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P62491

- RB11A_HUMAN

UniProt

P62491 - RB11A_HUMAN

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Protein

Ras-related protein Rab-11A

Gene

RAB11A

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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, 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 participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269GTP3 Publications
Nucleotide bindingi66 – 705GTP3 Publications
Nucleotide bindingi124 – 1274GTP3 Publications
Nucleotide bindingi154 – 1563GTP3 Publications

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. myosin V binding Source: UniProtKB
  4. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. cytokinesis Source: UniProtKB
  2. establishment of protein localization to membrane Source: UniProtKB
  3. exosomal secretion Source: UniProtKB
  4. GTP catabolic process Source: UniProtKB
  5. melanosome transport Source: UniProtKB
  6. multivesicular body assembly Source: UniProtKB
  7. neuron projection development Source: UniProtKB
  8. plasma membrane to endosome transport Source: UniProtKB
  9. positive regulation of axon extension Source: Ensembl
  10. protein localization to plasma membrane Source: UniProtKB
  11. protein transport Source: UniProtKB-KW
  12. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  13. regulation of multivesicular body size Source: UniProtKB
  14. regulation of protein transport Source: Ensembl
  15. small GTPase mediated signal transduction Source: InterPro
  16. transmembrane transport Source: Reactome
  17. vesicle-mediated transport Source: UniProtKB
  18. water transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
SignaLinkiP62491.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-11A
Short name:
Rab-11
Alternative name(s):
YL8
Gene namesi
Name:RAB11A
Synonyms:RAB11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:9760. RAB11A.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localizes to the cleavage furrow. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Recruited to phagosomes containing S.aureus or M.tuberculosis.

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cleavage furrow Source: UniProtKB
  3. cytoplasmic vesicle membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. mitochondrion Source: Ensembl
  6. multivesicular body Source: UniProtKB
  7. perinuclear region of cytoplasm Source: Ensembl
  8. phagocytic vesicle Source: UniProtKB
  9. plasma membrane Source: UniProtKB-KW
  10. protein complex Source: UniProtKB
  11. recycling endosome Source: UniProtKB
  12. trans-Golgi network Source: MGI
  13. transport vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251S → N: Dominant-negative mutant. Induces increased number of binucleated cells, indicating defects in cytokinesis. Inhibits the transport of NPC1L1 to the plama membrane. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 3 Publications
Mutagenesisi70 – 701Q → L: Constitutively active mutant. Decreases GTPase activity. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 5 Publications

Organism-specific databases

PharmGKBiPA34101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 213212Ras-related protein Rab-11APRO_0000121151Add
BLAST
Propeptidei214 – 2163Removed in mature formSequence AnalysisPRO_0000370807

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Lipidationi212 – 2121S-geranylgeranyl cysteine1 Publication
Modified residuei213 – 2131Cysteine methyl esterSequence Analysis
Lipidationi213 – 2131S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP62491.
PaxDbiP62491.
PRIDEiP62491.

2D gel databases

OGPiP62491.

PTM databases

PhosphoSiteiP62491.

Expressioni

Gene expression databases

BgeeiP62491.
CleanExiHS_RAB11A.
ExpressionAtlasiP62491. baseline and differential.
GenevestigatoriP62491.

Organism-specific databases

HPAiCAB013097.

Interactioni

Subunit structurei

Interacts with RIP11 and STXBP6. Interacts with SGSM1, SGSM2 and SGSM3 (By similarity). Interacts with EXOC6 in a GTP-dependent manner (By similarity). Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A. Interacts with VIPAS39. Interacts with MYO5B. Found in a complex with MYO5B and CFTR. Interacts with NPC1L1. Interacts (GDP-bound form) with ZFYVE27. Interacts with BIRC6/bruce. May interact with TBC1D14. Interacts with UNC119; in a cell cycle-dependent manner.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB11FIP2Q7L8042EBI-745098,EBI-1049676
ZFYVE27Q5T4F44EBI-745098,EBI-3892947

Protein-protein interaction databases

BioGridi114299. 49 interactions.
DIPiDIP-29138N.
IntActiP62491. 20 interactions.
MINTiMINT-1434585.
STRINGi9606.ENSP00000261890.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1810Combined sources
Helixi24 – 3310Combined sources
Beta strandi45 – 5511Combined sources
Beta strandi58 – 6710Combined sources
Beta strandi72 – 743Combined sources
Helixi78 – 814Combined sources
Beta strandi86 – 927Combined sources
Helixi96 – 1005Combined sources
Helixi102 – 11211Combined sources
Beta strandi118 – 1247Combined sources
Helixi126 – 1316Combined sources
Helixi136 – 14510Combined sources
Beta strandi149 – 1524Combined sources
Turni155 – 1573Combined sources
Helixi161 – 17212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OIVX-ray1.98A/B1-173[»]
1OIWX-ray2.05A1-173[»]
1OIXX-ray1.70A1-173[»]
1YZKX-ray2.00A8-175[»]
2D7CX-ray1.75A/B7-173[»]
2GZDX-ray2.44A/B2-173[»]
2GZHX-ray2.47A2-173[»]
2HV8X-ray1.86A/B/C6-175[»]
4C4PX-ray2.00A1-173[»]
4D0LX-ray2.94B/D/F1-216[»]
4D0MX-ray6.00B/D/H/J/N/P/R/T/X/Z/d/h1-216[»]
4LWZX-ray2.55A/C1-177[»]
4LX0X-ray2.19A/C1-177[»]
ProteinModelPortaliP62491.
SMRiP62491. Positions 6-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62491.

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.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP62491.
KOiK07904.
OMAiAMGTRDD.
PhylomeDBiP62491.
TreeFamiTF300099.

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: P62491-1) [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
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF
160 170 180 190 200
IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV
210
PPTTENKPKV QCCQNI
Length:216
Mass (Da):24,394
Last modified:January 23, 2007 - v3
Checksum:i76FC1E113A29B269
GO
Isoform 2 (identifier: P62491-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-216: GLSFIETSAL...KPKVQCCQNI → EANVRQTRK

Note: No experimental confirmation available.

Show »
Length:155
Mass (Da):17,659
Checksum:i70C3A0F378C9893A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei147 – 21670GLSFI…CCQNI → EANVRQTRK in isoform 2. 1 PublicationVSP_046755Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53143 mRNA. Translation: CAA37300.1.
X56740 mRNA. Translation: CAA40064.1.
AF000231 mRNA. Translation: AAC32887.1.
AF498946 mRNA. Translation: AAM21094.1.
CR407669 mRNA. Translation: CAG28597.1.
CR536493 mRNA. Translation: CAG38732.1.
BT020151 mRNA. Translation: AAV38953.1.
BT020154 mRNA. Translation: AAV38956.1.
AK300008 mRNA. Translation: BAG61825.1.
AK311770 mRNA. Translation: BAG34713.1.
AC011939 Genomic DNA. No translation available.
AC084854 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77752.1.
BC013348 mRNA. Translation: AAH13348.1.
CCDSiCCDS10212.1. [P62491-1]
CCDS58373.1. [P62491-2]
PIRiS47169.
RefSeqiNP_001193765.1. NM_001206836.1. [P62491-2]
NP_004654.1. NM_004663.4. [P62491-1]
UniGeneiHs.321541.

Genome annotation databases

EnsembliENST00000261890; ENSP00000261890; ENSG00000103769. [P62491-1]
ENST00000569896; ENSP00000456420; ENSG00000103769. [P62491-2]
GeneIDi8766.
KEGGihsa:8766.
UCSCiuc002apk.3. human. [P62491-1]

Polymorphism databases

DMDMi50402542.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53143 mRNA. Translation: CAA37300.1 .
X56740 mRNA. Translation: CAA40064.1 .
AF000231 mRNA. Translation: AAC32887.1 .
AF498946 mRNA. Translation: AAM21094.1 .
CR407669 mRNA. Translation: CAG28597.1 .
CR536493 mRNA. Translation: CAG38732.1 .
BT020151 mRNA. Translation: AAV38953.1 .
BT020154 mRNA. Translation: AAV38956.1 .
AK300008 mRNA. Translation: BAG61825.1 .
AK311770 mRNA. Translation: BAG34713.1 .
AC011939 Genomic DNA. No translation available.
AC084854 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77752.1 .
BC013348 mRNA. Translation: AAH13348.1 .
CCDSi CCDS10212.1. [P62491-1 ]
CCDS58373.1. [P62491-2 ]
PIRi S47169.
RefSeqi NP_001193765.1. NM_001206836.1. [P62491-2 ]
NP_004654.1. NM_004663.4. [P62491-1 ]
UniGenei Hs.321541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OIV X-ray 1.98 A/B 1-173 [» ]
1OIW X-ray 2.05 A 1-173 [» ]
1OIX X-ray 1.70 A 1-173 [» ]
1YZK X-ray 2.00 A 8-175 [» ]
2D7C X-ray 1.75 A/B 7-173 [» ]
2GZD X-ray 2.44 A/B 2-173 [» ]
2GZH X-ray 2.47 A 2-173 [» ]
2HV8 X-ray 1.86 A/B/C 6-175 [» ]
4C4P X-ray 2.00 A 1-173 [» ]
4D0L X-ray 2.94 B/D/F 1-216 [» ]
4D0M X-ray 6.00 B/D/H/J/N/P/R/T/X/Z/d/h 1-216 [» ]
4LWZ X-ray 2.55 A/C 1-177 [» ]
4LX0 X-ray 2.19 A/C 1-177 [» ]
ProteinModelPortali P62491.
SMRi P62491. Positions 6-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114299. 49 interactions.
DIPi DIP-29138N.
IntActi P62491. 20 interactions.
MINTi MINT-1434585.
STRINGi 9606.ENSP00000261890.

PTM databases

PhosphoSitei P62491.

Polymorphism databases

DMDMi 50402542.

2D gel databases

OGPi P62491.

Proteomic databases

MaxQBi P62491.
PaxDbi P62491.
PRIDEi P62491.

Protocols and materials databases

DNASUi 8766.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261890 ; ENSP00000261890 ; ENSG00000103769 . [P62491-1 ]
ENST00000569896 ; ENSP00000456420 ; ENSG00000103769 . [P62491-2 ]
GeneIDi 8766.
KEGGi hsa:8766.
UCSCi uc002apk.3. human. [P62491-1 ]

Organism-specific databases

CTDi 8766.
GeneCardsi GC15P066018.
HGNCi HGNC:9760. RAB11A.
HPAi CAB013097.
MIMi 605570. gene.
neXtProti NX_P62491.
PharmGKBi PA34101.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118841.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P62491.
KOi K07904.
OMAi AMGTRDD.
PhylomeDBi P62491.
TreeFami TF300099.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
SignaLinki P62491.

Miscellaneous databases

ChiTaRSi RAB11A. human.
EvolutionaryTracei P62491.
GeneWikii RAB11A.
GenomeRNAii 8766.
NextBioi 32876.
PROi P62491.
SOURCEi Search...

Gene expression databases

Bgeei P62491.
CleanExi HS_RAB11A.
ExpressionAtlasi P62491. baseline and differential.
Genevestigatori P62491.

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. "Identification and characterization of a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3."
    Drivas G.T., Shih A., Coutavas E.E., D'Eustachio P., Rush M.G.
    Oncogene 6:3-9(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Zahraoui A., Joberty G., Tavitian A.
    Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins."
    Gromov P.S., Celis J.E., Hansen C., Tommerup N., Gromova I., Madsen P.
    FEBS Lett. 429:359-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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.
  5. "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).
  6. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  8. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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: Brain.
  11. Bienvenut W.V.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-24; 34-58; 62-72; 75-95 AND 133-140, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Platelet.
  12. Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
  13. "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells."
    Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
    Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP4.
  14. Cited for: INTERACTION WITH RAB11FIP4.
    Tissue: Cervix carcinoma.
  15. "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
    Lindsay A.J., McCaffrey M.W.
    J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
    Lindsay A.J., McCaffrey M.W.
    FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP1.
  17. "Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins."
    Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., Prekeris R.
    J. Biol. Chem. 279:33430-33437(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP2.
  18. "The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane."
    Lindsay A.J., McCaffrey M.W.
    J. Cell Sci. 117:4365-4375(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  19. Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION.
  20. "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis."
    Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.
    EMBO J. 24:3389-3399(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
  21. "The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
    Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
    Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25.
  22. "Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
    Lock J.G., Stow J.L.
    Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-25 AND GLN-70.
  23. "Protrudin induces neurite formation by directional membrane trafficking."
    Shirane M., Nakayama K.I.
    Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFYVE27.
  24. "Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
    Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
    J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO5B, IDENTIFICATION IN A COMPLEX WITH MYO5B AND CFTR.
  25. Cited for: INTERACTION WITH RAB11FIP3 AND EVI5.
  26. "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.
  27. "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
    Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
    J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPC1L1, MUTAGENESIS OF SER-25.
  28. "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.
  29. Cited for: INTERACTION WITH VIPAS39.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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.
  32. "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.
  33. "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
    Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
    J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TBC1D14.
  34. "UNC119a bridges the transmission of Fyn signals to Rab11, leading to the completion of cytokinesis."
    Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.
    Cell Cycle 12:1303-1315(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC119.
  35. "Large-scale top down proteomics of the human proteome: membrane proteins, mitochondria, and senescence."
    Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T., Tran J.C., Thomas P.M., Kelleher N.L.
    Mol. Cell. Proteomics 12:3465-3473(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
  36. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
    Eathiraj S., Pan X., Ritacco C., Lambright D.G.
    Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP ANALOG.
  37. "Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein."
    Pasqualato S., Cherfils J.
    Structure 13:533-540(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP ANALOG AND GDP, MUTAGENESIS OF GLN-70.
  38. "Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."
    Eathiraj S., Mishra A., Prekeris R., Lambright D.G.
    J. Mol. Biol. 364:121-135(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP AND RAB11FIP3, MUTAGENESIS OF GLN-70.
  39. "Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1."
    Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.
    Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF GLN-70.
  40. "Crystal structure of rab11 in complex with rab11 family interacting protein 2."
    Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
    Structure 14:1273-1283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP2, MUTAGENESIS OF GLN-70.

Entry informationi

Entry nameiRB11A_HUMAN
AccessioniPrimary (citable) accession number: P62491
Secondary accession number(s): B2R4B6
, B4DT13, P24410, Q5TZN9, Q9JLX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 131 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 15
    Human chromosome 15: 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