P43487 (RANG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ran-specific GTPase-activating protein

Alternative name(s):
Ran-binding protein 1
Short name=RanBP1

Gene names

Name:

RANBP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular transport Inferred from electronic annotation. Source: InterPro positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC positive regulation of mitotic centrosome separation Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 16130169. Source: UniProtKB spindle organization Inferred from electronic annotation. Source: Compara viral reproduction Traceable author statement. Source: Reactome
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB nuclear envelope Traceable author statement. Source: Reactome
Molecular_function	GDP-dissociation inhibitor activity Traceable author statement Ref.2. Source: ProtInc GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Ran GTPase binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MPG	P29372	1	EBI-1032909,EBI-1043398

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Ran-specific GTPase-activating protein

PRO_0000213667

Regions

Domain

26 – 164

139

RanBD1

Amino acid modifications

Modified residue

13

1

Phosphothreonine Ref.4

Modified residue

18

1

Phosphothreonine Ref.4

Modified residue

21

1

Phosphoserine Ref.4

Modified residue

60

1

Phosphoserine Ref.9

Modified residue

150

1

N6-acetyllysine Ref.6

Modified residue

183

1

N6-acetyllysine Ref.6

Natural variations

Natural variant

16

1

E → D in a breast cancer sample; somatic mutation. Ref.10

VAR_036567

Natural variant

145

1

A → V.
Corresponds to variant rs5746863 [ dbSNP | Ensembl ].

VAR_053629

Experimental info

Sequence conflict

169

1

Missing in BAA07269. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

201

Helix Strand Turn

Details...

Beta strand

48 – 58

11

Beta strand

67 – 79

13

Beta strand

81 – 83

3

Beta strand

86 – 92

7

Turn

93 – 95

3

Beta strand

98 – 103

6

Beta strand

117 – 127

11

Beta strand

134 – 141

8

Helix

145 – 165

21

Sequences

	Sequence		Length	Mass (Da)
	P43487 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 05FC9B35DADA48C9	FASTA	201	23,310
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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.
[6]	"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, MASS SPECTROMETRY.
[7]	"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.
[8]	"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].
[9]	"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, MASS SPECTROMETRY.
[10]	"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. , 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.

IPI

IPI00414127.

PIR

S54290.

RefSeq

NP_002873.1. NM_002882.2.

UniGene

Hs.24763.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P43487.

ModBase

Search...

Protein-protein interaction databases

IntAct

P43487. 6 interactions.

MINT

MINT-1584597.

STRING

9606.ENSP00000327583.

PTM databases

PhosphoSite

P43487.

Polymorphism databases

DMDM

1172837.

2D gel databases

DOSAC-COBS-2DPAGE

P43487.

OGP

P43487.

REPRODUCTION-2DPAGE

IPI00414127.

Proteomic databases

PaxDb

P43487.

PeptideAtlas

P43487.

PRIDE

P43487.

Protocols and materials databases

DNASU

5902.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331821; ENSP00000327583; ENSG00000099901.
ENST00000402752; ENSP00000384925; ENSG00000099901.

GeneID

5902.

KEGG

hsa:5902.

UCSC

uc002zro.1. human.

Organism-specific databases

CTD

5902.

GeneCards

GC22P020103.

HGNC

HGNC:9847. RANBP1.

HPA

CAB046463.

MIM

601180. gene.

neXtProt

NX_P43487.

PharmGKB

PA34206.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5171.

HOGENOM

HOG000176323.

HOVERGEN

HBG006958.

InParanoid

P43487.

KO

K15306.

OMA

HEDRDTT.

OrthoDB

EOG4XD3S8.

PhylomeDB

P43487.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

P43487.

Bgee

P43487.

CleanEx

HS_RANBP1.

Genevestigator

P43487.

GermOnline

ENSG00000099901. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]

Pfam

PF00638. Ran_BP1. 1 hit.
[Graphical view]

SMART

SM00160. RanBD. 1 hit.
[Graphical view]

PROSITE

PS50196. RANBD1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RANBP1. human.

EvolutionaryTrace

P43487.

GenomeRNAi

5902.

NextBio

22960.

SOURCE

Search...

Entry information

Entry name

RANG_HUMAN

Accession

Primary (citable) accession number: P43487

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.