Reviewed,
UniProtKB/Swiss-Prot Q15276 (RABE1_HUMAN)
Last modified
January 19, 2010.
Version 91.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Rab GTPase-binding effector protein 1 Alternative name(s): Rabaptin-5 Rabaptin-5alpha Rabaptin-4 Renal carcinoma antigen NY-REN-17 | ||||
| Gene names |
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| 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 | 862 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Ref.1 Ref.2 Ref.9 Ref.11 |
| Subunit structure | Homodimer when bound to RAB5A. Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2. Ref.19 |
| Subcellular location | Cytoplasm. Early endosome. Recycling endosome Ref.1 Ref.2 Ref.11 Ref.10. |
| Post-translational modification | Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity. |
| Sequence similarities | Belongs to the rabaptin family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GGA1 | Q9UJY5 | 4 | EBI-447043,EBI-447141 | |
| GGA2 | Q9UJY4 | 2 | EBI-447043,EBI-447646 | |
| GGA3 | Q9NZ52 | 1 | EBI-447043,EBI-447404 | |
| YWHAG | P61981 | 1 | EBI-447043,EBI-359832 | |
| YWHAQ | P27348 | 1 | EBI-447043,EBI-359854 |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q15276-1) Also known as: Rabaptin-5; 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. | ||||||
| Isoform 2 (identifier: Q15276-2) Also known as: Rabaptin-4; The sequence of this isoform differs from the canonical sequence as follows: 758-790: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||
Molecule processing | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||||||||
| Chain | 2 – 862 | 861 | Rab GTPase-binding effector protein 1 | PRO_0000187556 | |||||||||||
Regions | |||||||||||||||
| Coiled coil | 11 – 345 | 335 | Potential | ||||||||||||
| Coiled coil | 534 – 816 | 283 | Potential | ||||||||||||
Amino acid modifications | |||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.16 | ||||||||||||
| Modified residue | 282 | 1 | N6-acetyllysine Ref.18 | ||||||||||||
| Modified residue | 407 | 1 | Phosphoserine Ref.16 Ref.12 Ref.14 Ref.17 | ||||||||||||
| Modified residue | 408 | 1 | Phosphothreonine Ref.16 Ref.13 | ||||||||||||
| Modified residue | 410 | 1 | Phosphoserine Ref.16 Ref.14 Ref.13 | ||||||||||||
Natural variations | |||||||||||||||
| Alternative sequence | 758 – 790 | 33 | Missing in isoform 2. | VSP_010451 | |||||||||||
| Natural variant | 640 | 1 | E → G: dbSNP rs3026099. | VAR_028106 | |||||||||||
Experimental info | |||||||||||||||
| Mutagenesis | 812 | 1 | D → K: No effect on RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 815 | 1 | E → K: No effect on RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 818 | 1 | Q → W: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 820 | 1 | D → K: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 821 | 1 | F → R: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 822 | 1 | V → D: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 826 | 1 | Q → A: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Mutagenesis | 829 | 1 | Q → A: Strongly decreases RAB5A binding affinty. Ref.19 | ||||||||||||
| Sequence conflict | 149 | 1 | S → Y Ref.1 | ||||||||||||
| Sequence conflict | 149 | 1 | S → Y Ref.2 | ||||||||||||
Secondary structure | |||||||||||||||
Helix Strand Turn | |||||||||||||||
| Helix | 553 – 639 | 87 | |||||||||||||
| Helix | 805 – 836 | 32 | |||||||||||||
| Helix | 841 – 847 | 7 | |||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion." Stenmark H., Vitale G., Ulrich O., Zerial M. Cell 83:423-432(1995) [PubMed: 8521472] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A. Tissue: Cervix carcinoma. |
| [2] | "Rabaptin4, a novel effector of the samll GTPase rab4a, is recruited to perinuclear recycling vesicles." Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K., van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P. Biochem. J. 346:593-601(2000) [PubMed: 10698684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB4A AND RAB5A. Tissue: Cervix carcinoma. |
| [3] | "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] (ISOFORM 1). Tissue: Testis. |
| [4] | Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 807-819, MASS SPECTROMETRY. Tissue: Fetal brain cortex. |
| [5] | "A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function." Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M. Cell 90:1149-1159(1997) [PubMed: 9323142] [Abstract] Cited for: INTERACTION WITH RABGEF1. |
| [6] | "Cleavage of rabaptin-5 blocks endosome fusion during apoptosis." Cosulich S.C., Horiuchi H., Zerial M., Clarke P.R., Woodman P.G. EMBO J. 16:6182-6191(1997) [PubMed: 9321397] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE BY CASPASES IN APOPTOTIC CELLS. |
| [7] | "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis." Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S. J. Biol. Chem. 272:6097-6100(1997) [PubMed: 9045618] [Abstract] Cited for: INTERACTION WITH TSC2. |
| [8] | "Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma. |
| [9] | "Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex." Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M. Mol. Biol. Cell 12:2219-2228(2001) [PubMed: 11452015] [Abstract] Cited for: FUNCTION, INTERACTION WITH RABGEF1. |
| [10] | "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex." Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S. EMBO J. 22:78-88(2003) [PubMed: 12505986] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, SUBCELLULAR LOCATION. |
| [11] | "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes." Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., Klumperman J., Schu P., van der Sluijs P. EMBO J. 22:2645-2657(2003) [PubMed: 12773381] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAB4A AND AP1G1, SUBCELLULAR LOCATION. |
| [12] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Epithelium. |
| [13] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-408 AND SER-410, MASS SPECTROMETRY. Tissue: Platelet. |
| [14] | "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-407 AND SER-410, MASS SPECTROMETRY. |
| [15] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [16] | "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 ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; THR-408 AND SER-410, MASS SPECTROMETRY. |
| [17] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: T-cell. |
| [18] | "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-282, MASS SPECTROMETRY. |
| [19] | "Structural basis of Rab5-Rabaptin5 interaction in endocytosis." Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C. Nat. Struct. Mol. Biol. 11:975-983(2004) [PubMed: 15378032] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 789-862 IN COMPLEX WITH RAB5A, SUBUNIT, MUTAGENESIS OF ASP-812; GLU-815; GLN-818; ASO-820; PHE-821; VAL-822; GLN-826 AND GLN-829. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X91141 mRNA. Translation: CAA62580.1. AF098638 mRNA. Translation: AAC70781.1. BC041700 mRNA. Translation: AAH41700.1. | ||||||||||||||||||
| IPI | IPI00293009. IPI00412712. | ||||||||||||||||||
| RefSeq | NP_001077054.1. NP_004694.2. | ||||||||||||||||||
| UniGene | Hs.584784 Hs.592121 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-29350N. | ||||||||||||||||||
| IntAct | Q15276. 11 interactions. | ||||||||||||||||||
| STRING | Q15276. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q15276. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q15276. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000262477; ENSP00000262477; ENSG00000029725; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 9135. | ||||||||||||||||||
| KEGG | hsa:9135. | ||||||||||||||||||
| NMPDR | fig|9606.3.peg.12951. | ||||||||||||||||||
| UCSC | uc002gbl.2. human. uc002gbm.2. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 9135. | ||||||||||||||||||
| GeneCards | GC17P005127. | ||||||||||||||||||
| H-InvDB | HIX0013466. | ||||||||||||||||||
| HGNC | HGNC:17677. RABEP1. | ||||||||||||||||||
| HPA | CAB004549. HPA019669. HPA024235. HPA024691. | ||||||||||||||||||
| MIM | 603616. gene. | ||||||||||||||||||
| PharmGKB | PA134884097. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | prNOG19092. | ||||||||||||||||||
| HOGENOM | HBG402862. | ||||||||||||||||||
| HOVERGEN | Q15276. | ||||||||||||||||||
| InParanoid | Q15276. | ||||||||||||||||||
| OMA | EIENCKE. | ||||||||||||||||||
| OrthoDB | EOG9G4K9B. | ||||||||||||||||||
| PhylomeDB | Q15276. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q15276. | ||||||||||||||||||
| Bgee | Q15276. | ||||||||||||||||||
| CleanEx | HS_RABEP1. | ||||||||||||||||||
| Genevestigator | Q15276. | ||||||||||||||||||
| GermOnline | ENSG00000029725. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003914. Rabaptin. IPR018514. Rabaptin_coiled-coil. IPR015390. Rabaptin_Rab5-bd. [Graphical view] | ||||||||||||||||||
| Pfam | PF09311. Rab5-bind. 1 hit. PF03528. Rabaptin. 2 hits. [Graphical view] | ||||||||||||||||||
| PRINTS | PR01432. RABAPTIN. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 34253. | ||||||||||||||||||
| PMAP-CutDB | Q15276. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | RABE1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q15276 Secondary accession number(s): O95369, Q8IVX3 | ||||||||
| 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 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


