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Q9ULW5 (RAB26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-26
Gene names
Name:RAB26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach. Plays a role in the secretion of amylase from acinar granules in the parotid gland. Ref.7 Ref.8

Subunit structure

Interacts with RIMS1 By similarity. Interacts with ADRA2B. Ref.8

Subcellular location

Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesiclesecretory vesicle membrane; Lipid-anchor; Cytoplasmic side Probable. Note: Not localized at the plasma membrane By similarity. Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location. Ref.8

Tissue specificity

Predominantly expressed in brain.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence BAA84707.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Ras-related protein Rab-26
PRO_0000121218

Regions

Nucleotide binding70 – 789GTP
Nucleotide binding119 – 1235GTP
Nucleotide binding177 – 1804GTP
Nucleotide binding207 – 2093GTP
Motif93 – 1019Effector region By similarity

Amino acid modifications

Lipidation2531S-geranylgeranyl cysteine By similarity
Lipidation2541S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis771T → N: Inactive, constitutively GDP-bound. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Ref.7 Ref.8
Mutagenesis1231Q → L: Constitutively activated. Ref.8
Mutagenesis1771N → I: Inactive, due to loss of GNP binding. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Ref.8
Sequence conflict2271Q → R in AAH66913. Ref.4

Secondary structure

........................... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ULW5 [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: 575232F4B9E7FA7E

FASTA25627,900
        10         20         30         40         50         60 
MSRKKTPKSK GASTPAASTL PTANGARPAR SGTALSGPDA PPNGPLQPGR PSLGGGVDFY 

        70         80         90        100        110        120 
DVAFKVMLVG DSGVGKTCLL VRFKDGAFLA GTFISTVGID FRNKVLDVDG VKVKLQMWDT 

       130        140        150        160        170        180 
AGQERFRSVT HAYYRDAHAL LLLYDVTNKA SFDNIQAWLT EIHEYAQHDV ALMLLGNKVD 

       190        200        210        220        230        240 
SAHERVVKRE DGEKLAKEYG LPFMETSAKT GLNVDLAFTA IAKELKQRSM KAPSEPRFRL 

       250 
HDYVKREGRG ASCCRP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and characterization of human Ras-related oncogene Rab26."
Zhu N., Xu Y., Yang J., Li R.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Hippocampus.
[5]"cDNA cloning of a human RAB26-related gene encoding a Ras-like GTP-binding protein on chromosome 16p13.3 region."
Seki N., Yoshikawa T., Hattori A., Miyajima N., Muramatsu M., Saito T.
J. Hum. Genet. 45:309-314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-256.
Tissue: Fetal brain.
[6]"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] OF 67-256.
Tissue: Brain.
[7]"RAB26 and RAB3D are direct transcriptional targets of MIST1 that regulate exocrine granule maturation."
Tian X., Jin R.U., Bredemeyer A.J., Oates E.J., Blazewska K.M., McKenna C.E., Mills J.C.
Mol. Cell. Biol. 30:1269-1284(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-77.
[8]"Rab26 modulates the cell surface transport of alpha2-adrenergic receptors from the Golgi."
Li C., Fan Y., Lan T.H., Lambert N.A., Wu G.
J. Biol. Chem. 287:42784-42794(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ADRA2B, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-77; GLN-123 AND ASN-177.
[9]"Crystal structure of human RAB26 in complex with a GTP analogue."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-233 IN COMPLEX WITH GTP ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY646153 mRNA. Translation: AAU88191.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85552.1.
BC066913 mRNA. Translation: AAH66913.1.
AB027137 mRNA. Translation: BAA84707.1. Different initiation.
AF498952 mRNA. Translation: AAM21100.1.
RefSeqNP_055168.2. NM_014353.4.
UniGeneHs.3797.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G6BX-ray2.00A56-233[»]
ProteinModelPortalQ9ULW5.
SMRQ9ULW5. Positions 58-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117364. 6 interactions.
IntActQ9ULW5. 1 interaction.
STRING9606.ENSP00000210187.

PTM databases

PhosphoSiteQ9ULW5.

Polymorphism databases

DMDM134044256.

Proteomic databases

PaxDbQ9ULW5.
PRIDEQ9ULW5.

Protocols and materials databases

DNASU25837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000210187; ENSP00000210187; ENSG00000167964.
GeneID25837.
KEGGhsa:25837.
UCSCuc002cou.3. human.

Organism-specific databases

CTD25837.
GeneCardsGC16P002190.
HGNCHGNC:14259. RAB26.
HPAHPA050223.
MIM605455. gene.
neXtProtNX_Q9ULW5.
PharmGKBPA34116.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9ULW5.
KOK07913.
OMAPSEPRFR.
PhylomeDBQ9ULW5.
TreeFamTF323428.

Gene expression databases

ArrayExpressQ9ULW5.
BgeeQ9ULW5.
CleanExHS_RAB26.
GenevestigatorQ9ULW5.

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

ChiTaRSRAB26. human.
EvolutionaryTraceQ9ULW5.
GeneWikiRAB26.
GenomeRNAi25837.
NextBio47147.
PROQ9ULW5.
SOURCESearch...

Entry information

Entry nameRAB26_HUMAN
AccessionPrimary (citable) accession number: Q9ULW5
Secondary accession number(s): Q3L6K5, Q6NXS7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM