Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RANBP3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RANBP3 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. Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling. Widely expressed with high levels in testis and heart. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Chromosomal Location of Human Ortholog: 19p13.3
Cellular Component: cytoplasm; nucleolus; nucleus
Molecular Function: protein binding; Ran GTPase binding
Biological Process: protein transport; intracellular transport
Reference #:  Q9H6Z4 (UniProtKB)
Alt. Names/Synonyms: DKFZp586I1520; RAN binding protein 3; Ran-binding protein 3; RAN-binding protein-3; RANB3; RANBP3
Gene Symbols: RANBP3
Molecular weight: 60,210 Da
Basal Isoelectric point: 4.7  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs
Select Structure to View Below

RANBP3

Protein Structure Not Found.


STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  InnateDB


Sites Implicated In
activity, inhibited: S126‑p
intracellular localization: S126‑p
molecular association, regulation: S126‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 K21-ac PPVFVFQkDKGQKsP
0 2 S27-p QkDKGQKsPAEQKNL
0 1 S72-p PPAPAGAsAstPPPP
0 1 S74-p APAGAsAstPPPPAP
0 1 T75-p PAGAsAstPPPPAPE
0 15 S96-p PRELAGRsAGGssPE
0 8 G99 LAGRsAGGssPEGGE
0 52 S100-p AGRsAGGssPEGGED
0 81 S101-p GRsAGGssPEGGEDs
0 109 S108-p sPEGGEDsDREDGNy
0 28 Y115-p sDREDGNyCPPVKRE
0 41 T124-p PPVKRERtssLtQFP
0 40 S125-p PVKRERtssLtQFPP
3 151 S126-p VKRERtssLtQFPPs
0 24 T128-p RERtssLtQFPPsQS
0 4 S133-p sLtQFPPsQSEERSS
0 1 K163-ac SAGLPSQkPKEQQRS
0 1 S186-p APQPKALsQtVPSSG
0 1 T188-p QPKALsQtVPSSGTN
0 1 S192 LsQtVPSSGTNGVsL
0 2 T194 QtVPSSGTNGVsLPA
0 2 S198-p SSGTNGVsLPADCTG
0 1 A209 DCTGAVPAAsPDtAA
0 7 S211-p TGAVPAAsPDtAAWR
0 1 T214-p VPAAsPDtAAWRsPs
0 14 S219-p PDtAAWRsPsEAADE
0 10 S221-p tAAWRsPsEAADEVC
0 1 A223 AWRsPsEAADEVCAL
0 1 S240-p KEPQKNEssNAsEEE
0 1 S241-p EPQKNEssNAsEEEA
0 2 S244-p KNEssNAsEEEACEK
0 1 S276-p RVKLINEsVDEADME
0 4 T292-p AGHPSADtPTATNyF
0 1 Y298-p DtPTATNyFLQYISS
0 1 S328-p FVFGQNMsERVLsPP
0 34 S333-p NMsERVLsPPKLNEV
0 2 S342 PKLNEVSSDANRENA
0 9 S353-p RENAAAEsGsEsssQ
0 5 S355-p NAAAEsGsEsssQEA
0 2 S357-p AAEsGsEsssQEAtP
0 1 S358-p AEsGsEsssQEAtPE
0 4 S359-p EsGsEsssQEAtPEK
0 3 T363-p EsssQEAtPEKESLA
0 1 K366 sQEAtPEKESLAEsA
0 2 S372-p EKESLAEsAAAYTKA
0 1 K413-ub CKLFVFDkTSQSWVE
0 1 T457-p SLRLILNtKLWAQMQ
0 1 S493-p KVFLISAsSKDTGQL
0 2 Y501-p SKDTGQLyAALHHRI
0 3 S533-p PEPGAAPsNEEDDsD
0 3 N534 EPGAAPsNEEDDsDD
0 9 S539-p PsNEEDDsDDDDVLA
0 1 A555 SGATAAGAGDEGDGQ
0 1 T567 DGQTTGST_______
9380 : Phospho-RanBP3 (Ser58) Antibody
  RANBP3 iso2  
K21 PPVFVFQKDKGQKSP
S27 QKDKGQKSPAEQKNL
S72 PPAPAGASASTPPPP
S74 APAGASASTPPPPAP
T75 PAGASASTPPPPAPE
S96 PRELAGRSAGGSSPE
G99 LAGRSAGGSSPEGGE
S100 AGRSAGGSSPEGGED
S101 GRSAGGSSPEGGEDS
S108 SPEGGEDSDREDGNY
Y115 SDREDGNYCPPVKRE
T124 PPVKRERTSSLTQFP
S125 PVKRERTSSLTQFPP
S126 VKRERTSSLTQFPPS
T128 RERTSSLTQFPPSQS
S133 SLTQFPPSQSEERSS
K163 SAGLPSQKPKEQQRS
S186 APQPKALSQTVPSSG
T188 QPKALSQTVPSSGTN
S192 LSQTVPSSGTNGVSL
T194 QTVPSSGTNGVSLPA
S198 SSGTNGVSLPADCTG
A209 DCTGAVPAASPDTAA
S211 TGAVPAASPDTAAWR
T214 VPAASPDTAAWRsPs
S219-p PDTAAWRsPsEAADE
S221-p TAAWRsPsEAADEEK
A223 AWRsPsEAADEEKEP
S235-p KEPQKNEssNAsEEE
S236-p EPQKNEssNAsEEEA
S239-p KNEssNAsEEEACEK
S271 RVKLINESVDEADME
T287 AGHPSADTPTATNYF
Y293 DTPTATNYFLQYISS
S323 FVFGQNMSERVLSPP
S328 NMSERVLSPPKLNEV
S337 PKLNEVSSDANRENA
S348 RENAAAESGSESSSQ
S350 NAAAESGSESSSQEA
S352 AAESGSESSSQEATP
S353 AESGSESSSQEATPE
S354 ESGSESSSQEATPEK
T358 ESSSQEATPEKESLA
K361 SQEATPEKESLAESA
S367 EKESLAESAAAYTKA
K408 CKLFVFDKTSQSWVE
T452 SLRLILNTKLWAQMQ
S488 KVFLISASSKDTGQL
Y496 SKDTGQLYAALHHRI
S528 PEPGAAPSNEEDDSD
N529 EPGAAPSNEEDDSDD
S534 PSNEEDDSDDDDVLA
A550 SGATAAGAGDEGDGQ
T562 DGQTTGST_______
  RANBP3 iso3  
K21 PPVFVFQKDKGQKRS
- gap
- gap
- gap
- gap
S28 KDKGQKRSAGGSsPE
G31 GQKRSAGGSsPEGGE
S32 QKRSAGGSsPEGGED
S33-p KRSAGGSsPEGGEDs
S40-p sPEGGEDsDREDGNY
Y47 sDREDGNYCPPVKRE
T56 PPVKRERTSsLTQFP
S57 PVKRERTSsLTQFPP
S58-p VKRERTSsLTQFPPS
T60 RERTSsLTQFPPSQS
S65 sLTQFPPSQSEERSS
K95 SAGLPSQKPKEQQRS
S118 APQPKALSQTVPSSG
T120 QPKALSQTVPSSGTN
S124 LSQTVPSSGTNGVSL
T126 QTVPSSGTNGVSLPA
S130 SSGTNGVSLPADCTG
A141 DCTGAVPAASPDTAA
S143 TGAVPAASPDTAAWR
T146 VPAASPDTAAWRSPS
S151 PDTAAWRSPSEAADE
S153 TAAWRSPSEAADEVC
A155 AWRSPSEAADEVCAL
S172 KEPQKNESSNASEEE
S173 EPQKNESSNASEEEA
S176 KNESSNASEEEACEK
S208 RVKLINESVDEADME
T224 AGHPSADTPTATNYF
Y230 DTPTATNYFLQYISS
S260 FVFGQNMSERVLSPP
S265 NMSERVLSPPKLNEV
S274 PKLNEVSSDANRENA
S285 RENAAAESGSESSSQ
S287 NAAAESGSESSSQEA
S289 AAESGSESSSQEATP
S290 AESGSESSSQEATPE
S291 ESGSESSSQEATPEK
T295 ESSSQEATPEKESLA
K298 SQEATPEKESLAESA
S304 EKESLAESAAAYTKA
K345 CKLFVFDKTSQSWVE
T389 SLRLILNTKLWAQMQ
S425 KVFLISASSKDTGQL
Y433 SKDTGQLYAALHHRI
S465 PEPGAAPSNEEDDSD
N466 EPGAAPSNEEDDSDD
S471 PSNEEDDSDDDDVLA
A487 SGATAAGAGDEGDGQ
T499 DGQTTGST_______
9380 : Phospho-RanBP3 (Ser58) Antibody
  mouse

