SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62820

- RAB1A_HUMAN

UniProt

P62820 - RAB1A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ras-related protein Rab-1A

Gene
RAB1A, RAB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269GTP
Nucleotide bindingi36 – 438GTP
Nucleotide bindingi66 – 705GTP By similarity
Nucleotide bindingi124 – 1274GTP
Nucleotide bindingi154 – 1563GTP

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. autophagy Source: UniProtKB
  3. cell migration Source: UniProtKB
  4. defense response to bacterium Source: UniProtKB
  5. endocytosis Source: UniProtKB
  6. ER to Golgi vesicle-mediated transport Source: UniProtKB
  7. growth hormone secretion Source: UniProtKB
  8. GTP catabolic process Source: UniProtKB
  9. interleukin-8 secretion Source: UniProtKB
  10. mitotic cell cycle Source: Reactome
  11. small GTPase mediated signal transduction Source: InterPro
  12. vesicle-mediated transport Source: ProtInc
  13. vesicle transport along microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Autophagy, ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-1A
Alternative name(s):
YPT1-related protein
Gene namesi
Name:RAB1A
Synonyms:RAB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9758. RAB1A.

Subcellular locationi

Golgi apparatus. Endoplasmic reticulum. Early endosome. Cytoplasmcytosol. Membrane. Melanosome By similarity
Note: Alternates between membrane-associated and cytosolic forms.4 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. early endosome Source: UniProtKB-SubCell
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. Golgi membrane Source: Reactome
  6. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241N → I: Dominant negative mutant. Strongly reduces the levels of CASR present at the cell-surface. 1 Publication

Organism-specific databases

PharmGKBiPA34107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 205204Ras-related protein Rab-1APRO_0000121056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei79 – 791O-(2-cholinephosphoryl)serine; by Legionella AnkX
Modified residuei194 – 1941Phosphoserine; by CDK1 Inferred
Lipidationi204 – 2041S-geranylgeranyl cysteine1 Publication
Lipidationi205 – 2051S-geranylgeranyl cysteine1 Publication

Post-translational modificationi

Phosphorylated by CDK1 kinase during mitosis.3 Publications
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.

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP62820.
PaxDbiP62820.
PRIDEiP62820.

PTM databases

PhosphoSiteiP62820.

Expressioni

Gene expression databases

ArrayExpressiP62820.
BgeeiP62820.
CleanExiHS_RAB1A.
GenevestigatoriP62820.

Organism-specific databases

HPAiCAB005331.

Interactioni

Subunit structurei

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
drrAQ5ZSQ37EBI-716845,EBI-7632432From a different organism.
OCRLQ019687EBI-716845,EBI-6148898

Protein-protein interaction databases

BioGridi111799. 52 interactions.
DIPiDIP-1063N.
IntActiP62820. 32 interactions.
MINTiMINT-1343792.
STRINGi9606.ENSP00000387286.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 178
Helixi24 – 285
Beta strandi30 – 323
Helixi39 – 446
Beta strandi47 – 559
Beta strandi58 – 658
Helixi70 – 723
Helixi78 – 803
Turni81 – 833
Beta strandi85 – 928
Helixi96 – 11217
Beta strandi117 – 1259
Helixi129 – 1313
Helixi136 – 14510
Beta strandi150 – 1545
Turni155 – 1573
Helixi159 – 17517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP62820.
SMRiP62820. Positions 6-176.

Miscellaneous databases

EvolutionaryTraceiP62820.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 489Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
KOiK07874.
OMAiIKNRVGP.
OrthoDBiEOG7VB2H4.
PhylomeDBiP62820.
TreeFamiTF300097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62820-1) [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

MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI    50
RTIELDGKTI KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN 100
NVKQWLQEID RYASENVNKL LVGNKCDLTT KKVVDYTTAK EFADSLGIPF 150
LETSAKNATN VEQSFMTMAA EIKKRMGPGA TAGGAEKSNV KIQSTPVKQS 200
GGGCC 205
Length:205
Mass (Da):22,678
Last modified:January 23, 2007 - v3
Checksum:iB2A8F4E3B0FB17D6
GO
Isoform 2 (identifier: P62820-2) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-96: Missing.

Note: No experimental confirmation available.

Show »
Length:141
Mass (Da):15,331
Checksum:i620F588CA34B3A77
GO
Isoform 3 (identifier: P62820-3) [UniParc] [UniParc]FASTAAdd to Basket

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

Show »
Length:129
Mass (Da):13,903
Checksum:i8325012BF5161AFE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 9664Missing in isoform 2. VSP_005525Add
BLAST
Alternative sequencei65 – 14076Missing in isoform 3. VSP_005526Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46305.1. [P62820-3]
CCDS46306.1.
PIRiA34323. TVHUYP.
RefSeqiNP_004152.1. NM_004161.4. [P62820-1]
NP_056358.1. NM_015543.1. [P62820-3]
UniGeneiHs.310645.

Genome annotation databases

EnsembliENST00000398529; ENSP00000381540; ENSG00000138069. [P62820-3]
ENST00000409784; ENSP00000387286; ENSG00000138069. [P62820-1]
ENST00000409892; ENSP00000386451; ENSG00000138069. [P62820-2]
GeneIDi5861.
KEGGihsa:5861.
UCSCiuc002sdm.3. human.
uc002sdn.3. human. [P62820-3]
uc002sdo.3. human. [P62820-2]

Polymorphism databases

DMDMi51338603.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS46305.1. [P62820-3 ]
CCDS46306.1.
PIRi A34323. TVHUYP.
RefSeqi NP_004152.1. NM_004161.4. [P62820-1 ]
NP_056358.1. NM_015543.1. [P62820-3 ]
UniGenei Hs.310645.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FOL X-ray 2.63 A 6-177 [» ]
2WWX X-ray 1.50 A 4-178 [» ]
3L0I X-ray 2.85 B/D 1-177 [» ]
3SFV X-ray 1.73 A 1-176 [» ]
3TKL X-ray 2.18 A 1-191 [» ]
4FMB X-ray 3.20 B/D/F 6-176 [» ]
4FMC X-ray 2.80 B/D 6-176 [» ]
F 14-115 [» ]
4FMD X-ray 3.05 B/D 6-176 [» ]
F 13-176 [» ]
4FME X-ray 4.10 B/E 6-176 [» ]
4IRU X-ray 3.20 B/D/F 4-177 [» ]
4JVS X-ray 2.78 B 1-177 [» ]
ProteinModelPortali P62820.
SMRi P62820. Positions 6-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111799. 52 interactions.
DIPi DIP-1063N.
IntActi P62820. 32 interactions.
MINTi MINT-1343792.
STRINGi 9606.ENSP00000387286.

PTM databases

PhosphoSitei P62820.

Polymorphism databases

DMDMi 51338603.

Proteomic databases

MaxQBi P62820.
PaxDbi P62820.
PRIDEi P62820.

Protocols and materials databases

DNASUi 5861.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398529 ; ENSP00000381540 ; ENSG00000138069 . [P62820-3 ]
ENST00000409784 ; ENSP00000387286 ; ENSG00000138069 . [P62820-1 ]
ENST00000409892 ; ENSP00000386451 ; ENSG00000138069 . [P62820-2 ]
GeneIDi 5861.
KEGGi hsa:5861.
UCSCi uc002sdm.3. human.
uc002sdn.3. human. [P62820-3 ]
uc002sdo.3. human. [P62820-2 ]

Organism-specific databases

CTDi 5861.
GeneCardsi GC02M065297.
HGNCi HGNC:9758. RAB1A.
HPAi CAB005331.
MIMi 179508. gene.
neXtProti NX_P62820.
PharmGKBi PA34107.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
KOi K07874.
OMAi IKNRVGP.
OrthoDBi EOG7VB2H4.
PhylomeDBi P62820.
TreeFami TF300097.

Enzyme and pathway databases

Reactomei REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

ChiTaRSi RAB1A. human.
EvolutionaryTracei P62820.
GeneWikii RAB1A.
GenomeRNAii 5861.
NextBioi 22762.
PROi P62820.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62820.
Bgeei P62820.
CleanExi HS_RAB1A.
Genevestigatori P62820.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  3. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiRAB1A_HUMAN
AccessioniPrimary (citable) accession number: P62820
Secondary accession number(s): P11476
, Q6FIE7, Q96N61, Q9Y3T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 118 of the entry and version 3 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi