN !!
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 P5CR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN2B_HUMANCDKN2Bphysical
23718855
ANM6_HUMANPRMT6physical
23455924
P5CR3_HUMANPYCRLphysical
25416956
GPD1L_HUMANGPD1Lphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00172L-Proline
Regulatory Network of P5CR3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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