LURA1_HUMAN - dbPTM
LURA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LURA1_HUMAN
UniProt AC Q96LR2
Protein Name Leucine rich adaptor protein 1
Gene Name LURAP1
Organism Homo sapiens (Human).
Sequence Length 239
Subcellular Localization Cytoplasm .
Protein Description Acts as an activator of the canonical NF-kappa-B pathway and drive the production of proinflammatory cytokines. Promotes the antigen (Ag)-presenting and priming function of dendritic cells via the canonical NF-kappa-B pathway. [PubMed: 21048106 In concert with MYO18A and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and MYH9/MYH10-dependent actomyosin assembly in the lamella (By similarity]
Protein Sequence MEGTVESQTPDLRDVEGKVGRKTPEGLLRGLRGECELGTSGALLLPGASSTGHDLGDKIMALKMELAYLRAIDVKILQQLVTLNEGIEAVRWLLEERGTLTSHCSSLTSSQYSLTGGSPGRSRRGSWDSLPDTSTTDRLDSVSIGSFLDTVAPSELDEQGPPGAPRSEMDWAKVIAGGERARTEVDVAATRLGSLRAVWKPPGERLQGGPPESPEDESAKLGFEAHWFWEQCQDDVTFL
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
115PhosphorylationTSSQYSLTGGSPGRS
CCCCCCCCCCCCCCC
33.2923312004
118PhosphorylationQYSLTGGSPGRSRRG
CCCCCCCCCCCCCCC
26.0624076635
126PhosphorylationPGRSRRGSWDSLPDT
CCCCCCCCCCCCCCC
26.3723927012
129PhosphorylationSRRGSWDSLPDTSTT
CCCCCCCCCCCCCCC
35.2323927012
133PhosphorylationSWDSLPDTSTTDRLD
CCCCCCCCCCCCCCC
26.4927251275
134PhosphorylationWDSLPDTSTTDRLDS
CCCCCCCCCCCCCCC
36.3722468782
135PhosphorylationDSLPDTSTTDRLDSV
CCCCCCCCCCCCCCC
34.5027251275
136PhosphorylationSLPDTSTTDRLDSVS
CCCCCCCCCCCCCCC
20.9127251275
141PhosphorylationSTTDRLDSVSIGSFL
CCCCCCCCCCHHHHH
23.5027251275
143PhosphorylationTDRLDSVSIGSFLDT
CCCCCCCCHHHHHHH
25.7827251275
194PhosphorylationVAATRLGSLRAVWKP
HHHHHCCCCEEEECC
21.1924719451
213PhosphorylationLQGGPPESPEDESAK
CCCCCCCCCCHHHHH
39.0929255136
218PhosphorylationPESPEDESAKLGFEA
CCCCCHHHHHCCCEE
42.9229255136

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 LURA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LURA1_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 LURA1_HUMAN !!

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

Oops, there are no PPI records of LURA1_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 LURA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASSSPECTROMETRY.

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