SPRY4_HUMAN - dbPTM
SPRY4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPRY4_HUMAN
UniProt AC Q8WW59
Protein Name SPRY domain-containing protein 4
Gene Name SPRYD4
Organism Homo sapiens (Human).
Sequence Length 207
Subcellular Localization
Protein Description
Protein Sequence MALLFARSLRLCRWGAKRLGVASTEAQRGVSFKLEEKTAHSSLALFRDDMGVKYGLVGLEPTKVALNVERFREWAVVLADTAVTSGRHYWEVTVKRSQQFRIGVADVDMSRDSCIGVDDRSWVFTYAQRKWYTMLANEKAPVEGIGQPEKVGLLLEYEAQKLSLVDVSQVSVVHTLQTDFRGPVVPAFALWDGELLTHSGLEVPEGL
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
23O-linked_GlycosylationAKRLGVASTEAQRGV
HHHHCCCCCHHHHCC
25.1128510447
23PhosphorylationAKRLGVASTEAQRGV
HHHHCCCCCHHHHCC
25.1129083192
24PhosphorylationKRLGVASTEAQRGVS
HHHCCCCCHHHHCCC
26.1329083192
53AcetylationFRDDMGVKYGLVGLE
HCCCCCCCEEEECCC
28.07-
95AcetylationHYWEVTVKRSQQFRI
EEEEEEEEECCCEEE
36.6519608861
125PhosphorylationDDRSWVFTYAQRKWY
CCCCEEEEEHHHHHH
14.3423401153
126PhosphorylationDRSWVFTYAQRKWYT
CCCEEEEEHHHHHHH
6.8323401153
130AcetylationVFTYAQRKWYTMLAN
EEEEHHHHHHHHHHC
32.2619608861
139AcetylationYTMLANEKAPVEGIG
HHHHHCCCCCCCCCC
58.7723954790
139SuccinylationYTMLANEKAPVEGIG
HHHHHCCCCCCCCCC
58.77-
139SuccinylationYTMLANEKAPVEGIG
HHHHHCCCCCCCCCC
58.77-
150AcetylationEGIGQPEKVGLLLEY
CCCCCHHHEEEEEEE
48.5723954790
168PhosphorylationKLSLVDVSQVSVVHT
ECCCCCHHHCEEEEE
22.0230257219
171PhosphorylationLVDVSQVSVVHTLQT
CCCHHHCEEEEECCC
15.7030257219
175PhosphorylationSQVSVVHTLQTDFRG
HHCEEEEECCCCCCC
14.6730257219

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 SPRY4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPRY4_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 SPRY4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPRY4_HUMANSPRYD4physical
27499296
HOGA1_HUMANHOGA1physical
27499296
IDE_HUMANIDEphysical
27499296
G6PI_HUMANGPIphysical
27499296
MPPB_HUMANPMPCBphysical
27499296
MPPA_HUMANPMPCAphysical
27499296
ECH1_HUMANECH1physical
27499296
ODBA_HUMANBCKDHAphysical
27499296
USMG5_HUMANUSMG5physical
27499296
ATP5I_HUMANATP5Iphysical
27499296
ATPG_HUMANATP5C1physical
27499296
CHCH2_HUMANCHCHD2physical
27499296

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
There are no disease associations of PTM sites.
Regulatory Network of SPRY4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95 AND LYS-130, AND MASSSPECTROMETRY.

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