P5CR2_HUMAN - dbPTM
P5CR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P5CR2_HUMAN
UniProt AC Q96C36
Protein Name Pyrroline-5-carboxylate reductase 2
Gene Name PYCR2
Organism Homo sapiens (Human).
Sequence Length 320
Subcellular Localization Cytoplasm . Mitochondrion .
Protein Description Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH. [PubMed: 2722838]
Protein Sequence MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRCMTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTLTPSSPGKLLTRSLALGGKKD
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
13PhosphorylationIGAGQLAYALARGFT
CCHHHHHHHHHHCCC		15.6729496907
20PhosphorylationYALARGFTAAGILSA
HHHHHCCCHHHHHHH		20.5824114839
26PhosphorylationFTAAGILSAHKIIAS
CCHHHHHHHHHHHHC		26.8027251275
33PhosphorylationSAHKIIASSPEMNLP
HHHHHHHCCCCCCCC		35.7020068231
34PhosphorylationAHKIIASSPEMNLPT
HHHHHHCCCCCCCCH		18.83-
41PhosphorylationSPEMNLPTVSALRKM
CCCCCCCHHHHHHHH		30.2028348404
43PhosphorylationEMNLPTVSALRKMGV
CCCCCHHHHHHHHCC		24.8628348404
47UbiquitinationPTVSALRKMGVNLTR
CHHHHHHHHCCCCCC		40.64-
47SuccinylationPTVSALRKMGVNLTR
CHHHHHHHHCCCCCC		40.6427452117
47MalonylationPTVSALRKMGVNLTR
CHHHHHHHHCCCCCC		40.6426320211
94PhosphorylationQARHIVVSCAAGVTI
CHHHHHHCCCCCCCH		6.2729083192
100PhosphorylationVSCAAGVTISSVEKK
HCCCCCCCHHHHHHH		17.7729083192
102PhosphorylationCAAGVTISSVEKKLM
CCCCCCHHHHHHHHH		20.9729083192
103PhosphorylationAAGVTISSVEKKLMA
CCCCCHHHHHHHHHH		30.3729083192
107UbiquitinationTISSVEKKLMAFQPA
CHHHHHHHHHHCCCC		29.95-
109SulfoxidationSSVEKKLMAFQPAPK
HHHHHHHHHCCCCCE		4.8821406390
116UbiquitinationMAFQPAPKVIRCMTN
HHCCCCCEEEEECCC		53.0221890473
228AcetylationEQHPCQLKDNVCSPG
CCCCCCCCCCEECCC		22.7525953088
233PhosphorylationQLKDNVCSPGGATIH
CCCCCEECCCCHHEH		23.4627050516
238PhosphorylationVCSPGGATIHALHFL
EECCCCHHEHHHHHH		19.3020873877
252PhosphorylationLESGGFRSLLINAVE
HHCCCCHHHHHHHHH		25.8524719451
261PhosphorylationLINAVEASCIRTREL
HHHHHHHHHHCHHHH		9.1421712546
262GlutathionylationINAVEASCIRTRELQ
HHHHHHHHHCHHHHH		2.9222555962
265PhosphorylationVEASCIRTRELQSMA
HHHHHHCHHHHHHHH		14.4824719451
276UbiquitinationQSMADQEKISPAALK
HHHHCHHCCCHHHHH		42.74-
276AcetylationQSMADQEKISPAALK
HHHHCHHCCCHHHHH		42.7419829087
2832-HydroxyisobutyrylationKISPAALKKTLLDRV
CCCHHHHHHHHHHHH		38.70-
283UbiquitinationKISPAALKKTLLDRV
CCCHHHHHHHHHHHH		38.70-
284UbiquitinationISPAALKKTLLDRVK
CCHHHHHHHHHHHHC		45.30-
291UbiquitinationKTLLDRVKLESPTVS
HHHHHHHCCCCCCCC		47.64-
294PhosphorylationLDRVKLESPTVSTLT
HHHHCCCCCCCCCCC		35.9924732914
296PhosphorylationRVKLESPTVSTLTPS
HHCCCCCCCCCCCCC		36.0524732914
298PhosphorylationKLESPTVSTLTPSSP
CCCCCCCCCCCCCCC		21.8524732914
299PhosphorylationLESPTVSTLTPSSPG
CCCCCCCCCCCCCCC		30.2524732914
301PhosphorylationSPTVSTLTPSSPGKL
CCCCCCCCCCCCCCH		22.6330266825
303PhosphorylationTVSTLTPSSPGKLLT
CCCCCCCCCCCCHHH		43.8830266825
304PhosphorylationVSTLTPSSPGKLLTR
CCCCCCCCCCCHHHH		38.5829255136
307UbiquitinationLTPSSPGKLLTRSLA
CCCCCCCCHHHHHHH		43.6521890473
307AcetylationLTPSSPGKLLTRSLA
CCCCCCCCHHHHHHH		43.6525953088
310PhosphorylationSSPGKLLTRSLALGG
CCCCCHHHHHHHCCC		28.7528152594
312PhosphorylationPGKLLTRSLALGGKK
CCCHHHHHHHCCCCC		16.8623312004
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
304SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P5CR2_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 P5CR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MYO1F_HUMANMYO1Fphysical
26186194
MY18A_HUMANMYO18Aphysical
26186194
SKA3_HUMANSKA3physical
26186194
NUDT5_HUMANNUDT5physical
26186194
SKA1_HUMANSKA1physical
26186194
AHNK2_HUMANAHNAK2physical
26186194
P5CR3_HUMANPYCRLphysical
26186194
P5CR1_HUMANPYCR1physical
26344197
SKA3_HUMANSKA3physical
28514442
SKA1_HUMANSKA1physical
28514442
NUDT5_HUMANNUDT5physical
28514442
MY18A_HUMANMYO18Aphysical
28514442
MYO1F_HUMANMYO1Fphysical
28514442
AHNK2_HUMANAHNAK2physical
28514442
P5CR3_HUMANPYCRLphysical
28514442
AHNK_HUMANAHNAKphysical
28514442
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 P5CR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-304, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASSSPECTROMETRY.

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