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Protein

Ras-related protein Rab-1A

Gene

RAB1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 705GTPBy similarity
Nucleotide bindingi124 – 1274GTP
Nucleotide bindingi154 – 1563GTP

GO - Molecular functioni

  1. GDP binding Source: GO_Central
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: GO_Central

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. autophagy Source: UniProtKB
  3. cargo loading into COPII-coated vesicle Source: UniProtKB
  4. cell migration Source: UniProtKB
  5. defense response to bacterium Source: UniProtKB
  6. endocytosis Source: UniProtKB
  7. ER to Golgi vesicle-mediated transport Source: UniProtKB
  8. Golgi organization Source: UniProtKB
  9. growth hormone secretion Source: UniProtKB
  10. interleukin-8 secretion Source: UniProtKB
  11. intracellular protein transport Source: GO_Central
  12. melanosome transport Source: Ensembl
  13. mitotic cell cycle Source: Reactome
  14. positive regulation of glycoprotein metabolic process Source: UniProtKB
  15. Rab protein signal transduction Source: GO_Central
  16. substrate adhesion-dependent cell spreading Source: Ensembl
  17. vesicle-mediated transport Source: ProtInc
  18. vesicle transport along microtubule Source: UniProtKB
  19. virion assembly 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 Componenti: 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.

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. early endosome Source: UniProtKB-SubCell
  3. endoplasmic reticulum membrane Source: GO_Central
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. Golgi membrane Source: GO_Central
  7. 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 AnkX2 Publications
Modified residuei194 – 1941Phosphoserine; by CDK11 Publication
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

BgeeiP62820.
CleanExiHS_RAB1A.
ExpressionAtlasiP62820. baseline and differential.
GenevestigatoriP62820.

Organism-specific databases

HPAiCAB005331.
HPA056141.

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.By similarity10 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111799. 56 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 – 178Combined sources
Helixi24 – 285Combined sources
Beta strandi30 – 323Combined sources
Helixi39 – 446Combined sources
Beta strandi47 – 559Combined sources
Beta strandi58 – 658Combined sources
Helixi70 – 723Combined sources
Helixi78 – 803Combined sources
Turni81 – 833Combined sources
Beta strandi85 – 928Combined sources
Helixi96 – 11217Combined sources
Beta strandi117 – 1259Combined sources
Helixi129 – 1313Combined sources
Helixi136 – 14510Combined sources
Beta strandi150 – 1545Combined sources
Turni155 – 1573Combined sources
Helixi159 – 17517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62820.

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP62820.
KOiK07874.
OMAiKERMGNT.
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. AlignAdd to basket

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

        10         20         30         40         50
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI
60 70 80 90 100
RTIELDGKTI KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN
110 120 130 140 150
NVKQWLQEID RYASENVNKL LVGNKCDLTT KKVVDYTTAK EFADSLGIPF
160 170 180 190 200
LETSAKNATN VEQSFMTMAA EIKKRMGPGA TAGGAEKSNV KIQSTPVKQS

GGGCC
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. 1 PublicationVSP_005525Add
BLAST
Alternative sequencei65 – 14076Missing in isoform 3. 2 PublicationsVSP_005526Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111799. 56 interactions.
DIPiDIP-1063N.
IntActiP62820. 32 interactions.
MINTiMINT-1343792.
STRINGi9606.ENSP00000387286.

PTM databases

PhosphoSiteiP62820.

Polymorphism databases

DMDMi51338603.

Proteomic databases

MaxQBiP62820.
PaxDbiP62820.
PRIDEiP62820.

Protocols and materials databases

DNASUi5861.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5861.
GeneCardsiGC02M065297.
HGNCiHGNC:9758. RAB1A.
HPAiCAB005331.
HPA056141.
MIMi179508. gene.
neXtProtiNX_P62820.
PharmGKBiPA34107.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP62820.
KOiK07874.
OMAiKERMGNT.
OrthoDBiEOG7VB2H4.
PhylomeDBiP62820.
TreeFamiTF300097.

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

ChiTaRSiRAB1A. human.
EvolutionaryTraceiP62820.
GeneWikiiRAB1A.
GenomeRNAii5861.
NextBioi22762.
PROiP62820.
SOURCEiSearch...

Gene expression databases

BgeeiP62820.
CleanExiHS_RAB1A.
ExpressionAtlasiP62820. baseline and differential.
GenevestigatoriP62820.

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]
ProtoNetiSearch...

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(1988) [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(2003) [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 (MAR-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 (MAY-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  9. Bienvenut W.V., Claeys D.
    Submitted (OCT-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(1990) [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(1993) [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(2008) [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(2008) [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(2009) [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(2009) [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(2010) [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(2010) [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(2010) [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(2011) [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(2012) [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 (JAN-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(2009) [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(2009) [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(2011) [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(2011) [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(2012) [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(2012) [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: April 1, 2015
This is version 125 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.