SMCR8_HUMAN - dbPTM
SMCR8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMCR8_HUMAN
UniProt AC Q8TEV9
Protein Name Guanine nucleotide exchange protein SMCR8 {ECO:0000305}
Gene Name SMCR8 {ECO:0000312|HGNC:HGNC:17921}
Organism Homo sapiens (Human).
Sequence Length 937
Subcellular Localization Cytoplasm . Nucleus . Localizes mainly in the cytoplasm.
Protein Description Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. [PubMed: 20562859]
Protein Sequence MISAPDVVAFTKEEEYEEEPYNEPALPEEYSVPLFPFASQGANPWSKLSGAKFSRDFILISEFSEQVGPQPLLTIPNDTKVFGTFDLNYFSLRIMSVDYQASFVGHPPGSAYPKLNFVEDSKVVLGDSKEGAFAYVHHLTLYDLEARGFVRPFCMAYISADQHKIMQQFQELSAEFSRASECLKTGNRKAFAGELEKKLKDLDYTRTVLHTETEIQKKANDKGFYSSQAIEKANELASVEKSIIEHQDLLKQIRSYPHRKLKGHDLCPGEMEHIQDQASQASTTSNPDESADTDLYTCRPAYTPKLIKAKSTKCFDKKLKTLEELCDTEYFTQTLAQLSHIEHMFRGDLCYLLTSQIDRALLKQQHITNFLFEDFVEVDDRMVEKQESIPSKPSQDRPPSSSLEECPIPKVLISVGSYKSSVESVLIKMEQELGDEEYKEVEVTELSSFDPQENLDYLDMDMKGSISSGESIEVLGTEKSTSVLSKSDSQASLTVPLSPQVVRSKAVSHRTISEDSIEVLSTCPSEALIPDDFKASYPSAINEEESYPDGNEGAIRFQASISPPELGETEEGSIENTPSQIDSSCCIGKESDGQLVLPSTPAHTHSDEDGVVSSPPQRHRQKDQGFRVDFSVENANPSSRDNSCEGFPAYELDPSHLLASRDISKTSLDNYSDTTSYVSSVASTSSDRIPSAYPAGLSSDRHKKRAGQNALKFIRQYPFAHPAIYSLLSGRTLVVLGEDEAIVRKLVTALAIFVPSYGCYAKPVKHWASSPLHIMDFQKWKLIGLQRVASPAGAGTLHALSRYSRYTSILDLDNKTLRCPLYRGTLVPRLADHRTQIKRGSTYYLHVQSMLTQLCSKAFLYTFCHHLHLPTHDKETEELVASRQMSFLKLTLGLVNEDVRVVQYLAELLKLHYMQESPGTSHPMLRFDYVPSFLYKI
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
47UbiquitinationQGANPWSKLSGAKFS
CCCCCHHHHCCCCCC		42.6929967540
49PhosphorylationANPWSKLSGAKFSRD
CCCHHHHCCCCCCCC		40.2024719451
61PhosphorylationSRDFILISEFSEQVG
CCCEEEEEECHHHHC		29.19-
84O-linked_GlycosylationNDTKVFGTFDLNYFS
CCCCEEEEEECCEEE		11.5130379171
184UbiquitinationSRASECLKTGNRKAF
HHHHHHHHHCCCHHH		67.0729967540
189UbiquitinationCLKTGNRKAFAGELE
HHHHCCCHHHHHHHH		52.4329967540
197UbiquitinationAFAGELEKKLKDLDY
HHHHHHHHHHHHCCC		75.84-
198UbiquitinationFAGELEKKLKDLDYT
HHHHHHHHHHHCCCH		51.93-
200UbiquitinationGELEKKLKDLDYTRT
HHHHHHHHHCCCHHE		66.1929967540
217UbiquitinationHTETEIQKKANDKGF
ECHHHHHHHHCCCCC		60.5629967540
222UbiquitinationIQKKANDKGFYSSQA
HHHHHCCCCCCCHHH		51.2129967540
225PhosphorylationKANDKGFYSSQAIEK
HHCCCCCCCHHHHHH		18.9729759185
226PhosphorylationANDKGFYSSQAIEKA
HCCCCCCCHHHHHHH		17.4529759185
227O-linked_GlycosylationNDKGFYSSQAIEKAN
CCCCCCCHHHHHHHH		16.5530379171
227PhosphorylationNDKGFYSSQAIEKAN
CCCCCCCHHHHHHHH		16.5529759185
232UbiquitinationYSSQAIEKANELASV
CCHHHHHHHHHHHHH		50.8529967540
238PhosphorylationEKANELASVEKSIIE
HHHHHHHHHHHHHHH		43.3524719451
241UbiquitinationNELASVEKSIIEHQD
HHHHHHHHHHHHCHH		44.8129967540
251UbiquitinationIEHQDLLKQIRSYPH
HHCHHHHHHHHCCCC		51.4829967540
282PhosphorylationQDQASQASTTSNPDE
HHHHHHHCCCCCCCC		25.2827251275
283PhosphorylationDQASQASTTSNPDES
HHHHHHCCCCCCCCC		36.9427251275
284PhosphorylationQASQASTTSNPDESA
HHHHHCCCCCCCCCC		24.8227251275
285PhosphorylationASQASTTSNPDESAD
HHHHCCCCCCCCCCC		46.5927251275
