RANB3_HUMAN - dbPTM
RANB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RANB3_HUMAN
UniProt AC Q9H6Z4
Protein Name Ran-binding protein 3
Gene Name RANBP3
Organism Homo sapiens (Human).
Sequence Length 567
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export..
Protein Sequence MADLANEEKPAIAPPVFVFQKDKGQKSPAEQKNLSDSGEEPRGEAEAPHHGTGHPESAGEHALEPPAPAGASASTPPPPAPEAQLPPFPRELAGRSAGGSSPEGGEDSDREDGNYCPPVKRERTSSLTQFPPSQSEERSSGFRLKPPTLIHGQAPSAGLPSQKPKEQQRSVLRPAVLQAPQPKALSQTVPSSGTNGVSLPADCTGAVPAASPDTAAWRSPSEAADEVCALEEKEPQKNESSNASEEEACEKKDPATQQAFVFGQNLRDRVKLINESVDEADMENAGHPSADTPTATNYFLQYISSSLENSTNSADASSNKFVFGQNMSERVLSPPKLNEVSSDANRENAAAESGSESSSQEATPEKESLAESAAAYTKATARKCLLEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDTEDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSDDDDVLAPSGATAAGAGDEGDGQTTGST
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------MADLANEEK
------CCCCCCCCC		22.1122223895
9AcetylationADLANEEKPAIAPPV
CCCCCCCCCCCCCCE		33.3025953088
21AcetylationPPVFVFQKDKGQKSP
CCEEEEECCCCCCCH		50.3619608861
21UbiquitinationPPVFVFQKDKGQKSP
CCEEEEECCCCCCCH		50.36-
23UbiquitinationVFVFQKDKGQKSPAE
EEEEECCCCCCCHHH		70.99-
27PhosphorylationQKDKGQKSPAEQKNL
ECCCCCCCHHHHCCC		22.8126657352
28 (in isoform 3)Phosphorylation-47.0220166139
32 (in isoform 3)Phosphorylation-51.8925849741
33 (in isoform 3)Phosphorylation-44.4625849741
35PhosphorylationPAEQKNLSDSGEEPR
HHHHCCCCCCCCCCC		38.8421815630
37PhosphorylationEQKNLSDSGEEPRGE
HHCCCCCCCCCCCCC		44.7421815630
40 (in isoform 3)Phosphorylation-43.7725849741
57PhosphorylationHGTGHPESAGEHALE
CCCCCCHHCCCCCCC		46.1319664995
72PhosphorylationPPAPAGASASTPPPP
CCCCCCCCCCCCCCC		23.1026074081
74PhosphorylationAPAGASASTPPPPAP
CCCCCCCCCCCCCCC		38.6626074081
75PhosphorylationPAGASASTPPPPAPE
CCCCCCCCCCCCCCH		39.2626074081
96PhosphorylationPRELAGRSAGGSSPE
CHHHCCCCCCCCCCC		30.2826846344
100PhosphorylationAGRSAGGSSPEGGED
CCCCCCCCCCCCCCC		41.6326846344
101PhosphorylationGRSAGGSSPEGGEDS
CCCCCCCCCCCCCCC		30.1926846344
108PhosphorylationSPEGGEDSDREDGNY
CCCCCCCCCCCCCCC		33.9822167270
115PhosphorylationSDREDGNYCPPVKRE
CCCCCCCCCCCCCCC		16.3223927012
124PhosphorylationPPVKRERTSSLTQFP
CCCCCCCCCCCCCCC		20.2222322096
125PhosphorylationPVKRERTSSLTQFPP
CCCCCCCCCCCCCCC		29.5722322096
126PhosphorylationVKRERTSSLTQFPPS
CCCCCCCCCCCCCCC		34.5222322096
128PhosphorylationRERTSSLTQFPPSQS
CCCCCCCCCCCCCCC		30.0622322096
133PhosphorylationSLTQFPPSQSEERSS
CCCCCCCCCCCCCCC		46.7217525332
135PhosphorylationTQFPPSQSEERSSGF
CCCCCCCCCCCCCCC		45.8423403867
139PhosphorylationPSQSEERSSGFRLKP
CCCCCCCCCCCCCCC		37.7921406692
140PhosphorylationSQSEERSSGFRLKPP
CCCCCCCCCCCCCCC		48.4421406692
145UbiquitinationRSSGFRLKPPTLIHG
CCCCCCCCCCEEECC		44.70-
163AcetylationSAGLPSQKPKEQQRS
CCCCCCCCCHHHHHH		63.4925953088
170PhosphorylationKPKEQQRSVLRPAVL
CCHHHHHHCHHHHHH		22.5922210691
186PhosphorylationAPQPKALSQTVPSSG
CCCCCCCCCCCCCCC		28.7626074081
188PhosphorylationQPKALSQTVPSSGTN
CCCCCCCCCCCCCCC		30.8926074081
191PhosphorylationALSQTVPSSGTNGVS
CCCCCCCCCCCCCCC		36.7430266825
192PhosphorylationLSQTVPSSGTNGVSL
CCCCCCCCCCCCCCC		43.5030266825
194PhosphorylationQTVPSSGTNGVSLPA
CCCCCCCCCCCCCCC		30.6530266825
198PhosphorylationSSGTNGVSLPADCTG
