Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61021 (RAB5B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-5B
Gene names
Name:Rab5b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein transport. Probably involved in vesicular traffic By similarity.

Enzyme regulation

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

Subunit structure

Binds EEA1. Interacts with RIN2 and RIN3, which probably regulate its pathway, possibly by acting as GEFs By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane; Lipid-anchor. Melanosome By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0072EBI-8320093,EBI-5323863From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214Ras-related protein Rab-5B
PRO_0000121108

Regions

Nucleotide binding27 – 359GTP By similarity
Nucleotide binding75 – 795GTP By similarity
Nucleotide binding133 – 1364GTP By similarity
Nucleotide binding163 – 1653GTP By similarity
Motif49 – 579Effector region Potential

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Lipidation2121S-geranylgeranyl cysteine By similarity
Lipidation2131S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict561A → G in AAK14835. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P61021 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: D47AD834BCF8B591

FASTA21523,707
        10         20         30         40         50         60 
MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ 

        70         80         90        100        110        120 
SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR 

       130        140        150        160        170        180 
QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK 

       190        200        210 
LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN 

« Hide

References

« Hide 'large scale' references
[1]"Co-operative regulation of endocytosis by three Rab5 isoforms."
Bucci C., Lutcke A., Steele Mortimer O., Olkkonen V.M., Dupree P., Chiariello M., Bruni C.B., Simons K., Zerial M.
FEBS Lett. 366:65-71(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Corpus striatum.
[3]"The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach."
Chavrier P., Simons K., Zerial M.
Gene 112:261-264(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-80.
Tissue: Kidney.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 82-110, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84239 mRNA. Translation: CAA59016.1.
AK081251 mRNA. Translation: BAC38176.1.
M79311 mRNA. Translation: AAK14835.1.
CCDSCCDS24287.1.
PIRJH0640.
S65932.
RefSeqNP_803130.1. NM_177411.4.
XP_006513447.1. XM_006513384.1.
UniGeneMm.12815.
Mm.490984.

3D structure databases

ProteinModelPortalP61021.
SMRP61021. Positions 17-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202548. 2 interactions.
IntActP61021. 3 interactions.
MINTMINT-1865771.

PTM databases

PhosphoSiteP61021.

Proteomic databases

MaxQBP61021.
PaxDbP61021.
PRIDEP61021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000727; ENSMUSP00000000727; ENSMUSG00000000711.
GeneID19344.
KEGGmmu:19344.
UCSCuc007hnv.2. mouse.

Organism-specific databases

CTD5869.
MGIMGI:105938. Rab5b.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00640000091139.
HOVERGENHBG009351.
InParanoidP61021.
KOK07888.
OMAMENTHFD.
OrthoDBEOG77DJ7M.
PhylomeDBP61021.
TreeFamTF300199.

Gene expression databases

BgeeP61021.
CleanExMM_RAB5B.
GenevestigatorP61021.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio22794.
PROP61021.
SOURCESearch...

Entry information

Entry nameRAB5B_MOUSE
AccessionPrimary (citable) accession number: P61021
Secondary accession number(s): P35239, P35277
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot