LRC41_HUMAN - dbPTM
LRC41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC41_HUMAN
UniProt AC Q15345
Protein Name Leucine-rich repeat-containing protein 41
Gene Name LRRC41
Organism Homo sapiens (Human).
Sequence Length 812
Subcellular Localization
Protein Description Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence MAAPEAWRARSCWFCEVAAATTMEATSREAAPAKSSASGPNAPPALFELCGRAVSAHMGVLESGVWALPGPILQSILPLLNIYYLERIEETALKKGLSTQAIWRRLWDELMKTRPSSLESVTCWRAKFMEAFFSHVLRGTIDVSSDRRLCDQRFSPLLHSSRHVRQLTICNMLQGATELVAEPNRRVLETLASSLHTLKFRHLLFSDVAAQQSLRQLLHQLIHHGAVSQVSLYSWPVPESALFILILTMSAGFWQPGPGGPPCRLCGEASRGRAPSRDEGSLLLGSRRPRRDAAERCAAALMASRRKSEAKQMPRAAPATRVTRRSTQESLTAGGTDLKRELHPPATSHEAPGTKRSPSAPAATSSASSSTSSYKRAPASSAPQPKPLKRFKRAAGKKGARTRQGPGAESEDLYDFVFIVAGEKEDGEEMEIGEVACGALDGSDPSCLGLPALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWVSLESLTLSYNGLGSNIFRLLDSLRALSGQAGCRLRALHLSDLFSPLPILELTRAIVRALPLLRVLSIRVDHPSQRDNPGVPGNAGPPSHIIGDEEIPENCLEQLEMGFPRGAQPAPLLCSVLKASGSLQQLSLDSATFASPQDFGLVLQTLKEYNLALKRLSFHDMNLADCQSEVLFLLQNLTLQEITFSFCRLFEKRPAQFLPEMVAAMKGNSTLKGLRLPGNRLGNAGLLALADVFSEDSSSSLCQLDISSNCIKPDGLLEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRATCHVVSDSWDSSQAFADYVSTM
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
34UbiquitinationSREAAPAKSSASGPN
CCCCCCCCCCCCCCC		43.83-
36PhosphorylationEAAPAKSSASGPNAP
CCCCCCCCCCCCCCC		26.2528555341
94UbiquitinationRIEETALKKGLSTQA
HHHHHHHHCCCCHHH		42.1927667366
95UbiquitinationIEETALKKGLSTQAI
HHHHHHHCCCCHHHH		66.97-
102UbiquitinationKGLSTQAIWRRLWDE
CCCCHHHHHHHHHHH		1.8027667366
127AcetylationSVTCWRAKFMEAFFS
HHHHHHHHHHHHHHH		36.3526051181
144PhosphorylationLRGTIDVSSDRRLCD
HHCCCCCCCCHHHCC		23.8328842319
155PhosphorylationRLCDQRFSPLLHSSR
HHCCCCCHHHHCCCH		19.4822617229
160PhosphorylationRFSPLLHSSRHVRQL
CCHHHHCCCHHHHHH		29.0925850435
199UbiquitinationASSLHTLKFRHLLFS
HHHHCHHHHHHHHHH		41.3223000965
199 (in isoform 3)Ubiquitination-41.3221890473
199UbiquitinationASSLHTLKFRHLLFS
HHHHCHHHHHHHHHH		41.3221890473
199AcetylationASSLHTLKFRHLLFS
HHHHCHHHHHHHHHH		41.3226051181
199 (in isoform 2)Ubiquitination-41.3221890473
207UbiquitinationFRHLLFSDVAAQQSL
HHHHHHHHHHHHHHH		27.0923000965
276PhosphorylationASRGRAPSRDEGSLL
HHCCCCCCCCCCCCC		51.9123401153
281PhosphorylationAPSRDEGSLLLGSRR
CCCCCCCCCCCCCCC		17.5023401153
286PhosphorylationEGSLLLGSRRPRRDA
CCCCCCCCCCCCHHH		25.7023403867
304PhosphorylationCAAALMASRRKSEAK
HHHHHHHHHHHHHHH		20.7420815410
323PhosphorylationAAPATRVTRRSTQES
CCCCCCCCCCHHHHH		19.6429116813
326PhosphorylationATRVTRRSTQESLTA
CCCCCCCHHHHHHHC		31.0225159151
327PhosphorylationTRVTRRSTQESLTAG
CCCCCCHHHHHHHCC		34.2517525332
330PhosphorylationTRRSTQESLTAGGTD
CCCHHHHHHHCCCCC		22.6228102081
332PhosphorylationRSTQESLTAGGTDLK
CHHHHHHHCCCCCCC		32.3223403867
336PhosphorylationESLTAGGTDLKRELH
HHHHCCCCCCCHHCC		36.9223312004
339UbiquitinationTAGGTDLKRELHPPA
HCCCCCCCHHCCCCC		46.7921906983
339 (in isoform 2)Ubiquitination-46.7921890473
339 (in isoform 3)Ubiquitination-46.7921890473
347UbiquitinationRELHPPATSHEAPGT
HHCCCCCCCCCCCCC		36.0721963094
347PhosphorylationRELHPPATSHEAPGT
HHCCCCCCCCCCCCC		36.0727174698
348PhosphorylationELHPPATSHEAPGTK
HCCCCCCCCCCCCCC		22.8027080861
354PhosphorylationTSHEAPGTKRSPSAP
CCCCCCCCCCCCCCC		23.4027174698
355UbiquitinationSHEAPGTKRSPSAPA
CCCCCCCCCCCCCCC		57.7132015554
357PhosphorylationEAPGTKRSPSAPAAT
CCCCCCCCCCCCCCC		25.4323927012
359PhosphorylationPGTKRSPSAPAATSS
CCCCCCCCCCCCCCC		48.4023401153
364PhosphorylationSPSAPAATSSASSST
CCCCCCCCCCCCCCC		25.8930576142
365PhosphorylationPSAPAATSSASSSTS
CCCCCCCCCCCCCCC		21.1223927012
366PhosphorylationSAPAATSSASSSTSS
CCCCCCCCCCCCCCC		28.0223927012
368PhosphorylationPAATSSASSSTSSYK
CCCCCCCCCCCCCCC		27.1130387612
369PhosphorylationAATSSASSSTSSYKR
CCCCCCCCCCCCCCC		37.0330387612
370PhosphorylationATSSASSSTSSYKRA
CCCCCCCCCCCCCCC		29.7923927012
371PhosphorylationTSSASSSTSSYKRAP
CCCCCCCCCCCCCCC		24.5223927012
372PhosphorylationSSASSSTSSYKRAPA
CCCCCCCCCCCCCCC		33.3523927012
373PhosphorylationSASSSTSSYKRAPAS
CCCCCCCCCCCCCCC		34.4623927012
374PhosphorylationASSSTSSYKRAPASS
CCCCCCCCCCCCCCC		12.3128176443
375UbiquitinationSSSTSSYKRAPASSA
CCCCCCCCCCCCCCC		43.9921890473
375 (in isoform 2)Ubiquitination-43.9921890473
375 (in isoform 3)Ubiquitination-43.9921890473
375UbiquitinationSSSTSSYKRAPASSA
CCCCCCCCCCCCCCC		43.9923000965
375AcetylationSSSTSSYKRAPASSA
CCCCCCCCCCCCCCC		43.9924471151
383UbiquitinationRAPASSAPQPKPLKR
CCCCCCCCCCCCHHH		53.6123000965
386UbiquitinationASSAPQPKPLKRFKR
CCCCCCCCCHHHHHH		58.7033845483
532PhosphorylationLHLSDLFSPLPILEL
EHHHHCCCCCHHHHH		32.59-
705UbiquitinationMKGNSTLKGLRLPGN
HCCCCCCCCCCCCCC		56.8629967540
802PhosphorylationVSDSWDSSQAFADYV
EECCCCHHHHHHHHH		24.05-
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 LRC41_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC41_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 LRC41_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBPMS_HUMANRBPMSphysical
16189514
MYO9B_HUMANMYO9Bphysical
16169070
ELOB_HUMANTCEB2physical
18187417
ELOC_HUMANTCEB1physical
18187417
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 LRC41_HUMAN

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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 SER-357, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND MASSSPECTROMETRY.

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