RIC8A_HUMAN - dbPTM
RIC8A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIC8A_HUMAN
UniProt AC Q9NPQ8
Protein Name Synembryn-A
Gene Name RIC8A
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Cytoplasm. Cell membrane. Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity)..
Protein Description Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation..
Protein Sequence MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRKRLAELLVSVLEQGLPPSHRVIWLQSVRILSRDRNCLDPFTSRQSLQALACYADISVSEGSVPESADMDVVLESLKCLCNLVLSSPVAQMLAAEARLVVKLTERVGLYRERSFPHDVQFFDLRLLFLLTALRTDVRQQLFQELKGVRLLTDTLELTLGVTPEGNPPPTLLPSQETERAMEILKVLFNITLDSIKGEVDEEDAALYRHLGTLLRHCVMIATAGDRTEEFHGHAVNLLGNLPLKCLDVLLTLEPHGDSTEFMGVNMDVIRALLIFLEKRLHKTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGEMLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVTMFDKLSRNRVIQPMGMSPRGHLTSLQDAMCETMEQQLSSDPDSDPD
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
12PhosphorylationAVAEAVETGEEDVIM
HHHHHHHHCCHHHHH		43.21-
19SulfoxidationTGEEDVIMEALRSYN
HCCHHHHHHHHHHCC		2.1821406390
24PhosphorylationVIMEALRSYNQEHSQ
HHHHHHHHCCHHHCC		29.3230108239
25PhosphorylationIMEALRSYNQEHSQS
HHHHHHHCCHHHCCC		17.9030108239
30PhosphorylationRSYNQEHSQSFTFDD
HHCCHHHCCCCCCCH		27.1117525332
30 (in isoform 3)Phosphorylation-27.11-
32PhosphorylationYNQEHSQSFTFDDAQ
CCHHHCCCCCCCHHH		29.3030108239
32 (in isoform 3)Phosphorylation-29.3027251275
34PhosphorylationQEHSQSFTFDDAQQE
HHHCCCCCCCHHHHH		31.2530108239
69PhosphorylationHRVIWLQSVRILSRD
HEEEEHHHHHHHHCC		15.9328857561
74PhosphorylationLQSVRILSRDRNCLD
HHHHHHHHCCCCCCC		29.75-
77UbiquitinationVRILSRDRNCLDPFT
HHHHHCCCCCCCCCC		34.3524816145
172PhosphorylationLRLLFLLTALRTDVR
HHHHHHHHHHCHHHH		26.2824719451
187UbiquitinationQQLFQELKGVRLLTD
HHHHHHHHCCEEEEE		55.3924816145
191UbiquitinationQELKGVRLLTDTLEL
HHHHCCEEEEEEEEE		5.8424816145
193PhosphorylationLKGVRLLTDTLELTL
HHCCEEEEEEEEEEE		31.37-
193 (in isoform 4)Phosphorylation-31.3726552605
195PhosphorylationGVRLLTDTLELTLGV
CCEEEEEEEEEEECC		19.52-
195 (in isoform 4)Phosphorylation-19.5226552605
199PhosphorylationLTDTLELTLGVTPEG
EEEEEEEEECCCCCC		16.46-
199 (in isoform 4)Phosphorylation-16.4626552605
203PhosphorylationLELTLGVTPEGNPPP
EEEEECCCCCCCCCC		17.52-
203 (in isoform 4)Phosphorylation-17.5226552605
210 (in isoform 4)Phosphorylation-36.6126552605
214 (in isoform 4)Phosphorylation-36.7626552605
217 (in isoform 4)Phosphorylation-57.9026552605
235PhosphorylationLFNITLDSIKGEVDE
HHHCCHHHHCCCCCH		29.3428064214
243UbiquitinationIKGEVDEEDAALYRH
HCCCCCHHHHHHHHH		48.7821890473
279UbiquitinationHGHAVNLLGNLPLKC
CCHHHHHCCCCCCCH		3.4524816145
299UbiquitinationTLEPHGDSTEFMGVN
HCCCCCCCCCCCCCC		34.1321890473
324PhosphorylationLEKRLHKTHRLKESV
HHHHHHHHHHCHHHH		11.07-
326PhosphorylationKRLHKTHRLKESVAP
HHHHHHHHCHHHHHH		53.3232142685
328UbiquitinationLHKTHRLKESVAPVL
HHHHHHCHHHHHHHH		48.15-
330PhosphorylationKTHRLKESVAPVLSV
HHHHCHHHHHHHHHH		23.2228857561
331PhosphorylationTHRLKESVAPVLSVL
HHHCHHHHHHHHHHH		7.9732142685
