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Q96S59 (RANB9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ran-binding protein 9

Short name=RanBP9
Alternative name(s):
BPM-L
BPM90
Ran-binding protein M
Short name=RanBPM
RanBP7
Gene names
Name:RANBP9
Synonyms:RANBPM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. Ref.6 Ref.9 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19

Subunit structure

Interacts with NGFR and DDX4 By similarity. Interacts with GTP-bound Ran, AR, CDC2L1/p110C, CALB1, S100A7, USP11, MKLN1, SOS1 or SOS2, GID8, and FMR1. Interacts with the Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform Alphabut 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. Directly interacts with RANBP10. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Subcellular location

Cytoplasmcytosol. Nucleus. Note: =Predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane. Ref.1 Ref.5 Ref.11 Ref.15 Ref.16 Ref.17 Ref.19

Tissue specificity

Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells. Ref.6 Ref.9 Ref.16

Domain

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

Post-translational modification

Phosphorylated in response to stress. Can be phosphorylated by the cleaved p110 form of CDC2L1 (p110C). Ref.11 Ref.15

Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system. Can be deubiquitinated by USP11. Ref.7

Sequence similarities

Belongs to the RANBP9/10 family.

Contains 1 B30.2/SPRY domain.

Contains 1 CTLH domain.

Contains 1 LisH domain.

Caution

According to some authors (Ref.4) RANBP9 would be located in centrosomes and involved in microtubule assembly, but other authors infirmed these results in (Ref.1).

Sequence caution

The sequence AAH19886.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH52781.1 differs from that shown. Reason: Frameshift at positions 13, 30 and 34.

The sequence AAK15469.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA23216.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96S59-1)

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.
Isoform 2 (identifier: Q96S59-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-341: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Ran-binding protein 9
PRO_0000097169

Regions

Domain147 – 334188B30.2/SPRY
Domain365 – 39733LisH
Domain403 – 46058CTLH
Region401 – 4077Interaction with CALB1 Probable
Region615 – 729115Interaction with FMR1
Compositional bias5 – 106Poly-Pro
Compositional bias11 – 188Poly-Gln
Compositional bias21 – 244Poly-Pro
Compositional bias25 – 131107Ala-rich
Compositional bias62 – 665Poly-Ala
Compositional bias71 – 777Poly-Pro
Compositional bias82 – 9211Poly-Pro

Amino acid modifications

Modified residue4051N6-acetyllysine Ref.21
Modified residue4871Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 341341Missing in isoform 2.
VSP_013175

Experimental info

Sequence conflict871P → S in BAA23216. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 50DF1127B7FDA6C8

FASTA72977,847
        10         20         30         40         50         60 
MSGQPPPPPP QQQQQQQQLS PPPPAALAPV SGVVLPAPPA VSAGSSPAGS PGGGAGGEGL 

        70         80         90        100        110        120 
GAAAAALLLH PPPPPPPATA APPPPPPPPP PPASAAAPAS GPPAPPGLAA GPGPAGGAPT 

       130        140        150        160        170        180 
PALVAGSSAA APFPHGDSAL NEQEKELQRR LKRLYPAVDE QETPLPRSWS PKDKFSYIGL 

       190        200        210        220        230        240 
SQNNLRVHYK GHGKTPKDAA SVRATHPIPA ACGIYYFEVK IVSKGRDGYM GIGLSAQGVN 

       250        260        270        280        290        300 
MNRLPGWDKH SYGYHGDDGH SFCSSGTGQP YGPTFTTGDV IGCCVNLINN TCFYTKNGHS 

       310        320        330        340        350        360 
LGIAFTDLPP NLYPTVGLQT PGEVVDANFG QHPFVFDIED YMREWRTKIQ AQIDRFPIGD 

       370        380        390        400        410        420 
REGEWQTMIQ KMVSSYLVHH GYCATAEAFA RSTDQTVLEE LASIKNRQRI QKLVLAGRMG 

       430        440        450        460        470        480 
EAIETTQQLY PSLLERNPNL LFTLKVRQFI EMVNGTDSEV RCLGGRSPKS QDSYPVSPRP 

       490        500        510        520        530        540 
FSSPSMSPSH GMNIHNLASG KGSTAHFSGF ESCSNGVISN KAHQSYCHSN KHQSSNLNVP 

       550        560        570        580        590        600 
ELNSINMSRS QQVNNFTSND VDMETDHYSN GVGETSSNGF LNGSSKHDHE MEDCDTEMEV 

       610        620        630        640        650        660 
DSSQLRRQLC GGSQAAIERM IHFGRELQAM SEQLRRDCGK NTANKKMLKD AFSLLAYSDP 

       670        680        690        700        710        720 
WNSPVGNQLD PIQREPVCSA LNSAILETHN LPKQPPLALA MGQATQCLGL MARSGIGSCA 


FATVEDYLH 

« Hide

Isoform 2 [UniParc].

