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Q9ULW5 (RAB26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. 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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Participates in exocrine secretion: regulates the secretion of acinar granules in the parotid gland By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity.

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.

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

Sequence conflict2271Q → R in AAH66913. Ref.2

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]"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: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[3]"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: 11043516] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-256.
Tissue: Fetal brain.
[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] OF 67-256.
Tissue: Brain.
[5]"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
AC009065 Genomic DNA. No translation available.
BC066913 mRNA. Translation: AAH66913.1.
AB027137 mRNA. Translation: BAA84707.1. Different initiation.
AF498952 mRNA. Translation: AAM21100.1.
IPIIPI00419883.
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 58-254.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9ULW5. 1 interaction.
STRINGQ9ULW5.

Polymorphism databases

DMDM134044256.

Proteomic databases

PRIDEQ9ULW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000210187; ENSP00000210187; ENSG00000167964.
GeneID25837.
KEGGhsa:25837.
UCSCuc002cou.1. human.

Organism-specific databases

CTD25837.
GeneCardsGC16P002198.
H-InvDBHIX0038522.
HGNCHGNC:14259. RAB26.
MIM605455. gene.
neXtProtNX_Q9ULW5.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00600000084225.
HOGENOMHBG745225.
HOVERGENHBG009351.
InParanoidQ9ULW5.
OMAHERVVKR.
OrthoDBEOG4VMFG9.
PhylomeDBQ9ULW5.

Gene expression databases

ArrayExpressQ9ULW5.
BgeeQ9ULW5.
CleanExHS_RAB26.
GenevestigatorQ9ULW5.
GermOnlineENSG00000167964. Homo sapiens.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
KOK07913.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio47147.
SOURCESearch...

Entry information

Entry nameRAB26_HUMAN
AccessionPrimary (citable) accession number: Q9ULW5
Secondary accession number(s): Q6NXS7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 6, 2007
Last modified: January 25, 2012
This is version 113 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

Human chromosome 16

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families