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Protein

Vacuolar protein sorting-associated protein 26A

Gene

VPS26A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins (Probable). The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902, PubMed:15078903). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15247922). Required for the endosomal localization of FAM21A (indicative for the WASH complex) (PubMed:22070227). Required for the endosomal localization of TBC1D5 (PubMed:20923837). Mediates retromer cargo reognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (PubMed:22279231). Involved in retromer-independent lysosomal sorting of F2R (PubMed:16407403). Involved in recycling of ADRB2 (PubMed:21602791). Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity).By similarity6 Publications4 PublicationsCurated

GO - Molecular functioni

  1. protein transporter activity Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: GO_Central
  2. retrograde transport, endosome to Golgi Source: UniProtKB
  3. retrograde transport, endosome to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 26A
Alternative name(s):
Vesicle protein sorting 26A
Short name:
hVPS26
Gene namesi
Name:VPS26A
Synonyms:VPS26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12711. VPS26A.

Subcellular locationi

Cytoplasm. Endosome membrane; Peripheral membrane protein. Early endosome 1 Publication
Note: Localizes to tubular profiles adjacent to endosomes (PubMed:15078903). Predominantly found in early not late endosomes (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. early endosome Source: UniProtKB
  3. endosome Source: UniProtKB
  4. endosome membrane Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProtKB
  6. intracellular membrane-bounded organelle Source: HPA
  7. retromer complex Source: GO_Central
  8. tubular endosome Source: UniProtKB
  9. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2362IM → DD: Abolishes interaction with VPS35 and endosomal subcellular location.

Organism-specific databases

PharmGKBiPA37326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Vacuolar protein sorting-associated protein 26APRO_0000073007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75436.
PaxDbiO75436.
PeptideAtlasiO75436.
PRIDEiO75436.

PTM databases

PhosphoSiteiO75436.

Expressioni

Inductioni

Down-regulated in Alzheimer disease. No polymorphism or variant is however associated with Alzheimer disease for VPS26A.2 Publications

Gene expression databases

BgeeiO75436.
CleanExiHS_VPS26A.
ExpressionAtlasiO75436. baseline and differential.
GenevestigatoriO75436.

Organism-specific databases

HPAiCAB011602.
HPA044581.

Interactioni

Subunit structurei

Component of the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:11102511). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (By similarity). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (Probable). Interacts with VPS29, VPS35, SNX1, SNX2, SNX5, SNX6, SNX3, SNX27, RAB7A, ECM29, EHD1, KIAA0196, SORL1 (PubMed:11102511, PubMed:16190980, PubMed:19619496, PubMed:17868075 PubMed:19531583, PubMed:20682791, PubMed:20923837PubMed:21725319, PubMed:22279231, PubMed:24344282, PubMed:16732284).By similarity11 Publications3 Publications

Protein-protein interaction databases

BioGridi114930. 61 interactions.
DIPiDIP-29075N.
IntActiO75436. 2 interactions.
MINTiMINT-5000831.
STRINGi9606.ENSP00000263559.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 115Combined sources
Beta strandi12 – 187Combined sources
Helixi21 – 233Combined sources
Beta strandi26 – 305Combined sources
Beta strandi36 – 427Combined sources
Beta strandi48 – 6013Combined sources
Beta strandi63 – 664Combined sources
Beta strandi68 – 7811Combined sources
Beta strandi85 – 9612Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi124 – 13613Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1519Combined sources
Beta strandi164 – 1707Combined sources
Turni171 – 1733Combined sources
Beta strandi174 – 1818Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi190 – 20011Combined sources
Beta strandi204 – 21815Combined sources
Helixi220 – 2223Combined sources
Beta strandi224 – 23411Combined sources
Beta strandi246 – 2527Combined sources
Turni253 – 2553Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi268 – 28013Combined sources
Beta strandi285 – 29511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FAUX-ray2.10A1-327[»]
ProteinModelPortaliO75436.
SMRiO75436. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75436.

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS26 family.Curated

Phylogenomic databases

eggNOGiNOG256244.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiO75436.
KOiK18466.
OMAiSDKSNTH.
OrthoDBiEOG7NW699.
PhylomeDBiO75436.
TreeFamiTF300907.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75436-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSFLGGFFGP ICEIDIVLND GETRKMAEMK TEDGKVEKHY LFYDGESVSG
60 70 80 90 100
KVNLAFKQPG KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE
110 120 130 140 150
LTQSRSYDFE FMQVEKPYES YIGANVRLRY FLKVTIVRRL TDLVKEYDLI
160 170 180 190 200
VHQLATYPDV NNSIKMEVGI EDCLHIEFEY NKSKYHLKDV IVGKIYFLLV
210 220 230 240 250
RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP VKGESIPIRL
260 270 280 290 300
FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE
310 320
KLRKQRTNFH QRFESPESQA SAEQPEM
Length:327
Mass (Da):38,170
Last modified:November 25, 2002 - v2
Checksum:iBD3B2EAA6CFCBFA9
GO
Isoform 2 (identifier: O75436-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     243-327: GESIPIRLFL...SQASAEQPEM → GDNFMEKSS

Note: No experimental confirmation available.Curated

Show »
Length:251
Mass (Da):28,938
Checksum:i1140DC4C2D80D257
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751Q → R in BAB14351. (PubMed:14702039)Curated
Sequence conflicti242 – 2421K → Q in BQ048905. (PubMed:15489334)Curated
Sequence conflicti285 – 2862RY → SS in AAF89954. (PubMed:11102511)Curated
Sequence conflicti285 – 2862RY → SS in AAC39912. (PubMed:9653160)Curated
Isoform 2 (identifier: O75436-2)
Sequence conflicti243 – 2431G → R in BQ048905. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei243 – 32785GESIP…EQPEM → GDNFMEKSS in isoform 2. 1 PublicationVSP_044910Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41536.1. [O75436-2]
CCDS7286.1. [O75436-1]
RefSeqiNP_001030337.1. NM_001035260.1. [O75436-2]
NP_004887.2. NM_004896.3. [O75436-1]
UniGeneiHs.499925.

Genome annotation databases

EnsembliENST00000263559; ENSP00000263559; ENSG00000122958. [O75436-1]
ENST00000373382; ENSP00000362480; ENSG00000122958. [O75436-1]
ENST00000395098; ENSP00000378532; ENSG00000122958. [O75436-2]
GeneIDi9559.
KEGGihsa:9559.
UCSCiuc001jpb.3. human. [O75436-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41536.1. [O75436-2]
CCDS7286.1. [O75436-1]
RefSeqiNP_001030337.1. NM_001035260.1. [O75436-2]
NP_004887.2. NM_004896.3. [O75436-1]
UniGeneiHs.499925.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FAUX-ray2.10A1-327[»]
ProteinModelPortaliO75436.
SMRiO75436. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114930. 61 interactions.
DIPiDIP-29075N.
IntActiO75436. 2 interactions.
MINTiMINT-5000831.
STRINGi9606.ENSP00000263559.

PTM databases

PhosphoSiteiO75436.

Proteomic databases

MaxQBiO75436.
PaxDbiO75436.
PeptideAtlasiO75436.
PRIDEiO75436.

Protocols and materials databases

DNASUi9559.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263559; ENSP00000263559; ENSG00000122958. [O75436-1]
ENST00000373382; ENSP00000362480; ENSG00000122958. [O75436-1]
ENST00000395098; ENSP00000378532; ENSG00000122958. [O75436-2]
GeneIDi9559.
KEGGihsa:9559.
UCSCiuc001jpb.3. human. [O75436-1]

Organism-specific databases

CTDi9559.
GeneCardsiGC10P070885.
HGNCiHGNC:12711. VPS26A.
HPAiCAB011602.
HPA044581.
MIMi605506. gene.
neXtProtiNX_O75436.
PharmGKBiPA37326.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256244.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiO75436.
KOiK18466.
OMAiSDKSNTH.
OrthoDBiEOG7NW699.
PhylomeDBiO75436.
TreeFamiTF300907.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Miscellaneous databases

ChiTaRSiVPS26A. human.
EvolutionaryTraceiO75436.
GeneWikiiVPS26A.
GenomeRNAii9559.
NextBioi35853.
PROiO75436.
SOURCEiSearch...

Gene expression databases

BgeeiO75436.
CleanExiHS_VPS26A.
ExpressionAtlasiO75436. baseline and differential.
GenevestigatoriO75436.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, SUBUNIT.
    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.
    , 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.
    , 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. 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. "Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer."
    Seaman M.N.J.
    J. Cell Biol. 165:111-122(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor."
    Arighi C.N., Hartnell L.M., Aguilar R.C., Haft C.R., Bonifacino J.S.
    J. Cell Biol. 165:123-133(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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.
  10. "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.
  11. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VPS35.
  12. "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.
  13. "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.
  14. "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.
  15. "EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate endosome-to-Golgi retrieval."
    Gokool S., Tattersall D., Seaman M.N.
    Traffic 8:1873-1886(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EHD1.
  16. "The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network."
    Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J., Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.
    Dev. Cell 17:110-122(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX1; SNX2; SNX5 AND SNX6.
  17. "Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5."
    Seaman M.N., Harbour M.E., Tattersall D., Read E., Bright N.
    J. Cell Sci. 122:2371-2382(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB7A.
  18. "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.
  19. "The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics."
    Harbour M.E., Breusegem S.Y., Antrobus R., Freeman C., Reid E., Seaman M.N.
    J. Cell Sci. 123:3703-3717(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KIAA0196.
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors."
    Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J., von Zastrow M.
    Nat. Cell Biol. 13:715-721(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion."
    Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M., Betist M.C., van Weering J.R., van Heesbeen R.G., Middelkoop T.C., Basler K., Cullen P.J., Korswagen H.C.
    Nat. Cell Biol. 13:914-923(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX3, FUNCTION OF THE SNX3-RETROMER.
  24. "Recruitment of the endosomal WASH complex is mediated by the extended 'tail' of Fam21 binding to the retromer protein Vps35."
    Harbour M.E., Breusegem S.Y., Seaman M.N.
    Biochem. J. 442:209-220(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing."
    Fjorback A.W., Seaman M., Gustafsen C., Mehmedbasic A., Gokool S., Wu C., Militz D., Schmidt V., Madsen P., Nyengaard J.R., Willnow T.E., Christensen E.I., Mobley W.B., Nykjaer A., Andersen O.M.
    J. Neurosci. 32:1467-1480(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SORL1.
  26. "A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport."
    Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J., Tavare J.M., Cullen P.J.
    Nat. Cell Biol. 15:461-471(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX27, FUNCTION OF THE SNX27-RETROMER.
  27. Cited for: INTERACTION WITH RAB7A.
  28. "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.

Entry informationi

Entry nameiVP26A_HUMAN
AccessioniPrimary (citable) accession number: O75436
Secondary accession number(s): A8MZ56
, B2RDD3, Q8TBH4, Q9H982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 25, 2002
Last modified: February 4, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.