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Protein

Ran-binding protein 3

Gene

Ranbp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-binding protein 3
Short name:
RanBP3
Gene namesi
Name:Ranbp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1919060. Ranbp3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 491490Ran-binding protein 3PRO_0000097167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91N6-acetyllysineCombined sources
Modified residuei21 – 211N6-acetyllysineCombined sources
Modified residuei32 – 321PhosphoserineCombined sources
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei56 – 561PhosphothreonineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei257 – 2571PhosphoserineCombined sources
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei279 – 2791PhosphoserineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CT10.
MaxQBiQ9CT10.
PaxDbiQ9CT10.
PeptideAtlasiQ9CT10.
PRIDEiQ9CT10.

PTM databases

iPTMnetiQ9CT10.
PhosphoSiteiQ9CT10.

Expressioni

Gene expression databases

BgeeiQ9CT10.
CleanExiMM_RANBP3.
GenevisibleiQ9CT10. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9CT10. 1 interaction.
MINTiMINT-4613884.
STRINGi10090.ENSMUSP00000002445.

Structurei

3D structure databases

ProteinModelPortaliQ9CT10.
SMRiQ9CT10. Positions 314-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini302 – 442141RanBD1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0866. Eukaryota.
ENOG4111NCK. LUCA.
GeneTreeiENSGT00530000063644.
HOGENOMiHOG000290662.
HOVERGENiHBG061383.
InParanoidiQ9CT10.
KOiK15304.
OMAiQMDKASE.
OrthoDBiEOG7TJ3JQ.
PhylomeDBiQ9CT10.
TreeFamiTF313181.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CT10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLANEEKP AVAPSVFVFQ KDKGQKRSAG SSSPEAGEDS DHEDGNYCPP
60 70 80 90 100
VKRERTSSLT HSEEKSSGFR LKPPTLIHGQ APSAGLPSQK PREQQRGVLR
110 120 130 140 150
PAVLQAPQPK VLSQTVPSSG TNGVSMPADC TGPATSVSPE NLTQRSPSES
160 170 180 190 200
AEETHTLEEK VPQKTPHGTS EEGHCEEEQA APQAFVFGQN LRDRVKLMNE
210 220 230 240 250
NASVADVDSA AHPSSETPSA TNYFLQYISS SADNATHSAD NSTKFVFGQN
260 270 280 290 300
MSERVLSPPK LNEANSDTSR ETTHAQSGSE SSSQEAAPKK ESLAESAAAY
310 320 330 340 350
TKATAWTCLL EKVEVITGEE AESNVLQIQC KLFVFDKTSQ SWVERGRGLL
360 370 380 390 400
RLNDMASTDD GTLQSRLVMR TQGSLRLILN TKLWAQMQMD KASEKSIRIT
410 420 430 440 450
ATDAEDQGVK VFLISASSKD TGQLYAALHH RILALRSRAE QEQEAKAPPP
460 470 480 490
EPGATRATEE EDSDEDAVLA PSGVTGAGTG DEGDGQAPGS T
Length:491
Mass (Da):52,573
Last modified:December 6, 2005 - v2
Checksum:i6BEFB98D5B0B38B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591P → T in BAE39772 (PubMed:16141072).Curated
Sequence conflicti293 – 2931L → P in BAB27684 (PubMed:16141072).Curated
Sequence conflicti317 – 3171T → K in BAB27684 (PubMed:16141072).Curated
Sequence conflicti472 – 4721S → P in BAB27684 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011541 mRNA. Translation: BAB27684.1.
AK133949 mRNA. Translation: BAE21946.1.
AK134696 mRNA. Translation: BAE22245.1.
AK155301 mRNA. Translation: BAE33176.1.
AK167731 mRNA. Translation: BAE39772.1.
BC145892 mRNA. Translation: AAI45893.1.
BC145894 mRNA. Translation: AAI45895.1.
CCDSiCCDS28911.1.
RefSeqiNP_082209.1. NM_027933.3.
UniGeneiMm.29608.
Mm.469805.

Genome annotation databases

EnsembliENSMUST00000002445; ENSMUSP00000002445; ENSMUSG00000002372.
GeneIDi71810.
KEGGimmu:71810.
UCSCiuc008dct.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011541 mRNA. Translation: BAB27684.1.
AK133949 mRNA. Translation: BAE21946.1.
AK134696 mRNA. Translation: BAE22245.1.
AK155301 mRNA. Translation: BAE33176.1.
AK167731 mRNA. Translation: BAE39772.1.
BC145892 mRNA. Translation: AAI45893.1.
BC145894 mRNA. Translation: AAI45895.1.
CCDSiCCDS28911.1.
RefSeqiNP_082209.1. NM_027933.3.
UniGeneiMm.29608.
Mm.469805.

3D structure databases

ProteinModelPortaliQ9CT10.
SMRiQ9CT10. Positions 314-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CT10. 1 interaction.
MINTiMINT-4613884.
STRINGi10090.ENSMUSP00000002445.

PTM databases

iPTMnetiQ9CT10.
PhosphoSiteiQ9CT10.

Proteomic databases

EPDiQ9CT10.
MaxQBiQ9CT10.
PaxDbiQ9CT10.
PeptideAtlasiQ9CT10.
PRIDEiQ9CT10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002445; ENSMUSP00000002445; ENSMUSG00000002372.
GeneIDi71810.
KEGGimmu:71810.
UCSCiuc008dct.2. mouse.

Organism-specific databases

CTDi8498.
MGIiMGI:1919060. Ranbp3.

Phylogenomic databases

eggNOGiKOG0866. Eukaryota.
ENOG4111NCK. LUCA.
GeneTreeiENSGT00530000063644.
HOGENOMiHOG000290662.
HOVERGENiHBG061383.
InParanoidiQ9CT10.
KOiK15304.
OMAiQMDKASE.
OrthoDBiEOG7TJ3JQ.
PhylomeDBiQ9CT10.
TreeFamiTF313181.

Miscellaneous databases

ChiTaRSiRanbp3. mouse.
PROiQ9CT10.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CT10.
CleanExiMM_RANBP3.
GenevisibleiQ9CT10. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Liver and Medulla oblongata.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-40; SER-146 AND SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-40; SER-146 AND SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRANB3_MOUSE
AccessioniPrimary (citable) accession number: Q9CT10
Secondary accession number(s): A6H6I9
, Q3TIS4, Q3U2G4, Q3UYG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 6, 2005
Last modified: July 6, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.