339PhosphorylationAPVLSVLTECARMHR
HHHHHHHHHHHHCCC		27.1930576142
340UbiquitinationPVLSVLTECARMHRP
HHHHHHHHHHHCCCH		23.2433845483
341GlutathionylationVLSVLTECARMHRPA
HHHHHHHHHHCCCHH		2.1622555962
346 (in isoform 2)Ubiquitination-19.7521890473
352 (in isoform 1)Ubiquitination-5.1521890473
352 (in isoform 4)Ubiquitination-5.15-
353MalonylationRPARKFLKAQVLPPL
CHHHHHHHCCCCCCC		39.6532601280
353UbiquitinationRPARKFLKAQVLPPL
CHHHHHHHCCCCCCC		39.6533845483
357UbiquitinationKFLKAQVLPPLRDVR
HHHHCCCCCCCCCCC		2.1021890473
372SulfoxidationTRPEVGEMLRNKLVR
CCHHHHHHHHHHHHH		3.3321406390
379UbiquitinationMLRNKLVRLMTHLDT
HHHHHHHHHHHHCCH		29.2223000965
382PhosphorylationNKLVRLMTHLDTDVK
HHHHHHHHHCCHHHH		24.7128857561
389UbiquitinationTHLDTDVKRVAAEFL
HHCCHHHHHHHHHHH		43.9224816145
392PhosphorylationDTDVKRVAAEFLFVL
CHHHHHHHHHHHHHH		12.8132142685
393UbiquitinationTDVKRVAAEFLFVLC
HHHHHHHHHHHHHHH		12.7624816145
395UbiquitinationVKRVAAEFLFVLCSE
HHHHHHHHHHHHHCC		5.7124816145
402 (in isoform 2)Ubiquitination-55.5521890473
408 (in isoform 1)Ubiquitination-3.3521890473
408 (in isoform 4)Ubiquitination-3.35-
409UbiquitinationESVPRFIKYTGYGNA
CCCCCHHHHCCCCCH		33.7623000965
413UbiquitinationRFIKYTGYGNAAGLL
CHHHHCCCCCHHHHH		10.2121890473
415UbiquitinationIKYTGYGNAAGLLAA
HHHCCCCCHHHHHHH		20.3821890473
415 (in isoform 3)Ubiquitination-20.3821890473
434PhosphorylationAGGRPEGQYSEDEDT
CCCCCCCCCCCCCCC		36.6018669648
435PhosphorylationGGRPEGQYSEDEDTD
CCCCCCCCCCCCCCC		25.5322167270
436PhosphorylationGRPEGQYSEDEDTDT
CCCCCCCCCCCCCCH		30.5919664994
440PhosphorylationGQYSEDEDTDTDEYK
CCCCCCCCCCHHHHH		63.3032142685
441PhosphorylationQYSEDEDTDTDEYKE
CCCCCCCCCHHHHHH		38.4619664994
441 (in isoform 3)Phosphorylation-38.46-
442PhosphorylationYSEDEDTDTDEYKEA
CCCCCCCCHHHHHHH		65.5632142685
442 (in isoform 3)Phosphorylation-65.5621406692
443PhosphorylationSEDEDTDTDEYKEAK
CCCCCCCHHHHHHHH		32.5919664994
445PhosphorylationDEDTDTDEYKEAKAS
CCCCCHHHHHHHHHH		61.6732142685
446PhosphorylationEDTDTDEYKEAKASI
CCCCHHHHHHHHHHC		19.5523401153
447PhosphorylationDTDTDEYKEAKASIN
CCCHHHHHHHHHHCC		49.5032142685
447 (in isoform 3)Phosphorylation-49.5021406692
449 (in isoform 3)Phosphorylation-14.4621406692
450UbiquitinationTDEYKEAKASINPVT
HHHHHHHHHHCCCCC		43.7033845483
452PhosphorylationEYKEAKASINPVTGR
HHHHHHHHCCCCCCC		23.3818669648
452 (in isoform 3)Phosphorylation-23.38-
454UbiquitinationKEAKASINPVTGRVE
HHHHHHCCCCCCCCC		23.6133845483
456UbiquitinationAKASINPVTGRVEEK
HHHHCCCCCCCCCCC		8.4033845483
457PhosphorylationKASINPVTGRVEEKP
HHHCCCCCCCCCCCC		22.1121406692
458 (in isoform 3)Phosphorylation-31.6921406692
468SulfoxidationEEKPPNPMEGMTEEQ
CCCCCCCCCCCCHHH		9.8730846556
471SulfoxidationPPNPMEGMTEEQKEH
CCCCCCCCCHHHHHH		2.4430846556
472PhosphorylationPNPMEGMTEEQKEHE
CCCCCCCCHHHHHHH		47.4229083192
481SulfoxidationEQKEHEAMKLVTMFD
HHHHHHHHHHHHHHH		2.9230846556
485PhosphorylationHEAMKLVTMFDKLSR
HHHHHHHHHHHHHCC		23.66-
486SulfoxidationEAMKLVTMFDKLSRN
HHHHHHHHHHHHCCC		2.9721406390
489MalonylationKLVTMFDKLSRNRVI
