SRR_HUMAN - dbPTM
SRR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRR_HUMAN
UniProt AC Q9GZT4
Protein Name Serine racemase {ECO:0000303|PubMed:11054547}
Gene Name SRR
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization
Protein Description Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine..
Protein Sequence MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
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
5Phosphorylation---MCAQYCISFADV
---CCCCEEEEHHHH
3.5324043423
8PhosphorylationMCAQYCISFADVEKA
CCCCEEEEHHHHHHH
15.7224043423
45UbiquitinationTGRNLFFKCELFQKT
CCCCCEEEEEEEECC
21.33-
51UbiquitinationFKCELFQKTGSFKIR
EEEEEEECCCCEEHH
47.74-
56N6-(pyridoxal phosphate)lysineFQKTGSFKIRGALNA
EECCCCEEHHHHHHH
32.94-
56MethylationFQKTGSFKIRGALNA
EECCCCEEHHHHHHH
32.941147570889
56OtherFQKTGSFKIRGALNA
EECCCCEEHHHHHHH
32.94-
56UbiquitinationFQKTGSFKIRGALNA
EECCCCEEHHHHHHH
32.94-
66PhosphorylationGALNAVRSLVPDALE
HHHHHHHHHCHHHHH
27.4125003641
113S-nitrosylationVPQTAPDCKKLAIQA
CCCCCCCHHHHHHHH
4.0022178444
113S-nitrosocysteineVPQTAPDCKKLAIQA
CCCCCCCHHHHHHHH
4.00-
115UbiquitinationQTAPDCKKLAIQAYG
CCCCCHHHHHHHHCC
49.86-
134PhosphorylationYCEPSDESRENVAKR
EECCCHHHHHHHHHH
50.30-
205UbiquitinationKALKPSVKVYAAEPS
EHHCCCCEEEECCCC
33.59-
207PhosphorylationLKPSVKVYAAEPSNA
HCCCCEEEECCCCCH
8.38-
212PhosphorylationKVYAAEPSNADDCYQ
EEEECCCCCHHHHHH
35.83-
218PhosphorylationPSNADDCYQSKLKGK
CCCHHHHHHHHHCCC
23.86-
220PhosphorylationNADDCYQSKLKGKLM
CHHHHHHHHHCCCCC
17.30-
221UbiquitinationADDCYQSKLKGKLMP
HHHHHHHHHCCCCCC
38.40-
223UbiquitinationDCYQSKLKGKLMPNL
HHHHHHHCCCCCCCC
58.71-
225UbiquitinationYQSKLKGKLMPNLYP
HHHHHCCCCCCCCCC
39.77-
231PhosphorylationGKLMPNLYPPETIAD
CCCCCCCCCCHHHCH
24.3120049867
242PhosphorylationTIADGVKSSIGLNTW
HHCHHHHHHCCCCCH
25.45-
320PhosphorylationSGGNVDLTSSITWVK
ECCCEECCCEEEEEE
18.9029978859
321PhosphorylationGGNVDLTSSITWVKQ
CCCEECCCEEEEEEC
27.3429978859
322PhosphorylationGNVDLTSSITWVKQA
CCEECCCEEEEEECC
20.8529978859
324PhosphorylationVDLTSSITWVKQAER
EECCCEEEEEECCCC
26.5929978859
339PhosphorylationPASYQSVSV------
CCCCCCCCC------
27.6222617229

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 SRR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRR_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 SRR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRR_HUMANSRRphysical
12021263
GOGA3_HUMANGOLGA3physical
16714286
A4_HUMANAPPphysical
21832049
DISC1_HUMANDISC1physical
22801410
DISC1_MOUSEDisc1physical
22801410
FBX22_HUMANFBXO22physical
25336657

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
DB00133L-Serine
Regulatory Network of SRR_HUMAN

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Related Literatures of Post-Translational Modification

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