SPRE_HUMAN - dbPTM
SPRE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPRE_HUMAN
UniProt AC P35270
Protein Name Sepiapterin reductase
Gene Name SPR
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin..
Protein Sequence MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSGLRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQVNNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDMLFQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQKLLSLLEKDEFKSGAHVDFYDK
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
1Acetylation-------MEGGLGRA
-------CCCCHHHH		11.02-
13PhosphorylationGRAVCLLTGASRGFG
HHHHHHHHCCCCCCC		20.1123312004
16PhosphorylationVCLLTGASRGFGRTL
HHHHHCCCCCCCHHH		33.9927050516
22PhosphorylationASRGFGRTLAPLLAS
CCCCCCHHHHHHHHH		27.8720071362
29PhosphorylationTLAPLLASLLSPGSV
HHHHHHHHHCCCCCE		29.7920071362
32PhosphorylationPLLASLLSPGSVLVL
HHHHHHCCCCCEEEE		32.2920071362
35PhosphorylationASLLSPGSVLVLSAR
HHHCCCCCEEEEECC		18.70-
40PhosphorylationPGSVLVLSARNDEAL
CCCEEEEECCCHHHH		20.08-
90UbiquitinationLRELPRPKGLQRLLL
HHHCCCCCCHHHEEE		73.8024816145
103PhosphorylationLLINNAGSLGDVSKG
EEEECCCCCCCCCCC		27.1130266825
108PhosphorylationAGSLGDVSKGFVDLS
CCCCCCCCCCCCCCC		31.6230266825
145PhosphorylationVLKAFPDSPGLNRTV
HHHHCCCCCCCCCEE		22.5522985185
170PhosphorylationPFKGWALYCAGKAAR
CCCCHHHHHCHHHHH		3.4325147952
174AcetylationWALYCAGKAARDMLF
HHHHHCHHHHHHHHH		21.9826051181
212PhosphorylationMQQLARETSVDPDMR
HHHHHHHHCCCHHHH		28.6228857561
213PhosphorylationQQLARETSVDPDMRK
HHHHHHHCCCHHHHH		21.5516650784
226AcetylationRKGLQELKAKGKLVD
HHHHHHHHHCCCEEE		47.5025953088
226UbiquitinationRKGLQELKAKGKLVD
HHHHHHHHHCCCEEE		47.5027667366
230UbiquitinationQELKAKGKLVDCKVS
HHHHHCCCEEECHHH		44.6333845483
230AcetylationQELKAKGKLVDCKVS
HHHHHCCCEEECHHH		44.6323749302
235UbiquitinationKGKLVDCKVSAQKLL
CCCEEECHHHHHHHH		34.4623000965
2352-HydroxyisobutyrylationKGKLVDCKVSAQKLL
CCCEEECHHHHHHHH		34.46-
240AcetylationDCKVSAQKLLSLLEK
ECHHHHHHHHHHHHH		51.6225953088
240UbiquitinationDCKVSAQKLLSLLEK
ECHHHHHHHHHHHHH		51.6223000965
243PhosphorylationVSAQKLLSLLEKDEF
HHHHHHHHHHHHCCC		41.1524719451
247AcetylationKLLSLLEKDEFKSGA
HHHHHHHHCCCCCCC		63.6327452117
247UbiquitinationKLLSLLEKDEFKSGA
HHHHHHHHCCCCCCC		63.6329967540
2472-HydroxyisobutyrylationKLLSLLEKDEFKSGA
HHHHHHHHCCCCCCC		63.63-
251UbiquitinationLLEKDEFKSGAHVDF
HHHHCCCCCCCCCCC		46.0333845483
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
213SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
213SPhosphorylationKinaseCAMK2BQ13554
GPS
213SPhosphorylationKinaseCAMK2-FAMILY-GPS
213SPhosphorylationKinaseCAMK2-Uniprot
213SPhosphorylationKinaseCCDPK-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
213SPhosphorylation

11825621
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 SPRE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRPRB_HUMANSRPRBphysical
22939629
THIC_HUMANACAT2physical
26344197
MMSA_HUMANALDH6A1physical
26344197
PUR9_HUMANATICphysical
26344197
COX17_HUMANCOX17physical
26344197
DUT_HUMANDUTphysical
26344197
FUBP1_HUMANFUBP1physical
26344197
HINT1_HUMANHINT1physical
26344197
CH10_HUMANHSPE1physical
26344197
LEG3_HUMANLGALS3physical
26344197
LKHA4_HUMANLTA4Hphysical
26344197
MDHC_HUMANMDH1physical
26344197
MIF_HUMANMIFphysical
26344197
PIMT_HUMANPCMT1physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PEBP1_HUMANPEBP1physical
26344197
PIN1_HUMANPIN1physical
26344197
PRDX1_HUMANPRDX1physical
26344197
PRDX2_HUMANPRDX2physical
26344197
PRDX5_HUMANPRDX5physical
26344197
PRDX6_HUMANPRDX6physical
26344197
DHPR_HUMANQDPRphysical
26344197
SERPH_HUMANSERPINH1physical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TKT_HUMANTKTphysical
26344197
UFC1_HUMANUFC1physical
26344197
UFM1_HUMANUFM1physical
26344197
YKT6_HUMANYKT6physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612716Dystonia, DOPA-responsive, due to sepiapterin reductase deficiency (DRDSPRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPRE_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mutational analysis of sites in sepiapterin reductase phosphorylatedby Ca2+/calmodulin-dependent protein kinase II.";
Fujimoto K., Takahashi S.Y., Katoh S.;
Biochim. Biophys. Acta 1594:191-198(2002).
Cited for: KINETIC PARAMETERS, PHOSPHORYLATION AT SER-213, AND MUTAGENESIS OFSER-213.

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