RBCC1_MOUSE - dbPTM
RBCC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBCC1_MOUSE
UniProt AC Q9ESK9
Protein Name RB1-inducible coiled-coil protein 1
Gene Name Rb1cc1
Organism Mus musculus (Mouse).
Sequence Length 1588
Subcellular Localization Nucleus . Cytoplasm, cytosol . Cytoplasm . Preautophagosomal structure . Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formati
Protein Description Involved in autophagy. [PubMed: 23262492]
Protein Sequence MKLYVFLVNTGTTLTFDTELTVQTVADLKHAIQSKYKIAIQHQVLVVNGGECMAADRRVCTYSAGTDTNPIFLFNKEMILCDRAPAIPKATFSTENDMEIKVEESLMMPAVFHTVASRTQLAVEMYDVAKKLCSFCEGLVHDEHLQHQGWAAIMANLEDCSNSYQKLLFKFESIYSDYLQSIEDIKLKLTHLGTAVSVMAKIPLLECLTRHSYRECLGRPDSLNEHEGSEKAEMKRSTELVLSPDMPRTTNTSLVTSFHKSMEHVAPDPTGTERGKELRESCQSTVQQEEASVDAKDSDLPFFNVSLLDWINVQDRPNDVESLVRKCFDSMSRLDPKIIQPFMLECHQTIAKLDNQNMKAIKGLEDRLYALDQMIASCSRLVNEQKELAQGFLANQMRAENLKDASVLPDLCLSHANQLMIMLQNHRKLLDIKQKCTTAKQELANNLHVRLKWCCFVMLHADQDGEKLQALLRLVIELLERVRIVEALSTVPQMYCLAVVEVVRRKMFIKHYREWAGALVKDGKQLYEAEKSKRESFGKLFRKSFLRNRLFKGLDSWPSSFCTQKPRKFDCELPDISLKDLQFLQSFCPSEVQPFLRVPLLCDFEPLHQHVLALHNLVKAAQSLDEMSQTITDLLNEQKVSTSQASPQSAASPRIESTTGITTTTSPKTPPPLTVQDTLCPAVCPLEELSPDSIDAHTFDFETISHPNTEQPVHQASIDLDSLAESPESDFMSAVNEFVIEENLSSPNPISDPQSPEMMVESLYSSVINAIDSRRMQDTSTRGNEGFGDRAALHVQLEKCRAAAQDSHSSIQTIKDDLCHFRTFVQKEQCDLANYLKCTAVEIRNIIEKVKCSLEITLKEKHQQELQSLKIEYECKLDALVKDSEENVNKILKLKENLVSLEEALQNKDNEFTSIKHEKDAIVCVQQEKDQKLLEMEKIMHTQHCEIKELKQSREMALEDLKKLHDEKIESLRAEFQCLEQNHLKELEDTLHIRHTQEFEKVMTDHNMSLEKLKKENQQRIDQMLESHASTIQEKEQQLQELKLKVSDLSDMRCKLEVELALKEAETDEIKILLEESRTQQKEMLKSLLEQETENLRTEISKLNQKIHDNNESYQVGLSELRALMTIEKDQCISELISRHEEESNILKAELDNVTSLHRQAYEIEKKLKEQIVELQTRLNSELSALEKQKDEKITQQEEKYEALIQNLEKDKERLVKNHEQDKEHLIQELNFEKNKAVQTALDEFKVERELVEKELLEKVKHLENQIAKTPAFESAREDSSSLVAELQEKLQEEKAKFLEQLEEQEKRKNEEMQNVRTSLIAEQQTNFNTVLTREKMRKENIINDLSDKLKSTMQQQERDKDLIESLSEDRARLLEEKKQLEEEVSKLRTSSFLSSAPVAAAPELYGACAPELPGEPERSVMETADEGRLDSAMETSMMSVQENMLSEEKQRIMLLERTLQLKEEENKRLNQRLMSQSLSSVSSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV
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
105PhosphorylationMEIKVEESLMMPAVF
CEEEHHHHHCCCHHH		14.2022817900
114PhosphorylationMMPAVFHTVASRTQL
CCCHHHHHHHHCHHH		13.3022817900
117PhosphorylationAVFHTVASRTQLAVE
HHHHHHHHCHHHHHH		31.3722817900
201AcetylationTAVSVMAKIPLLECL
HHHHHHHHCHHHHHH		27.1030987125
212PhosphorylationLECLTRHSYRECLGR
HHHHHHCCHHHHHCC		23.6927681418
213PhosphorylationECLTRHSYRECLGRP
HHHHHCCHHHHHCCC		12.3326643407
222PhosphorylationECLGRPDSLNEHEGS
HHHCCCCCCCCCCCC		35.4626824392
229PhosphorylationSLNEHEGSEKAEMKR
CCCCCCCCHHHHHHH		32.7026643407
237PhosphorylationEKAEMKRSTELVLSP
HHHHHHHCCEEEECC		22.2525521595
238PhosphorylationKAEMKRSTELVLSPD
HHHHHHCCEEEECCC		37.0526824392
243PhosphorylationRSTELVLSPDMPRTT
HCCEEEECCCCCCCC		16.0425521595
246OxidationELVLSPDMPRTTNTS
EEEECCCCCCCCCHH		2.4817242355
249PhosphorylationLSPDMPRTTNTSLVT
ECCCCCCCCCHHHHH		20.6621743459
250PhosphorylationSPDMPRTTNTSLVTS
CCCCCCCCCHHHHHH		37.4722324799
252PhosphorylationDMPRTTNTSLVTSFH
CCCCCCCHHHHHHHH		22.7321743459
253PhosphorylationMPRTTNTSLVTSFHK
CCCCCCHHHHHHHHH		23.9425521595
256PhosphorylationTTNTSLVTSFHKSME
CCCHHHHHHHHHHHH		30.8525521595
257PhosphorylationTNTSLVTSFHKSMEH
CCHHHHHHHHHHHHH		20.2026824392
261PhosphorylationLVTSFHKSMEHVAPD
HHHHHHHHHHHCCCC		22.3425521595
270PhosphorylationEHVAPDPTGTERGKE
HHCCCCCCCCHHHHH		65.2026060331
281PhosphorylationRGKELRESCQSTVQQ
HHHHHHHHHHHHHHH		15.8325521595
284PhosphorylationELRESCQSTVQQEEA
HHHHHHHHHHHHHHH		34.5727087446
285PhosphorylationLRESCQSTVQQEEAS
HHHHHHHHHHHHHHH		9.1027087446
386UbiquitinationSRLVNEQKELAQGFL
HHHHHHHHHHHHHHH		48.82-
521AcetylationEWAGALVKDGKQLYE
HHHHHHHHCHHHHHH		62.717712993
568AcetylationFCTQKPRKFDCELPD
HCCCCCCCCCCCCCC		54.8222826441
623PhosphorylationNLVKAAQSLDEMSQT
HHHHHHHCHHHHHHH		32.8226824392
628PhosphorylationAQSLDEMSQTITDLL
HHCHHHHHHHHHHHH		23.3222324799
630PhosphorylationSLDEMSQTITDLLNE
CHHHHHHHHHHHHHH		20.6628833060
632PhosphorylationDEMSQTITDLLNEQK
HHHHHHHHHHHHHCC		24.7928833060
641PhosphorylationLLNEQKVSTSQASPQ
HHHHCCCCCCCCCCC		29.4025521595
642PhosphorylationLNEQKVSTSQASPQS
HHHCCCCCCCCCCCC		28.0425159016
643PhosphorylationNEQKVSTSQASPQSA
HHCCCCCCCCCCCCC		19.0825521595
646PhosphorylationKVSTSQASPQSAASP
CCCCCCCCCCCCCCC		18.8125521595
649PhosphorylationTSQASPQSAASPRIE
CCCCCCCCCCCCCEE		29.2323684622
652PhosphorylationASPQSAASPRIESTT
CCCCCCCCCCEEECC		17.9025521595
657PhosphorylationAASPRIESTTGITTT
CCCCCEEECCCCCCC		28.9728066266
658PhosphorylationASPRIESTTGITTTT
CCCCEEECCCCCCCC		19.0928066266
662PhosphorylationIESTTGITTTTSPKT
EEECCCCCCCCCCCC		21.3120415495
663PhosphorylationESTTGITTTTSPKTP
EECCCCCCCCCCCCC		26.5920415495
664PhosphorylationSTTGITTTTSPKTPP
ECCCCCCCCCCCCCC		19.3420415495
665PhosphorylationTTGITTTTSPKTPPP
