LRCH1_HUMAN - dbPTM
LRCH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRCH1_HUMAN
UniProt AC Q9Y2L9
Protein Name Leucine-rich repeat and calponin homology domain-containing protein 1
Gene Name LRCH1
Organism Homo sapiens (Human).
Sequence Length 728
Subcellular Localization Cytoplasm .
Protein Description Acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. Probably by preventing CDC42 activation, negatively regulates CD4(+) T-cell migration..
Protein Sequence MATPGSEPQPFVPALSVATLHPLHHPHHHHHHHQHHGGTGAPGGAGGGGGGSGGFNLPLNRGLERALEEAANSGGLNLSARKLKEFPRTAAPGHDLSDTVQADLSKNRLVEVPMELCHFVSLEILNLYHNCIRVIPEAIVNLQMLTYLNLSRNQLSALPACLCGLPLKVLIASNNKLGSLPEEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPQELVDLSLVKFDFSCNKVLVIPICFREMKQLQVLLLENNPLQSPPAQICTKGKVHIFKYLSIQACQIKTADSLYLHTMERPHLHQHVEDGKKDSDSGVGSDNGDKRLSATEPSDEDTVSLNVPMSNIMEEEQIIKEDSCHRLSPVKGEFHQEFQPEPSLLGDSTNSGEERDQFTDRADGLHSEFMNYKARAEDCEELLRIEEDVHWQTEGIISSSKDQDMDIAMIEQLREAVDLLQDPNGLSTDITERSVLNLYPMGSAEALELQDSALNGQIQLETSPVCEVQSDLTLQSNGSQYSPNEIRENSPAVSPTTNSTAPFGLKPRSVFLRPQRNLESIDPQFTIRRKMEQMREEKELVEQLRESIEMRLKVSLHEDLGAALMDGVVLCHLVNHIRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPEADLCSPCDILQLDFRHIRKTVDTLLALGEKAPPPTSALRSRDLIGFCLVHILFIVLVYITYHWNALSA
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
156PhosphorylationNLSRNQLSALPACLC
CCCHHHHHHHHHHHH		20.28-
224 (in isoform 2)Ubiquitination-31.2221906983
224 (in isoform 1)Ubiquitination-31.2221906983
224UbiquitinationNVRRNYLKVLPQELV
CCCHHHHHHCCHHHH		31.222190698
234PhosphorylationPQELVDLSLVKFDFS
CHHHHCHHCEEEECC		27.0124719451
323PhosphorylationDGKKDSDSGVGSDNG
CCCCCCCCCCCCCCC		39.0528985074
327PhosphorylationDSDSGVGSDNGDKRL
CCCCCCCCCCCCCCC		26.0425849741
335PhosphorylationDNGDKRLSATEPSDE
CCCCCCCCCCCCCCC		36.8628192239
337PhosphorylationGDKRLSATEPSDEDT
CCCCCCCCCCCCCCC		45.0822199227
340PhosphorylationRLSATEPSDEDTVSL
CCCCCCCCCCCCEEE		47.6123090842
344PhosphorylationTEPSDEDTVSLNVPM
CCCCCCCCEEECCCH		15.2223090842
346PhosphorylationPSDEDTVSLNVPMSN
CCCCCCEEECCCHHH		19.1323090842
352PhosphorylationVSLNVPMSNIMEEEQ
EEECCCHHHHCCHHH		19.6826471730
365PhosphorylationEQIIKEDSCHRLSPV
HHEECCCCCCCCCCC		16.9623401153
370PhosphorylationEDSCHRLSPVKGEFH
CCCCCCCCCCCCCCC		27.8329255136
385PhosphorylationQEFQPEPSLLGDSTN
HHCCCCCCCCCCCCC		34.2730108239
390PhosphorylationEPSLLGDSTNSGEER
CCCCCCCCCCCHHHH		27.9130108239
391PhosphorylationPSLLGDSTNSGEERD
CCCCCCCCCCHHHHH		37.8430108239
393PhosphorylationLLGDSTNSGEERDQF
CCCCCCCCHHHHHHH		47.9030108239
401PhosphorylationGEERDQFTDRADGLH
HHHHHHHHHCCCHHC		20.9530108239
409PhosphorylationDRADGLHSEFMNYKA
HCCCHHCHHHHCHHH		37.26-
415UbiquitinationHSEFMNYKARAEDCE
CHHHHCHHHCHHHHH		26.7929967540
521PhosphorylationLTLQSNGSQYSPNEI
EEEECCCCCCCHHHH		30.1426074081
523PhosphorylationLQSNGSQYSPNEIRE
EECCCCCCCHHHHHC		28.0026074081
524PhosphorylationQSNGSQYSPNEIREN
ECCCCCCCHHHHHCC		17.3826074081
532PhosphorylationPNEIRENSPAVSPTT
HHHHHCCCCCCCCCC		14.9622167270
536PhosphorylationRENSPAVSPTTNSTA
HCCCCCCCCCCCCCC		20.7322167270
538PhosphorylationNSPAVSPTTNSTAPF
CCCCCCCCCCCCCCC		30.9730266825
539PhosphorylationSPAVSPTTNSTAPFG
CCCCCCCCCCCCCCC		30.4730266825
541PhosphorylationAVSPTTNSTAPFGLK
CCCCCCCCCCCCCCC		24.6930266825
542PhosphorylationVSPTTNSTAPFGLKP
CCCCCCCCCCCCCCC		40.1825022875
551PhosphorylationPFGLKPRSVFLRPQR
CCCCCCCCEEECCCC		26.2523898821
562PhosphorylationRPQRNLESIDPQFTI
CCCCCHHHCCCCHHH		35.1425159151
568PhosphorylationESIDPQFTIRRKMEQ
HHCCCCHHHHHHHHH		14.3419664994
603PhosphorylationVSLHEDLGAALMDGV
HHHCHHHHHHHHHHH		22.5624719451
623PhosphorylationVNHIRPRSVASIHVP
HHCCCCCCEEEEECC		25.3928857561
626PhosphorylationIRPRSVASIHVPSPA
CCCCCEEEEECCCCC		15.8628857561
631PhosphorylationVASIHVPSPAVPKLS
EEEEECCCCCCCCCC		25.1329743597
662UbiquitinationKLGVPEADLCSPCDI
HHCCCHHHCCCHHCH		46.6929967540
673UbiquitinationPCDILQLDFRHIRKT
HHCHHHCCHHHHHHH		26.1029967540
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 LRCH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRCH1_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 LRCH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOCK8_HUMANDOCK8physical
25416956
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 LRCH1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory