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Protein Page:
RANBP3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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
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:  MAPK/Erk in Growth and Differentiation
Select Structure to View Below

RANBP3
Protein Structure Not Found.


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Sites Implicated In
inhibition: 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 1 K21-a PPVFVFQkDKGQKsP
0 1 S27-p QkDKGQKsPAEQKNL
0 9 S96-p PRELAGRsAGGssPE
0 7 G99 LAGRsAGGssPEGGE
0 43 S100-p AGRsAGGssPEGGED
0 70 S101-p GRsAGGssPEGGEDs
0 97 S108-p sPEGGEDsDREDGNy
0 28 Y115-p sDREDGNyCPPVKRE
0 40 T124-p PPVKRERtssLtQFP
0 37 S125-p PVKRERtssLtQFPP
3 146 S126-p VKRERtssLtQFPPs
0 23 T128-p RERtssLtQFPPsQS
0 5 S133-p sLtQFPPsQSEERSS
0 1 S186-p APQPKALsQtVPSSG
0 1 T188-p QPKALsQtVPSSGTN
0 5 S211-p TGAVPAAsPDTAAWR
0 11 S219-p PDTAAWRsPSEAADE
0 7 S221 TAAWRsPSEAADEVC
0 1 A223 AWRsPSEAADEVCAL
0 4 T292-p AGHPSADtPTATNyF
0 1 Y298-p DtPTATNyFLQYISS
0 22 S333-p NMSERVLsPPKLNEV
0 2 S342 PKLNEVSSDANRENA
0 6 S353-p RENAAAEsGsEsssQ
0 3 S355-p NAAAEsGsEsssQEA
0 1 S357-p AAEsGsEsssQEAtP
0 1 S358-p AEsGsEsssQEAtPE
0 3 S359-p EsGsEsssQEAtPEK
0 1 T363-p EsssQEAtPEKESLA
0 1 K366 sQEAtPEKESLAESA
0 1 K413-u CKLFVFDkTSQSWVE
0 1 T457-p SLRLILNtKLWAQMQ
0 1 S493-p KVFLISAsSKDTGQL
0 2 Y501-p SKDTGQLyAALHHRI
0 2 S533-p PEPGAAPsNEEDDsD
0 2 N534 EPGAAPsNEEDDsDD
0 5 S539-p PsNEEDDsDDDDVLA
0 1 T567 DGQTTGST_______
9380 : Phospho-RanBP3 (Ser58) Antibody
  RANBP3 iso2  
K21 PPVFVFQKDKGQKSP
S27 QKDKGQKSPAEQKNL
S96 PRELAGRSAGGSSPE
G99 LAGRSAGGSSPEGGE
S100 AGRSAGGSSPEGGED
S101 GRSAGGSSPEGGEDS
S108 SPEGGEDSDREDGNY
Y115 SDREDGNYCPPVKRE
T124 PPVKRERTSSLTQFP
S125 PVKRERTSSLTQFPP
S126 VKRERTSSLTQFPPS
T128 RERTSSLTQFPPSQS
S133 SLTQFPPSQSEERSS
S186 APQPKALSQTVPSSG
T188 QPKALSQTVPSSGTN
S211 TGAVPAASPDTAAWR
S219-p PDTAAWRsPsEAADE
S221-p TAAWRsPsEAADEEK
A223 AWRsPsEAADEEKEP
T287 AGHPSADTPTATNYF
Y293 DTPTATNYFLQYISS
S328 NMSERVLSPPKLNEV
S337 PKLNEVSSDANRENA
S348 RENAAAESGSESSSQ
S350 NAAAESGSESSSQEA
S352 AAESGSESSSQEATP
S353 AESGSESSSQEATPE
S354 ESGSESSSQEATPEK
T358 ESSSQEATPEKESLA
K361 SQEATPEKESLAESA
K408 CKLFVFDKTSQSWVE
T452 SLRLILNTKLWAQMQ
S488 KVFLISASSKDTGQL
Y496 SKDTGQLYAALHHRI
S528 PEPGAAPSNEEDDSD
N529 EPGAAPSNEEDDSDD
S534 PSNEEDDSDDDDVLA
T562 DGQTTGST_______
  RANBP3 iso3  
K21 PPVFVFQKDKGQKRS
- gap
S28 KDKGQKRSAGGSSPE
G31 GQKRSAGGSSPEGGE
S32 QKRSAGGSSPEGGED
S33 KRSAGGSSPEGGEDS
S40 SPEGGEDSDREDGNY
Y47 SDREDGNYCPPVKRE
T56 PPVKRERTSsLTQFP
S57 PVKRERTSsLTQFPP
S58-p VKRERTSsLTQFPPS
T60 RERTSsLTQFPPSQS
S65 sLTQFPPSQSEERSS
S118 APQPKALSQTVPSSG
T120 QPKALSQTVPSSGTN
S143 TGAVPAASPDTAAWR
S151 PDTAAWRSPSEAADE
S153 TAAWRSPSEAADEVC
A155 AWRSPSEAADEVCAL
T224 AGHPSADTPTATNYF
Y230 DTPTATNYFLQYISS
S265 NMSERVLSPPKLNEV
S274 PKLNEVSSDANRENA
S285 RENAAAESGSESSSQ
S287 NAAAESGSESSSQEA
S289 AAESGSESSSQEATP
S290 AESGSESSSQEATPE
S291 ESGSESSSQEATPEK
T295 ESSSQEATPEKESLA
K298 SQEATPEKESLAESA
K345 CKLFVFDKTSQSWVE
T389 SLRLILNTKLWAQMQ
S425 KVFLISASSKDTGQL
Y433 SKDTGQLYAALHHRI
S465 PEPGAAPSNEEDDSD
N466 EPGAAPSNEEDDSDD
S471 PSNEEDDSDDDDVLA
T499 DGQTTGST_______
9380 : Phospho-RanBP3 (Ser58) Antibody
  mouse

 
K21 PSVFVFQKDKGQKRs
- 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
S113 APQPKVLSQTVPSSG
T115 QPKVLSQTVPSSGTN
S138-p TGPATSVsPENLTQR
S146-p PENLTQRsPsEsAEE
S148-p NLTQRsPsEsAEETH
S150-p TQRsPsEsAEETHTL
T217 AAHPSSETPSATNYF
Y223 ETPSATNYFLQYISS
S257-p NMSERVLsPPKLNEA
S266-p PKLNEANsDTSRETT
S277-p RETTHAQsGSESSsQ
S279 TTHAQsGSESSsQEA
S281 HAQsGSESSsQEAAP
S282 AQsGSESSsQEAAPK
S283-p QsGSESSsQEAAPKk
A287 ESSsQEAAPKkESLA
K290-u sQEAAPKkESLAESA
K337 CKLFVFDKTSQSWVE
T381 SLRLILNTKLWAQMQ
S417 KVFLISASSKDTGQL
Y425 SKDTGQLYAALHHRI
A457 PEPGATRAtEEEDsD
T458-p EPGATRAtEEEDsDE
S463-p RAtEEEDsDEDAVLA
T491-p DGQAPGSt_______
  rat

 
K21 PSVFVFQKDKGQKRs
- gap
S28-p KDKGQKRsAGsSsPE
S31-p GQKRsAGsSsPEAGE
S32 QKRsAGsSsPEAGED
S33-p KRsAGsSsPEAGEDs
S40-p sPEAGEDsDHEDGNY
Y47 sDHEDGNYCPPVKRE
T56 PPVKRERTSsLTHSE
S57 PVKRERTSsLTHSEE
S58-p VKRERTSsLTHSEEK
T60 RERTSsLTHSEEKSS
- gap
S113 APQPKVLSQTVPSSG
T115 QPKVLSQTVPSSGTN
S138 TGPATSASPENLTQR
S146-p PENLTQRsPSESAEG
S148 NLTQRsPSESAEGTH
S150 TQRsPSESAEGTHTF
T217 AAHPGSETPTATNYF
Y223 ETPTATNYFLQYISS
S257-p NMSERVLsPPKLNEA
S266 PKLNEANSDTSRETT
S277 RETTHAQSGSESSSQ
S279 TTHAQSGSESSSQEA
S281 HAQSGSESSSQEAVP
S282 AQSGSESSSQEAVPK
S283 QSGSESSSQEAVPKK
V287 ESSSQEAVPKKESLA
K290 SQEAVPKKESLAESA
K337 CKLFVFDKTSQSWVE
T381 SLRLILNTKLWAQMQ
S417 KVFLISASSKDTGQL
Y425 SKDTGQLYAALHHRI
A457 PEPGATRAAEEEDsD
A458 EPGATRAAEEEDsDE
S463-p RAAEEEDsDEDAVLA
T491 DGQATGST_______
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