RBP10_MOUSE - dbPTM
RBP10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBP10_MOUSE
UniProt AC Q6VN19
Protein Name Ran-binding protein 10
Gene Name Ranbp10
Organism Mus musculus (Mouse).
Sequence Length 620
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic. Associates with cytoplasmic microtubules in mature megakaryocytes and platelets.
Protein Description May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function..
Protein Sequence MAAATADPGAGNPQAGDSSGGDSGGGLPSPGEQELSRRLQRLYPAVNQHETPLPRSWSPKDKYNYIGLSQGNLRVHYKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPANLYPTVGLQTPGEIVDANFGQQPFLFDIEDYMREWRAKVQGTVHGFPISARLGEWQAVLQNMVSSYLVHHGYCSTATAFARMTETPIQEEQASIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSEVRSLSSRSPKSQDSYPGSPSLSPRHGPSSSHIHNTGADSPSCSNGVASTKNKQNHSKYPAPSSSSSSSSSSSSSSPSSVNYSESNSTDSTKSQPHSSTSNQETSDSEMEMEAEHYPNGVLESVSTRIVNGAYKHDDLQTDESSMDDGHPRRQLCGGNQAATERIILFGRELQALSEQLGREYGKNLAHTEMLQDAFSLLAYSDPWSCPVGHQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECLRLMARAGLGSCSFARVDDYLH
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		13.05-
5Phosphorylation---MAAATADPGAGN
---CCCCCCCCCCCC		27.2030635358
18PhosphorylationGNPQAGDSSGGDSGG
CCCCCCCCCCCCCCC		29.9330635358
19PhosphorylationNPQAGDSSGGDSGGG
CCCCCCCCCCCCCCC		52.0830635358
23PhosphorylationGDSSGGDSGGGLPSP
CCCCCCCCCCCCCCC		42.4830635358
29PhosphorylationDSGGGLPSPGEQELS
CCCCCCCCCCHHHHH		51.0530352176
36PhosphorylationSPGEQELSRRLQRLY
CCCHHHHHHHHHHHH		18.0130635358
62UbiquitinationRSWSPKDKYNYIGLS
CCCCCCCCCCEEEEC		41.33-
69PhosphorylationKYNYIGLSQGNLRVH
CCCEEEECCCCEEEE		30.72-
291PhosphorylationPIQEEQASIKNRQKI
CCHHHHHHHHCHHHH		33.52-
293UbiquitinationQEEQASIKNRQKIQK
HHHHHHHHCHHHHHH		43.51-
293AcetylationQEEQASIKNRQKIQK
HHHHHHHHCHHHHHH		43.5123236377
350PhosphorylationGTDSEVRSLSSRSPK
CCHHHHHHHHCCCCC		37.4727717184
352PhosphorylationDSEVRSLSSRSPKSQ
HHHHHHHHCCCCCCC		25.5922817900
353PhosphorylationSEVRSLSSRSPKSQD
HHHHHHHCCCCCCCC		41.9122817900
355PhosphorylationVRSLSSRSPKSQDSY
HHHHHCCCCCCCCCC		38.3325266776
357UbiquitinationSLSSRSPKSQDSYPG
HHHCCCCCCCCCCCC		63.09-
358PhosphorylationLSSRSPKSQDSYPGS
HHCCCCCCCCCCCCC		42.4727087446
361PhosphorylationRSPKSQDSYPGSPSL
CCCCCCCCCCCCCCC		26.1125521595
362PhosphorylationSPKSQDSYPGSPSLS
CCCCCCCCCCCCCCC		21.6527742792
365PhosphorylationSQDSYPGSPSLSPRH
CCCCCCCCCCCCCCC		13.5527087446
367PhosphorylationDSYPGSPSLSPRHGP
CCCCCCCCCCCCCCC		43.0827742792
369PhosphorylationYPGSPSLSPRHGPSS
CCCCCCCCCCCCCCC		24.9927087446
375PhosphorylationLSPRHGPSSSHIHNT
CCCCCCCCCCCCCCC		49.4125777480
376PhosphorylationSPRHGPSSSHIHNTG
CCCCCCCCCCCCCCC		29.1225777480
377PhosphorylationPRHGPSSSHIHNTGA
CCCCCCCCCCCCCCC		30.6925777480
382PhosphorylationSSSHIHNTGADSPSC
CCCCCCCCCCCCCCC		21.4225777480
386PhosphorylationIHNTGADSPSCSNGV
CCCCCCCCCCCCCCC		20.4127087446
388PhosphorylationNTGADSPSCSNGVAS
CCCCCCCCCCCCCCC		33.8426643407
390PhosphorylationGADSPSCSNGVASTK
CCCCCCCCCCCCCCC		40.7423684622
393PhosphorylationSPSCSNGVASTKNKQ
CCCCCCCCCCCCCCC		4.4415345747
395PhosphorylationSCSNGVASTKNKQNH
CCCCCCCCCCCCCCC		37.1925777480
396PhosphorylationCSNGVASTKNKQNHS
CCCCCCCCCCCCCCC		28.9723684622
397PhosphorylationSNGVASTKNKQNHSK
CCCCCCCCCCCCCCC		60.7015345747
405PhosphorylationNKQNHSKYPAPSSSS
CCCCCCCCCCCCCCC		13.9829472430
409PhosphorylationHSKYPAPSSSSSSSS
CCCCCCCCCCCCCCC		44.9829472430
410PhosphorylationSKYPAPSSSSSSSSS
CCCCCCCCCCCCCCC		32.9329472430
411PhosphorylationKYPAPSSSSSSSSSS
CCCCCCCCCCCCCCC		38.2829472430
412PhosphorylationYPAPSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8729472430
413PhosphorylationPAPSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8729472430
414PhosphorylationAPSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8729472430
415PhosphorylationPSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8729472430
416PhosphorylationSSSSSSSSSSSSSSP
CCCCCCCCCCCCCCC		35.8729472430
417PhosphorylationSSSSSSSSSSSSSPS
CCCCCCCCCCCCCCC		35.8729472430
418PhosphorylationSSSSSSSSSSSSPSS
CCCCCCCCCCCCCCC		35.8729472430
419PhosphorylationSSSSSSSSSSSPSSV
CCCCCCCCCCCCCCC		35.8729472430
420PhosphorylationSSSSSSSSSSPSSVN
CCCCCCCCCCCCCCC		36.4629472430
421PhosphorylationSSSSSSSSSPSSVNY
CCCCCCCCCCCCCCC		48.4929472430
422PhosphorylationSSSSSSSSPSSVNYS
CCCCCCCCCCCCCCC		30.6529472430
424PhosphorylationSSSSSSPSSVNYSES
CCCCCCCCCCCCCCC		49.1929472430
425PhosphorylationSSSSSPSSVNYSESN
CCCCCCCCCCCCCCC		20.1229472430
439PhosphorylationNSTDSTKSQPHSSTS
CCCCCCCCCCCCCCC		49.3726160508
443PhosphorylationSTKSQPHSSTSNQET
CCCCCCCCCCCCCCC		41.8326160508
444PhosphorylationTKSQPHSSTSNQETS
CCCCCCCCCCCCCCC		32.5926160508
445PhosphorylationKSQPHSSTSNQETSD
CCCCCCCCCCCCCCH		34.4126160508
446PhosphorylationSQPHSSTSNQETSDS
CCCCCCCCCCCCCHH		38.1626160508
450PhosphorylationSSTSNQETSDSEMEM
CCCCCCCCCHHHHHH		28.2422802335
451PhosphorylationSTSNQETSDSEMEME
CCCCCCCCHHHHHHH		38.0821082442
453PhosphorylationSNQETSDSEMEMEAE
CCCCCCHHHHHHHHH		38.3122942356
462PhosphorylationMEMEAEHYPNGVLES
HHHHHHHCCCCHHHC		7.0126160508
469PhosphorylationYPNGVLESVSTRIVN
CCCCHHHCCHHEHHC		19.7322802335
471PhosphorylationNGVLESVSTRIVNGA
CCHHHCCHHEHHCCC		22.6522802335
472PhosphorylationGVLESVSTRIVNGAY
CHHHCCHHEHHCCCC		23.4322802335
479PhosphorylationTRIVNGAYKHDDLQT
HEHHCCCCCCCCCCC		15.3921183079
486PhosphorylationYKHDDLQTDESSMDD
CCCCCCCCCHHHCCC		49.3727087446
489PhosphorylationDDLQTDESSMDDGHP
CCCCCCHHHCCCCCC		33.5027087446
490PhosphorylationDLQTDESSMDDGHPR
CCCCCHHHCCCCCCH		24.9627087446
501S-palmitoylationGHPRRQLCGGNQAAT
CCCHHHHCCCCHHHH		5.0626165157
611PhosphorylationRAGLGSCSFARVDDY
HCCCCCCCEECCCCC		24.5228576409
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBP10_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 RBP10_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAN_MOUSERanphysical
18347012
TBB1_MOUSETubb1physical
18347012
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBP10_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-369, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, ANDMASS SPECTROMETRY.

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