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Q9H6Z4 (RANB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ran-binding protein 3

Short name=RanBP3
Gene names
Name:RANBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13

Subunit structure

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13

Subcellular location

Cytoplasm. Nucleus Ref.13.

Tissue specificity

Widely expressed with high levels in testis and heart. Ref.1

Sequence similarities

Contains 1 RanBD1 domain.

Sequence caution

The sequence AAH04349.1 differs from that shown. Reason: Aberrant splicing.

The sequence CAB43293.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular transport

Inferred from electronic annotation. Source: InterPro

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: LIFEdb

   Molecular_functionR-SMAD binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Ran GTPase binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H6Z4-1)

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: Q9H6Z4-2)

Also known as: Ranbp3-a;

The sequence of this isoform differs from the canonical sequence as follows:
     226-230: Missing.
Isoform 3 (identifier: Q9H6Z4-3)

Also known as: Ranbp3-b;

The sequence of this isoform differs from the canonical sequence as follows:
     27-94: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 567566Ran-binding protein 3
PRO_0000097165

Regions

Domain378 – 518141RanBD1
Compositional bias76 – 816Poly-Pro
Compositional bias537 – 5437Poly-Asp

Amino acid modifications

Modified residue21N-acetylalanine Ref.19
Modified residue91N6-acetyllysine By similarity
Modified residue211N6-acetyllysine Ref.15
Modified residue1001Phosphoserine Ref.11
Modified residue1011Phosphoserine Ref.11
Modified residue1081Phosphoserine Ref.9 Ref.11
Modified residue1241Phosphothreonine Ref.11
Modified residue2191Phosphoserine By similarity
Modified residue3331Phosphoserine Ref.11 Ref.14 Ref.18
Modified residue3531Phosphoserine Ref.11
Modified residue3551Phosphoserine Ref.11
Modified residue5391Phosphoserine Ref.11

Natural variations

Alternative sequence27 – 9468Missing in isoform 3.
VSP_011163
Alternative sequence226 – 2305Missing in isoform 2.
VSP_011162
Natural variant3141A → V.
Corresponds to variant rs10417885 [ dbSNP | Ensembl ].
VAR_051303

Experimental info

Sequence conflict358 – 3592SS → PF in CAA69956. Ref.1
Sequence conflict3671E → G in CAA69957. Ref.1

Secondary structure

...................... 567
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 203B5A900512743C

FASTA56760,210
        10         20         30         40         50         60 
MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE 

        70         80         90        100        110        120 
HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK 

       130        140        150        160        170        180 
RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP 

       190        200        210        220        230        240 
QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES 

       250        260        270        280        290        300 
SNASEEEACE KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL 

       310        320        330        340        350        360 
QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA AESGSESSSQ 

       370        380        390        400        410        420 
EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN VLQMQCKLFV FDKTSQSWVE 

       430        440        450        460        470        480 
RGRGLLRLND MASTDDGTLQ SRLVMRTQGS LRLILNTKLW AQMQIDKASE KSIRITAMDT 

       490        500        510        520        530        540 
EDQGVKVFLI SASSKDTGQL YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD 

       550        560 
DDDVLAPSGA TAAGAGDEGD GQTTGST 

« Hide

Isoform 2 (Ranbp3-a) [UniParc].

Checksum: 453AF2CD380BA7F1
Show »

FASTA56259,694
Isoform 3 (Ranbp3-b) [UniParc].

Checksum: 3356FC66E6A21796
Show »

FASTA49953,411

References

« Hide 'large scale' references
[1]"Human RanBP3, a group of nuclear RanGTP binding proteins."
Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H.
FEBS Lett. 427:330-336(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CHC1.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Colon and Testis.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] OF 1-418 (ISOFORM 3).
Tissue: Eye.
[6]"RanBP3 influences interactions between CRM1 and its nuclear protein export substrates."
Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.
EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH XPO1.
[7]"Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export."
Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.
J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH XPO1.
[8]"Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor."
Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.
J. Biol. Chem. 277:17385-17388(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHC1.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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.
[11]"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-100; SER-101; SER-108; THR-124; SER-333; SER-353; SER-355 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling."
Dai F., Lin X., Chang C., Feng X.H.
Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, FUNCTION.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"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].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"Solution structure of the RAN_BP1 domain of RAN-binding protein-3."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 380-516.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08697 mRNA. Translation: CAA69956.1.
Y08698 mRNA. Translation: CAA69957.1.
AK025300 mRNA. Translation: BAB15106.1.
AK314343 mRNA. Translation: BAG36985.1.
AL050149 mRNA. Translation: CAB43293.1. Different initiation.
AC004602 Genomic DNA. Translation: AAC14485.1.
AC104532 Genomic DNA. No translation available.
AC093050 Genomic DNA. No translation available.
AC005784 Genomic DNA. No translation available.
BC004349 mRNA. Translation: AAH04349.1. Sequence problems.
PIRT08778.
RefSeqNP_003615.2. NM_003624.2.
NP_015559.2. NM_007320.2.
NP_015561.1. NM_007322.2.
UniGeneHs.531752.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRFNMR-A380-511[»]
2Y8FX-ray2.10A/B/C/D388-522[»]
2Y8GX-ray1.61A/B388-522[»]
ProteinModelPortalQ9H6Z4.
SMRQ9H6Z4. Positions 390-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114070. 37 interactions.
IntActQ9H6Z4. 7 interactions.
MINTMINT-3068756.
STRING9606.ENSP00000341483.

PTM databases

PhosphoSiteQ9H6Z4.

Polymorphism databases

DMDM51316528.

Proteomic databases

PaxDbQ9H6Z4.
PeptideAtlasQ9H6Z4.
PRIDEQ9H6Z4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000034275; ENSP00000034275; ENSG00000031823. [Q9H6Z4-3]
ENST00000340578; ENSP00000341483; ENSG00000031823. [Q9H6Z4-1]
ENST00000439268; ENSP00000404837; ENSG00000031823. [Q9H6Z4-2]
GeneID8498.
KEGGhsa:8498.
UCSCuc002mdv.3. human. [Q9H6Z4-1]
uc002mdx.3. human. [Q9H6Z4-2]
uc002mdy.3. human. [Q9H6Z4-3]

Organism-specific databases

CTD8498.
GeneCardsGC19M005916.
HGNCHGNC:9850. RANBP3.
HPAHPA043375.
HPA043389.
MIM603327. gene.
neXtProtNX_Q9H6Z4.
PharmGKBPA34211.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304969.
HOVERGENHBG061383.
InParanoidQ9H6Z4.
KOK15304.
OMATSFASPN.
OrthoDBEOG7TJ3JQ.
PhylomeDBQ9H6Z4.
TreeFamTF313181.

Enzyme and pathway databases

SignaLinkQ9H6Z4.

Gene expression databases

ArrayExpressQ9H6Z4.
BgeeQ9H6Z4.
CleanExHS_RANBP3.
GenevestigatorQ9H6Z4.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRANBP3. human.
EvolutionaryTraceQ9H6Z4.
GeneWikiRANBP3.
GenomeRNAi8498.
NextBio31793.
PROQ9H6Z4.
SOURCESearch...

Entry information

Entry nameRANB3_HUMAN
AccessionPrimary (citable) accession number: Q9H6Z4
Secondary accession number(s): B2RAT8 expand/collapse secondary AC list , O60405, O75759, O75760, Q9BT47, Q9UG74
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 109 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM