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Q6VN20 (RBP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ran-binding protein 10

Short name=RanBP10
Gene names
Name:RANBP10
Synonyms:KIAA1464
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length620 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 guanine nucleotide exchange factor (GEF) for RAN GTPase By similarity. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function By similarity. May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway. Ref.4

Subunit structure

May form homodimers. Interacts with RAN and RANBP9. Interacts with the HGF receptor MET. Interacts with AR. Interacts with TUBB1. May interact with TUBB5 By similarity. Ref.1 Ref.4 Ref.5

Subcellular location

Cytoplasmcytosol. Nucleus. Note: Predominantly cytoplasmic. Ref.4

Tissue specificity

Broadly expressed, with highest levels in skeletal muscle. Ref.1

Domain

The SPRY domain mediates the interaction with MET By similarity.

Sequence similarities

Belongs to the RANBP9/10 family.

Contains 1 B30.2/SPRY domain.

Contains 1 CTLH domain.

Contains 1 LisH domain.

Sequence caution

The sequence BAA95988.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 620619Ran-binding protein 10
PRO_0000305237

Regions

Domain35 – 222188B30.2/SPRY
Domain253 – 28533LisH
Domain291 – 34858CTLH
Compositional bias346 – 453108Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.11
Modified residue3651Phosphoserine Ref.6 Ref.8
Modified residue3691Phosphoserine Ref.6 Ref.8 Ref.10

Experimental info

Sequence conflict2231L → P in AAH99917. Ref.3
Sequence conflict4551M → V in AAH99917. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6VN20 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 66744ADBCB36D308

FASTA62067,257
        10         20         30         40         50         60 
MAAATADPGA GNPQPGDSSG GGAGGGLPSP GEQELSRRLQ RLYPAVNQQE TPLPRSWSPK 

        70         80         90        100        110        120 
DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI 

       130        140        150        160        170        180 
GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC 

       190        200        210        220        230        240 
FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT 

       250        260        270        280        290        300 
VHCFPISARL GEWQAVLQNM VSSYLVHHGY CATATAFARM TETPIQEEQA SIKNRQKIQK 

       310        320        330        340        350        360 
LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD 

       370        380        390        400        410        420 
SYPGSPSLSP RHGPSSSHMH NTGADSPSCS NGVASTKSKQ NHSKYPAPSS SSSSSSSSSS 

       430        440        450        460        470        480 
SSPSSVNYSE SNSTDSTKSQ HHSSTSNQET SDSEMEMEAE HYPNGVLGSM STRIVNGAYK 

       490        500        510        520        530        540 
HEDLQTDESS MDDRHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ 

       550        560        570        580        590        600 
DAFSLLAYSD PWSCPVGQQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR 

       610        620 
LMARAGLGSC SFARVDDYLH 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH RAN AND MET.
[2]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[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].
Tissue: Placenta.
[4]"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, HOMODIMERIZATION, INTERACTION WITH AR AND RANBP9, SUBCELLULAR LOCATION.
[5]"RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUBB1.
[6]"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-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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].
[10]"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-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY337313 mRNA. Translation: AAR01220.1.
AB040897 mRNA. Translation: BAA95988.1. Different initiation.
BC099917 mRNA. Translation: AAH99917.1.
BC121176 mRNA. Translation: AAI21177.1.
BC121177 mRNA. Translation: AAI21178.1.
RefSeqNP_065901.1. NM_020850.1.
UniGeneHs.368569.

3D structure databases

ProteinModelPortalQ6VN20.
SMRQ6VN20. Positions 63-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121657. 13 interactions.
IntActQ6VN20. 5 interactions.
STRING9606.ENSP00000316589.

PTM databases

PhosphoSiteQ6VN20.

Polymorphism databases

DMDM74710336.

Proteomic databases

PaxDbQ6VN20.
PRIDEQ6VN20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317506; ENSP00000316589; ENSG00000141084.
GeneID57610.
KEGGhsa:57610.
UCSCuc002eud.3. human.

Organism-specific databases

CTD57610.
GeneCardsGC16M067757.
H-InvDBHIX0013157.
HGNCHGNC:29285. RANBP10.
HPAHPA045523.
MIM614031. gene.
neXtProtNX_Q6VN20.
PharmGKBPA134929520.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316575.
HOGENOMHOG000008133.
HOVERGENHBG053444.
InParanoidQ6VN20.
OMAYKGHGKN.
OrthoDBEOG76MK7Z.
PhylomeDBQ6VN20.
TreeFamTF331658.

Gene expression databases

ArrayExpressQ6VN20.
BgeeQ6VN20.
CleanExHS_RANBP10.
GenevestigatorQ6VN20.

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

GenomeRNAi57610.
NextBio64259.
PROQ6VN20.
SOURCESearch...

Entry information

Entry nameRBP10_HUMAN
AccessionPrimary (citable) accession number: Q6VN20
Secondary accession number(s): A4FTY2, Q9P264
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 83 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 16

Human chromosome 16: entries, gene names and cross-references to MIM