SPRY3_HUMAN - dbPTM
SPRY3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPRY3_HUMAN
UniProt AC Q8NCJ5
Protein Name SPRY domain-containing protein 3
Gene Name SPRYD3
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization
Protein Description
Protein Sequence MRRTRRPRFVLMNKMDDLNLHYRFLNWRRRIREIREVRAFRYQERFKHILVDGDTLSYHGNSGEVGCYVASRPLTKDSNYFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLYNGRAKGRQFGSKCNSGDRIGCGIEPVSFDVQTAQIFFTKNGKRVGSTIMPMSPDGLFPAVGMHSLGEEVRLHLNAELGREDDSVMMVDSYEDEWGRLHDVRVCGTLLEYLGKGKSIVDVGLAQARHPLSTRSHYFEVEIVDPGEKCYIALGLARKDYPKNRHPGWSRGSVAYHADDGKIFHGSGVGDPFGPRCYKGDIMGCGIMFPRDYILDSEGDSDDSCDTVILSPTARAVRNVRNVMYLHQEGEEEEEEEEEEEDGEEIEPEHEGRKVVVFFTRNGKIIGKKDAVVPSGGFFPTIGMLSCGEKVKVDLHPLSG
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
14UbiquitinationPRFVLMNKMDDLNLH
CEEEEEECCCCCCHH
29.7321890473
22PhosphorylationMDDLNLHYRFLNWRR
CCCCCHHHHHHHHHH
13.2622817900
138UbiquitinationKGRQFGSKCNSGDRI
CCCCCCCCCCCCCCC
37.50-
240SumoylationLEYLGKGKSIVDVGL
HHHHCCCCCEEEHHH
40.26-
240UbiquitinationLEYLGKGKSIVDVGL
HHHHCCCCCEEEHHH
40.2621890473
240SumoylationLEYLGKGKSIVDVGL
HHHHCCCCCEEEHHH
40.26-
304UbiquitinationAYHADDGKIFHGSGV
EEECCCCCCCCCCCC
49.55-
321UbiquitinationPFGPRCYKGDIMGCG
CCCCCCCCCCCCCCE
54.45-
335PhosphorylationGIMFPRDYILDSEGD
EEECCCCEEECCCCC
12.5023663014
339PhosphorylationPRDYILDSEGDSDDS
CCCEEECCCCCCCCC
39.7823663014
343PhosphorylationILDSEGDSDDSCDTV
EECCCCCCCCCCCEE
54.9223663014
346PhosphorylationSEGDSDDSCDTVILS
CCCCCCCCCCEEEEC
20.9123663014
349PhosphorylationDSDDSCDTVILSPTA
CCCCCCCEEEECHHH
17.4823663014
353PhosphorylationSCDTVILSPTARAVR
CCCEEEECHHHHHHH
14.7421712546
355PhosphorylationDTVILSPTARAVRNV
CEEEECHHHHHHHHH
25.9630177828

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 SPRY3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPRY3_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 SPRY3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPRY3_HUMAN !!

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 SPRY3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, AND MASSSPECTROMETRY.

TOP