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Protein

Vacuolar protein sorting-associated protein 35

Gene

VPS35

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 CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. 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 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for endosomal localization of FAM21C (PubMed:22070227). Mediates the association of the CSC with the WASH complex via FAM21 (PubMed:22070227, PubMed:24980502, PubMed:24819384). Required for the endosomal localization of TBC1D5 (PubMed:20923837).4 Publications8 Publications

GO - Molecular functioni

  1. protein transporter activity Source: GO_Central

GO - Biological processi

  1. intracellular protein transport Source: GO_Central
  2. negative regulation of late endosome to lysosome transport Source: UniProtKB
  3. retrograde transport, endosome to Golgi Source: UniProtKB
  4. retrograde transport, endosome to plasma membrane Source: UniProtKB
  5. transcytosis 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 35
Short name:
hVPS35
Alternative name(s):
Maternal-embryonic 3
Vesicle protein sorting 35
Gene namesi
Name:VPS35
Synonyms:MEM3
ORF Names:TCCCTA00141
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:13487. VPS35.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein. Endosome 1 Publication. Early endosome Curated. Late endosome Curated
Note: Localizes to tubular profiles adjacent to endosomes.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. early endosome Source: UniProtKB-SubCell
  3. endosome Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. late endosome Source: GO_Central
  6. lysosomal membrane Source: UniProtKB
  7. retromer complex Source: GO_Central
  8. tubular endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 173 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant, adult-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.

See also OMIM:614203
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti620 – 6201D → N in PARK17; decreases interaction with FAM21C, FKBP15 and the WASH complex; impairs recruitment of the WASH complex to endosomes; shows reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows a progressive reduction in neurite length and branching. 6 Publications
VAR_066659

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081L → P: Disrupts interaction with VPS26; no effect on interaction with VPS29. 1 Publication
Mutagenesisi675 – 6751H → R: Disrupts interaction with VPS29. Does not effect interaction with VPS26. 1 Publication

Keywords - Diseasei

Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

MIMi614203. phenotype.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA37783.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Vacuolar protein sorting-associated protein 35PRO_0000065896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei791 – 7911PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96QK1.
PaxDbiQ96QK1.
PeptideAtlasiQ96QK1.
PRIDEiQ96QK1.

PTM databases

PhosphoSiteiQ96QK1.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in heart, brain, placenta, skeletal muscle, spleen, thymus, testis, ovary, small intestine, kidney and colon.

Gene expression databases

BgeeiQ96QK1.
ExpressionAtlasiQ96QK1. baseline.
GenevestigatoriQ96QK1.

Organism-specific databases

HPAiHPA040802.

Interactioni

Subunit structurei

Component of the heterotrimeric retromer cargo-selective complex (CSC), also decribed 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 VPS26A, VPS26B, VPS29, SNX1, SNX2, IGF2R, SNX3, GOLPH3, LRRK2, SLC11A2, FAM21A, FAM21C, FKBP15, WASH1, RAB7A, SNX27, KIAA0196, EHD1 (PubMed:11102511, PubMed:15078903, PubMed:17868075PubMed:22070227, PubMed:19553991, PubMed:21725319, PubMed:22070227, PubMed:22513087, PubMed:23331060, PubMed:23563491, PubMed:23395371, PubMed:24344282, PubMed:24980502, PubMed:17891154, PubMed:19531583). Interacts with MAGEL2; leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase complex retromer-containing endosomes (PubMed:23452853).2 PublicationsBy similarity14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNX1Q135962EBI-1054634,EBI-2822329
VPS26AO754366EBI-1054634,EBI-1043891
VPS29Q9UBQ02EBI-1054634,EBI-718596

Protein-protein interaction databases

BioGridi120855. 69 interactions.
DIPiDIP-29076N.
IntActiQ96QK1. 24 interactions.
MINTiMINT-5001902.

