RIC1_HUMAN - dbPTM
RIC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIC1_HUMAN
UniProt AC Q4ADV7
Protein Name RAB6A-GEF complex partner protein 1 {ECO:0000312|HGNC:HGNC:17686}
Gene Name RIC1 {ECO:0000312|HGNC:HGNC:17686}
Organism Homo sapiens (Human).
Sequence Length 1423
Subcellular Localization Cytoplasm, cytosol . Membrane
Single-pass membrane protein .
Protein Description The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. Required for phosphorylation and localization of GJA1..
Protein Sequence MYFLSGWPKRLLCPLGSPAEAPFHVQSDPQRAFFAVLAAARLSIWYSRPSVLIVTYKEPAKSSTQFGSYKQAEWRPDSTMIAVSTANGYILFFHITSTRGDKYLYEPVYPKGSPQMKGTPHFKEEQCAPALNLEMRKILDLQAPIMSLQSVLEDLLVATSDGLLHLIHWEGMTNGRKAINLCTVPFSVDLQSSRVGSFLGFTDVHIRDMEYCATLDGFAVVFNDGKVGFITPVSSRFTAEQLHGVWPQDVVDGTCVAVNNKYRLMAFGCVSGSVQVYTIDNSTGAMLLSHKLELTAKQYPDIWNKTGAVKLMRWSPDNSVVIVTWEYGGLSLWSVFGAQLICTLGGDFAYRSDGTKKDPLKINSMSWGAEGYHLWVISGFGSQNTEIESDLRSVVKQPSILLFQFIKSVLTVNPCMSNQEQVLLQGEDRLYLNCGEASQTQNPRSSSTHSEHKPSREKSPFADGGLESQGLSTLLGHRHWHVVQISSTYLESNWPIRFSAIDKLGQNIAVVGKFGFAHYSLLTKKWKLFGNITQEQNMIVTGGLAWWNDFMVLACYNINDRQEELRVYLRTSNLDNAFAHVTKAQAETLLLSVFQDMVIVFRADCSICLYSIERKSDGPNTTAGIQVLQEVSMSRYIPHPFLVVSVTLTSVSTENGITLKMPQQARGAESIMLNLAGQLIMMQRDRSGPQIREKDSNPNNQRKLLPFCPPVVLAQSVENVWTTCRANKQKRHLLEALWLSCGGAGMKVWLPLFPRDHRKPHSFLSQRIMLPFHINIYPLAVLFEDALVLGAVNDTLLYDSLYTRNNAREQLEVLFPFCVVERTSQIYLHHILRQLLVRNLGEQALLLAQSCATLPYFPHVLELMLHEVLEEEATSREPIPDPLLPTVAKFITEFPLFLQTVVHCARKTEYALWNYLFAAVGNPKDLFEECLMAQDLDTAASYLIILQNMEVPAVSRQHATLLFNTALEQGKWDLCRHMIRFLKAIGSGESETPPSTPTAQEPSSSGGFEFFRNRSISLSQSAENVPASKFSLQKTLSMPSGPSGKRWSKDSDCAENMYIDMMLWRHARRLLEDVRLKDLGCFAAQLGFELISWLCKERTRAARVDNFVIALKRLHKDFLWPLPIIPASSISSPFKNGKYRTVGEQLLKSQSADPFLNLEMDAGISNIQRSQSWLSNIGPTHHEIDTASSHGPQMQDAFLSPLSNKGDECSIGSATDLTESSSMVDGDWTMVDENFSTLSLTQSELEHISMELASKGPHKSQVQLRYLLHIFMEAGCLDWCIVIGLILRESSIINQILVITQSSEVDGEMLQNIKTGLHAVDRWASTDCPGYKPFLNIIKPQLQKLSEITEEQVQPDAFQPITMGKTPEQTSPRAEESRGSSSHGSIPQGEVGSSNMVSRKEEDTAQAEEEEPFQDGTYDCSVS
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
9UbiquitinationYFLSGWPKRLLCPLG
CCCCCCCCEEECCCC		49.52-
105PhosphorylationTRGDKYLYEPVYPKG
CCCCEEEEECCCCCC		18.3325159151
111UbiquitinationLYEPVYPKGSPQMKG
EEECCCCCCCCCCCC		55.0921906983
111 (in isoform 1)Ubiquitination-55.0921906983
111 (in isoform 2)Ubiquitination-55.0921906983
113PhosphorylationEPVYPKGSPQMKGTP
ECCCCCCCCCCCCCC		20.34-
123UbiquitinationMKGTPHFKEEQCAPA
CCCCCCCCHHHCHHH		58.26-
277PhosphorylationVSGSVQVYTIDNSTG
ECCCEEEEEECCCCC		4.85-
355PhosphorylationFAYRSDGTKKDPLKI
EEECCCCCCCCCCEE		39.6523285258
364PhosphorylationKDPLKINSMSWGAEG
CCCCEECEEECCCCC		20.0519690332
372PhosphorylationMSWGAEGYHLWVISG
EECCCCCEEEEEEEC		5.8019690332
378PhosphorylationGYHLWVISGFGSQNT
CEEEEEEECCCCCCC		20.6019690332
385PhosphorylationSGFGSQNTEIESDLR
ECCCCCCCCCHHHHH		30.6119690332
396UbiquitinationSDLRSVVKQPSILLF
HHHHHHHCCHHHHHH		55.10-
431PhosphorylationLQGEDRLYLNCGEAS
ECCCCEEEEECCCCC		9.2121406692
438PhosphorylationYLNCGEASQTQNPRS
EEECCCCCCCCCCCC		29.4721406692
440PhosphorylationNCGEASQTQNPRSSS
ECCCCCCCCCCCCCC		28.0221406692
445PhosphorylationSQTQNPRSSSTHSEH
CCCCCCCCCCCCCCC		29.8729978859
446PhosphorylationQTQNPRSSSTHSEHK
CCCCCCCCCCCCCCC		40.3029978859
447PhosphorylationTQNPRSSSTHSEHKP
CCCCCCCCCCCCCCC		31.2429978859
448PhosphorylationQNPRSSSTHSEHKPS
CCCCCCCCCCCCCCC		31.2229978859
450PhosphorylationPRSSSTHSEHKPSRE
CCCCCCCCCCCCCCC		41.2929978859
453UbiquitinationSSTHSEHKPSREKSP
CCCCCCCCCCCCCCC		40.4129967540
458 (in isoform 1)Ubiquitination-63.4221906983
458 (in isoform 2)Ubiquitination-63.4221906983
458UbiquitinationEHKPSREKSPFADGG
CCCCCCCCCCCCCCC		63.4221906983
459PhosphorylationHKPSREKSPFADGGL
CCCCCCCCCCCCCCH		22.0921712546
503AcetylationIRFSAIDKLGQNIAV
CCHHHHHHCCCCEEE		48.6925953088
520PhosphorylationKFGFAHYSLLTKKWK
ECCHHHHHHHHHHHH		13.6724719451
575UbiquitinationYLRTSNLDNAFAHVT
HHHHCCCCHHHHHCH		48.9721987572
632PhosphorylationIQVLQEVSMSRYIPH
HHHHHHHHCHHCCCC		15.41-
636PhosphorylationQEVSMSRYIPHPFLV
HHHHCHHCCCCCEEE		16.1130243723
645PhosphorylationPHPFLVVSVTLTSVS
CCCEEEEEEEEEEEE		11.2530243723
647PhosphorylationPFLVVSVTLTSVSTE
CEEEEEEEEEEEECC		19.4730243723
649PhosphorylationLVVSVTLTSVSTENG
EEEEEEEEEEECCCC		20.0930243723
650PhosphorylationVVSVTLTSVSTENGI
EEEEEEEEEECCCCE		19.7230243723
652PhosphorylationSVTLTSVSTENGITL
EEEEEEEECCCCEEE		29.7630243723
653PhosphorylationVTLTSVSTENGITLK
EEEEEEECCCCEEEE		31.1730243723
658PhosphorylationVSTENGITLKMPQQA
EECCCCEEEECCHHH		23.0230243723
759UbiquitinationLFPRDHRKPHSFLSQ
CCCCCCCCCCCHHHC		43.60-
777PhosphorylationLPFHINIYPLAVLFE
ECCCCCCHHHHHHHC		6.41-
801UbiquitinationDTLLYDSLYTRNNAR
CCHHHHCCCCCCCHH		4.6521987572
987PhosphorylationRFLKAIGSGESETPP
HHHHHHCCCCCCCCC		33.0228176443
990PhosphorylationKAIGSGESETPPSTP
HHHCCCCCCCCCCCC		50.7428176443
992UbiquitinationIGSGESETPPSTPTA
HCCCCCCCCCCCCCC		50.1829967540
992PhosphorylationIGSGESETPPSTPTA
HCCCCCCCCCCCCCC		50.1825159151
995PhosphorylationGESETPPSTPTAQEP
CCCCCCCCCCCCCCC		48.5028176443
996PhosphorylationESETPPSTPTAQEPS
CCCCCCCCCCCCCCC		30.3628176443
997UbiquitinationSETPPSTPTAQEPSS
CCCCCCCCCCCCCCC		30.0321987572
998PhosphorylationETPPSTPTAQEPSSS
CCCCCCCCCCCCCCC		40.8528176443
1003PhosphorylationTPTAQEPSSSGGFEF
CCCCCCCCCCCCCCC		36.0630108239
1004PhosphorylationPTAQEPSSSGGFEFF
CCCCCCCCCCCCCCC		43.6630108239
1005PhosphorylationTAQEPSSSGGFEFFR
CCCCCCCCCCCCCCC		47.4730108239
1015PhosphorylationFEFFRNRSISLSQSA
CCCCCCCCEECCHHC		21.7830266825
1017PhosphorylationFFRNRSISLSQSAEN
CCCCCCEECCHHCCC		24.1825159151
1019PhosphorylationRNRSISLSQSAENVP
CCCCEECCHHCCCCC		18.4630266825
1021PhosphorylationRSISLSQSAENVPAS
CCEECCHHCCCCCHH		33.8930266825
1028PhosphorylationSAENVPASKFSLQKT
HCCCCCHHHCEEEEE		28.3223403867
1029 (in isoform 2)Ubiquitination-40.8721906983
