Q9ULW5 (RAB26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-26

Gene names

Name:

RAB26

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › secretory 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasmic vesicle Golgi apparatus Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi to plasma membrane protein transport Inferred from mutant phenotype Ref.8. Source: UniProtKB exocrine system development Inferred from mutant phenotype Ref.7. Source: UniProtKB regulated secretory pathway Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of exocytosis Inferred from sequence or structural similarity. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi membrane Inferred from direct assay Ref.8. Source: UniProtKB intrinsic to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB secretory granule membrane Inferred from sequence or structural similarity. Source: UniProtKB transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GMP binding Inferred from mutant phenotype Ref.8. Source: UniProtKB GTP binding Inferred from mutant phenotype Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 256

256

Ras-related protein Rab-26

PRO_0000121218

Regions

Nucleotide binding

70 – 78

9

GTP

Nucleotide binding

119 – 123

5

GTP

Nucleotide binding

177 – 180

4

GTP

Nucleotide binding

207 – 209

3

GTP

Motif

93 – 101

9

Effector region By similarity

Amino acid modifications

Lipidation

253

1

S-geranylgeranyl cysteine By similarity

Lipidation

254

1

S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis

77

1

T → 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

Mutagenesis

123

1

Q → L: Constitutively activated. Ref.8

Mutagenesis

177

1

N → 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 conflict

227

1

Q → R in AAH66913. Ref.4

Secondary structure

1

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256

Helix Strand Turn

Details...

Beta strand

61 – 69

9

Helix

76 – 85

10

Beta strand

100 – 108

9

Beta strand

111 – 119

9

Helix

134 – 136

3

Beta strand

138 – 145

8

Helix

149 – 153

5

Helix

155 – 165

11

Beta strand

171 – 177

7

Helix

189 – 198

10

Beta strand

203 – 205

3

Turn

208 – 210

3

Helix

214 – 226

13

Sequences

	Sequence		Length	Mass (Da)
	Q9ULW5 [UniParc]. Last modified March 6, 2007. Version 3. Checksum: 575232F4B9E7FA7E	FASTA	256	27,900
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00419883.

RefSeq

NP_055168.2. NM_014353.4.

UniGene

Hs.3797.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G6B	X-ray	2.00	A	56-233	[»]

ProteinModelPortal

Q9ULW5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9ULW5. 1 interaction.

STRING

9606.ENSP00000210187.

PTM databases

PhosphoSite

Q9ULW5.

Polymorphism databases

DMDM

134044256.

Proteomic databases

PaxDb

Q9ULW5.

PRIDE

Q9ULW5.

Protocols and materials databases

DNASU

25837.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000210187; ENSP00000210187; ENSG00000167964.

GeneID

25837.

KEGG

hsa:25837.

UCSC

uc002cou.3. human.

Organism-specific databases

CTD

25837.

GeneCards

GC16P002190.

HGNC

HGNC:14259. RAB26.

HPA

HPA050223.

MIM

605455. gene.

neXtProt

NX_Q9ULW5.

PharmGKB

PA34116.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

Q9ULW5.

KO

K07913.

OMA

PSEPRFR.

OrthoDB

EOG4VMFG9.

PhylomeDB

Q9ULW5.

Gene expression databases

ArrayExpress

Q9ULW5.

Bgee

Q9ULW5.

CleanEx

HS_RAB26.

Genevestigator

Q9ULW5.

GermOnline

ENSG00000167964. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB26. human.

EvolutionaryTrace

Q9ULW5.

GenomeRNAi

25837.

NextBio

47147.

SOURCE

Search...

Entry information

Entry name

RAB26_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.