CCCCCCCCCCCCCCC		29.9930266825
204PhosphorylationVSLPADCTGAVPAAS
CCCCCCCCCCCCCCC		28.8230266825
211PhosphorylationTGAVPAASPDTAAWR
CCCCCCCCCCCCCCC		25.9730266825
211 (in isoform 2)Phosphorylation-25.9727251275
214PhosphorylationVPAASPDTAAWRSPS
CCCCCCCCCCCCCHH		22.9730266825
214 (in isoform 2)Phosphorylation-22.9727251275
219PhosphorylationPDTAAWRSPSEAADE
CCCCCCCCHHHHHHH		23.2919664994
219 (in isoform 2)Phosphorylation-23.2925849741
221PhosphorylationTAAWRSPSEAADEVC
CCCCCCHHHHHHHHH		40.9129255136
221 (in isoform 2)Phosphorylation-40.9123663014
233UbiquitinationEVCALEEKEPQKNES
HHHHHCCCCCCCCCC		66.38-
233AcetylationEVCALEEKEPQKNES
HHHHHCCCCCCCCCC		66.3827452117
235 (in isoform 2)Phosphorylation-62.6123663014
236 (in isoform 2)Phosphorylation-63.4023663014
239 (in isoform 2)Phosphorylation-63.6823663014
240PhosphorylationKEPQKNESSNASEEE
CCCCCCCCCCCCHHH		37.9823401153
241PhosphorylationEPQKNESSNASEEEA
CCCCCCCCCCCHHHH		30.1825159151
244PhosphorylationKNESSNASEEEACEK
CCCCCCCCHHHHHHH		50.2029255136
256PhosphorylationCEKKDPATQQAFVFG
HHHCCHHHHHHHHHC		26.9723312004
276PhosphorylationRVKLINESVDEADME
HHHHHHCCCCHHHHH		30.3127251275
289PhosphorylationMENAGHPSADTPTAT
HHHCCCCCCCCCHHH		32.8518669648
292PhosphorylationAGHPSADTPTATNYF
CCCCCCCCCHHHHHH		23.4326074081
294PhosphorylationHPSADTPTATNYFLQ
CCCCCCCHHHHHHHH		48.4826074081
296PhosphorylationSADTPTATNYFLQYI
CCCCCHHHHHHHHHH		32.6926074081
298PhosphorylationDTPTATNYFLQYISS
CCCHHHHHHHHHHHH		11.0022817900
304PhosphorylationNYFLQYISSSLENST
HHHHHHHHHHHCCCC		14.6726074081
305PhosphorylationYFLQYISSSLENSTN
HHHHHHHHHHCCCCC		29.4126074081
306PhosphorylationFLQYISSSLENSTNS
HHHHHHHHHCCCCCC		32.6726074081
310PhosphorylationISSSLENSTNSADAS
HHHHHCCCCCCCCCC		21.4226657352
311PhosphorylationSSSLENSTNSADASS
HHHHCCCCCCCCCCC		44.7826074081
313PhosphorylationSLENSTNSADASSNK
HHCCCCCCCCCCCCC		27.8426074081
317PhosphorylationSTNSADASSNKFVFG
CCCCCCCCCCCCCCC		34.6826074081
318PhosphorylationTNSADASSNKFVFGQ
CCCCCCCCCCCCCCC		45.8426074081
327SulfoxidationKFVFGQNMSERVLSP
CCCCCCCHHHCCCCC		3.1921406390
328PhosphorylationFVFGQNMSERVLSPP
CCCCCCHHHCCCCCC		29.7820166139
333PhosphorylationNMSERVLSPPKLNEV
CHHHCCCCCCCHHHC		35.9829255136
341PhosphorylationPPKLNEVSSDANREN
CCCHHHCCCHHHHHH		19.1329255136
342PhosphorylationPKLNEVSSDANRENA
CCHHHCCCHHHHHHH		46.0129255136
345 (in isoform 3)Ubiquitination-57.7121890473
353PhosphorylationRENAAAESGSESSSQ
HHHHHHHHCCCCCCC		42.7829255136
355PhosphorylationNAAAESGSESSSQEA
HHHHHHCCCCCCCCC		43.5129255136
357PhosphorylationAAESGSESSSQEATP
HHHHCCCCCCCCCCH		36.6722167270
358PhosphorylationAESGSESSSQEATPE
HHHCCCCCCCCCCHH		31.8023401153
359PhosphorylationESGSESSSQEATPEK
HHCCCCCCCCCCHHH		41.1217525332
363PhosphorylationESSSQEATPEKESLA
CCCCCCCCHHHHHHH		31.0922167270
368PhosphorylationEATPEKESLAESAAA
CCCHHHHHHHHHHHH		43.9023403867
372PhosphorylationEKESLAESAAAYTKA
HHHHHHHHHHHHHHH		20.0130576142
376PhosphorylationLAESAAAYTKATARK
HHHHHHHHHHHHHHH		12.2125159151
377PhosphorylationAESAAAYTKATARKC
HHHHHHHHHHHHHHH		14.9623186163
378UbiquitinationESAAAYTKATARKCL
HHHHHHHHHHHHHHH		30.94-
408 (in isoform 2)Ubiquitination-6.1021890473
413UbiquitinationCKLFVFDKTSQSWVE
EEEEEEECCCHHHHH		38.3121890473
413 (in isoform 1)Ubiquitination-38.3121890473
431SulfoxidationGLLRLNDMASTDDGT
CEEEHHHCCCCCCCC		2.8621406390
433PhosphorylationLRLNDMASTDDGTLQ
EEHHHCCCCCCCCHH		26.2326270265
434PhosphorylationRLNDMASTDDGTLQS
EHHHCCCCCCCCHHH		28.6826270265
438PhosphorylationMASTDDGTLQSRLVM
CCCCCCCCHHHHEEE		28.7226270265
441PhosphorylationTDDGTLQSRLVMRTQ
CCCCCHHHHEEEECC		30.6026270265
457PhosphorylationSLRLILNTKLWAQMQ
CEEHHHCHHHHHHHC		24.86-
478SulfoxidationKSIRITAMDTEDQGV
CCEEEEEEECCCCCE		4.9821406390
493PhosphorylationKVFLISASSKDTGQL
EEEEEECCCCCHHHH		31.00-
501PhosphorylationSKDTGQLYAALHHRI
CCCHHHHHHHHHHHH		5.0728064214
533PhosphorylationPEPGAAPSNEEDDSD
CCCCCCCCCCCCCCC		52.7430278072
539PhosphorylationPSNEEDDSDDDDVLA
CCCCCCCCCCCCCCC		56.0928355574
548PhosphorylationDDDVLAPSGATAAGA
CCCCCCCCCCCCCCC		35.1425137130
551PhosphorylationVLAPSGATAAGAGDE
CCCCCCCCCCCCCCC		22.1425137130
563PhosphorylationGDEGDGQTTGST---
CCCCCCCCCCCC---		38.3620068231
564PhosphorylationDEGDGQTTGST----
CCCCCCCCCCC----		22.6520068231
566PhosphorylationGDGQTTGST------
CCCCCCCCC------		28.9320068231
567PhosphorylationDGQTTGST-------
CCCCCCCC-------		43.9320068231
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
126SPhosphorylationKinaseAKT1P31749
PSP
126SPhosphorylationKinaseRPS6KA1Q15418
GPS
126SPhosphorylationKinaseRPS6KA3P51812
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RANB3_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 RANB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO1_HUMANXPO1physical
11425870
KHK_HUMANKHKphysical
17353931
XPO1_HUMANXPO1physical
12176322
RCC1_HUMANRCC1physical
11932251
RAN_HUMANRANphysical
9637251
RCC1_HUMANRCC1physical
9637251
RGPD1_HUMANRGPD1physical
22939629
AURKA_HUMANAURKAphysical
22939629
HS74L_HUMANHSPA4Lphysical
22863883
NP1L1_HUMANNAP1L1physical
22863883
PUR1_HUMANPPATphysical
22863883
RO60_HUMANTROVE2physical
22863883
GO45_HUMANBLZF1physical
25416956
ZMIZ2_HUMANZMIZ2physical
25416956
MORN4_HUMANMORN4physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
PPARG_HUMANPPARGphysical
20026644
XPO1_HUMANXPO1physical
20026644
RAN_HUMANRANphysical
26344197
RCC1_HUMANRCC1physical
26344197
SMRD1_HUMANSMARCD1physical
26344197
SMRD3_HUMANSMARCD3physical
26344197
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 RANB3_HUMAN

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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 SER-100; SER-101; SER-108; SER-125; SER-126;SER-211; THR-214; SER-533 AND SER-539, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
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-333, AND MASSSPECTROMETRY.
"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 SER-100; SER-101; SER-108; SER-125; SER-126;SER-211; THR-214; SER-533 AND SER-539, 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-100; SER-101; SER-108;THR-124; SER-126; SER-333; SER-353; SER-355; SER-357; SER-359 ANDSER-539, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASSSPECTROMETRY.
"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-126; SER-133 ANDSER-359, 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-96; SER-100; SER-101 ANDSER-108, AND MASS SPECTROMETRY.

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