P5CR1_HUMAN - dbPTM
P5CR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P5CR1_HUMAN
UniProt AC P32322
Protein Name Pyrroline-5-carboxylate reductase 1, mitochondrial
Gene Name PYCR1
Organism Homo sapiens (Human).
Sequence Length 319
Subcellular Localization Mitochondrion .
Protein Description Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress..
Protein Sequence MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPAAIKKTILDKVKLDSPAGTALSPSGHTKLLPRSLAPAGKD
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------MSVGFIGAG
------CCCCCCCHH		30.8320071362
2Acetylation------MSVGFIGAG
------CCCCCCCHH		30.8319413330
17MalonylationQLAFALAKGFTAAGV
HHHHHHHHCCCHHHH		56.2426320211
20PhosphorylationFALAKGFTAAGVLAA
HHHHHCCCHHHHHHH		25.0229396449
31SulfoxidationVLAAHKIMASSPDMD
HHHHHHHHHCCCCCC		3.3621406390
33PhosphorylationAAHKIMASSPDMDLA
HHHHHHHCCCCCCHH		25.6428634298
34PhosphorylationAHKIMASSPDMDLAT
HHHHHHCCCCCCHHH		18.5128634298
41PhosphorylationSPDMDLATVSALRKM
CCCCCHHHHHHHHHC		23.4528634298
43PhosphorylationDMDLATVSALRKMGV
CCCHHHHHHHHHCCC		19.7528634298
51AcetylationALRKMGVKLTPHNKE
HHHHCCCCCCCCCCC		40.7025953088
51UbiquitinationALRKMGVKLTPHNKE
HHHHCCCCCCCCCCC		40.70-
109PhosphorylationSSIEKKLSAFRPAPR
HHHHHHHHCCCCCCE		33.9524719451
122PhosphorylationPRVIRCMTNTPVVVR
CEEEEECCCCCEEEE		39.3029449344
133PhosphorylationVVVREGATVYATGTH
EEEECCCEEEECCCC		25.5528152594
135PhosphorylationVREGATVYATGTHAQ
EECCCEEEECCCCCC		8.2928152594
137PhosphorylationEGATVYATGTHAQVE
CCCEEEECCCCCCCC		25.5628152594
139PhosphorylationATVYATGTHAQVEDG
CEEEECCCCCCCCCC		15.0828152594
215AcetylationQALLGAAKMLLHSEQ
HHHHHHHHHHHCCCC		29.5525953088
215UbiquitinationQALLGAAKMLLHSEQ
HHHHHHHHHHHCCCC		29.5521906983
228UbiquitinationEQHPGQLKDNVSSPG
CCCCCCCCCCCCCCC		39.0921906983
232PhosphorylationGQLKDNVSSPGGATI
CCCCCCCCCCCCCEE		36.7530108239
233PhosphorylationQLKDNVSSPGGATIH
CCCCCCCCCCCCEEE		24.2325159151
238PhosphorylationVSSPGGATIHALHVL
CCCCCCCEEEEEEEH		19.3030108239
242UbiquitinationGGATIHALHVLESGG
CCCEEEEEEEHHHCC		1.45-
242UbiquitinationGGATIHALHVLESGG
CCCEEEEEEEHHHCC		1.4521906983
247PhosphorylationHALHVLESGGFRSLL
EEEEEHHHCCCHHHH		39.8022210691
252PhosphorylationLESGGFRSLLINAVE
HHHCCCHHHHHHHHH		25.85-
255UbiquitinationGGFRSLLINAVEASC
CCCHHHHHHHHHHHH		3.64-
255UbiquitinationGGFRSLLINAVEASC
CCCHHHHHHHHHHHH		3.6421906983
261PhosphorylationLINAVEASCIRTREL
HHHHHHHHHHCHHHH		9.1421712546
262S-nitrosocysteineINAVEASCIRTRELQ
HHHHHHHHHCHHHHH		2.92-
262GlutathionylationINAVEASCIRTRELQ
HHHHHHHHHCHHHHH		2.9222555962
262S-nitrosylationINAVEASCIRTRELQ
HHHHHHHHHCHHHHH		2.9219483679
265PhosphorylationVEASCIRTRELQSMA
HHHHHHCHHHHHHHC		14.48-
270PhosphorylationIRTRELQSMADQEQV
HCHHHHHHHCCHHCC		28.67-
271SulfoxidationRTRELQSMADQEQVS
CHHHHHHHCCHHCCC		2.8421406390
278PhosphorylationMADQEQVSPAAIKKT
HCCHHCCCHHHHHHH		14.4430266825
283UbiquitinationQVSPAAIKKTILDKV
CCCHHHHHHHHHHHC		38.8521906983
289UbiquitinationIKKTILDKVKLDSPA
HHHHHHHHCCCCCCC		37.51-
291UbiquitinationKTILDKVKLDSPAGT
HHHHHHCCCCCCCCC		52.93-
294PhosphorylationLDKVKLDSPAGTALS
HHHCCCCCCCCCCCC		27.3825159151
298PhosphorylationKLDSPAGTALSPSGH
CCCCCCCCCCCCCCC		26.9130266825
301PhosphorylationSPAGTALSPSGHTKL
CCCCCCCCCCCCCCC		17.9830266825
303PhosphorylationAGTALSPSGHTKLLP
CCCCCCCCCCCCCCC		39.5730266825
306PhosphorylationALSPSGHTKLLPRSL
CCCCCCCCCCCCHHH		27.2320068231
310UbiquitinationSGHTKLLPRSLAPAG
CCCCCCCCHHHCCCC		33.96-
310UbiquitinationSGHTKLLPRSLAPAG
CCCCCCCCHHHCCCC		33.9621906983
318UbiquitinationRSLAPAGKD------
HHHCCCCCC------		63.47-
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 P5CR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P5CR1_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 P5CR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUDT5_HUMANNUDT5physical
26186194
P5CR2_HUMANPYCR2physical
26186194
KLD10_HUMANKLHDC10physical
26186194
P5CR3_HUMANPYCRLphysical
26186194
CCD47_HUMANCCDC47physical
26344197
P5CR2_HUMANPYCR2physical
28514442
KLD10_HUMANKLHDC10physical
28514442
NUDT5_HUMANNUDT5physical
28514442
P5CR3_HUMANPYCRLphysical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
612940Cutis laxa, autosomal recessive, 2B (ARCL2B)
614438Cutis laxa, autosomal recessive, 3B (ARCL3B)
Kegg Drug
DrugBank
DB00172L-Proline
Regulatory Network of P5CR1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory