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O75436 (VP26A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein sorting-associated protein 26A
Alternative name(s):
Vesicle protein sorting 26A
Short name=hVPS26
Gene names
Name:VPS26A
Synonyms:VPS26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Ref.8 Ref.11

Subunit structure

Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts directly with VPS35. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with ECM29. Ref.1 Ref.7 Ref.10 Ref.14 Ref.17

Subcellular location

Cytoplasm. Endosome membrane; Peripheral membrane protein Ref.10 Ref.14 Ref.17.

Induction

Down-regulated in Alzheimer disease. No polymorphism or variant is however associated with Alzheimer disease for VPS26A. Ref.9 Ref.13

Sequence similarities

Belongs to the VPS26 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75436-1)

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.
Isoform 2 (identifier: O75436-2)

The sequence of this isoform differs from the canonical sequence as follows:
     243-327: GESIPIRLFL...SQASAEQPEM → GDNFMEKSS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Vacuolar protein sorting-associated protein 26A
PRO_0000073007

Amino acid modifications

Modified residue3151Phosphoserine Ref.15

Natural variations

Alternative sequence243 – 32785GESIP…EQPEM → GDNFMEKSS in isoform 2.
VSP_044910

Experimental info

Mutagenesis235 – 2362IM → DD: Abolishes interaction with VPS35 and endosomal subcellular location. Ref.17
Sequence conflict751Q → R in BAB14351. Ref.3
Sequence conflict2421K → Q in BQ048905. Ref.6
Sequence conflict285 – 2862RY → SS in AAF89954. Ref.1
Sequence conflict285 – 2862RY → SS in AAC39912. Ref.2
Isoform 2:
Sequence conflict2431G → R in BQ048905. Ref.6

Secondary structure

................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: BD3B2EAA6CFCBFA9

FASTA32738,170
        10         20         30         40         50         60 
MSFLGGFFGP ICEIDIVLND GETRKMAEMK TEDGKVEKHY LFYDGESVSG KVNLAFKQPG 

        70         80         90        100        110        120 
KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE LTQSRSYDFE FMQVEKPYES 

       130        140        150        160        170        180 
YIGANVRLRY FLKVTIVRRL TDLVKEYDLI VHQLATYPDV NNSIKMEVGI EDCLHIEFEY 

       190        200        210        220        230        240 
NKSKYHLKDV IVGKIYFLLV RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP 

       250        260        270        280        290        300 
VKGESIPIRL FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE 

       310        320 
KLRKQRTNFH QRFESPESQA SAEQPEM 

« Hide

Isoform 2 [UniParc].

Checksum: 1140DC4C2D80D257
Show »

FASTA25128,938

References

« Hide 'large scale' references
[1]"Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes."
Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A., Barr V.A., Taylor S.I.
Mol. Biol. Cell 11:4105-4116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VPS29; VPS35; SNX1 AND SNX2.
Tissue: Colon.
[2]"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Tongue.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-249 (ISOFORM 2).
Tissue: Brain and Embryonic testis carcinoma.
[7]"Exportin 7 defines a novel general nuclear export pathway."
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS29; VPS35 AND SFN.
[8]"The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor."
Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L., Burlingame A.L., Haft C.R., Mostov K.E.
Nat. Cell Biol. 6:763-769(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Model-guided microarray implicates the retromer complex in Alzheimer's disease."
Small S.A., Kent K., Pierce A., Leung C., Kang M.S., Okada H., Honig L., Vonsattel J.-P., Kim T.-W.
Ann. Neurol. 58:909-919(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"A novel mammalian retromer component, Vps26B."
Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C., Gleeson P.A., Wicking C., Teasdale R.D.
Traffic 6:991-1001(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VPS35.
[11]"An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins."
Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T., Trejo J.
Mol. Biol. Cell 17:1228-1238(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"No association of vacuolar protein sorting 26 polymorphisms with Alzheimer's disease."
Riemenschneider M., Schoepfer-Wendels A., Friedrich P., Konta L., Laws S.M., Mueller J.C., Kurz A., Forstl H.
Neurobiol. Aging 28:883-884(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain."
Shi H., Rojas R., Bonifacino J.S., Hurley J.H.
Nat. Struct. Mol. Biol. 13:540-548(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, INTERACTION WITH VPS35, MUTAGENESIS OF 236-ILE-MET-237.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF175266 mRNA. Translation: AAF89954.1.
AF054179 mRNA. Translation: AAC39912.1.
AK022992 mRNA. Translation: BAB14351.1.
AK315496 mRNA. Translation: BAG37880.1.
AL596223, AL442635 Genomic DNA. Translation: CAH71501.1.
AL442635, AL596223 Genomic DNA. Translation: CAH71779.1.
CH471083 Genomic DNA. Translation: EAW54313.1.
BC022505 mRNA. Translation: AAH22505.1.
BQ048905 mRNA. No translation available.
CCDSCCDS41536.1. [O75436-2]
CCDS7286.1. [O75436-1]
RefSeqNP_001030337.1. NM_001035260.1. [O75436-2]
NP_004887.2. NM_004896.3. [O75436-1]
UniGeneHs.499925.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FAUX-ray2.10A1-327[»]
ProteinModelPortalO75436.
SMRO75436. Positions 6-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114930. 58 interactions.
DIPDIP-29075N.
IntActO75436. 2 interactions.
MINTMINT-5000831.
STRING9606.ENSP00000263559.

PTM databases

PhosphoSiteO75436.

Proteomic databases

MaxQBO75436.
PaxDbO75436.
PeptideAtlasO75436.
PRIDEO75436.

Protocols and materials databases

DNASU9559.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263559; ENSP00000263559; ENSG00000122958. [O75436-1]
ENST00000373382; ENSP00000362480; ENSG00000122958. [O75436-1]
ENST00000395098; ENSP00000378532; ENSG00000122958. [O75436-2]
GeneID9559.
KEGGhsa:9559.
UCSCuc001jpb.3. human. [O75436-1]

Organism-specific databases

CTD9559.
GeneCardsGC10P070885.
HGNCHGNC:12711. VPS26A.
HPACAB011602.
HPA044581.
MIM605506. gene.
neXtProtNX_O75436.
PharmGKBPA37326.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256244.
HOGENOMHOG000191799.
HOVERGENHBG082914.
InParanoidO75436.
OMAPVCEIDV.
OrthoDBEOG7NW699.
PhylomeDBO75436.
TreeFamTF300907.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO75436.
BgeeO75436.
CleanExHS_VPS26A.
GenevestigatorO75436.

Family and domain databases

InterProIPR028934. Vps26-related.
[Graphical view]
PfamPF03643. Vps26. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVPS26A. human.
EvolutionaryTraceO75436.
GeneWikiVPS26A.
GenomeRNAi9559.
NextBio35853.
PROO75436.
SOURCESearch...

Entry information

Entry nameVP26A_HUMAN
AccessionPrimary (citable) accession number: O75436
Secondary accession number(s): A8MZ56 expand/collapse secondary AC list , B2RDD3, Q8TBH4, Q9H982
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 25, 2002
Last modified: July 9, 2014
This is version 125 of the entry and version 2 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 10

Human chromosome 10: entries, gene names and cross-references to MIM