302PhosphorylationLYTCRPAYTPKLIKA
CEECCCCCCHHHHHC		26.68-
388PhosphorylationRMVEKQESIPSKPSQ
HHHHCHHCCCCCCCC		36.9926074081
391PhosphorylationEKQESIPSKPSQDRP
HCHHCCCCCCCCCCC		56.3730266825
392UbiquitinationKQESIPSKPSQDRPP
CHHCCCCCCCCCCCC		43.2529967540
394PhosphorylationESIPSKPSQDRPPSS
HCCCCCCCCCCCCCC		48.7426657352
400PhosphorylationPSQDRPPSSSLEECP
CCCCCCCCCCCCCCC		34.9330266825
401PhosphorylationSQDRPPSSSLEECPI
CCCCCCCCCCCCCCC		44.7230266825
402PhosphorylationQDRPPSSSLEECPIP
CCCCCCCCCCCCCCC		44.1030266825
414PhosphorylationPIPKVLISVGSYKSS
CCCEEEEEECCCHHH		19.1030266825
417PhosphorylationKVLISVGSYKSSVES
EEEEEECCCHHHHHH		27.5119664994
418PhosphorylationVLISVGSYKSSVESV
EEEEECCCHHHHHHH		14.6828176443
420PhosphorylationISVGSYKSSVESVLI
EEECCCHHHHHHHHH		31.2322777824
421PhosphorylationSVGSYKSSVESVLIK
EECCCHHHHHHHHHH		26.2527732954
424PhosphorylationSYKSSVESVLIKMEQ
CCHHHHHHHHHHHHH		21.7728060719
438PhosphorylationQELGDEEYKEVEVTE
HHHCCCCCEEEEEEE		15.4827642862
447PhosphorylationEVEVTELSSFDPQEN
EEEEEECCCCCCCCC		23.7928102081
448PhosphorylationVEVTELSSFDPQENL
EEEEECCCCCCCCCC		46.4228102081
457PhosphorylationDPQENLDYLDMDMKG
CCCCCCCCCCCCCCC		14.0427642862
465PhosphorylationLDMDMKGSISSGESI
CCCCCCCCCCCCCCE		17.4925159151
467PhosphorylationMDMKGSISSGESIEV
CCCCCCCCCCCCEEE		33.7125159151
468PhosphorylationDMKGSISSGESIEVL
CCCCCCCCCCCEEEE		44.9325159151
471PhosphorylationGSISSGESIEVLGTE
CCCCCCCCEEEECCC		27.8125159151
477PhosphorylationESIEVLGTEKSTSVL
CCEEEECCCCCCCCC		35.7630206219
480PhosphorylationEVLGTEKSTSVLSKS
EEECCCCCCCCCCCC		21.4924211406
481PhosphorylationVLGTEKSTSVLSKSD
EECCCCCCCCCCCCC		33.6430206219
482PhosphorylationLGTEKSTSVLSKSDS
ECCCCCCCCCCCCCC		28.3124211406
485PhosphorylationEKSTSVLSKSDSQAS
CCCCCCCCCCCCCCC		28.1426434776
487PhosphorylationSTSVLSKSDSQASLT
CCCCCCCCCCCCCEE		38.8325159151
489PhosphorylationSVLSKSDSQASLTVP
CCCCCCCCCCCEEEE		34.4425159151
492PhosphorylationSKSDSQASLTVPLSP
CCCCCCCCEEEECCH		19.5525159151
494PhosphorylationSDSQASLTVPLSPQV
CCCCCCEEEECCHHH		19.9930266825
498PhosphorylationASLTVPLSPQVVRSK
CCEEEECCHHHHHCC		13.7619664994
504PhosphorylationLSPQVVRSKAVSHRT
CCHHHHHCCCCCCCC		17.2329514088
511PhosphorylationSKAVSHRTISEDSIE
CCCCCCCCCCHHHHH		24.3528450419
513PhosphorylationAVSHRTISEDSIEVL
CCCCCCCCHHHHHHH		34.4428450419
516PhosphorylationHRTISEDSIEVLSTC
CCCCCHHHHHHHHCC		19.3225106551
521PhosphorylationEDSIEVLSTCPSEAL
HHHHHHHHCCCHHHC		32.8928634120
522PhosphorylationDSIEVLSTCPSEALI
HHHHHHHCCCHHHCC		25.0328634120
525PhosphorylationEVLSTCPSEALIPDD
HHHHCCCHHHCCCCC		37.3328348404
562PhosphorylationIRFQASISPPELGET
EEEEEEECCCCCCCC		31.72-
591PhosphorylationSCCIGKESDGQLVLP
CCCCEECCCCCEEEC		50.9928464451
599PhosphorylationDGQLVLPSTPAHTHS
CCCEEECCCCCCCCC		42.7529255136
600PhosphorylationGQLVLPSTPAHTHSD
CCEEECCCCCCCCCC		23.6629255136
604PhosphorylationLPSTPAHTHSDEDGV
ECCCCCCCCCCCCCC		25.7730266825
606PhosphorylationSTPAHTHSDEDGVVS
CCCCCCCCCCCCCCC		43.8030266825
613PhosphorylationSDEDGVVSSPPQRHR
CCCCCCCCCCCCHHC		34.4230266825
614PhosphorylationDEDGVVSSPPQRHRQ
CCCCCCCCCCCHHCC		29.0530266825
638PhosphorylationSVENANPSSRDNSCE
EEECCCCCCCCCCCC		37.5026657352
639PhosphorylationVENANPSSRDNSCEG
EECCCCCCCCCCCCC		44.9326657352
643PhosphorylationNPSSRDNSCEGFPAY
CCCCCCCCCCCCCCC		20.1726657352
650PhosphorylationSCEGFPAYELDPSHL
CCCCCCCCCCCHHHH		19.7727251275
655PhosphorylationPAYELDPSHLLASRD
CCCCCCHHHHHEECC		26.8327251275
660PhosphorylationDPSHLLASRDISKTS
CHHHHHEECCCCCCC		30.3827251275
665UbiquitinationLASRDISKTSLDNYS
HEECCCCCCCCCCCC		42.3329967540
666PhosphorylationASRDISKTSLDNYSD
EECCCCCCCCCCCCC		27.94-
667PhosphorylationSRDISKTSLDNYSDT
ECCCCCCCCCCCCCC		37.15-
683PhosphorylationSYVSSVASTSSDRIP
HHHHHHCCCCCCCCC		27.0228348404
684PhosphorylationYVSSVASTSSDRIPS
HHHHHCCCCCCCCCC		23.6327251275
685PhosphorylationVSSVASTSSDRIPSA
HHHHCCCCCCCCCCC		27.9628348404
686PhosphorylationSSVASTSSDRIPSAY
HHHCCCCCCCCCCCC		30.8828348404
691PhosphorylationTSSDRIPSAYPAGLS
CCCCCCCCCCCCCCC		37.7629743597
698PhosphorylationSAYPAGLSSDRHKKR
CCCCCCCCCHHHHHH		29.3129743597
699PhosphorylationAYPAGLSSDRHKKRA
CCCCCCCCHHHHHHH		43.6429743597
726PhosphorylationFAHPAIYSLLSGRTL
CCCHHHHHHHCCCEE		19.4028355574
790PhosphorylationIGLQRVASPAGAGTL
EECEECCCCCCHHHH		16.6627134283
796PhosphorylationASPAGAGTLHALSRY
CCCCCHHHHHHHHHH		18.1611997338
815 (in isoform 1)Ubiquitination-48.9121906983
815UbiquitinationSILDLDNKTLRCPLY
CEEECCCCEECCCCC		48.912190698
816PhosphorylationILDLDNKTLRCPLYR
EEECCCCEECCCCCC		26.20-
822PhosphorylationKTLRCPLYRGTLVPR
CEECCCCCCCCCCCH		7.6725884760
886PhosphorylationLVASRQMSFLKLTLG
HHHHHHHHHHHHHHH		21.0624719451
929PhosphorylationHPMLRFDYVPSFLYK
CCCCCCCCCCHHHHC		16.14-
932PhosphorylationLRFDYVPSFLYKI--
CCCCCCCHHHHCC--		20.1723879269
935PhosphorylationDYVPSFLYKI-----
CCCCHHHHCC-----		12.4823879269
936UbiquitinationYVPSFLYKI------
CCCHHHHCC------		44.05-
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
400SPhosphorylationKinaseULK1O75385
PSP
402SPhosphorylationKinaseTBK1Q9UHD2
Uniprot
492SPhosphorylationKinaseULK1O75385
PSP
562SPhosphorylationKinaseULK1O75385
PSP
666TPhosphorylationKinaseULK1O75385
PSP
796TPhosphorylationKinaseTBK1Q9UHD2
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCR8_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 SMCR8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCA_HUMANFANCAphysical
28215707
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 SMCR8_HUMAN

loading...

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-417 AND SER-498, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-489; SER-492;THR-494 AND SER-498, AND MASS SPECTROMETRY.
"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-487; SER-492 ANDSER-498, AND MASS SPECTROMETRY.
"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-465; SER-467; SER-468AND SER-471, AND MASS SPECTROMETRY.

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