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P61006

- RAB8A_HUMAN

UniProt

P61006 - RAB8A_HUMAN

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Protein

Ras-related protein Rab-8A

Gene

RAB8A

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. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis.3 Publications

Enzyme regulationi

Activated in response to insulin.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB
  4. myosin V binding Source: UniProtKB
  5. Rab GTPase binding Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: UniProtKB
  2. cellular response to insulin stimulus Source: UniProtKB
  3. cilium assembly Source: UniProtKB
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. Golgi vesicle fusion to target membrane Source: BHF-UCL
  6. GTP catabolic process Source: UniProtKB
  7. membrane organization Source: Reactome
  8. mitotic cell cycle Source: Reactome
  9. protein localization to plasma membrane Source: UniProtKB
  10. protein transport Source: UniProtKB-KW
  11. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  12. regulation of protein transport Source: Ensembl
  13. small GTPase mediated signal transduction Source: InterPro
  14. vesicle docking involved in exocytosis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-8A
Alternative name(s):
Oncogene c-mel
Gene namesi
Name:RAB8A
Synonyms:MEL, RAB8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:7007. RAB8A.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Golgi apparatus. Recycling endosome membrane. Cell projectioncilium. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
Note: Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis.

GO - Cellular componenti

  1. centrosome Source: MGI
  2. ciliary basal body Source: Ensembl
  3. cilium Source: MGI
  4. cytoplasmic vesicle membrane Source: Reactome
  5. dendrite Source: Ensembl
  6. extracellular vesicular exosome Source: UniProt
  7. Golgi membrane Source: Reactome
  8. neuronal cell body Source: Ensembl
  9. nonmotile primary cilium Source: BHF-UCL
  10. phagocytic vesicle Source: UniProtKB
  11. plasma membrane Source: UniProtKB-KW
  12. postsynaptic density Source: Ensembl
  13. primary cilium Source: UniProtKB
  14. recycling endosome membrane Source: UniProtKB
  15. trans-Golgi network transport vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221T → N: Loss of interaction with MICALL1. 1 Publication
Mutagenesisi67 – 671Q → L: Probable constitutively active mutant locked in the active GTP-bound form. Stimulates interaction with MICALL1. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA30743.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Ras-related protein Rab-8APRO_0000121130Add
BLAST
Propeptidei205 – 2073Removed in mature formSequence AnalysisPRO_0000370793

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine3 Publications
Modified residuei204 – 2041Cysteine methyl esterSequence Analysis
Lipidationi204 – 2041S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP61006.
PaxDbiP61006.
PeptideAtlasiP61006.
PRIDEiP61006.

PTM databases

PhosphoSiteiP61006.

Expressioni

Gene expression databases

BgeeiP61006.
CleanExiHS_RAB8A.
ExpressionAtlasiP61006. baseline and differential.
GenevestigatoriP61006.

Interactioni

Subunit structurei

Interacts (GTP-bound form) with MICALL1; regulates RAB8A association with recycling endosomes. Interacts with MICALL2; competes with RAB13 and is involved in E-cadherin endocytic recycling. Interacts with MICAL1. Interacts with EHD1. Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and SGSM3. Interacts with RABIF, RIMS2, RPH3A and RPH3A. Interacts with OPTN. Interacts with RAB3IP. Interacts with MYO5B. Interacts with PIFO. Interacts with BIRC6/bruce. Interacts with OCRL.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OCRLQ0196811EBI-722293,EBI-6148898
OPTNQ96CV94EBI-722293,EBI-748974
RABIFP472242EBI-722293,EBI-713992

Protein-protein interaction databases

BioGridi110382. 40 interactions.
DIPiDIP-43703N.
IntActiP61006. 14 interactions.
MINTiMINT-1416277.
STRINGi9606.ENSP00000300935.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Helixi21 – 3010Combined sources
Turni38 – 414Combined sources
Beta strandi42 – 5211Combined sources
Beta strandi55 – 6410Combined sources
Turni69 – 724Combined sources
Helixi73 – 786Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 975Combined sources
Helixi99 – 10911Combined sources
Beta strandi115 – 1217Combined sources
Turni122 – 1243Combined sources
Helixi126 – 1283Combined sources
Helixi133 – 14210Combined sources
Beta strandi146 – 1494Combined sources
Turni152 – 1554Combined sources
Helixi158 – 17417Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBTX-ray2.00A/C/E/G6-176[»]
3TNFX-ray2.50A6-176[»]
4LHVX-ray1.95A/B/C/D/E6-176[»]
4LHWX-ray1.55A/B/C/D/E6-176[»]
4LHXX-ray3.05A/B1-184[»]
4LHYX-ray3.10A/B1-184[»]
4LHZX-ray3.20A/B1-184[»]
4LI0X-ray3.30A/B1-184[»]
ProteinModelPortaliP61006.
SMRiP61006. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61006.
KOiK07901.
OMAiIDKAFYS.
PhylomeDBiP61006.
TreeFamiTF314097.

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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61006-1) [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
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI
60 70 80 90 100
ELDGKRIKLQ IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR
110 120 130 140 150
NWIRNIEEHA SADVEKMILG NKCDVNDKRQ VSKERGEKLA LDYGIKFMET
160 170 180 190 200
SAKANINVEN AFFTLARDIK AKMDKKLEGN SPQGSNQGVK ITPDQQKRSS

FFRCVLL
Length:207
Mass (Da):23,668
Last modified:April 26, 2004 - v1
Checksum:iAA52DBF54A2CD056
GO
Isoform 2 (identifier: P61006-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-205: AFFTLARDIK...QKRSSFFRCV → RYQSKNGQKI...PMCSSVRNTA

Note: No experimental confirmation available.

Show »
Length:207
Mass (Da):23,564
Checksum:i249CB68DDF955162
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1837LEGNSPQ → WKATAP in AAB19681. (PubMed:1886711)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei161 – 20545AFFTL…FFRCV → RYQSKNGQKIGRQQPPGEQP GSQNHTGPAEEEQLFPMCSS VRNTA in isoform 2. 1 PublicationVSP_056399Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56741 mRNA. Translation: CAA40065.1.
S53268 mRNA. Translation: AAB19681.1.
AF498943 mRNA. Translation: AAM21091.1.
BT007184 mRNA. Translation: AAP35848.1.
AK293676 mRNA. Translation: BAG57118.1.
CR536583 mRNA. Translation: CAG38820.1.
AC008894 Genomic DNA. No translation available.
CR542274 mRNA. Translation: CAG47070.1.
CH471106 Genomic DNA. Translation: EAW84526.1.
BC002977 mRNA. Translation: AAH02977.1.
CCDSiCCDS12339.1. [P61006-1]
PIRiB49647.
RefSeqiNP_005361.2. NM_005370.4.
UniGeneiHs.642874.

Genome annotation databases

EnsembliENST00000300935; ENSP00000300935; ENSG00000167461. [P61006-1]
ENST00000586682; ENSP00000467501; ENSG00000167461. [P61006-2]
GeneIDi4218.
KEGGihsa:4218.
UCSCiuc002ndn.4. human. [P61006-1]

Polymorphism databases

DMDMi46810392.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56741 mRNA. Translation: CAA40065.1 .
S53268 mRNA. Translation: AAB19681.1 .
AF498943 mRNA. Translation: AAM21091.1 .
BT007184 mRNA. Translation: AAP35848.1 .
AK293676 mRNA. Translation: BAG57118.1 .
CR536583 mRNA. Translation: CAG38820.1 .
AC008894 Genomic DNA. No translation available.
CR542274 mRNA. Translation: CAG47070.1 .
CH471106 Genomic DNA. Translation: EAW84526.1 .
BC002977 mRNA. Translation: AAH02977.1 .
CCDSi CCDS12339.1. [P61006-1 ]
PIRi B49647.
RefSeqi NP_005361.2. NM_005370.4.
UniGenei Hs.642874.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QBT X-ray 2.00 A/C/E/G 6-176 [» ]
3TNF X-ray 2.50 A 6-176 [» ]
4LHV X-ray 1.95 A/B/C/D/E 6-176 [» ]
4LHW X-ray 1.55 A/B/C/D/E 6-176 [» ]
4LHX X-ray 3.05 A/B 1-184 [» ]
4LHY X-ray 3.10 A/B 1-184 [» ]
4LHZ X-ray 3.20 A/B 1-184 [» ]
4LI0 X-ray 3.30 A/B 1-184 [» ]
ProteinModelPortali P61006.
SMRi P61006. Positions 6-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110382. 40 interactions.
DIPi DIP-43703N.
IntActi P61006. 14 interactions.
MINTi MINT-1416277.
STRINGi 9606.ENSP00000300935.

PTM databases

PhosphoSitei P61006.

Polymorphism databases

DMDMi 46810392.

Proteomic databases

MaxQBi P61006.
PaxDbi P61006.
PeptideAtlasi P61006.
PRIDEi P61006.

Protocols and materials databases

DNASUi 4218.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300935 ; ENSP00000300935 ; ENSG00000167461 . [P61006-1 ]
ENST00000586682 ; ENSP00000467501 ; ENSG00000167461 . [P61006-2 ]
GeneIDi 4218.
KEGGi hsa:4218.
UCSCi uc002ndn.4. human. [P61006-1 ]

Organism-specific databases

CTDi 4218.
GeneCardsi GC19P016222.
HGNCi HGNC:7007. RAB8A.
MIMi 165040. gene.
neXtProti NX_P61006.
PharmGKBi PA30743.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118937.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P61006.
KOi K07901.
OMAi IDKAFYS.
PhylomeDBi P61006.
TreeFami TF314097.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi RAB8A. human.
GeneWikii RAB8A.
GenomeRNAii 4218.
NextBioi 16637.
PROi P61006.
SOURCEi Search...

Gene expression databases

Bgeei P61006.
CleanExi HS_RAB8A.
ExpressionAtlasi P61006. baseline and differential.
Genevestigatori P61006.

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. "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells."
    Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A., Louvard D.
    J. Cell Biol. 124:101-115(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The MEL gene: a new member of the RAB/YPT class of RAS-related genes."
    Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R., Johnson K.J.
    Oncogene 6:1347-1351(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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.
  4. "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] (ISOFORM 1).
  5. "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).
    Tissue: Cerebellum.
  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 1).
  7. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Skin.
  10. "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif."
    Joberty G., Tavitian A., Zahraoui A.
    FEBS Lett. 330:323-328(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-204.
  11. "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
    Hattula K., Furuhjelm J., Arffman A., Peranen J.
    Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION.
    Tissue: Brain.
  12. "Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
    Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
    J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
    Pohl C., Jentsch S.
    Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC6/BRUCE.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: INTERACTION WITH PIFO.
  18. "A molecular network for de novo generation of the apical surface and lumen."
    Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
    Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
    Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
    Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF THR-22 AND GLN-67.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
    Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO5B.
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
    Seto S., Tsujimura K., Koide Y.
    Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."
    Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., Shu X., Pei D.
    Cell Res. 22:333-345(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CILIOGENESIS, SUBCELLULAR LOCATION.
  26. Cited for: INTERACTION WITH OCRL.
  27. "A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1."
    Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S., Erdmann K.S., Itzen A.
    EMBO J. 30:1659-1670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-176 IN COMPLEX WITH OCRL.

Entry informationi

Entry nameiRAB8A_HUMAN
AccessioniPrimary (citable) accession number: P61006
Secondary accession number(s): B4DEK7, P24407, Q6FHV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: October 29, 2014
This is version 122 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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