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P43487

- RANG_HUMAN

UniProt

P43487 - RANG_HUMAN

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Protein

Ran-specific GTPase-activating protein

Gene
RANBP1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. GDP-dissociation inhibitor activity Source: ProtInc
  2. GTPase activator activity Source: UniProtKB-KW
  3. Ran GTPase binding Source: ProtInc

GO - Biological processi

  1. intracellular transport Source: InterPro
  2. positive regulation of mitotic centrosome separation Source: Ensembl
  3. regulation of catalytic activity Source: GOC
  4. signal transduction Source: UniProtKB
  5. spindle organization Source: Ensembl
  6. 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: Chromosome 22

Organism-specific databases

HGNCiHGNC:9847. RANBP1.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. nuclear envelope Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34206.

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 – 601Phosphoserine1 Publication
Modified residuei150 – 1501N6-acetyllysine; alternate1 Publication
Modified residuei150 – 1501N6-succinyllysine; alternate By 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

ArrayExpressiP43487.
BgeeiP43487.
CleanExiHS_RANBP1.
GenevestigatoriP43487.

Organism-specific databases

HPAiCAB046463.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111838. 25 interactions.
IntActiP43487. 7 interactions.
MINTiMINT-1584597.
STRINGi9606.ENSP00000327583.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP43487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 164139RanBD1Add
BLAST

Sequence similaritiesi

Belongs to the RANBP1 family.
Contains 1 RanBD1 domain.

Phylogenomic databases

eggNOGiCOG5171.
HOGENOMiHOG000176323.
HOVERGENiHBG006958.
InParanoidiP43487.
KOiK15306.
OMAiPGKNDNA.
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. Align

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

MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK    50
MRAKLFRFAS ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA 100
NHYITPMMEL KPNAGSDRAW VWNTHADFAD ECPKPELLAI RFLNAENAQK 150
FKTKFEECRK EIEEREKKAG SGKNDHAEKV AEKLEALSVK EETKEDAEEK 200
Q 201
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

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. VSP_055104

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611E → V in BAD97226. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
PIRiS54290.
RefSeqiNP_001265568.1. NM_001278639.1.
NP_001265569.1. NM_001278640.1.
NP_002873.1. NM_002882.3.
UniGeneiHs.24763.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS13775.1. [P43487-1 ]
PIRi S54290.
RefSeqi NP_001265568.1. NM_001278639.1.
NP_001265569.1. NM_001278640.1.
NP_002873.1. NM_002882.3.
UniGenei Hs.24763.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K5D X-ray 2.70 B/E/H/K 1-201 [» ]
1K5G X-ray 3.10 B/E/H/K 1-201 [» ]
ProteinModelPortali P43487.
SMRi P43487. Positions 22-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111838. 25 interactions.
IntActi P43487. 7 interactions.
MINTi MINT-1584597.
STRINGi 9606.ENSP00000327583.

PTM databases

PhosphoSitei P43487.

2D gel databases

DOSAC-COBS-2DPAGE P43487.
OGPi P43487.
REPRODUCTION-2DPAGE IPI00414127.

Proteomic databases

MaxQBi P43487.
PaxDbi P43487.
PeptideAtlasi P43487.
PRIDEi P43487.

Protocols and materials databases

DNASUi 5902.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331821 ; ENSP00000327583 ; ENSG00000099901 .
ENST00000402752 ; ENSP00000384925 ; ENSG00000099901 .
GeneIDi 5902.
KEGGi hsa:5902.
UCSCi uc002zro.1. human. [P43487-1 ]

Organism-specific databases

CTDi 5902.
GeneCardsi GC22P020103.
HGNCi HGNC:9847. RANBP1.
HPAi CAB046463.
MIMi 601180. gene.
neXtProti NX_P43487.
PharmGKBi PA34206.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5171.
HOGENOMi HOG000176323.
HOVERGENi HBG006958.
InParanoidi P43487.
KOi K15306.
OMAi PGKNDNA.
PhylomeDBi P43487.

Enzyme and pathway databases

Reactomei REACT_6190. Rev-mediated nuclear export of HIV RNA.

Miscellaneous databases

ChiTaRSi RANBP1. human.
EvolutionaryTracei P43487.
GeneWikii RANBP1.
GenomeRNAii 5902.
NextBioi 22960.
PROi P43487.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43487.
Bgeei P43487.
CleanExi HS_RANBP1.
Genevestigatori P43487.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view ]
Pfami PF00638. Ran_BP1. 1 hit.
[Graphical view ]
SMARTi SM00160. RanBD. 1 hit.
[Graphical view ]
PROSITEi PS50196. RANBD1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: September 3, 2014
This is version 133 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

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