EURL_HUMAN - dbPTM
EURL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EURL_HUMAN
UniProt AC Q9NYK6
Protein Name Protein EURL homolog {ECO:0000305}
Gene Name EURL {ECO:0000250|UniProtKB:Q9I8W6}
Organism Homo sapiens (Human).
Sequence Length 297
Subcellular Localization
Protein Description Plays a role in cortical progenitor cell proliferation and differentiation. Promotes dendritic spine development of post-migratory cortical projection neurons by modulating the beta-catenin signaling pathway..
Protein Sequence MNEEEQFVNIDLNDDNICSVCKLGTDKETLSFCHICFELNIEGVPKSDLLHTKSLRGHKDCFEKYHLIANQGCPRSKLSKSTYEEVKTILSKKINWIVQYAQNKDLDSDSECSKNPQHHLFNFRHKPEEKLLPQFDSQVPKYSAKWIDGSAGGISNCTQRILEQRENTDFGLSMLQDSGATLCRNSVLWPHSHNQAQKKEETISSPEANVQTQHPHYSREELNSMTLGEVEQLNAKLLQQIQEVFEELTHQVQEKDSLASQLHVRHVAIEQLLKNCSKLPCLQVGRTGMKSHLPINN
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
53UbiquitinationKSDLLHTKSLRGHKD
HHHHCCCCCCCCCHH
36.42-
54PhosphorylationSDLLHTKSLRGHKDC
HHHCCCCCCCCCHHH
25.18-
64UbiquitinationGHKDCFEKYHLIANQ
CCHHHHHHHHHHHCC
20.09-
76PhosphorylationANQGCPRSKLSKSTY
HCCCCCHHHCCCHHH
24.0829396449
79PhosphorylationGCPRSKLSKSTYEEV
CCCHHHCCCHHHHHH
28.4429396449
80UbiquitinationCPRSKLSKSTYEEVK
CCHHHCCCHHHHHHH
58.20-
81PhosphorylationPRSKLSKSTYEEVKT
CHHHCCCHHHHHHHH
32.6129396449
82PhosphorylationRSKLSKSTYEEVKTI
HHHCCCHHHHHHHHH
38.3929396449
83PhosphorylationSKLSKSTYEEVKTIL
HHCCCHHHHHHHHHH
19.7228796482
88PhosphorylationSTYEEVKTILSKKIN
HHHHHHHHHHHHHHH
32.1222817900
108PhosphorylationAQNKDLDSDSECSKN
HHCCCCCCCCHHHCC
50.7828985074
114UbiquitinationDSDSECSKNPQHHLF
CCCCHHHCCCCHHCC
81.79-
141UbiquitinationQFDSQVPKYSAKWID
CCCCCCCCCCEEECC
53.64-
198UbiquitinationHSHNQAQKKEETISS
CCCCCHHHHHHCCCC
66.23-
199UbiquitinationSHNQAQKKEETISSP
CCCCHHHHHHCCCCC
49.02-
202PhosphorylationQAQKKEETISSPEAN
CHHHHHHCCCCCCHH
27.5321955146
204PhosphorylationQKKEETISSPEANVQ
HHHHHCCCCCCHHHC
47.4625159151
205PhosphorylationKKEETISSPEANVQT
HHHHCCCCCCHHHCC
23.9425159151
212PhosphorylationSPEANVQTQHPHYSR
CCCHHHCCCCCCCCH
25.2721955146
217PhosphorylationVQTQHPHYSREELNS
HCCCCCCCCHHHHHC
17.5521955146
218PhosphorylationQTQHPHYSREELNSM
CCCCCCCCHHHHHCC
30.1321955146
290UbiquitinationQVGRTGMKSHLPINN
EECCCCCCCCCCCCC
35.75-

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 EURL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EURL_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 EURL_HUMAN !!

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

Oops, there are no PPI records of EURL_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 EURL_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP