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Protein

Ras-related protein Rab-5A

Gene

RAB5A

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. 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. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. early endosome to late endosome transport Source: UniProtKB
  3. endocytosis Source: UniProtKB
  4. GTP catabolic process Source: UniProtKB
  5. intracellular protein transport Source: GO_Central
  6. positive regulation of exocytosis Source: UniProtKB
  7. positive regulation of smooth muscle cell migration Source: Ensembl
  8. positive regulation of smooth muscle cell proliferation Source: Ensembl
  9. Rab protein signal transduction Source: GO_Central
  10. receptor internalization involved in canonical Wnt signaling pathway Source: BHF-UCL
  11. regulation of endocytosis Source: GO_Central
  12. regulation of endosome size Source: UniProtKB
  13. regulation of filopodium assembly Source: UniProtKB
  14. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  15. regulation of synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  16. synaptic vesicle recycling Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Biological processi

Endocytosis, 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 By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Early endosome membrane By similarity; 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.

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. axon Source: ParkinsonsUK-UCL
  3. axon terminus Source: ParkinsonsUK-UCL
  4. cytoplasm Source: MGI
  5. cytoplasmic side of early endosome membrane Source: UniProtKB
  6. cytosol Source: UniProtKB
  7. dendrite Source: ParkinsonsUK-UCL
  8. early endosome Source: UniProtKB
  9. endocytic vesicle Source: GO_Central
  10. endosome Source: ParkinsonsUK-UCL
  11. endosome membrane Source: Reactome
  12. extracellular vesicular exosome Source: UniProtKB
  13. melanosome Source: UniProtKB-SubCell
  14. membrane raft Source: Ensembl
  15. neuronal cell body Source: ParkinsonsUK-UCL
  16. perinuclear region of cytoplasm Source: Ensembl
  17. phagocytic vesicle Source: Ensembl
  18. plasma membrane Source: GO_Central
  19. protein complex Source: Ensembl
  20. recycling endosome Source: Ensembl
  21. ruffle Source: UniProtKB-SubCell
  22. somatodendritic compartment Source: ParkinsonsUK-UCL
  23. synaptic vesicle Source: ParkinsonsUK-UCL
  24. terminal bouton Source: ParkinsonsUK-UCL
  25. zymogen granule membrane Source: Ensembl
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-5APRO_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

BgeeiP20339.
CleanExiHS_RAB5A.
ExpressionAtlasiP20339. baseline and differential.
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.By similarity11 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. 71 interactions.
DIPiDIP-380N.
IntActiP20339. 21 interactions.
MINTiMINT-209361.
STRINGi9606.ENSP00000273047.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 2610Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 4210Combined sources
Beta strandi53 – 6412Combined sources
Beta strandi67 – 7610Combined sources
Helixi80 – 856Combined sources
Helixi86 – 905Combined sources
Beta strandi94 – 1018Combined sources
Helixi105 – 12117Combined sources
Beta strandi127 – 1337Combined sources
Helixi135 – 1406Combined sources
Helixi145 – 15410Combined sources
Beta strandi158 – 1614Combined sources
Turni164 – 1663Combined sources
Helixi170 – 17910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4Q9UX-ray4.62B/F15-184[»]
ProteinModelPortaliP20339.
SMRiP20339. Positions 15-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20339.

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
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. AlignAdd to basket

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

        10         20         30         40         50
MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE
60 70 80 90 100
STIGAAFLTQ TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY
110 120 130 140 150
DITNEESFAR AKNWVKELQR QASPNIVIAL SGNKADLANK RAVDFQEAQS
160 170 180 190 200
YADDNSLLFM ETSAKTSMNV NEIFMAIAKK LPKNEPQNPG ANSARGRGVD
210
LTEPTQPTRN QCCSN
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811R → G in AAA60245 (PubMed:2501306).Curated
Sequence conflicti197 – 1971R → G in AAA60245 (PubMed:2501306).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 6814Missing in isoform 2. 1 PublicationVSP_055830Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P20339-1]
PIRiF34323.
RefSeqiNP_001278977.1. NM_001292048.1. [P20339-2]
NP_004153.2. NM_004162.4. [P20339-1]
UniGeneiHs.475663.

Genome annotation databases

EnsembliENST00000273047; ENSP00000273047; ENSG00000144566. [P20339-1]
ENST00000422242; ENSP00000411941; ENSG00000144566. [P20339-2]
GeneIDi5868.
KEGGihsa:5868.
UCSCiuc003cbn.3. human. [P20339-1]
uc011awg.2. human.

Polymorphism databases

DMDMi1346958.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P20339-1]
PIRiF34323.
RefSeqiNP_001278977.1. NM_001292048.1. [P20339-2]
NP_004153.2. NM_004162.4. [P20339-1]
UniGeneiHs.475663.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4Q9UX-ray4.62B/F15-184[»]
ProteinModelPortaliP20339.
SMRiP20339. Positions 15-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111806. 71 interactions.
DIPiDIP-380N.
IntActiP20339. 21 interactions.
MINTiMINT-209361.
STRINGi9606.ENSP00000273047.

PTM databases

PhosphoSiteiP20339.

Polymorphism databases

DMDMi1346958.

Proteomic databases

MaxQBiP20339.
PaxDbiP20339.
PRIDEiP20339.

Protocols and materials databases

DNASUi5868.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273047; ENSP00000273047; ENSG00000144566. [P20339-1]
ENST00000422242; ENSP00000411941; ENSG00000144566. [P20339-2]
GeneIDi5868.
KEGGihsa:5868.
UCSCiuc003cbn.3. human. [P20339-1]
uc011awg.2. human.

Organism-specific databases

CTDi5868.
GeneCardsiGC03P019963.
HGNCiHGNC:9783. RAB5A.
HPAiCAB004567.
MIMi179512. gene.
neXtProtiNX_P20339.
PharmGKBiPA34143.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP20339.
KOiK07887.
OMAiPKSQCCS.
OrthoDBiEOG77DJ7M.
PhylomeDBiP20339.
TreeFamiTF300199.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiRAB5A. human.
EvolutionaryTraceiP20339.
GeneWikiiRAB5A.
GenomeRNAii5868.
NextBioi22790.
PROiP20339.
SOURCEiSearch...

Gene expression databases

BgeeiP20339.
CleanExiHS_RAB5A.
ExpressionAtlasiP20339. baseline and differential.
GenevestigatoriP20339.

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(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: March 4, 2015
This is version 169 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

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.