Q96S59 (RANB9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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	Cytoplasm › cytosol. 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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome microtubule nucleation Non-traceable author statement Ref.5. Source: UniProtKB protein complex assembly Traceable author statement Ref.4. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule associated complex Traceable author statement Ref.4. Source: ProtInc nucleus Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	Ran GTPase binding Traceable author statement Ref.4. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	6	EBI-636085,EBI-529989
DYRK1B	Q9Y463	4	EBI-636085,EBI-634187
OPRM1	P35372	2	EBI-636085,EBI-2624570
PPP1CC	P36873-2	3	EBI-636085,EBI-3964623
S100A7	P31151	3	EBI-636085,EBI-357520

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 729	729	Ran-binding protein 9		PRO_0000097169
Regions
	Domain	147 – 334	188	B30.2/SPRY
	Domain	365 – 397	33	LisH
	Domain	403 – 460	58	CTLH
	Region	401 – 407	7	Interaction with CALB1 Probable
	Region	615 – 729	115	Interaction with FMR1
	Compositional bias	5 – 10	6	Poly-Pro
	Compositional bias	11 – 18	8	Poly-Gln
	Compositional bias	21 – 24	4	Poly-Pro
	Compositional bias	25 – 131	107	Ala-rich
	Compositional bias	62 – 66	5	Poly-Ala
	Compositional bias	71 – 77	7	Poly-Pro
	Compositional bias	82 – 92	11	Poly-Pro
Amino acid modifications
	Modified residue	405	1	N6-acetyllysine Ref.21
	Modified residue	487	1	Phosphoserine Ref.20
Natural variations
	Alternative sequence	1 – 341	341	Missing in isoform 2.		VSP_013175
Experimental info
	Sequence conflict	87	1	P → S in BAA23216. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 50DF1127B7FDA6C8	FASTA	729	77,847
	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
	Isoform 2 [UniParc]. Checksum: 28332F38EEB013B8	FASTA	388	43,064
	10 20 30 40 50 60 MREWRTKIQA QIDRFPIGDR EGEWQTMIQK MVSSYLVHHG YCATAEAFAR STDQTVLEEL 70 80 90 100 110 120 ASIKNRQRIQ KLVLAGRMGE AIETTQQLYP SLLERNPNLL FTLKVRQFIE MVNGTDSEVR 130 140 150 160 170 180 CLGGRSPKSQ DSYPVSPRPF SSPSMSPSHG MNIHNLASGK GSTAHFSGFE SCSNGVISNK 190 200 210 220 230 240 AHQSYCHSNK HQSSNLNVPE LNSINMSRSQ QVNNFTSNDV DMETDHYSNG VGETSSNGFL 250 260 270 280 290 300 NGSSKHDHEM EDCDTEMEVD SSQLRRQLCG GSQAAIERMI HFGRELQAMS EQLRRDCGKN 310 320 330 340 350 360 TANKKMLKDA FSLLAYSDPW NSPVGNQLDP IQREPVCSAL NSAILETHNL PKQPPLALAM 370 380 GQATQCLGLM ARSGIGSCAF ATVEDYLH

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
IPI	IPI00465275. IPI00554545.
RefSeq	NP_005484.2. NM_005493.2.
UniGene	Hs.708182.
3D structure databases
ProteinModelPortal	Q96S59.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96S59. 20 interactions.
MINT	MINT-243263.
STRING	9606.ENSP00000011619.
PTM databases
PhosphoSite	Q96S59.
Polymorphism databases
DMDM	61215334.
Proteomic databases
PaxDb	Q96S59.
PRIDE	Q96S59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000011619; ENSP00000011619; ENSG00000010017.
GeneID	10048.
KEGG	hsa:10048.
UCSC	uc003nba.3. human.
Organism-specific databases
CTD	10048.
GeneCards	GC06M013621.
H-InvDB	HIX0032741.
HGNC	HGNC:13727. RANBP9.
HPA	CAB033767. HPA050007.
MIM	603854. gene.
neXtProt	NX_Q96S59.
PharmGKB	PA34215.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG316575.
HOGENOM	HOG000008133.
HOVERGEN	HBG053444.
InParanoid	Q96S59.
OMA	CDADMEV.
OrthoDB	EOG4868C1.
PhylomeDB	Q96S59.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_pathway. Coregulation of Androgen receptor activity. met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q96S59.
Bgee	Q96S59.
CleanEx	HS_RANBP9.
Genevestigator	Q96S59.
GermOnline	ENSG00000010017. Homo sapiens.
Family and domain databases
InterPro	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]
Pfam	PF10607. CLTH. 1 hit. PF08513. LisH. 1 hit. PF00622. SPRY. 1 hit. [Graphical view]
SMART	SM00757. CRA. 1 hit. SM00668. CTLH. 1 hit. SM00667. LisH. 1 hit. SM00449. SPRY. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50188. B302_SPRY. 1 hit. PS50897. CTLH. 1 hit. PS50896. LISH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RANBP9. human.
GenomeRNAi	10048.
NextBio	37955.
SOURCE	Search...

Entry information

Entry name

RANB9_HUMAN

Accession

Primary (citable) accession number: Q96S59
Secondary accession number(s): A0PJA2 , O94764, Q6P3T7, Q7LBR2, Q7Z7F9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.