 
K21 PSVFVFQKDKGQKRs
- gap
- gap
- gap
- gap
S28-p KDKGQKRsAGsssPE
S31-p GQKRsAGsssPEAGE
S32-p QKRsAGsssPEAGED
S33-p KRsAGsssPEAGEDs
S40-p sPEAGEDsDHEDGNy
Y47-p sDHEDGNyCPPVKRE
T56-p PPVKRERtssLtHSE
S57-p PVKRERtssLtHSEE
S58-p VKRERtssLtHSEEK
T60-p RERtssLtHSEEKSS
- gap
K90 SAGLPSQKPREQQRG
S113 APQPKVLSQTVPSsG
T115 QPKVLSQTVPSsGtN
S119-p LSQTVPSsGtNGVsM
T121-p QTVPSsGtNGVsMPA
S125-p SsGtNGVsMPADCTG
S136-p DCTGPATsVsPENLT
S138-p TGPATsVsPENLTQR
N141 ATsVsPENLTQRsPs
S146-p PENLTQRsPsEsAEE
S148-p NLTQRsPsEsAEETH
S150-p TQRsPsEsAEETHTL
H167 KVPQKTPHGTsEEGH
G168 VPQKTPHGTsEEGHC
S170-p QKTPHGTsEEGHCEE
N201 RVKLMNENASVADVD
T217 AAHPSSETPSATNYF
Y223 ETPSATNYFLQYISS
S252 FVFGQNMSERVLsPP
S257-p NMSERVLsPPKLNEA
S266-p PKLNEANsDTSRETT
S277-p RETTHAQsGSESSsQ
S279 TTHAQsGSESSsQEA
S281 HAQsGSESSsQEAAP
S282 AQsGSESSsQEAAPK
S283-p QsGSESSsQEAAPKk
A287 ESSsQEAAPKkESLA
K290-ub sQEAAPKkESLAESA
S296 KkESLAESAAAYTKA
K337 CKLFVFDKTSQSWVE
T381 SLRLILNTKLWAQMQ
S417 KVFLISASSKDTGQL
Y425 SKDTGQLYAALHHRI
A457 PEPGATRAtEEEDsD
T458-p EPGATRAtEEEDsDE
S463-p RAtEEEDsDEDAVLA
T479-p SGVTGAGtGDEGDGQ
T491-p DGQAPGSt_______
  rat

 
K21 PSVFVFQKDKGQKRs
- gap
- gap
- gap
- gap
S28-p KDKGQKRsAGsssPE
S31-p GQKRsAGsssPEAGE
S32-p QKRsAGsssPEAGED
S33-p KRsAGsssPEAGEDs
S40-p sPEAGEDsDHEDGNY
Y47 sDHEDGNYCPPVKRE
T56-p PPVKRERtSsLTHSE
S57 PVKRERtSsLTHSEE
S58-p VKRERtSsLTHSEEK
T60 RERtSsLTHSEEKSS
- gap
K90-ac SAGLPSQkPREQQRG
S113 APQPKVLSQTVPSSG
T115 QPKVLSQTVPSSGTN
S119 LSQTVPSSGTNGVSM
T121 QTVPSSGTNGVSMPA
S125 SSGTNGVSMPADCTG
S136 DCTGPATSASPENLT
S138 TGPATSASPENLTQR
N141 ATSASPENLTQRsPs
S146-p PENLTQRsPsESAEG
S148-p NLTQRsPsESAEGTH
S150 TQRsPsESAEGTHTF
S167 KVPQKTPSGGSEETH
G168 VPQKTPSGGSEETHC
S170 QKTPSGGSEETHCEE
K201 RVKLMNEKANVADVD
T217 AAHPGSETPTATNYF
Y223 ETPTATNYFLQYISS
S252 FVFGQNMSERVLsPP
S257-p NMSERVLsPPKLNEA
S266 PKLNEANSDTSRETT
S277 RETTHAQSGSESSsQ
S279 TTHAQSGSESSsQEA
S281 HAQSGSESSsQEAVP
S282 AQSGSESSsQEAVPK
S283-p QSGSESSsQEAVPKK
V287 ESSsQEAVPKKESLA
K290 sQEAVPKKESLAESA
S296 KKESLAESAAAYTKA
K337 CKLFVFDKTSQSWVE
T381 SLRLILNTKLWAQMQ
S417 KVFLISASSKDTGQL
Y425 SKDTGQLYAALHHRI
A457 PEPGATRAAEEEDsD
A458 EPGATRAAEEEDsDE
S463-p RAAEEEDsDEDAVLA
A479 SGVTGAGAGDDGDGQ
T491 DGQATGST_______
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.