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P69566

- RANB9_MOUSE

UniProt

P69566 - RANB9_MOUSE

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Protein

Ran-binding protein 9

Gene
Ranbp9, Ranbpm
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation By similarity. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA By similarity.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. Ran GTPase binding Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-binding protein 9
Short name:
RanBP9
Alternative name(s):
B-cell antigen receptor Ig beta-associated protein 1
Short name:
IBAP-1
Ran-binding protein M
Short name:
RanBPM
Gene namesi
Name:Ranbp9
Synonyms:Ranbpm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1928741. Ranbp9.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: Perinuclear in spermatids.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Ran-binding protein 9PRO_0000097170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei330 – 3301N6-acetyllysine By similarity
Modified residuei412 – 4121Phosphoserine By similarity

Post-translational modificationi

Phosphorylated in response to stress By similarity.
Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP69566.
PaxDbiP69566.
PRIDEiP69566.

PTM databases

PhosphoSiteiP69566.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in maturating spermatocytes.2 Publications

Gene expression databases

CleanExiMM_RANBP9.
GenevestigatoriP69566.

Interactioni

Subunit structurei

Interacts with GTP-bound Ran, AR, CDC2L1, CALB1, S100A7, USP11, MKLN1, SOS1 or SOS2, GID8, and FMR1. Interacts with the Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform Alpha but not with TP53. Interacts with the HGF receptor MET and the integrins ITGB1 and ITGB2, but not with ITGAL. Part of a complex consisting of RANBP9, MKLN1 and GID8. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 By similarity. Interacts with NGFR and DDX4. Directly interacts with RANBP10 By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lrp1bQ9JI182EBI-772305,EBI-8294317

Protein-protein interaction databases

BioGridi208133. 2 interactions.
IntActiP69566. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliP69566.
SMRiP69566. Positions 141-250.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 259188B30.2/SPRYAdd
BLAST
Domaini290 – 32233LisHAdd
BLAST
Domaini328 – 38558CTLHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni326 – 3327Interaction with CALB1 By similarity
Regioni539 – 653115Interaction with FMR1 By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 106Poly-Pro
Compositional biasi14 – 207Poly-Pro

Domaini

The SPRY domain mediates the interaction with MET, AR, and CDC2L1 By similarity.

Sequence similaritiesi

Belongs to the RANBP9/10 family.
Contains 1 B30.2/SPRY domain.
Contains 1 CTLH domain.
Contains 1 LisH domain.

Phylogenomic databases

eggNOGiNOG316575.
HOGENOMiHOG000008133.
HOVERGENiHBG053444.
InParanoidiP69566.
PhylomeDBiP69566.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PfamiPF10607. CLTH. 1 hit.
PF08513. LisH. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P69566-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSGQPPPPPP QQQPPPPPPP ASAAAPATAP PGLAVGPGPA AGVPVPGLAA    50
GSSAAAPFPH GDSALNEQEK ELQRRLKRLY PAVDEQETPL PRSWSPKDKF 100
SYIGLSQNNL RVHYKGHGKT PKDAASVRAT HPIPAACGIY YFEVKIVSKG 150
RDGYMGIGLS AQGVNMNRLP GWDKHSYGYH GDDGHSFCSS GTGQPYGPTF 200
TTGDVIGCCV NLINNTCFYT KNGHSLGIAF TDLPPNLYPT VGLQTPGEVV 250
DANFGQHPFV FDIEDYMREW RTKIQAQIDR FPIGDREGEW QTMIQKMVSS 300
YLVHHGYCAT AEAFARSTDQ TVLEELASIK NRQRIQKLVL AGRMGEAIET 350
TQQLYPSLLE RNPNLLFTLK VRQFIEMVNG TDSEVRCLGG RSPKSQDSYP 400
VSPRPFSSPS MSPSHGMSIH SLAPGKSSTA HFSGFESCSN GVISNKAHQS 450
YCHSKHQLSS LTVPELNSLN VSRSQQVNNF TSNDVDMETD HYSNGVGETS 500
SNGFLNGSSK HDHEMEDCDT EMEVDCSQLR RQLCGGSQAA IERMIHFGRE 550
LQAMSEQLRR ECGKNTANKK MLKDAFSLLA YSDPWNSPVG NQLDPIQREP 600
VCSALNSAIL ETHNLPKQPP LALAMGQATQ CLGLMARSGV GSCAFATVED 650
YLH 653
Length:653
Mass (Da):71,012
Last modified:March 29, 2005 - v1
Checksum:iBE810E69B238BBD5
GO
Isoform 2 (identifier: P69566-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.
     108-115: NNLRVHYK → MWESSWVL

Note: No experimental confirmation available.

Show »
Length:546
Mass (Da):60,086
Checksum:i8B74E3D4F271875F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107Missing in isoform 2. VSP_028266Add
BLAST
Alternative sequencei108 – 1158NNLRVHYK → MWESSWVL in isoform 2. VSP_028267

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921R → P1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006465 mRNA. Translation: AAD01272.1.
AK132714 mRNA. Translation: BAE21317.1.
PIRiJC8013.
RefSeqiNP_064314.2. NM_019930.2.
UniGeneiMm.148781.

Genome annotation databases

GeneIDi56705.
KEGGimmu:56705.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006465 mRNA. Translation: AAD01272.1 .
AK132714 mRNA. Translation: BAE21317.1 .
PIRi JC8013.
RefSeqi NP_064314.2. NM_019930.2.
UniGenei Mm.148781.

3D structure databases

ProteinModelPortali P69566.
SMRi P69566. Positions 141-250.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208133. 2 interactions.
IntActi P69566. 6 interactions.

PTM databases

PhosphoSitei P69566.

Proteomic databases

MaxQBi P69566.
PaxDbi P69566.
PRIDEi P69566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 56705.
KEGGi mmu:56705.

Organism-specific databases

CTDi 10048.
MGIi MGI:1928741. Ranbp9.

Phylogenomic databases

eggNOGi NOG316575.
HOGENOMi HOG000008133.
HOVERGENi HBG053444.
InParanoidi P69566.
PhylomeDBi P69566.

Miscellaneous databases

ChiTaRSi RANBP9. mouse.
NextBioi 313155.
PROi P69566.
SOURCEi Search...

Gene expression databases

CleanExi MM_RANBP9.
Genevestigatori P69566.

Family and domain databases

InterProi IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view ]
Pfami PF10607. CLTH. 1 hit.
PF08513. LisH. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view ]
SMARTi SM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse RanBPM is a partner gene to a germline specific RNA helicase, mouse vasa homolog protein."
    Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A., Noce T.
    Mol. Reprod. Dev. 67:1-7(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX4, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Testis.
  2. "B cell antigen receptor Ig beta associated protein."
    Doi T., Watanabe T.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-653 (ISOFORM 1), INTERACTION WITH NGFR.
    Tissue: Brain.
  5. "RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."
    Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E.
    J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiRANB9_MOUSE
AccessioniPrimary (citable) accession number: P69566
Secondary accession number(s): P84500, Q3V136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 11, 2014
This is version 84 of the entry and version 1 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

External Data

Dasty 3

Similar proteinsi