Structurei

Secondary structure

1
796
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni484 – 4874Combined sources
Helixi488 – 49811Combined sources
Helixi503 – 51816Combined sources
Beta strandi522 – 5243Combined sources
Helixi525 – 54420Combined sources
Turni545 – 5495Combined sources
Helixi553 – 57321Combined sources
Helixi578 – 59417Combined sources
Helixi599 – 61719Combined sources
Helixi621 – 63515Combined sources
Helixi643 – 65816Combined sources
Helixi663 – 67210Combined sources
Helixi674 – 6785Combined sources
Turni683 – 6875Combined sources
Helixi693 – 70917Combined sources
Helixi713 – 73119Combined sources
Turni732 – 7343Combined sources
Helixi740 – 75112Combined sources
Turni752 – 7554Combined sources
Helixi761 – 77616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R17X-ray2.80C/D483-780[»]
ProteinModelPortaliQ96QK1.
SMRiQ96QK1. Positions 483-780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96QK1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 4420Interaction with SNX31 PublicationAdd
BLAST
Regioni205 – 21511Interaction with SNX31 PublicationAdd
BLAST
Regioni438 – 796359Interaction with SLC11A21 PublicationAdd
BLAST
Regioni500 – 693194Interaction with IGF2R cytoplasmic domain1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the VPS35 family.Curated

Phylogenomic databases

eggNOGiNOG252873.
GeneTreeiENSGT00390000007315.
HOVERGENiHBG054277.
InParanoidiQ96QK1.
KOiK18468.
OMAiHIRSRME.
OrthoDBiEOG7TMZR5.
PhylomeDBiQ96QK1.
TreeFamiTF105659.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR005378. Vps35.
[Graphical view]
PANTHERiPTHR11099. PTHR11099. 1 hit.
PfamiPF03635. Vps35. 1 hit.
[Graphical view]
PIRSFiPIRSF009375. Retromer_Vps35. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q96QK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML
60 70 80 90 100
GELRTSMLSP KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY
110 120 130 140 150
AGNIIPRLYL LITVGVVYVK SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR
160 170 180 190 200
NYLLQCTRNI LPDEGEPTDE ETTGDISDSM DFVLLNFAEM NKLWVRMQHQ
210 220 230 240 250
GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ IVLTGILEQV
260 270 280 290 300
VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII
310 320 330 340 350
ALIDRLALFA HREDGPGIPA DIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL
360 370 380 390 400
QVSLINLAMK CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR
410 420 430 440 450
LLKIPVDTYN NILTVLKLKH FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE
460 470 480 490 500
IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD PEDFADEQSL VGRFIHLLRS
510 520 530 540 550
EDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA FRYKENSKVD
560 570 580 590 600
DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
610 620 630 640 650
TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR
660 670 680 690 700
TQCALAASKL LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL
710 720 730 740 750
KKALKIANQC MDPSLQVQLF IEILNRYIYF YEKENDAVTI QVLNQLIQKI
760 770 780 790
REDLPNLESS EETEQINKHF HNTLEHLRLR RESPESEGPI YEGLIL
Length:796
Mass (Da):91,707
Last modified:November 25, 2002 - v2
Checksum:i28D2DD1C6B920A0A
GO

Sequence cautioni

The sequence AAG01989.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91137.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14626.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421A → S in CAB66822 (PubMed:11230166).Curated
Sequence conflicti160 – 1601I → T in BAB14626 (PubMed:14702039).Curated
Sequence conflicti168 – 1681T → P in AAF89953 (PubMed:11102511).Curated
Sequence conflicti453 – 4531S → F in AAH10362 (PubMed:15489334).Curated
Sequence conflicti526 – 5261R → G in BAA91790 (PubMed:14702039).Curated
Sequence conflicti694 – 6941K → E in BAA91790 (PubMed:14702039).Curated
Sequence conflicti796 – 7961L → H in BAA91137 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511G → S.1 Publication
VAR_066653
Natural varianti57 – 571M → I.1 Publication
VAR_066654
Natural varianti82 – 821T → R.1 Publication
VAR_066655
Natural varianti241 – 2411I → M Found in a patient with Parkinson disease. 1 Publication
VAR_066656
Natural varianti316 – 3161P → S Found in a patient with Parkinson disease. 1 Publication
VAR_066657
Natural varianti524 – 5241R → W Found in a patient with Parkinson disease. 1 Publication
VAR_066658
Natural varianti602 – 6021V → D.
Corresponds to variant rs34687100 [ dbSNP | Ensembl ].
VAR_054046
Natural varianti620 – 6201D → N in PARK17; decreases interaction with FAM21C, FKBP15 and the WASH complex; impairs recruitment of the WASH complex to endosomes; shows reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows a progressive reduction in neurite length and branching. 6 Publications
VAR_066659
Natural varianti737 – 7371A → V.1 Publication
VAR_066660
Natural varianti774 – 7741L → M.1 Publication
VAR_066661

