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P20339

- RAB5A_HUMAN

UniProt

P20339 - RAB5A_HUMAN

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Protein
Ras-related protein Rab-5A
Gene
RAB5A, RAB5
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. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension.5 Publications

Enzyme regulationi

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359GTP
Nucleotide bindingi46 – 527GTP
Nucleotide bindingi75 – 795GTP
Nucleotide bindingi133 – 1364GTP
Nucleotide bindingi163 – 1653GTP

GO - Molecular functioni

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

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. blood coagulation Source: Reactome
  3. cell differentiation Source: UniProtKB-KW
  4. endocytosis Source: UniProtKB
  5. nervous system development Source: UniProtKB-KW
  6. positive regulation of exocytosis Source: UniProtKB
  7. protein transport Source: UniProtKB-KW
  8. receptor internalization involved in canonical Wnt signaling pathway Source: BHF-UCL
  9. regulation of filopodium assembly Source: UniProtKB
  10. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Differentiation, Endocytosis, Neurogenesis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-5A
Gene namesi
Name:RAB5A
Synonyms:RAB5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9783. RAB5A.

Subcellular locationi

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Early endosome membrane; Lipid-anchor By similarity. Melanosome. Cytoplasmic vesicle By similarity. Cell projectionruffle By similarity. Membrane. Cytoplasmcytosol
Note: Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms.2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cytoplasm Source: MGI
  3. cytosol Source: UniProtKB-SubCell
  4. early endosome Source: UniProtKB
  5. early endosome membrane Source: UniProtKB-SubCell
  6. endocytic vesicle Source: Ensembl
  7. endosome membrane Source: Reactome
  8. extracellular vesicular exosome Source: UniProt
  9. melanosome Source: UniProtKB-SubCell
  10. membrane raft Source: Ensembl
  11. plasma membrane Source: UniProtKB-SubCell
  12. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541G → Q: Strongly decreases ZFYVE20 binding affinity. 1 Publication
Mutagenesisi56 – 561A → E: Strongly decreases ZFYVE20 binding affinity. 1 Publication
Mutagenesisi57 – 571F → A: Strongly decreases RABEP1 and ZFYVE20 binding affinity. 2 Publications
Mutagenesisi74 – 741W → A: Strongly decreases RABEP1 binding affinity. 1 Publication
Mutagenesisi79 – 791Q → L: Loss of GTPase activity. Does not inhibit filopodia formation. 2 Publications
Mutagenesisi82 – 821Y → A: Strongly decreases RABEP1 binding affinity. Impairs endosome fusion. 1 Publication
Mutagenesisi89 – 891Y → A: Strongly decreases RABEP1 binding affinity. 1 Publication
Mutagenesisi116 – 1161K → E: No effect on RABEP1 binding affinity. 1 Publication
Mutagenesisi120 – 1201R → E: No effect on RABEP1 binding affinity. 1 Publication

Organism-specific databases

PharmGKBiPA34143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Ras-related protein Rab-5A
PRO_0000121104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi212 – 2121S-geranylgeranyl cysteine1 Publication
Lipidationi213 – 2131S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiP20339.
PaxDbiP20339.
PRIDEiP20339.

PTM databases

PhosphoSiteiP20339.

Expressioni

Gene expression databases

ArrayExpressiP20339.
BgeeiP20339.
CleanExiHS_RAB5A.
GenevestigatoriP20339.

Organism-specific databases

HPAiCAB004567.

Interactioni

Subunit structurei

Interacts with SGSM1 and SGSM3 By similarity. Interacts with PIK3CB By similarity. Interacts with GDI1; this promotes dissociation from membranes. Interacts with EEA1. Interacts with RIN1 and GAPVD1, which regulate its pathway, probably by acting as a GEF. Interacts with RINL. Interacts with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RABEP1; one RABEP1 homodimer binds two RAB5A chains, but at opposite sides of the dimer.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALS2Q96Q422EBI-399437,EBI-1044902
APPL1Q9UKG117EBI-399437,EBI-741243
EEA1Q150754EBI-399437,EBI-298113
OCRLQ0196810EBI-399437,EBI-6148898
PIK3R1P237275EBI-399437,EBI-520244From a different organism.

Protein-protein interaction databases

BioGridi111806. 63 interactions.
DIPiDIP-380N.
IntActiP20339. 21 interactions.
MINTiMINT-209361.
STRINGi9606.ENSP00000273047.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 2610
Beta strandi28 – 325
Helixi33 – 4210
Beta strandi53 – 6412
Beta strandi67 – 7610
Helixi80 – 856
Helixi86 – 905
Beta strandi94 – 1018
Helixi105 – 12117
Beta strandi127 – 1337
Helixi135 – 1406
Helixi145 – 15410
Beta strandi158 – 1614
Turni164 – 1663
Helixi170 – 17910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6HX-ray1.51A15-184[»]
1N6IX-ray1.60A15-184[»]
1N6KX-ray1.55A15-184[»]
1N6LX-ray1.60A15-184[»]
1N6NX-ray1.60A15-184[»]
1N6OX-ray1.80A15-184[»]
1N6PX-ray1.54A15-184[»]
1N6RX-ray1.55A15-184[»]
1R2QX-ray1.05A15-184[»]
1TU3X-ray2.31A/B/C/D/E15-184[»]
1TU4X-ray2.20A/B/C/D15-184[»]
3MJHX-ray2.03A/C16-183[»]
ProteinModelPortaliP20339.
SMRiP20339. Positions 15-184.

Miscellaneous databases

EvolutionaryTraceiP20339.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 579Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP20339.
KOiK07887.
OMAiPKSQCCS.
OrthoDBiEOG77DJ7M.
PhylomeDBiP20339.
TreeFamiTF300199.

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.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20339-1) [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

MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE    50
STIGAAFLTQ TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY 100
DITNEESFAR AKNWVKELQR QASPNIVIAL SGNKADLANK RAVDFQEAQS 150
YADDNSLLFM ETSAKTSMNV NEIFMAIAKK LPKNEPQNPG ANSARGRGVD 200
LTEPTQPTRN QCCSN 215
Length:215
Mass (Da):23,659
Last modified:February 1, 1996 - v2
Checksum:iEC03DDF96BBEF821
GO
Isoform 2 (identifier: P20339-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-68: Missing.

Note: No experimental confirmation available.

Show »
Length:201
Mass (Da):22,178
Checksum:i4A63017DEF84F328
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 6814Missing in isoform 2.
VSP_055830Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811R → G in AAA60245. 1 Publication
Sequence conflicti197 – 1971R → G in AAA60245. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28215 mRNA. Translation: AAA60245.1.
AF464088 mRNA. Translation: AAO15677.1.
AF498936 mRNA. Translation: AAM21084.1.
AK295992 mRNA. Translation: BAG58767.1.
AK312618 mRNA. Translation: BAG35504.1.
CR536492 mRNA. Translation: CAG38731.1.
AC097635 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64301.1.
BC001267 mRNA. Translation: AAH01267.1.
BC018288 mRNA. Translation: AAH18288.1.
CCDSiCCDS2633.1.
PIRiF34323.
RefSeqiNP_004153.2. NM_004162.4.
UniGeneiHs.475663.

Genome annotation databases

EnsembliENST00000273047; ENSP00000273047; ENSG00000144566.
ENST00000422242; ENSP00000411941; ENSG00000144566.
GeneIDi5868.
KEGGihsa:5868.
UCSCiuc003cbn.3. human.

Polymorphism databases

DMDMi1346958.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28215 mRNA. Translation: AAA60245.1 .
AF464088 mRNA. Translation: AAO15677.1 .
AF498936 mRNA. Translation: AAM21084.1 .
AK295992 mRNA. Translation: BAG58767.1 .
AK312618 mRNA. Translation: BAG35504.1 .
CR536492 mRNA. Translation: CAG38731.1 .
AC097635 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64301.1 .
BC001267 mRNA. Translation: AAH01267.1 .
BC018288 mRNA. Translation: AAH18288.1 .
CCDSi CCDS2633.1.
PIRi F34323.
RefSeqi NP_004153.2. NM_004162.4.
UniGenei Hs.475663.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N6H X-ray 1.51 A 15-184 [» ]
1N6I X-ray 1.60 A 15-184 [» ]
1N6K X-ray 1.55 A 15-184 [» ]
1N6L X-ray 1.60 A 15-184 [» ]
1N6N X-ray 1.60 A 15-184 [» ]
1N6O X-ray 1.80 A 15-184 [» ]
1N6P X-ray 1.54 A 15-184 [» ]
1N6R X-ray 1.55 A 15-184 [» ]
1R2Q X-ray 1.05 A 15-184 [» ]
1TU3 X-ray 2.31 A/B/C/D/E 15-184 [» ]
1TU4 X-ray 2.20 A/B/C/D 15-184 [» ]
3MJH X-ray 2.03 A/C 16-183 [» ]
ProteinModelPortali P20339.
SMRi P20339. Positions 15-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111806. 63 interactions.
DIPi DIP-380N.
IntActi P20339. 21 interactions.
MINTi MINT-209361.
STRINGi 9606.ENSP00000273047.

PTM databases

PhosphoSitei P20339.

Polymorphism databases

DMDMi 1346958.

Proteomic databases

MaxQBi P20339.
PaxDbi P20339.
PRIDEi P20339.

Protocols and materials databases

DNASUi 5868.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000273047 ; ENSP00000273047 ; ENSG00000144566 .
ENST00000422242 ; ENSP00000411941 ; ENSG00000144566 .
GeneIDi 5868.
KEGGi hsa:5868.
UCSCi uc003cbn.3. human.

Organism-specific databases

CTDi 5868.
GeneCardsi GC03P019963.
HGNCi HGNC:9783. RAB5A.
HPAi CAB004567.
MIMi 179512. gene.
neXtProti NX_P20339.
PharmGKBi PA34143.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P20339.
KOi K07887.
OMAi PKSQCCS.
OrthoDBi EOG77DJ7M.
PhylomeDBi P20339.
TreeFami TF300199.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi RAB5A. human.
EvolutionaryTracei P20339.
GeneWikii RAB5A.
GenomeRNAii 5868.
NextBioi 22790.
PROi P20339.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20339.
Bgeei P20339.
CleanExi HS_RAB5A.
Genevestigatori P20339.

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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Identification of a new oncogene in human cancers."
    Kim J.W.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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. "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 and Subthalamic nucleus.
  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, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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: Cervix and Placenta.
  10. Cited for: INTERACTION WITH EEA1.
  11. "A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion."
    Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E., Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.
    J. Biol. Chem. 275:24661-24669(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN2, FUNCTION.
  12. "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain."
    Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M., Dewitte F., Wilm M., Hoflack B., Zerial M.
    J. Cell Biol. 151:601-612(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFYVE20.
    Tissue: Cervix carcinoma.
  13. "Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1."
    Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.
    Dev. Cell 1:73-82(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION BY RIN1.
  14. "ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics."
    Hadano S., Otomo A., Suzuki-Utsunomiya K., Kunita R., Yanagisawa Y., Showguchi-Miyata J., Mizumura H., Ikeda J.-E.
    FEBS Lett. 575:64-70(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALS2CL.
  15. Cited for: FUNCTION, INTERACTION WITH RUFY1.
  16. "Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
    Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
    Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-79.
  17. "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: INTERACTION WITH ZFYVE20, MUTAGENESIS OF GLY-54; ALA-56 AND PHE-57.
  18. "Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis."
    Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L., Barbieri M.A.
    Biochem. Biophys. Res. Commun. 340:967-975(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GAPVD1.
  19. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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: INTERACTION WITH GDI1, SUBCELLULAR LOCATION.
  23. "High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop."
    Zhu G., Liu J., Terzyan S., Zhai P., Li G., Zhang X.C.
    J. Biol. Chem. 278:2452-2460(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  24. "Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution."
    Terzyan S., Zhu G., Li G., Zhang X.C.
    Acta Crystallogr. D 60:54-60(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP ANALOG.
  25. "Structural basis of Rab5-Rabaptin5 interaction in endocytosis."
    Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.
    Nat. Struct. Mol. Biol. 11:975-983(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP ANALOG; GDP AND RABEP1, FUNCTION, INTERACTION WITH RABEP1, MUTAGENESIS OF PHE-57; TRP-74; GLN-79; TYR-82; TYR-89; LYS-116 AND ARG-120.
  26. "Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of early endosomal autoantigen 1 (EEA1)."
    Mishra A., Eathiraj S., Corvera S., Lambright D.G.
    Proc. Natl. Acad. Sci. U.S.A. 107:10866-10871(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 16-183 OF MUTANT LEU-79 IN COMPLEX WITH EEA1, INTERACTION WITH EEA1.

Entry informationi

Entry nameiRAB5A_HUMAN
AccessioniPrimary (citable) accession number: P20339
Secondary accession number(s): B4DJA5, Q6FI44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 163 of the entry and version 2 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 3
    Human chromosome 3: 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

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