Reviewed,
UniProtKB/Swiss-Prot P50395 (GDIB_HUMAN)
Last modified
January 19, 2010.
Version 88.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Rab GDP dissociation inhibitor beta Short name=Rab GDI beta Alternative name(s): Guanosine diphosphate dissociation inhibitor 2 Short name=GDI-2 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. |
| Subunit structure | Interacts with RHOH. Ref.7 |
| Subcellular location | Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. |
| Tissue specificity | Ubiquitous. Ref.6 |
| Sequence similarities | Belongs to the Rab GDI family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Membrane |
| Molecular function | GTPase activation |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein transport Inferred from electronic annotation. Source: InterPro regulation of GTPase activityInferred from electronic annotation. Source: InterPro signal transductionTraceable author statement. Source: UniProtKB |
| Cellular component | cell surface Inferred from direct assay. Source: UniProtKB cytoplasmTraceable author statement. Source: UniProtKB extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rab GDP-dissociation inhibitor activity Ref.6Traceable author statement. Source: ProtInc protein binding Ref.7Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 445 | 445 | Rab GDP dissociation inhibitor beta | PRO_0000056679 | |||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.11 | ||||||
| Modified residue | 61 | 1 | Phosphoserine Ref.11 Ref.9 | ||||||
| Modified residue | 112 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 203 | 1 | Phosphotyrosine Ref.8 | ||||||
| Modified residue | 269 | 1 | N6-acetyllysine Ref.12 | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | N → D in BAA03095. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Asada M., Kaibuchi K., Takai Y. Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [2] | "The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13." Sedlacek Z., Munstermann E., Mincheva A., Lichter P., Poutska A. Mamm. Genome 9:78-80(1998) [PubMed: 9434952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. |
| [3] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta. |
| [5] | "Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells." Caillol N., Pasqualini E., Lloubes R., Lombardo D. J. Cell. Biochem. 79:628-647(2000) [PubMed: 10996854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-439. Tissue: Pancreas. |
| [6] | "Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport." Bachner D., Sedlacek Z., Korn B., Hameister H., Poustka A. Hum. Mol. Genet. 4:701-708(1995) [PubMed: 7543319] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [7] | "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function." Li X., Bu X., Lu B., Avraham H., Flavell R.A., Lim B. Mol. Cell. Biol. 22:1158-1171(2002) [PubMed: 11809807] [Abstract] Cited for: INTERACTION WITH RHOH. |
| [8] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, MASS SPECTROMETRY. |
| [9] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY. |
| [10] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [11] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY. |
| [12] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-269, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D13988 mRNA. Translation: BAA03095.1. Y13286 mRNA. Translation: CAA73734.1. Y13287 Y13297 Genomic DNA. Translation: CAA73735.1. BT006868 mRNA. Translation: AAP35514.1. BC005145 mRNA. Translation: AAH05145.1. AF144713 mRNA. Translation: AAD34588.1. |
| IPI | IPI00940148. |
| RefSeq | NP_001108628.1. NP_001485.2. |
| UniGene | Hs.299055 |
3D structure databases | |
| SMR | P50395. Positions 1-431. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P50395. 13 interactions. |
| STRING | P50395. |
PTM databases | |
| PhosphoSite | P50395. |
2-D gel databases | |
| OGP | P50395. |
| REPRODUCTION-2DPAGE | IPI00031461. P50395. |
Proteomic databases | |
| PRIDE | P50395. |
Genome annotation databases | |
| Ensembl | ENST00000380191; ENSP00000369538; ENSG00000057608; Homo sapiens. [Genome view] |
| GeneID | 2665. |
| KEGG | hsa:2665. |
| UCSC | uc001iil.2. human. |
Organism-specific databases | |
| CTD | 2665. |
| GeneCards | GC01P072513. GC10M005848. |
| H-InvDB | HIX0008614. |
| HGNC | HGNC:4227. GDI2. |
| MIM | 600767. gene. |
| PharmGKB | PA28642. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG18194. |
| HOVERGEN | P50395. |
| InParanoid | P50395. |
| OrthoDB | EOG947JCP. |
| PhylomeDB | P50395. |
Enzyme and pathway databases | |
| Reactome | REACT_11044. Signaling by Rho GTPases. |
Gene expression databases | |
| ArrayExpress | P50395. |
| Bgee | P50395. |
| CleanEx | HS_GDI2. |
| Genevestigator | P50395. |
| GermOnline | ENSG00000057608. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR018203. GDP_dissociation_inhibitor. IPR002005. Rab_GDI_REP. IPR000806. RabGDI. [Graphical view] |
| PANTHER | PTHR11787. Rab_GDI_REP. 1 hit. |
| Pfam | PF00996. GDI. 1 hit. [Graphical view] |
| PRINTS | PR00892. RABGDI. PR00891. RABGDIREP. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 10516. |
| SOURCE | Search... |
Entry information
| Entry name | GDIB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P50395 Secondary accession number(s): O43928, Q9UQM6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

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