Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62820 (RAB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-1A
Alternative name(s):
YPT1-related protein
Gene names
Name:RAB1A
Synonyms:RAB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport. Ref.14 Ref.15 Ref.17 Ref.25

Subunit structure

May interact with YIPF5. Interacts with C9orf72 By similarity. Interacts with GDI1; this promotes dissociation from membranes. Interacts with L.pneumophila AnkX, LidA and Lem3. Interacts with L.pneumophila and L.drancourtii LepB; this enhances RAB1A GTPase activity. Interacts with L.pneumophila DrrA; this disrupts the interaction between RAB1A and GDI1 and promotes the exchange of RAB1A-bound GDP with GTP. Interacts with E.coli EspG and S.flexneri VirA; this impairs ER to Golgi trafficking and protein secretion. Identified in a complex composed of RAB1A, ARF6 and E.coli EspG. Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Subcellular location

Golgi apparatus. Endoplasmic reticulum. Early endosome. Cytoplasmcytosol. Membrane. Melanosome By similarity. Note: Alternates between membrane-associated and cytosolic forms. Ref.17 Ref.21 Ref.23 Ref.25

Post-translational modification

Phosphorylated by CDK1 kinase during mitosis. Ref.10 Ref.18 Ref.19

Phosphocholinated at Ser-79 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processAutophagy
ER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from mutant phenotype Ref.25. Source: UniProtKB

GTP catabolic process

Inferred from direct assay Ref.25. Source: UniProtKB

autophagic vacuole assembly

Inferred from mutant phenotype Ref.25. Source: UniProtKB

autophagy

Inferred from mutant phenotype Ref.25. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.15. Source: UniProtKB

defense response to bacterium

Inferred from mutant phenotype Ref.25. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.17. Source: UniProtKB

growth hormone secretion

Inferred from mutant phenotype Ref.25. Source: UniProtKB

interleukin-8 secretion

Inferred from mutant phenotype Ref.25. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle transport along microtubule

Inferred from mutant phenotype Ref.17. Source: UniProtKB

vesicle-mediated transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.25. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15186776. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

drrAQ5ZSQ37EBI-716845,EBI-7632432From a different organism.
OCRLQ019687EBI-716845,EBI-6148898

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62820-1)

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: P62820-2)

The sequence of this isoform differs from the canonical sequence as follows:
     33-96: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P62820-3)

The sequence of this isoform differs from the canonical sequence as follows:
     65-140: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 205204Ras-related protein Rab-1A
PRO_0000121056

Regions

Nucleotide binding18 – 269GTP
Nucleotide binding36 – 438GTP
Nucleotide binding66 – 705GTP By similarity
Nucleotide binding124 – 1274GTP
Nucleotide binding154 – 1563GTP
Motif40 – 489Effector region By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue791O-(2-cholinephosphoryl)serine; by Legionella AnkX
Modified residue1941Phosphoserine; by CDK1 Probable
Lipidation2041S-geranylgeranyl cysteine Ref.11
Lipidation2051S-geranylgeranyl cysteine Ref.11

Natural variations

Alternative sequence33 – 9664Missing in isoform 2.
VSP_005525
Alternative sequence65 – 14076Missing in isoform 3.
VSP_005526

Experimental info

Mutagenesis1241N → I: Dominant negative mutant. Strongly reduces the levels of CASR present at the cell-surface. Ref.14

Secondary structure

................................. 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B2A8F4E3B0FB17D6

FASTA20522,678
        10         20         30         40         50         60 
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI 

        70         80         90        100        110        120 
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL 

       130        140        150        160        170        180 
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA 

       190        200 
TAGGAEKSNV KIQSTPVKQS GGGCC 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 620F588CA34B3A77
Show »

FASTA14115,331
Isoform 3 [UniParc] [UniParc].

Checksum: 8325012BF5161AFE
Show »

FASTA12913,903

References

« Hide 'large scale' references
[1]"The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
Zahraoui A., Touchot N., Chardin P., Tavitian A.
J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[9]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-30; 52-58; 62-72; 75-111; 176-187 AND 192-198, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[10]"Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2."
Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.
Nature 350:715-718(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CDK1.
[11]"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-204 AND CYS-205, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Rab GTPases as coordinators of vesicle traffic."
Stenmark H.
Nat. Rev. Mol. Cell Biol. 10:513-525(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"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.
[14]"Rab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor."
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.
Endocrinology 151:5114-5123(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASN-124.
[15]"Regulation of integrin beta 1 recycling to lipid rafts by Rab1a to promote cell migration."
Wang C., Yoo Y., Fan H., Kim E., Guan K.L., Guan J.L.
J. Biol. Chem. 285:29398-29405(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"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].
[17]"Proteomic analysis of endocytic vesicles: Rab1a regulates motility of early endocytic vesicles."
Mukhopadhyay A., Nieves E., Che F.Y., Wang J., Jin L., Murray J.W., Gordon K., Angeletti R.H., Wolkoff A.W.
J. Cell Sci. 124:765-775(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Modulation of Rab GTPase function by a protein phosphocholine transferase."
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX, PHOSPHORYLATION AT SER-79.
[19]"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination."
Tan Y., Arnold R.J., Luo Z.Q.
Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA LEM3, PHOSPHORYLATION AT SER-79.
[20]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy."
Kirsten M.L., Baron R.A., Seabra M.C., Ces O.
Mol. Membr. Biol. 30:303-314(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GDI1.
[22]"Crystal structure of human RAB1A in complex with GDP."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 6-177 IN COMPLEX WITH GDP.
[23]"Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA."
Suh H.Y., Lee D.W., Lee K.H., Ku B., Choi S.J., Woo J.S., Kim Y.G., Oh B.H.
EMBO J. 29:496-504(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 4-178 OF MUTANT ILE-124 IN COMPLEX WITH L.PNEUMOPHILA DRRA, GTP-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA.
[24]"Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA."
Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F.
Proc. Natl. Acad. Sci. U.S.A. 107:4699-4704(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-177 IN COMPLEX WITH L.PNEUMOPHILA DRRA, INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA.
[25]"Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses."
Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.
Cell 150:1029-1041(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-176 IN COMPLEXES WITH GDP; ARF6; E.COLI ESPG AND S.FLEXNERI VIRA, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ARF6 AND E.COLI ESPG, INTERACTION WITH E.COLI ESPG AND S.FLEXNERI VIRA.
[26]"Structural insights into a unique Legionella pneumophila effector LidA recognizing both GDP and GTP bound Rab1 in their active state."
Cheng W., Yin K., Lu D., Li B., Zhu D., Chen Y., Zhang H., Xu S., Chai J., Gu L.
PLoS Pathog. 8:E1002528-E1002528(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-176 IN COMPLEXES WITH GTP; GDP AND L.PNEUMOPHILA LIDA, INTERACTION WITH L.PNEUMOPHILA LIDA.
[27]"Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP."
Yu Q., Hu L., Yao Q., Zhu Y., Dong N., Wang D.C., Shao F.
Cell Res. 23:775-787(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP AND L.DRANCOURTII LEPB, INTERACTION WITH L.PNEUMOPHILA AND L.DRANCOURTII LEPB.
[28]"The Legionella pneumophila GTPase activating protein LepB accelerates Rab1 deactivation by a non-canonical hydrolytic mechanism."
Mishra A.K., Del Campo C.M., Collins R.E., Roy C.R., Lambright D.G.
J. Biol. Chem. 288:24000-24011(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 4-177 IN COMPLEX WITH GDP AND L.PNEUMOPHILA LEPB, INTERACTION WITH L.PNEUMOPHILA LEPB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28209 mRNA. Translation: AAA60240.1.
AL050268 mRNA. Translation: CAB43369.1.
BX571747 mRNA. Translation: CAE11872.1.
AK055927 mRNA. Translation: BAB71048.1.
AF498929 mRNA. Translation: AAM21077.1.
CR533479 mRNA. Translation: CAG38510.1.
CH471053 Genomic DNA. Translation: EAW99921.1.
BC000905 mRNA. Translation: AAH00905.1.
CCDSCCDS46305.1. [P62820-3]
CCDS46306.1.
PIRTVHUYP. A34323.
RefSeqNP_004152.1. NM_004161.4. [P62820-1]
NP_056358.1. NM_015543.1. [P62820-3]
UniGeneHs.310645.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FOLX-ray2.63A6-177[»]
2WWXX-ray1.50A4-178[»]
3L0IX-ray2.85B/D1-177[»]
3SFVX-ray1.73A1-176[»]
3TKLX-ray2.18A1-191[»]
4FMBX-ray3.20B/D/F6-176[»]
4FMCX-ray2.80B/D6-176[»]
F14-115[»]
4FMDX-ray3.05B/D6-176[»]
F13-176[»]
4FMEX-ray4.10B/E6-176[»]
4IRUX-ray3.20B/D/F4-177[»]
4JVSX-ray2.78B1-177[»]
ProteinModelPortalP62820.
SMRP62820. Positions 6-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111799. 52 interactions.
DIPDIP-1063N.
IntActP62820. 32 interactions.
MINTMINT-1343792.
STRING9606.ENSP00000387286.

PTM databases

PhosphoSiteP62820.

Polymorphism databases

DMDM51338603.

Proteomic databases

MaxQBP62820.
PaxDbP62820.
PRIDEP62820.

Protocols and materials databases

DNASU5861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398529; ENSP00000381540; ENSG00000138069. [P62820-3]
ENST00000409784; ENSP00000387286; ENSG00000138069. [P62820-1]
ENST00000409892; ENSP00000386451; ENSG00000138069. [P62820-2]
GeneID5861.
KEGGhsa:5861.
UCSCuc002sdm.3. human.
uc002sdn.3. human. [P62820-3]
uc002sdo.3. human. [P62820-2]

Organism-specific databases

CTD5861.
GeneCardsGC02M065297.
HGNCHGNC:9758. RAB1A.
HPACAB005331.
MIM179508. gene.
neXtProtNX_P62820.
PharmGKBPA34107.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
KOK07874.
OMAIKNRVGP.
OrthoDBEOG7VB2H4.
PhylomeDBP62820.
TreeFamTF300097.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP62820.
BgeeP62820.
CleanExHS_RAB1A.
GenevestigatorP62820.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB1A. human.
EvolutionaryTraceP62820.
GeneWikiRAB1A.
GenomeRNAi5861.
NextBio22762.
PROP62820.
SOURCESearch...

Entry information

Entry nameRAB1A_HUMAN
AccessionPrimary (citable) accession number: P62820
Secondary accession number(s): P11476 expand/collapse secondary AC list , Q6FIE7, Q96N61, Q9Y3T2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM