RBP10_HUMAN - dbPTM
RBP10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBP10_HUMAN
UniProt AC Q6VN20
Protein Name Ran-binding protein 10
Gene Name RANBP10
Organism Homo sapiens (Human).
Sequence Length 620
Subcellular Localization Cytoplasm, cytosol . Nucleus . Predominantly cytoplasmic.
Protein Description Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase (By similarity). May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway..
Protein Sequence MAAATADPGAGNPQPGDSSGGGAGGGLPSPGEQELSRRLQRLYPAVNQQETPLPRSWSPKDKYNYIGLSQGNLRVHYKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPANLYPTVGLQTPGEIVDANFGQQPFLFDIEDYMREWRAKVQGTVHCFPISARLGEWQAVLQNMVSSYLVHHGYCATATAFARMTETPIQEEQASIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSEVRSLSSRSPKSQDSYPGSPSLSPRHGPSSSHMHNTGADSPSCSNGVASTKSKQNHSKYPAPSSSSSSSSSSSSSSPSSVNYSESNSTDSTKSQHHSSTSNQETSDSEMEMEAEHYPNGVLGSMSTRIVNGAYKHEDLQTDESSMDDRHPRRQLCGGNQAATERIILFGRELQALSEQLGREYGKNLAHTEMLQDAFSLLAYSDPWSCPVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECLRLMARAGLGSCSFARVDDYLH
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
2Acetylation------MAAATADPG
------CCCCCCCCC		13.0522814378
18PhosphorylationGNPQPGDSSGGGAGG
CCCCCCCCCCCCCCC		36.4825002506
19PhosphorylationNPQPGDSSGGGAGGG
CCCCCCCCCCCCCCC		46.3125850435
29PhosphorylationGAGGGLPSPGEQELS
CCCCCCCCCCHHHHH		51.0528188228
36PhosphorylationSPGEQELSRRLQRLY
CCCHHHHHHHHHHHH		18.0125850435
58PhosphorylationTPLPRSWSPKDKYNY
CCCCCCCCCCCCCCE		24.2624719451
60UbiquitinationLPRSWSPKDKYNYIG
CCCCCCCCCCCCEEE		62.43-
60UbiquitinationLPRSWSPKDKYNYIG
CCCCCCCCCCCCEEE		62.43-
62UbiquitinationRSWSPKDKYNYIGLS
CCCCCCCCCCEEEEC		41.33-
62UbiquitinationRSWSPKDKYNYIGLS
CCCCCCCCCCEEEEC		41.33-
63PhosphorylationSWSPKDKYNYIGLSQ
CCCCCCCCCEEEECC		24.2722617229
65PhosphorylationSPKDKYNYIGLSQGN
CCCCCCCEEEECCCC		8.0229759185
69PhosphorylationKYNYIGLSQGNLRVH
CCCEEEECCCCEEEE		30.7229759185
85UbiquitinationKGHGKNHKDAASVRA
CCCCCCCCCCHHHCC		59.46-
236UbiquitinationYMREWRAKVQGTVHC
HHHHHHHHHCCEEEE		26.90-
237UbiquitinationMREWRAKVQGTVHCF
HHHHHHHHCCEEEEE		6.5621906983
293UbiquitinationQEEQASIKNRQKIQK
HHHHHHHHCHHHHHH		43.5121906983
293AcetylationQEEQASIKNRQKIQK
HHHHHHHHCHHHHHH		43.5123236377
300AcetylationKNRQKIQKLVLEGRV
HCHHHHHHHHHCCCH		44.0025953088
300UbiquitinationKNRQKIQKLVLEGRV
HCHHHHHHHHHCCCH		44.00-
301UbiquitinationNRQKIQKLVLEGRVG
CHHHHHHHHHCCCHH		2.8121906983
333UbiquitinationPNLLFMLKCRQFVEM
CCEEEEEEHHHHHHH		18.64-
344PhosphorylationFVEMVNGTDSEVRSL
HHHHHCCCHHHHHHH		31.0228985074
346PhosphorylationEMVNGTDSEVRSLSS
HHHCCCHHHHHHHHC		37.5228985074
350PhosphorylationGTDSEVRSLSSRSPK
CCHHHHHHHHCCCCC		37.4723403867
352PhosphorylationDSEVRSLSSRSPKSQ
HHHHHHHHCCCCCCC		25.5920363803
353PhosphorylationSEVRSLSSRSPKSQD
HHHHHHHCCCCCCCC		41.9128450419
355PhosphorylationVRSLSSRSPKSQDSY
HHHHHCCCCCCCCCC		38.3322115753
357UbiquitinationSLSSRSPKSQDSYPG
HHHCCCCCCCCCCCC		63.092190698
358PhosphorylationLSSRSPKSQDSYPGS
HHCCCCCCCCCCCCC		42.4723927012
361PhosphorylationRSPKSQDSYPGSPSL
CCCCCCCCCCCCCCC		26.1123927012
362PhosphorylationSPKSQDSYPGSPSLS
CCCCCCCCCCCCCCC		21.6523401153
365PhosphorylationSQDSYPGSPSLSPRH
CCCCCCCCCCCCCCC		13.5523927012
367PhosphorylationDSYPGSPSLSPRHGP
CCCCCCCCCCCCCCC		43.0825159151
369PhosphorylationYPGSPSLSPRHGPSS
CCCCCCCCCCCCCCC		24.9923927012
375PhosphorylationLSPRHGPSSSHMHNT
CCCCCCCCCCCCCCC		49.4123927012
376PhosphorylationSPRHGPSSSHMHNTG
CCCCCCCCCCCCCCC		27.6523927012
377PhosphorylationPRHGPSSSHMHNTGA
CCCCCCCCCCCCCCC		29.2129496963
382PhosphorylationSSSHMHNTGADSPSC
CCCCCCCCCCCCCCC		21.0423927012
386PhosphorylationMHNTGADSPSCSNGV
CCCCCCCCCCCCCCC		20.4123927012
388PhosphorylationNTGADSPSCSNGVAS
CCCCCCCCCCCCCCC		33.8423927012
390PhosphorylationGADSPSCSNGVASTK
CCCCCCCCCCCCCCC		40.7423927012
395PhosphorylationSCSNGVASTKSKQNH
CCCCCCCCCCCCCCC		33.6823927012
396PhosphorylationCSNGVASTKSKQNHS
CCCCCCCCCCCCCCC		29.6023927012
409PhosphorylationHSKYPAPSSSSSSSS
CCCCCCCCCCCCCCC		44.9823186163
410PhosphorylationSKYPAPSSSSSSSSS
CCCCCCCCCCCCCCC		32.9323186163
411PhosphorylationKYPAPSSSSSSSSSS
CCCCCCCCCCCCCCC		38.2823186163
412PhosphorylationYPAPSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8723186163
413PhosphorylationPAPSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8723186163
414PhosphorylationAPSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8730576142
415PhosphorylationPSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8723186163
416PhosphorylationSSSSSSSSSSSSSSP
CCCCCCCCCCCCCCC		35.8723186163
417PhosphorylationSSSSSSSSSSSSSPS
CCCCCCCCCCCCCCC		35.8723186163
418PhosphorylationSSSSSSSSSSSSPSS
CCCCCCCCCCCCCCC		35.8723186163
419PhosphorylationSSSSSSSSSSSPSSV
CCCCCCCCCCCCCCC		35.8723186163
420PhosphorylationSSSSSSSSSSPSSVN
CCCCCCCCCCCCCCC		36.4623186163
421PhosphorylationSSSSSSSSSPSSVNY
CCCCCCCCCCCCCCC		48.4923186163
422PhosphorylationSSSSSSSSPSSVNYS
CCCCCCCCCCCCCCC		30.6523186163
424PhosphorylationSSSSSSPSSVNYSES
CCCCCCCCCCCCCCC		49.1925262027
425PhosphorylationSSSSSPSSVNYSESN
CCCCCCCCCCCCCCC		20.1225262027
428PhosphorylationSSPSSVNYSESNSTD
CCCCCCCCCCCCCCC		16.2025262027
429PhosphorylationSPSSVNYSESNSTDS
CCCCCCCCCCCCCCC		29.3724275569
431PhosphorylationSSVNYSESNSTDSTK
CCCCCCCCCCCCCCC		30.09-
434PhosphorylationNYSESNSTDSTKSQH
CCCCCCCCCCCCCCC		37.91-
437PhosphorylationESNSTDSTKSQHHSS
CCCCCCCCCCCCCCC		37.21-
439PhosphorylationNSTDSTKSQHHSSTS
CCCCCCCCCCCCCCC		34.5323927012
443PhosphorylationSTKSQHHSSTSNQET
CCCCCCCCCCCCCCC		32.9423927012
444PhosphorylationTKSQHHSSTSNQETS
CCCCCCCCCCCCCCC		31.3423927012
445PhosphorylationKSQHHSSTSNQETSD
CCCCCCCCCCCCCCH		34.4123927012
446PhosphorylationSQHHSSTSNQETSDS
CCCCCCCCCCCCCHH		38.1623927012
450PhosphorylationSSTSNQETSDSEMEM
CCCCCCCCCHHHHHH		28.2423927012
451PhosphorylationSTSNQETSDSEMEME
CCCCCCCCHHHHHHH		38.0830576142
453PhosphorylationSNQETSDSEMEMEAE
CCCCCCHHHHHHHHH		38.3130576142
462PhosphorylationMEMEAEHYPNGVLGS
HHHHHHHCCCCHHHC		7.0130576142
469PhosphorylationYPNGVLGSMSTRIVN
CCCCHHHCCHHEECC		12.8530576142
471PhosphorylationNGVLGSMSTRIVNGA
CCHHHCCHHEECCCC		19.0727080861
472PhosphorylationGVLGSMSTRIVNGAY
CHHHCCHHEECCCCC		18.7727080861
480UbiquitinationRIVNGAYKHEDLQTD
EECCCCCCCCCCCCC		39.73-
480AcetylationRIVNGAYKHEDLQTD
EECCCCCCCCCCCCC		39.7326051181
486PhosphorylationYKHEDLQTDESSMDD
CCCCCCCCCCCCCCC		49.3723927012
489PhosphorylationEDLQTDESSMDDRHP
CCCCCCCCCCCCCCH		33.5023927012
490PhosphorylationDLQTDESSMDDRHPR
CCCCCCCCCCCCCHH		24.9623927012
494MethylationDESSMDDRHPRRQLC
CCCCCCCCCHHHHHC		37.13115490235
522PhosphorylationGRELQALSEQLGREY
HHHHHHHHHHHHHHH		26.7223898821
529PhosphorylationSEQLGREYGKNLAHT
HHHHHHHHHHCHHHH		31.8523898821
536PhosphorylationYGKNLAHTEMLQDAF
HHHCHHHHHHHHHHH		19.9226552605
544PhosphorylationEMLQDAFSLLAYSDP
HHHHHHHHHHHHCCC		24.9726552605
548PhosphorylationDAFSLLAYSDPWSCP
HHHHHHHHCCCCCCC		17.3626552605
549PhosphorylationAFSLLAYSDPWSCPV
HHHHHHHCCCCCCCC		31.4326552605
553PhosphorylationLAYSDPWSCPVGQQL
HHHCCCCCCCCCCCC		17.5826552605
596PhosphorylationMLALGQASECLRLMA
CHHHHCHHHHHHHHH		22.43-
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 RBP10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBP10_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 RBP10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAN_HUMANRANphysical
14684163
MET_HUMANMETphysical
14684163
WDR26_HUMANWDR26physical
22939629
WDR26_HUMANWDR26physical
26344197
ARMC8_HUMANARMC8physical
27173435
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 RBP10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-362; SER-365 AND SER-369, AND MASSSPECTROMETRY.
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-365 AND SER-369, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-362; SER-365 AND SER-369, AND MASSSPECTROMETRY.
"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-361; SER-365 ANDSER-369, AND MASS SPECTROMETRY.

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