Checksum: 28332F38EEB013B8
Show »

FASTA38843,064

References

« Hide 'large scale' references
[1]"Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex."
Nishitani H., Hirose E., Uchimura Y., Nakamura M., Umeda M., Nishii K., Mori N., Nishimoto T.
Gene 272:25-33(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Lymph, Spinal ganglion and Testis.
[4]"When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin."
Nakamura M., Masuda H., Horii J., Kuma K., Yokoyama N., Ohba T., Nishitani H., Miyata T., Tanaka M., Nishimoto T.
J. Cell Biol. 143:1041-1052(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-729 (ISOFORM 1), INTERACTION WITH RAN.
[5]"HIPK2 associates with RanBPM."
Wang Y., Marion Schneider E., Li X., Duttenhoefer I., Debatin K.-M., Hug H.
Biochem. Biophys. Res. Commun. 297:148-153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-729 (ISOFORM 1), INTERACTION WITH HIPK2, SUBCELLULAR LOCATION.
[6]"RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor."
Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C., Rennie P.S.
J. Biol. Chem. 277:48020-48027(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-729 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AR.
Tissue: Prostate.
[7]"Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM."
Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E., Aoki A., Ishigatsubo Y.
Biochem. J. 367:87-95(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP11, UBIQUITINATION.
[8]"RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer."
Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C., Watson P.H.
BMC Cancer 2:28-28(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A7.
[9]"Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM."
Wang D., Li Z., Messing E.M., Wu G.
J. Biol. Chem. 277:36216-36222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RAS SIGNALING, INTERACTION WITH MET AND SOS, TISSUE SPECIFICITY.
[10]"Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy."
Lutz W., Frank E.M., Craig T.A., Thompson R., Venters R.A., Kojetin D., Cavanagh J., Kumar R.
Biochem. Biophys. Res. Commun. 303:1186-1192(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALB1.
[11]"The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM."
Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.
Biochem. Biophys. Res. Commun. 310:14-18(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC2L1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[12]"A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM."
Umeda M., Nishitani H., Nishimoto T.
Gene 303:47-54(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKLN1 AND GID8, IDENTIFICATION IN A COMPLEX WITH MKLN1 AND GID8.
[13]"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
Zou Y., Lim S., Lee K., Deng X., Friedman E.
J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DYRK1A AND DYRK1B, IDENTIFICATION IN A COMPLEX WITH RAN; DYRK1B AND COPS5.
[14]"A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAN AND MET.
[15]"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: FUNCTION, INTERACTION WITH ITGB1 AND ITGB2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[16]"The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
Menon R.P., Gibson T.J., Pastore A.
J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FMR1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[17]"Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells."
Kramer S., Ozaki T., Miyazaki K., Kato C., Hanamoto T., Nakagawara A.
Oncogene 24:938-944(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP73.
[18]"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[19]"RanBP10 acts as a novel coactivator for the androgen receptor."
Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.
Biochem. Biophys. Res. Commun. 368:121-125(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RANBP10, SUBCELLULAR LOCATION.
[20]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB055311 mRNA. Translation: BAB62525.1.
AL441883, Z93020 Genomic DNA. Translation: CAI19841.1.
Z93020, AL441883 Genomic DNA. Translation: CAI21594.1.
BC019886 mRNA. Translation: AAH19886.1. Sequence problems.
BC052781 mRNA. Translation: AAH52781.1. Frameshift.
BC063849 mRNA. Translation: AAH63849.1.
AB008515 mRNA. Translation: BAA23216.1. Different initiation.
AF306510 mRNA. Translation: AAK15469.1. Different initiation.
RefSeqNP_005484.2. NM_005493.2.
UniGeneHs.708182.

3D structure databases

ProteinModelPortalQ96S59.
SMRQ96S59. Positions 175-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115359. 67 interactions.
IntActQ96S59. 34 interactions.
MINTMINT-243263.
STRING9606.ENSP00000011619.

PTM databases

PhosphoSiteQ96S59.

Polymorphism databases

DMDM61215334.

Proteomic databases

PaxDbQ96S59.
PRIDEQ96S59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000011619; ENSP00000011619; ENSG00000010017. [Q96S59-1]
GeneID10048.
KEGGhsa:10048.
UCSCuc003nba.3. human. [Q96S59-1]

Organism-specific databases

CTD10048.
GeneCardsGC06M013621.
H-InvDBHIX0032741.
HGNCHGNC:13727. RANBP9.
HPACAB033767.
HPA050007.
MIM603854. gene.
neXtProtNX_Q96S59.
PharmGKBPA34215.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316575.
HOGENOMHOG000008133.
HOVERGENHBG053444.
InParanoidQ96S59.
OMARMLEFGR.
OrthoDBEOG76MK7Z.
PhylomeDBQ96S59.
TreeFamTF331658.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkQ96S59.

Gene expression databases

ArrayExpressQ96S59.
BgeeQ96S59.
CleanExHS_RANBP9.
GenevestigatorQ96S59.

Family and domain databases

InterProIPR001870. 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.
IPR027713. RANBP9/RANBP10/Ssh4.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERPTHR12864:SF1. PTHR12864:SF1. 1 hit.
PfamPF10607. CLTH. 1 hit.
PF08513. LisH. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRANBP9. human.
GeneWikiRANBP9.
GenomeRNAi10048.
NextBio37955.
PROQ96S59.
SOURCESearch...

Entry information

Entry nameRANB9_HUMAN
AccessionPrimary (citable) accession number: Q96S59
Secondary accession number(s): A0PJA2 expand/collapse secondary AC list , O94764, Q6P3T7, Q7LBR2, Q7Z7F9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM