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Protein

Vacuolar protein sorting-associated protein 29

Gene

VPS29

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. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (Probable). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27 (PubMed:24856514).3 PublicationsBy similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Zinc 1By similarity
Metal bindingi10 – 101Zinc 1By similarity
Metal bindingi39 – 391Zinc 1By similarity
Metal bindingi39 – 391Zinc 2By similarity
Metal bindingi62 – 621Zinc 2By similarity
Metal bindingi86 – 861Zinc 2By similarity
Metal bindingi115 – 1151Zinc 2By similarity
Metal bindingi117 – 1171Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 29
Short name:
hVPS29
Alternative name(s):
PEP11 homolog
Vesicle protein sorting 29
Gene namesi
Name:VPS29
ORF Names:DC15, DC7, MDS007
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:14340. VPS29.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: LIFEdb
  • endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • late endosome Source: UniProtKB-SubCell
  • retromer complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81D → A: Loss of in vitro protein phosphatase activity. 1 Publication
Mutagenesisi39 – 391N → A: Loss of in vitro protein phosphatase activity. 1 Publication
Mutagenesisi39 – 391N → D: No effect on in vitro protein phosphatase activity. 1 Publication
Mutagenesisi62 – 621D → A or N: Loss of in vitro protein phosphatase activity. 1 Publication
Mutagenesisi86 – 861H → A: Loss of in vitro protein phosphatase activity. 1 Publication
Mutagenesisi90 – 901V → D: Decreases interaction with VPS35.
Mutagenesisi91 – 911I → D: Disrupts interaction with VPS35.
Mutagenesisi117 – 1171H → A: Loss of in vitro protein phosphatase activity. 1 Publication
Mutagenesisi152 – 1521L → E: Disrupts interaction with TBC1D5. 1 Publication

Organism-specific databases

PharmGKBiPA37875.

Polymorphism and mutation databases

DMDMi25453325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 182182Vacuolar protein sorting-associated protein 29PRO_0000065894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UBQ0.
PaxDbiQ9UBQ0.
PRIDEiQ9UBQ0.

PTM databases

DEPODiQ9UBQ0.
PhosphoSiteiQ9UBQ0.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in heart, lung, placenta, spleen, peripheral blood leukocytes, thymus, colon skeletal muscle, kidney and brain.

Gene expression databases

BgeeiQ9UBQ0.
CleanExiHS_VPS29.
ExpressionAtlasiQ9UBQ0. baseline and differential.
GenevisibleiQ9UBQ0. HS.

Organism-specific databases

HPAiHPA039748.

Interactioni

Subunit structurei

Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:11102511, PubMed:16737443, PubMed:17891154). 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 VPS26A, VPS35, SNX1, SNX2, SNX27, KIAA0196, TBC1D5 (PubMed:11102511, PubMed:20923837, PubMed:23331060, PubMed:23563491). Interacts with VPS26B and ANKRD27 (By similarity).2 PublicationsBy similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TBC1D5B9A6K13EBI-718596,EBI-10217641
TBC1D5Q926093EBI-718596,EBI-742381
VPS26AO754364EBI-718596,EBI-1043891
VPS35Q96QK15EBI-718596,EBI-1054634

Protein-protein interaction databases

BioGridi119683. 62 interactions.
DIPiDIP-29077N.
IntActiQ9UBQ0. 10 interactions.
MINTiMINT-1422473.
STRINGi9606.ENSP00000380795.

Structurei

Secondary structure

1
182
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni11 – 144Combined sources
Beta strandi16 – 183Combined sources
Helixi20 – 256Combined sources
Beta strandi32 – 365Combined sources
Helixi43 – 5210Combined sources
Beta strandi54 – 585Combined sources
Beta strandi71 – 777Combined sources
Beta strandi80 – 856Combined sources
Beta strandi90 – 923Combined sources
Helixi96 – 10611Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi171 – 18010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W24X-ray2.10A1-182[»]
2R17X-ray2.80A/B1-182[»]
ProteinModelPortaliQ9UBQ0.
SMRiQ9UBQ0. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBQ0.

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS29 family.Curated

Phylogenomic databases

eggNOGiCOG0622.
GeneTreeiENSGT00390000012669.
HOVERGENiHBG056165.
InParanoidiQ9UBQ0.
KOiK18467.
OrthoDBiEOG7JHM6S.
PhylomeDBiQ9UBQ0.
TreeFamiTF300880.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR024654. Calcineurin-like_PHP_lpxH.
IPR029052. Metallo-depent_PP-like.
IPR000979. Phosphodiesterase_MJ0936/Vps29.
[Graphical view]
PANTHERiPTHR11124. PTHR11124. 1 hit.
PfamiPF12850. Metallophos_2. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR00040. yfcE. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBQ0-1) [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
MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK
60 70 80 90 100
TLAGDVHIVR GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA
110 120 130 140 150
LLQRQFDVDI LISGHTHKFE AFEHENKFYI NPGSATGAYN ALETNIIPSF
160 170 180
VLMDIQASTV VTYVYQLIGD DVKVERIEYK KP
Length:182
Mass (Da):20,506
Last modified:May 1, 2000 - v1
Checksum:i6E0CDE6B720C9BF8
GO
Isoform 2 (identifier: Q9UBQ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAGHR

Show »
Length:186
Mass (Da):20,927
Checksum:i7875116A30665D6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22ML → MKIVLYPV in AAF86872 (Ref. 4) Curated
Sequence conflicti119 – 1191F → S in CAB66549 (PubMed:11230166).Curated
Sequence conflicti119 – 1191F → S in CAG38499 (Ref. 6) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAGHR in isoform 2. 4 PublicationsVSP_004073

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193795 mRNA. Translation: AAF04596.1.
AF175264 mRNA. Translation: AAF89952.1.
AF168716 mRNA. Translation: AAF87318.1.
AF201936 mRNA. Translation: AAF86872.1.
AF201946 mRNA. Translation: AAF17238.1.
AL136614 mRNA. Translation: CAB66549.1.
CR457182 mRNA. Translation: CAG33463.1.
CR533468 mRNA. Translation: CAG38499.1.
BC000880 mRNA. Translation: AAH00880.1.
BC095446 mRNA. Translation: AAH95446.1.
CCDSiCCDS41832.1. [Q9UBQ0-1]
CCDS53832.1. [Q9UBQ0-2]
PIRiJC7515.
RefSeqiNP_057310.1. NM_016226.4. [Q9UBQ0-1]
NP_476528.1. NM_057180.2. [Q9UBQ0-2]
UniGeneiHs.600114.

Genome annotation databases

EnsembliENST00000360579; ENSP00000353786; ENSG00000111237. [Q9UBQ0-2]
ENST00000549578; ENSP00000447058; ENSG00000111237. [Q9UBQ0-1]
GeneIDi51699.
KEGGihsa:51699.
UCSCiuc001tqx.3. human. [Q9UBQ0-2]
uc001tqy.3. human. [Q9UBQ0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193795 mRNA. Translation: AAF04596.1.
AF175264 mRNA. Translation: AAF89952.1.
AF168716 mRNA. Translation: AAF87318.1.
AF201936 mRNA. Translation: AAF86872.1.
AF201946 mRNA. Translation: AAF17238.1.
AL136614 mRNA. Translation: CAB66549.1.
CR457182 mRNA. Translation: CAG33463.1.
CR533468 mRNA. Translation: CAG38499.1.
BC000880 mRNA. Translation: AAH00880.1.
BC095446 mRNA. Translation: AAH95446.1.
CCDSiCCDS41832.1. [Q9UBQ0-1]
CCDS53832.1. [Q9UBQ0-2]
PIRiJC7515.
RefSeqiNP_057310.1. NM_016226.4. [Q9UBQ0-1]
NP_476528.1. NM_057180.2. [Q9UBQ0-2]
UniGeneiHs.600114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W24X-ray2.10A1-182[»]
2R17X-ray2.80A/B1-182[»]
ProteinModelPortaliQ9UBQ0.
SMRiQ9UBQ0. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119683. 62 interactions.
DIPiDIP-29077N.
IntActiQ9UBQ0. 10 interactions.
MINTiMINT-1422473.
STRINGi9606.ENSP00000380795.

PTM databases

DEPODiQ9UBQ0.
PhosphoSiteiQ9UBQ0.

Polymorphism and mutation databases

DMDMi25453325.

Proteomic databases

MaxQBiQ9UBQ0.
PaxDbiQ9UBQ0.
PRIDEiQ9UBQ0.

Protocols and materials databases

DNASUi51699.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360579; ENSP00000353786; ENSG00000111237. [Q9UBQ0-2]
ENST00000549578; ENSP00000447058; ENSG00000111237. [Q9UBQ0-1]
GeneIDi51699.
KEGGihsa:51699.
UCSCiuc001tqx.3. human. [Q9UBQ0-2]
uc001tqy.3. human. [Q9UBQ0-1]

Organism-specific databases

CTDi51699.
GeneCardsiGC12M110929.
HGNCiHGNC:14340. VPS29.
HPAiHPA039748.
MIMi606932. gene.
neXtProtiNX_Q9UBQ0.
PharmGKBiPA37875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0622.
GeneTreeiENSGT00390000012669.
HOVERGENiHBG056165.
InParanoidiQ9UBQ0.
KOiK18467.
OrthoDBiEOG7JHM6S.
PhylomeDBiQ9UBQ0.
TreeFamiTF300880.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Miscellaneous databases

ChiTaRSiVPS29. human.
EvolutionaryTraceiQ9UBQ0.
GeneWikiiVPS29.
GenomeRNAii51699.
NextBioi55714.
PROiQ9UBQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBQ0.
CleanExiHS_VPS29.
ExpressionAtlasiQ9UBQ0. baseline and differential.
GenevisibleiQ9UBQ0. HS.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR024654. Calcineurin-like_PHP_lpxH.
IPR029052. Metallo-depent_PP-like.
IPR000979. Phosphodiesterase_MJ0936/Vps29.
[Graphical view]
PANTHERiPTHR11124. PTHR11124. 1 hit.
PfamiPF12850. Metallophos_2. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR00040. yfcE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human homologues of yeast vacuolar protein sorting 29 and 35."
    Edgar A.J., Polak J.M.
    Biochem. Biophys. Res. Commun. 277:622-630(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung.
  2. "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 VPS26A; VPS35; SNX1 AND SNX2.
    Tissue: Parathyroid.
  3. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
    Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J., Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G., Li N.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hematopoietic stem cell.
  4. "Novel genes expressed in human dendritic cells."
    Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Cervix.
  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. "The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide."
    Damen E., Krieger E., Nielsen J.E., Eygensteyn J., van Leeuwen J.E.M.
    Biochem. J. 398:399-409(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-8; ASN-39; ASP-62; HIS-86 AND HIS-117, SUBUNIT.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: INTERACTION WITH TBC1D5, MUTAGENESIS OF LEU-152.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: FUNCTION OF THE SNX3-RETROMER, SUBUNIT.
  14. "VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins."
    Swarbrick J.D., Shaw D.J., Chhabra S., Ghai R., Valkov E., Norwood S.J., Seaman M.N., Collins B.M.
    PLoS ONE 6:E20420-E20420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF PHOSPHATASE ACTIVITY.
  15. "Endosomal recruitment of the WASH complex: active sequences and mutations impairing interaction with the retromer."
    Helfer E., Harbour M.E., Henriot V., Lakisic G., Sousa-Blin C., Volceanov L., Seaman M.N., Gautreau A.
    Biol. Cell 105:191-207(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPS35, MUTAGENESIS OF VAL-90 AND ILE-91.
  16. "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 AND KIAA0196, SUBUNIT, FUNCTION OF THE SNX27-RETROMER.
  17. "VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface."
    Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B., Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R., Seaman M.N., Luzio J.P., Owen D.J.
    Dev. Cell 29:591-606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites."
    Wang D., Guo M., Liang Z., Fan J., Zhu Z., Zang J., Zhu Z., Li X., Teng M., Niu L., Dong Y., Liu P.
    J. Biol. Chem. 280:22962-22967(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), METAL-BINDING.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH VPS35, ELECTRON MICROSCOPY OF THE RETROMER COMPLEX CONTAINING VPS29; VPS35 AND VPS26.

Entry informationi

Entry nameiVPS29_HUMAN
AccessioniPrimary (citable) accession number: Q9UBQ0
Secondary accession number(s): Q502Y5
, Q6FIF8, Q6IAH3, Q9H0W0, Q9NRP1, Q9NRU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 138 of the entry and version 1 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

Caution

Was originally believed to be a metal-dependent phosphatase but shown to lack catalytic activity; can bind metals with very low affinity suggesting that metal binding is not required for its function.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.