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191298 mRNA. Translation: AAF02778.2.
AF186382 mRNA. Translation: AAG40619.1.
AF175265 mRNA. Translation: AAF89953.1.
AF183418 mRNA. Translation: AAG09687.1.
AK001614 mRNA. Translation: BAA91790.1.
AK023650 mRNA. Translation: BAB14626.1. Different initiation.
AK000395 mRNA. Translation: BAA91137.1. Different initiation.
AL136888 mRNA. Translation: CAB66822.1.
AL512769 mRNA. Translation: CAC21686.1.
BC002414 mRNA. Translation: AAH02414.1.
BC010362 mRNA. Translation: AAH10362.1.
BC093036 mRNA. Translation: AAH93036.1.
AY007112 mRNA. Translation: AAG01989.1. Different initiation.
CCDSiCCDS10721.1.
PIRiJC7516.
RefSeqiNP_060676.2. NM_018206.4.
UniGeneiHs.454528.

Genome annotation databases

EnsembliENST00000299138; ENSP00000299138; ENSG00000069329.
GeneIDi55737.
KEGGihsa:55737.
UCSCiuc002eed.3. human.

Polymorphism databases

DMDMi25453321.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191298 mRNA. Translation: AAF02778.2.
AF186382 mRNA. Translation: AAG40619.1.
AF175265 mRNA. Translation: AAF89953.1.
AF183418 mRNA. Translation: AAG09687.1.
AK001614 mRNA. Translation: BAA91790.1.
AK023650 mRNA. Translation: BAB14626.1. Different initiation.
AK000395 mRNA. Translation: BAA91137.1. Different initiation.
AL136888 mRNA. Translation: CAB66822.1.
AL512769 mRNA. Translation: CAC21686.1.
BC002414 mRNA. Translation: AAH02414.1.
BC010362 mRNA. Translation: AAH10362.1.
BC093036 mRNA. Translation: AAH93036.1.
AY007112 mRNA. Translation: AAG01989.1. Different initiation.
CCDSiCCDS10721.1.
PIRiJC7516.
RefSeqiNP_060676.2. NM_018206.4.
UniGeneiHs.454528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R17X-ray2.80C/D483-780[»]
ProteinModelPortaliQ96QK1.
SMRiQ96QK1. Positions 483-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120855. 69 interactions.
DIPiDIP-29076N.
IntActiQ96QK1. 24 interactions.
MINTiMINT-5001902.

Chemistry

ChEMBLiCHEMBL2216744.

PTM databases

PhosphoSiteiQ96QK1.

Polymorphism databases

DMDMi25453321.

Proteomic databases

MaxQBiQ96QK1.
PaxDbiQ96QK1.
PeptideAtlasiQ96QK1.
PRIDEiQ96QK1.

Protocols and materials databases

DNASUi55737.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299138; ENSP00000299138; ENSG00000069329.
GeneIDi55737.
KEGGihsa:55737.
UCSCiuc002eed.3. human.

Organism-specific databases

CTDi55737.
GeneCardsiGC16M046691.
GeneReviewsiVPS35.
HGNCiHGNC:13487. VPS35.
HPAiHPA040802.
MIMi601501. gene.
614203. phenotype.
neXtProtiNX_Q96QK1.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA37783.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252873.
GeneTreeiENSGT00390000007315.
HOVERGENiHBG054277.
InParanoidiQ96QK1.
KOiK18468.
OMAiHIRSRME.
OrthoDBiEOG7TMZR5.
PhylomeDBiQ96QK1.
TreeFamiTF105659.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Miscellaneous databases

ChiTaRSiVPS35. human.
EvolutionaryTraceiQ96QK1.
GeneWikiiVPS35.
GenomeRNAii55737.
NextBioi60680.
PROiQ96QK1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96QK1.
ExpressionAtlasiQ96QK1. baseline.
GenevestigatoriQ96QK1.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR005378. Vps35.
[Graphical view]
PANTHERiPTHR11099. PTHR11099. 1 hit.
PfamiPF03635. Vps35. 1 hit.
[Graphical view]
PIRSFiPIRSF009375. Retromer_Vps35. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.
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].
    Tissue: Lung.
  2. "Cloning and characterization of human VPS35 and mouse Vps35 and mapping of VPS35 to human chromosome 16q13-q21."
    Zhang P., Yu L., Gao J., Fu Q., Dai F., Zhao Y., Zheng L., Zhao S.
    Genomics 70:253-257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  3. "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], INTERACTION WITH VPS29; VPS26A; SNX1 AND SNX2.
    Tissue: Colon.
  4. "A novel gene expressed in human pheochromocytoma."
    Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pheochromocytoma.
  5. "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].
    Tissue: Ileal mucosa, Placenta and Teratocarcinoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  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].
    Tissue: Brain, Placenta and Prostate.
  8. "Pediatric leukemia cDNA sequencing project."
    Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-796.
    Tissue: Leukemia.
  9. "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, INTERACTION WITH IGF2R.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: INTERACTION WITH GOLPH3.
  14. "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.
  15. "Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1."
    Tabuchi M., Yanatori I., Kawai Y., Kishi F.
    J. Cell Sci. 123:756-766(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "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-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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, INTERACTION WITH FAM21C; FKBP15 AND WASH1.
  20. "Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer."
    Jia D., Gomez T.S., Billadeau D.D., Rosen M.K.
    Mol. Biol. Cell 23:2352-2361(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FAM21C.
  21. "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 VPS29 AND VPS26, MUTAGENESIS OF LEU-108 AND HIS-675.
  22. "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGEL2.
  23. "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: FUNCTION OF THE SNX27-RETROMER, SUBUNIT, INTERACTION WITH SNX27 AND KIAA0196.
  24. "RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk."
    MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G., McCabe B.D., MacCabe B.D., Marder K.S., Honig L.S., Clark L.N., Small S.A., Abeliovich A.
    Neuron 77:425-439(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RETROGRADE TRANSPORT, INTERACTION WITH LRRK2, CHARACTERIZATION OF VARIANT PARK17 ASN-620.
  25. "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.
  26. Cited for: INTERACTION WITH SNX3 AND SLC11A2.
  27. "Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation."
    McGough I.J., Steinberg F., Jia D., Barbuti P.A., McMillan K.J., Heesom K.J., Whone A.L., Caldwell M.A., Billadeau D.D., Rosen M.K., Cullen P.J.
    Curr. Biol. 24:1670-1676(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FAM21C, CHARACTERIZATION OF VARIANT PARK17 ASN-620.
  28. "Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy."
    Zavodszky E., Seaman M.N., Moreau K., Jimenez-Sanchez M., Breusegem S.Y., Harbour M.E., Rubinsztein D.C.
    Nat. Commun. 5:3828-3828(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT PARK17 ASN-620.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 483-780 IN COMPLEX WITH VPS29, ELECTRON MICROSCOPY OF THE RETROMER COMPLEX CONTAINING VPS29; VPS35 AND VPS26.
  30. Cited for: VARIANT PARK17 ASN-620, VARIANTS SER-316 AND VAL-737.
  31. Cited for: VARIANT PARK17 ASN-620, VARIANTS SER-51; ILE-57; ARG-82; MET-241; TRP-524 AND MET-774.
  32. "Identification of VPS35 mutations replicated in French families with Parkinson disease."
    Lesage S., Condroyer C., Klebe S., Honore A., Tison F., Brefel-Courbon C., Durr A., Brice A.
    Neurology 78:1449-1450(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK17 ASN-620.

Entry informationi

Entry nameiVPS35_HUMAN
AccessioniPrimary (citable) accession number: Q96QK1
Secondary accession number(s): Q561W2
, Q9H016, Q9H096, Q9H4P3, Q9H8J0, Q9NRS7, Q9NVG2, Q9NX80, Q9NZK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 25, 2002
Last modified: March 4, 2015
This is version 136 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.