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Protein

Ran-specific GTPase-activating protein

Gene

RANBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • GDP-dissociation inhibitor activity Source: ProtInc
  • GTPase activator activity Source: UniProtKB-KW
  • Ran GTPase binding Source: ProtInc

GO - Biological processi

  • intracellular transport Source: InterPro
  • regulation of catalytic activity Source: GOC
  • signal transduction Source: UniProtKB
  • viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_6190. Rev-mediated nuclear export of HIV RNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-specific GTPase-activating protein
Alternative name(s):
Ran-binding protein 1
Short name:
RanBP1
Gene namesi
Name:RANBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9847. RANBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34206.

Polymorphism and mutation databases

BioMutaiRANBP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Ran-specific GTPase-activating proteinPRO_0000213667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei13 – 131Phosphothreonine1 Publication
Modified residuei18 – 181Phosphothreonine1 Publication
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei60 – 601Phosphoserine2 Publications
Modified residuei150 – 1501N6-acetyllysine; alternate1 Publication
Modified residuei150 – 1501N6-succinyllysine; alternateBy similarity
Modified residuei183 – 1831N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP43487.
PaxDbiP43487.
PeptideAtlasiP43487.
PRIDEiP43487.

2D gel databases

DOSAC-COBS-2DPAGEP43487.
OGPiP43487.
REPRODUCTION-2DPAGEIPI00414127.

PTM databases

PhosphoSiteiP43487.

Expressioni

Gene expression databases

BgeeiP43487.
CleanExiHS_RANBP1.
ExpressionAtlasiP43487. baseline and differential.
GenevisibleiP43487. HS.

Organism-specific databases

HPAiCAB046463.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MPGP293721EBI-1032909,EBI-1043398

Protein-protein interaction databases

BioGridi111838. 23 interactions.
DIPiDIP-35058N.
IntActiP43487. 8 interactions.
MINTiMINT-1584597.
STRINGi9606.ENSP00000327583.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 5811Combined sources
Beta strandi67 – 7913Combined sources
Beta strandi81 – 833Combined sources
Beta strandi86 – 927Combined sources
Turni93 – 953Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi117 – 12711Combined sources
Beta strandi134 – 1418Combined sources
Helixi145 – 16521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5DX-ray2.70B/E/H/K1-201[»]
1K5GX-ray3.10B/E/H/K1-201[»]
ProteinModelPortaliP43487.
SMRiP43487. Positions 22-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 164139RanBD1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RANBP1 family.Curated
Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00720000108825.
HOGENOMiHOG000176323.
HOVERGENiHBG006958.
InParanoidiP43487.
KOiK15306.
PhylomeDBiP43487.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P43487-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK
60 70 80 90 100
MRAKLFRFAS ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA
110 120 130 140 150
NHYITPMMEL KPNAGSDRAW VWNTHADFAD ECPKPELLAI RFLNAENAQK
160 170 180 190 200
FKTKFEECRK EIEEREKKAG SGKNDHAEKV AEKLEALSVK EETKEDAEEK

Q
Length:201
Mass (Da):23,310
Last modified:November 1, 1995 - v1
Checksum:i05FC9B35DADA48C9
GO
Isoform 2 (identifier: P43487-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-169: Missing.

Show »
Length:200
Mass (Da):23,239
Checksum:i11E4114E1392C43D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611E → V in BAD97226 (PubMed:10591208).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036567
Natural varianti145 – 1451A → V.
Corresponds to variant rs5746863 [ dbSNP | Ensembl ].
VAR_053629

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 1691Missing in isoform 2. 2 PublicationsVSP_055104

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83617 mRNA. Translation: CAA58592.1.
D38076 mRNA. Translation: BAA07269.1.
CR456556 mRNA. Translation: CAG30442.1.
AK223506 mRNA. Translation: BAD97226.1.
AC006547 Genomic DNA. No translation available.
CCDSiCCDS13775.1. [P43487-1]
CCDS63408.1. [P43487-2]
PIRiS54290.
RefSeqiNP_001265568.1. NM_001278639.1.
NP_001265569.1. NM_001278640.1. [P43487-2]
NP_002873.1. NM_002882.3. [P43487-1]
UniGeneiHs.24763.

Genome annotation databases

EnsembliENST00000331821; ENSP00000327583; ENSG00000099901.
ENST00000402752; ENSP00000384925; ENSG00000099901. [P43487-2]
GeneIDi5902.
KEGGihsa:5902.
UCSCiuc002zro.1. human. [P43487-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83617 mRNA. Translation: CAA58592.1.
D38076 mRNA. Translation: BAA07269.1.
CR456556 mRNA. Translation: CAG30442.1.
AK223506 mRNA. Translation: BAD97226.1.
AC006547 Genomic DNA. No translation available.
CCDSiCCDS13775.1. [P43487-1]
CCDS63408.1. [P43487-2]
PIRiS54290.
RefSeqiNP_001265568.1. NM_001278639.1.
NP_001265569.1. NM_001278640.1. [P43487-2]
NP_002873.1. NM_002882.3. [P43487-1]
UniGeneiHs.24763.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5DX-ray2.70B/E/H/K1-201[»]
1K5GX-ray3.10B/E/H/K1-201[»]
ProteinModelPortaliP43487.
SMRiP43487. Positions 22-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111838. 23 interactions.
DIPiDIP-35058N.
IntActiP43487. 8 interactions.
MINTiMINT-1584597.
STRINGi9606.ENSP00000327583.

PTM databases

PhosphoSiteiP43487.

Polymorphism and mutation databases

BioMutaiRANBP1.

2D gel databases

DOSAC-COBS-2DPAGEP43487.
OGPiP43487.
REPRODUCTION-2DPAGEIPI00414127.

Proteomic databases

MaxQBiP43487.
PaxDbiP43487.
PeptideAtlasiP43487.
PRIDEiP43487.

Protocols and materials databases

DNASUi5902.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331821; ENSP00000327583; ENSG00000099901.
ENST00000402752; ENSP00000384925; ENSG00000099901. [P43487-2]
GeneIDi5902.
KEGGihsa:5902.
UCSCiuc002zro.1. human. [P43487-1]

Organism-specific databases

CTDi5902.
GeneCardsiGC22P020103.
HGNCiHGNC:9847. RANBP1.
HPAiCAB046463.
MIMi601180. gene.
neXtProtiNX_P43487.
PharmGKBiPA34206.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00720000108825.
HOGENOMiHOG000176323.
HOVERGENiHBG006958.
InParanoidiP43487.
KOiK15306.
PhylomeDBiP43487.

Enzyme and pathway databases

ReactomeiREACT_6190. Rev-mediated nuclear export of HIV RNA.

Miscellaneous databases

ChiTaRSiRANBP1. human.
EvolutionaryTraceiP43487.
GeneWikiiRANBP1.
GenomeRNAii5902.
NextBioi22960.
PROiP43487.
SOURCEiSearch...

Gene expression databases

BgeeiP43487.
CleanExiHS_RANBP1.
ExpressionAtlasiP43487. baseline and differential.
GenevisibleiP43487. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 2).
    Tissue: Blood.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Coronary arterial endothelium.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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].
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-16.

Entry informationi

Entry nameiRANG_HUMAN
AccessioniPrimary (citable) accession number: P43487
Secondary accession number(s): Q53EY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.