HHHHHHHHHCCCCCC		36.7826320211
489UbiquitinationKLVTMFDKLSRNRVI
HHHHHHHHHCCCCCC		36.7823000965
491PhosphorylationVTMFDKLSRNRVIQP
HHHHHHHCCCCCCCC		33.0028348404
493UbiquitinationMFDKLSRNRVIQPMG
HHHHHCCCCCCCCCC		38.9123000965
495UbiquitinationDKLSRNRVIQPMGMS
HHHCCCCCCCCCCCC		5.6423000965
495 (in isoform 3)Ubiquitination-5.64-
497 (in isoform 3)Phosphorylation-21.0427251275
501PhosphorylationRVIQPMGMSPRGHLT
CCCCCCCCCCCHHCH		3.9718669648
502PhosphorylationVIQPMGMSPRGHLTS
CCCCCCCCCCHHCHH		13.0125159151
506PhosphorylationMGMSPRGHLTSLQDA
CCCCCCHHCHHHHHH		27.4932142685
508PhosphorylationMSPRGHLTSLQDAMC
CCCCHHCHHHHHHHH		23.0118669648
508 (in isoform 3)Phosphorylation-23.0124719451
509PhosphorylationSPRGHLTSLQDAMCE
CCCHHCHHHHHHHHH		30.3221406692
517PhosphorylationLQDAMCETMEQQLSS
HHHHHHHHHHHHHHC		22.5325137130
522PhosphorylationCETMEQQLSSDPDSD
HHHHHHHHHCCCCCC		5.4518669648
523PhosphorylationETMEQQLSSDPDSDP
HHHHHHHHCCCCCCC		28.4917081983
524PhosphorylationTMEQQLSSDPDSDPD
HHHHHHHCCCCCCCC		62.8517081983
527PhosphorylationQQLSSDPDSDPD---
HHHHCCCCCCCC---		71.3318669648
528PhosphorylationQLSSDPDSDPD----
HHHCCCCCCCC----		57.3311230166
529 (in isoform 3)Phosphorylation-59.7827251275
530 (in isoform 3)Phosphorylation-53.8427251275
534 (in isoform 3)Phosphorylation-27251275
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 RIC8A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIC8A_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 RIC8A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNA13_HUMANGNA13physical
12509430
GNAQ_HUMANGNAQphysical
12509430
GNAI3_HUMANGNAI3physical
12509430
GNAI2_HUMANGNAI2physical
12509430
GNAO_HUMANGNAO1physical
12509430
GNAI1_HUMANGNAI1physical
12509430
XPO1_HUMANXPO1physical
21988832
GNAQ_HUMANGNAQphysical
16629901
APEX1_HUMANAPEX1physical
22863883
MSHR_HUMANMC1Rphysical
22863883
PLCG1_HUMANPLCG1physical
22863883
PYGB_HUMANPYGBphysical
22863883
NUTM1_HUMANNUTM1physical
25416956
SPAG5_HUMANSPAG5physical
28514442
DCTN4_HUMANDCTN4physical
28514442
DCTN3_HUMANDCTN3physical
28514442
DCTN6_HUMANDCTN6physical
28514442
DCTN5_HUMANDCTN5physical
28514442
DCTN1_HUMANDCTN1physical
28514442
ARP10_HUMANACTR10physical
28514442
ACTY_HUMANACTR1Bphysical
28514442
MTCH1_HUMANMTCH1physical
28514442
ACTZ_HUMANACTR1Aphysical
28514442
DCTN2_HUMANDCTN2physical
28514442
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 RIC8A_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-436; THR-441 ANDSER-502, AND MASS SPECTROMETRY.
"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 TYR-435 AND SER-436, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, 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 SER-436; THR-441; SER-502;SER-523; SER-524 AND SER-528, 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-436; THR-441 ANDSER-502, AND MASS SPECTROMETRY.
"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 SER-30, AND MASSSPECTROMETRY.

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