CCCCCCCCCCCCCCC		40.7225521595
666PhosphorylationTGITTTTSPKTPPPL
CCCCCCCCCCCCCCC		23.4725521595
868PhosphorylationKHQQELQSLKIEYEC
HHHHHHHHCCEEEEH		44.2328066266
900PhosphorylationKLKENLVSLEEALQN
HHHHHHHCHHHHHCC		32.9828066266
929AcetylationIVCVQQEKDQKLLEM
EEEEECHHHHHHHHH		62.217921103
951AcetylationHCEIKELKQSREMAL
CHHHHHHHHHHHHHH		47.5215630893
962AcetylationEMALEDLKKLHDEKI
HHHHHHHHHHCHHHH		66.6615630903
971PhosphorylationLHDEKIESLRAEFQC
HCHHHHHHHHHHHHH		26.9928066266
1004PhosphorylationQEFEKVMTDHNMSLE
HHHHHHHCCCCCCHH		36.7728285833
1087PhosphorylationQQKEMLKSLLEQETE
HHHHHHHHHHHHHHH		33.9427180971
1155PhosphorylationKAELDNVTSLHRQAY
HHHHHHHHHHHHHHH		31.6528066266
1156PhosphorylationAELDNVTSLHRQAYE
HHHHHHHHHHHHHHH		20.2128066266
1275PhosphorylationAKTPAFESAREDSSS
HCCHHHHHHCCCCHH		26.6023984901
1280PhosphorylationFESAREDSSSLVAEL
HHHHCCCCHHHHHHH		19.6428833060
1281PhosphorylationESAREDSSSLVAELQ
HHHCCCCHHHHHHHH		39.7628833060
1282PhosphorylationSAREDSSSLVAELQE
HHCCCCHHHHHHHHH		30.7128833060
1318PhosphorylationEEMQNVRTSLIAEQQ
HHHHHHHHHHHHHHH		24.4928464351
1339AcetylationLTREKMRKENIINDL
HCHHHHHHHCHHHHH		52.172384461
1349AcetylationIINDLSDKLKSTMQQ
HHHHHHHHHHHHHHH		55.212384469
1366PhosphorylationRDKDLIESLSEDRAR
HHHHHHHHHHHHHHH		30.1523737553
1368PhosphorylationKDLIESLSEDRARLL
HHHHHHHHHHHHHHH		46.8928066266
1406PhosphorylationVAAAPELYGACAPEL
CHHCHHHHCCCCCCC		10.8729514104
1450AcetylationENMLSEEKQRIMLLE
HHCCCHHHHHHHHHH		40.6019859309
1476PhosphorylationRLNQRLMSQSLSSVS
HHHHHHHHHHHHHHH		22.6228066266
1478PhosphorylationNQRLMSQSLSSVSSR
HHHHHHHHHHHHHHH		23.9426745281
1480PhosphorylationRLMSQSLSSVSSRHS
HHHHHHHHHHHHHCC		33.6628066266
1481PhosphorylationLMSQSLSSVSSRHSE
HHHHHHHHHHHHCCC		31.1728066266
1483PhosphorylationSQSLSSVSSRHSEKI
HHHHHHHHHHCCCCE		24.4928066266
1484PhosphorylationQSLSSVSSRHSEKIA
HHHHHHHHHCCCCEE		31.6828066266
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 RBCC1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBCC1_MOUSE !!
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 RBCC1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K5_MOUSEMap3k5physical
17015619
TRAF2_MOUSETraf2physical
17015619
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBCC1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-665, AND MASSSPECTROMETRY.

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