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P43487 (RANG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ran-specific GTPase-activating protein
Alternative name(s):
Ran-binding protein 1
Short name=RanBP1
Gene names
Name:RANBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Sequence similarities

Belongs to the RANBP1 family.

Contains 1 RanBD1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPGP293721EBI-1032909,EBI-1043398

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 201200Ran-specific GTPase-activating protein
PRO_0000213667

Regions

Domain26 – 164139RanBD1

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue131Phosphothreonine Ref.4
Modified residue181Phosphothreonine Ref.4
Modified residue211Phosphoserine Ref.4
Modified residue601Phosphoserine Ref.10
Modified residue1501N6-acetyllysine; alternate
Modified residue1501N6-succinyllysine; alternate By similarity
Modified residue1831N6-acetyllysine Ref.7

Natural variations

Natural variant161E → D in a breast cancer sample; somatic mutation. Ref.11
VAR_036567
Natural variant1451A → V.
Corresponds to variant rs5746863 [ dbSNP | Ensembl ].
VAR_053629

Experimental info

Sequence conflict1691Missing in BAA07269. Ref.2

Secondary structure

.................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43487 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 05FC9B35DADA48C9

FASTA20123,310
        10         20         30         40         50         60 
MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS 

        70         80         90        100        110        120 
ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW 

       130        140        150        160        170        180 
VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKAG SGKNDHAEKV 

       190        200 
AEKLEALSVK EETKEDAEEK Q 

« Hide

References

« Hide 'large scale' references
[1]"Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1."
Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H.
EMBO J. 14:705-715(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4."
Hayashi N., Yokoyama N., Seki T., Azuma Y., Ohba T., Nishimoto T.
Mol. Gen. Genet. 247:661-669(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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 THR-13; THR-18 AND SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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].
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"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-150 AND LYS-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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.
[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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83617 mRNA. Translation: CAA58592.1.
D38076 mRNA. Translation: BAA07269.1.
CR456556 mRNA. Translation: CAG30442.1.
PIRS54290.
RefSeqNP_001265568.1. NM_001278639.1.
NP_001265569.1. NM_001278640.1.
NP_002873.1. NM_002882.3.
UniGeneHs.24763.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5DX-ray2.70B/E/H/K1-201[»]
1K5GX-ray3.10B/E/H/K1-201[»]
ProteinModelPortalP43487.
SMRP43487. Positions 22-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111838. 24 interactions.
IntActP43487. 7 interactions.
MINTMINT-1584597.
STRING9606.ENSP00000327583.

PTM databases

PhosphoSiteP43487.

Polymorphism databases

DMDM1172837.

2D gel databases

DOSAC-COBS-2DPAGEP43487.
OGPP43487.
REPRODUCTION-2DPAGEIPI00414127.

Proteomic databases

PaxDbP43487.
PeptideAtlasP43487.
PRIDEP43487.

Protocols and materials databases

DNASU5902.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331821; ENSP00000327583; ENSG00000099901.
ENST00000402752; ENSP00000384925; ENSG00000099901.
GeneID5902.
KEGGhsa:5902.
UCSCuc002zro.1. human.

Organism-specific databases

CTD5902.
GeneCardsGC22P020103.
HGNCHGNC:9847. RANBP1.
HPACAB046463.
MIM601180. gene.
neXtProtNX_P43487.
PharmGKBPA34206.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5171.
HOGENOMHOG000176323.
HOVERGENHBG006958.
InParanoidP43487.
KOK15306.
OMAENELPEW.
PhylomeDBP43487.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP43487.
BgeeP43487.
CleanExHS_RANBP1.
GenevestigatorP43487.

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

ChiTaRSRANBP1. human.
EvolutionaryTraceP43487.
GeneWikiRANBP1.
GenomeRNAi5902.
NextBio22960.
PROP43487.
SOURCESearch...

Entry information

Entry nameRANG_HUMAN
AccessionPrimary (citable) accession number: P43487
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 129 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 22

Human chromosome 22: entries, gene names and cross-references to MIM