RUBIC_HUMAN - dbPTM
RUBIC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUBIC_HUMAN
UniProt AC Q92622
Protein Name Run domain Beclin-1-interacting and cysteine-rich domain-containing protein {ECO:0000312|HGNC:HGNC:28991}
Gene Name RUBCN {ECO:0000312|HGNC:HGNC:28991}
Organism Homo sapiens (Human).
Sequence Length 972
Subcellular Localization Late endosome . Lysosome . Early endosome . Predominantly located in late endosomes/lysosomes, only partially detected in early endosome and not at all in the Golgi apparatus.
Protein Description Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation. [PubMed: 20974968]
Protein Sequence MRPEGAGMELGGGEERLPEESRREHWQLLGNLKTTVEGLVSTNSPNVWSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKHESPLLVTKSQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSSLYMEYEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT
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
44PhosphorylationEGLVSTNSPNVWSKY
HHHHCCCCCCHHHHH		20.2425159151
50UbiquitinationNSPNVWSKYGGLERL
CCCCHHHHHCHHHHH		32.00-
81PhosphorylationACRRQTDYWQFVKDI
HHHHCCCHHHHHHHH		12.4228509920
92PhosphorylationVKDIRWLSPHSALHV
HHHHCCCCHHHCEEH		17.3825159151
194UbiquitinationDASMFARKHESPLLV
CHHHHHHCCCCCEEE		48.58-
197PhosphorylationMFARKHESPLLVTKS
HHHHCCCCCEEEECC		22.1430266825
206PhosphorylationLLVTKSQSLTALPSS
EEEECCCCCCCCCCC		34.4818691976
246PhosphorylationNNGSERRSTSFPLSG
CCCCCCCCCCCCCCC		34.3230266825
247PhosphorylationNGSERRSTSFPLSGP
CCCCCCCCCCCCCCC		32.3530266825
248PhosphorylationGSERRSTSFPLSGPP
CCCCCCCCCCCCCCC		26.5530266825
252PhosphorylationRSTSFPLSGPPRKPQ
CCCCCCCCCCCCCCC		49.8730266825
266PhosphorylationQESRGHVSPAEDQTI
CCCCCCCCCCCCCCC		16.8430266825
272PhosphorylationVSPAEDQTIQAPPVS
CCCCCCCCCCCCCCC		27.6430266825
298PhosphorylationPNEMSSSTLTSPIEA
CCCCCCCCCCCCCEE		35.6828787133
306PhosphorylationLTSPIEASWVSSQND
CCCCCEEHHHCCCCC		18.4128787133
319PhosphorylationNDSPGDASEGPEYLA
CCCCCCCCCCCCEEE		48.0728787133
341PhosphorylationGRTASCQSHSSNAES
CCCCCCCCCCCCCCC		29.6630576142
350PhosphorylationSSNAESSSSNLFSSS
CCCCCCCCCCCCCCC		32.3118691976
355PhosphorylationSSSSNLFSSSSSQKP
CCCCCCCCCCCCCCC		32.2630576142
356PhosphorylationSSSNLFSSSSSQKPD
CCCCCCCCCCCCCCC		27.2330576142
367PhosphorylationQKPDSAASSLGDQEG
CCCCCHHHHCCCCCC		26.3024247654
368PhosphorylationKPDSAASSLGDQEGG
CCCCHHHHCCCCCCC		31.4824247654
378PhosphorylationDQEGGGESQLSSVLR
CCCCCCHHHHHHHHH		39.4326074081
381PhosphorylationGGGESQLSSVLRRSS
CCCHHHHHHHHHHCC		15.6826074081
382PhosphorylationGGESQLSSVLRRSSF
CCHHHHHHHHHHCCC		33.4926074081
387PhosphorylationLSSVLRRSSFSEGQT
HHHHHHHCCCCCCCE		29.3330266825
388PhosphorylationSSVLRRSSFSEGQTL
HHHHHHCCCCCCCEE		30.8630266825
390PhosphorylationVLRRSSFSEGQTLTV
HHHHCCCCCCCEEEE		42.6430266825
394PhosphorylationSSFSEGQTLTVTSGA
CCCCCCCEEEECCCC		34.9428464451
396PhosphorylationFSEGQTLTVTSGAKK
CCCCCEEEECCCCCH		25.7323927012
398PhosphorylationEGQTLTVTSGAKKSH
CCCEEEECCCCCHHH		19.0623927012
399PhosphorylationGQTLTVTSGAKKSHI
CCEEEECCCCCHHHC		32.2023927012
403UbiquitinationTVTSGAKKSHIRSHS
EECCCCCHHHCCCCC		46.89-
408PhosphorylationAKKSHIRSHSDTSIA
CCHHHCCCCCCCCHH		27.0923927012
410PhosphorylationKSHIRSHSDTSIASR
HHHCCCCCCCCHHHC		43.7828355574
412PhosphorylationHIRSHSDTSIASRGA
HCCCCCCCCHHHCCC		25.6625159151
413PhosphorylationIRSHSDTSIASRGAP
CCCCCCCCHHHCCCC		22.5825159151
416PhosphorylationHSDTSIASRGAPESC
CCCCCHHHCCCCCCC		29.5825159151
422PhosphorylationASRGAPESCNDKAKL
HHCCCCCCCCCCCHH		19.7030576142
444PhosphorylationGQSSEVSTPSSLYME
CCCCCCCCCCCEEEE		32.16-
449PhosphorylationVSTPSSLYMEYEGGR
CCCCCCEEEEECCCE		6.9922817900
457PhosphorylationMEYEGGRYLCSGEGM
EEECCCEEEECCCCC		18.48-
460PhosphorylationEGGRYLCSGEGMFRR
CCCEEEECCCCCCCC		36.9728102081
469PhosphorylationEGMFRRPSEGQSLIS
CCCCCCCCCCCCHHH		53.1725849741
473PhosphorylationRRPSEGQSLISYLSE
CCCCCCCCHHHHHHH		38.2328450419
476PhosphorylationSEGQSLISYLSEQDF
CCCCCHHHHHHHCCC		25.8928450419
477PhosphorylationEGQSLISYLSEQDFG
CCCCHHHHHHHCCCC		13.7828450419
479PhosphorylationQSLISYLSEQDFGSC
CCHHHHHHHCCCCCC		25.6128102081
485PhosphorylationLSEQDFGSCADLEKE
HHHCCCCCCCCHHHH		13.2130576142
528PhosphorylationEEVEEEDSDREIQEL
HHHCCCCCHHHHHHH		41.6830576142
555PhosphorylationTKNLLPMYQEAEHGS
HCCCHHHHHHHHCCC		10.9728796482
562PhosphorylationYQEAEHGSFRVTSSS
HHHHHCCCEEEECCC		16.2825849741
568PhosphorylationGSFRVTSSSSQFSSR
CCEEEECCCCCCCCC		25.3327251275
569PhosphorylationSFRVTSSSSQFSSRD
CEEEECCCCCCCCCC		28.1127251275
570PhosphorylationFRVTSSSSQFSSRDS
EEEECCCCCCCCCCC		36.8727251275
573PhosphorylationTSSSSQFSSRDSAQL
ECCCCCCCCCCCCCC		19.4827251275
577PhosphorylationSQFSSRDSAQLSDSG
CCCCCCCCCCCCCCC		19.4618691976
581PhosphorylationSRDSAQLSDSGSADE
CCCCCCCCCCCCCCC		20.0417192257
583PhosphorylationDSAQLSDSGSADEVD
CCCCCCCCCCCCCCC		31.1317192257
585PhosphorylationAQLSDSGSADEVDEF
CCCCCCCCCCCCCEE		36.1817192257
609PhosphorylationNTASSSKSFVSSQSF
CCCCCCCCCCCCCCC		32.5928348404
612 (in isoform 3)Phosphorylation-22.2028122231
612PhosphorylationSSSKSFVSSQSFSHC
CCCCCCCCCCCCCCC		22.2028348404
613PhosphorylationSSKSFVSSQSFSHCF
CCCCCCCCCCCCCCC		25.2528348404
614 (in isoform 3)Phosphorylation-40.7828122231
615PhosphorylationKSFVSSQSFSHCFLH
CCCCCCCCCCCCCCC		30.5728348404
617 (in isoform 3)Phosphorylation-25.2928122231
617PhosphorylationFVSSQSFSHCFLHST
CCCCCCCCCCCCCCC		25.2928348404
623PhosphorylationFSHCFLHSTSAEAVA
CCCCCCCCCCHHHHH		26.6328348404
624PhosphorylationSHCFLHSTSAEAVAM
CCCCCCCCCHHHHHH		22.6228348404
625PhosphorylationHCFLHSTSAEAVAMG
CCCCCCCCHHHHHHH		27.4228348404
660UbiquitinationPEHDAPQKLLPIPDS
CCCCCCCCCCCCCCC		51.43-
667PhosphorylationKLLPIPDSLPISPDD
CCCCCCCCCCCCCCC		30.5928450419
671PhosphorylationIPDSLPISPDDGQHA
CCCCCCCCCCCCCCC		21.9725159151
681PhosphorylationDGQHADIYKLRIRVR
CCCCCEEEEEEEEEE		12.4326074081
682UbiquitinationGQHADIYKLRIRVRG
CCCCEEEEEEEEEEC		31.46-
709PhosphorylationFNVHPAPTRKIAVAK
EEECCCCCCHHEEEC		46.85-
716UbiquitinationTRKIAVAKQNYRCAG
CCHHEEECCCEECCC		32.26-
728PhosphorylationCAGCGIRTDPDYIKR
CCCCCCCCCHHHHHH		50.3825159151
732PhosphorylationGIRTDPDYIKRLRYC
CCCCCHHHHHHHHHH		17.46-
734UbiquitinationRTDPDYIKRLRYCEY
CCCHHHHHHHHHHHH		38.87-
772PhosphorylationKWDFSKYYVSNFSKD
HCCCHHHHHHCCCHH		10.92-
774PhosphorylationDFSKYYVSNFSKDLL
CCHHHHHHCCCHHHH		18.94-
777PhosphorylationKYYVSNFSKDLLIKI
HHHHHCCCHHHHHHH		29.52-
778UbiquitinationYYVSNFSKDLLIKIW
HHHHCCCHHHHHHHH		48.54-
830UbiquitinationFKTCRLAKELLDSFD
HHHHHHHHHHHHCCC		54.19-
851PhosphorylationTEDLHLYSLNDLTAT
CCCEEEEEHHHCCCC		27.36-
856PhosphorylationLYSLNDLTATRKGEL
EEEHHHCCCCCCCCC		28.93-
860UbiquitinationNDLTATRKGELGPRL
HHCCCCCCCCCCHHH		53.00-
921UbiquitinationECKACYHKACFKSGS
HHHHHHHHHHHHCCC		22.00-
946PhosphorylationREALARQSLESYLSD
HHHHHHHHHHHHHHC		28.6619369195
952PhosphorylationQSLESYLSDYEEEPA
HHHHHHHHCCCCCHH		29.8819369195
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 RUBIC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUBIC_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 RUBIC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC1_HUMANEXOC1physical
21241894
UVRAG_HUMANUVRAGphysical
19270696
BECN1_HUMANBECN1physical
19270696
PI3R4_HUMANPIK3R4physical
19270696
PK3C3_HUMANPIK3C3physical
19270696
PK3C3_HUMANPIK3C3physical
24980960
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615705Spinocerebellar ataxia, autosomal recessive, 15 (SCAR15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RUBIC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND MASSSPECTROMETRY.
"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-197; THR-247; SER-248;SER-266; SER-387; SER-388; SER-410; SER-528; SER-577; SER-581;SER-583; SER-585; SER-946 AND SER-952, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-272; SER-410;SER-581; SER-583; SER-585 AND SER-671, AND MASS SPECTROMETRY.

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