1029 (in isoform 1)Ubiquitination-40.8721906983
1029UbiquitinationAENVPASKFSLQKTL
CCCCCHHHCEEEEEC		40.8721906983
1031PhosphorylationNVPASKFSLQKTLSM
CCCHHHCEEEEECCC		33.3624076635
1034 (in isoform 2)Ubiquitination-57.6421906983
1034UbiquitinationASKFSLQKTLSMPSG
HHHCEEEEECCCCCC		57.6421906983
1034 (in isoform 1)Ubiquitination-57.6421906983
1035PhosphorylationSKFSLQKTLSMPSGP
HHCEEEEECCCCCCC		15.8823403867
1037PhosphorylationFSLQKTLSMPSGPSG
CEEEEECCCCCCCCC		33.6025159151
1040PhosphorylationQKTLSMPSGPSGKRW
EEECCCCCCCCCCCC		55.4823403867
1043PhosphorylationLSMPSGPSGKRWSKD
CCCCCCCCCCCCCCC		61.5423403867
1045AcetylationMPSGPSGKRWSKDSD
CCCCCCCCCCCCCCC		55.8425953088
1058PhosphorylationSDCAENMYIDMMLWR
CCHHHHHHHHHHHHH		12.83-
1075UbiquitinationRRLLEDVRLKDLGCF
HHHHHHCCHHHHHHH		48.6321987572
1111UbiquitinationVDNFVIALKRLHKDF
CCCHHHHHHHHCCCC		1.9721987572
1112 (in isoform 2)Ubiquitination-43.8421906983
1112UbiquitinationDNFVIALKRLHKDFL
CCHHHHHHHHCCCCC		43.842190698
1112 (in isoform 1)Ubiquitination-43.8421906983
1128PhosphorylationPLPIIPASSISSPFK
CCCCCCHHHCCCCCC		23.8928450419
1129PhosphorylationLPIIPASSISSPFKN
CCCCCHHHCCCCCCC		28.7028450419
1131PhosphorylationIIPASSISSPFKNGK
CCCHHHCCCCCCCCC		33.6328450419
1132PhosphorylationIPASSISSPFKNGKY
CCHHHCCCCCCCCCC		32.4628450419
1148MethylationTVGEQLLKSQSADPF
CHHHHHHHCCCCCCC		55.85115976657
1149PhosphorylationVGEQLLKSQSADPFL
HHHHHHHCCCCCCCC		29.3628348404
1151PhosphorylationEQLLKSQSADPFLNL
HHHHHCCCCCCCCCC		41.5528348404
1165PhosphorylationLEMDAGISNIQRSQS
CCCCCCCCHHHHHHH		27.2826074081
1170PhosphorylationGISNIQRSQSWLSNI
CCCHHHHHHHHHHHC		16.5226074081
1172PhosphorylationSNIQRSQSWLSNIGP
CHHHHHHHHHHHCCC		31.0926074081
1175PhosphorylationQRSQSWLSNIGPTHH
HHHHHHHHHCCCCCC		21.8326074081
1346PhosphorylationKPQLQKLSEITEEQV
HHHHHHHHHCCHHHC		33.7124719451
1362PhosphorylationPDAFQPITMGKTPEQ
CCCCCCCCCCCCCCC		26.9324719451
1366PhosphorylationQPITMGKTPEQTSPR
CCCCCCCCCCCCCCC		26.7426055452
1370PhosphorylationMGKTPEQTSPRAEES
CCCCCCCCCCCHHHH		38.7525159151
1371PhosphorylationGKTPEQTSPRAEESR
CCCCCCCCCCHHHHC		16.4525159151
1380PhosphorylationRAEESRGSSSHGSIP
CHHHHCCCCCCCCCC		27.79-
1393PhosphorylationIPQGEVGSSNMVSRK
CCCCCCCCCCCCCCC		24.58-
1394PhosphorylationPQGEVGSSNMVSRKE
CCCCCCCCCCCCCCH		24.02-
1398PhosphorylationVGSSNMVSRKEEDTA
CCCCCCCCCCHHCCC		27.1928270605
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 RIC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIC1_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 RIC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RIC1_HUMAN !!
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 RIC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1017 AND SER-1037, ANDMASS 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 THR-992 AND THR-996, ANDMASS SPECTROMETRY.

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