Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vacuolar protein sorting-associated protein 35

Gene

vps35

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor vps10. Required to form proper forespore membranes.2 Publications

GO - Molecular functioni

GO - Biological processi

  • intracellular protein transport Source: PomBase
  • retrograde transport, endosome to Golgi Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-SPO-3238698. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 35
Gene namesi
Name:vps35
ORF Names:SPCC777.13
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC777.13.
PomBaseiSPCC777.13. vps35.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • endosome Source: PomBase
  • retromer complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to sensitivity to thiabendazole and microtubule depolymerizing drugs.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 836836Vacuolar protein sorting-associated protein 35PRO_0000065898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei783 – 7831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74552.

PTM databases

iPTMnetiO74552.

Interactioni

Subunit structurei

Component of the retromer complex.By similarity

Protein-protein interaction databases

BioGridi276025. 283 interactions.
MINTiMINT-4680031.

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS35 family.Curated

Phylogenomic databases

HOGENOMiHOG000196946.
InParanoidiO74552.
KOiK18468.
OMAiRIRYTTP.
OrthoDBiEOG761C34.

Family and domain databases

InterProiIPR005378. Vps35.
[Graphical view]
PANTHERiPTHR11099. PTHR11099. 3 hits.
PfamiPF03635. Vps35. 1 hit.
[Graphical view]
PIRSFiPIRSF009375. Retromer_Vps35. 1 hit.

Sequencei

Sequence statusi: Complete.

O74552-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGINTANEE ITRSLEESLN ICKQSSRLMQ RNLQTGRLMD AFRNCSISLV
60 70 80 90 100
EMRNSALTPK QYYELYMFNM ESLRLLGGTL LETHLNGTHN LMDLYELVQY
110 120 130 140 150
AGSIVPRLYL MITVGSAYLE TPNALVREIM NDLLDMCRGV QHPLRGLFLR
160 170 180 190 200
HYLLTQTRKG LPLGSEDEED ASRKGTVLDS VKFLVINFTE MNKLWVRIQH
210 220 230 240 250
LGPIKEFSKR TQERNELKVL VGLNLVRLSQ LNLDIDTYRD HVLPAIIEQI
260 270 280 290 300
IECRDSLAQE YLVEVICQAF SDNMHLQTLD TYFGTVIKLS PSVNVTQLVV
310 320 330 340 350
AMLNRLTDYV QREYESDSSN EDESETVTEK LGDIKINEEV QQKDEQECPG
360 370 380 390 400
DKVIPPEYAI QEVLWSHVVE VIQSRSGLPL DCIVSILSSI LNFFLRCYPY
410 420 430 440 450
KPQYADRVFQ YINEHIINQP SLRSALHERP LQKSLCAILL LPLTYFPSFS
460 470 480 490 500
YCLELQNFLP VFNAQDPNLR YDIARMIVQK IIEKGHSLSE LTEAQELLGF
510 520 530 540 550
VSVIIEKKGV DSLDDLQNVA LMVHYLNNDD PQIQIEILRS LKDTFIKAGE
560 570 580 590 600
NVKYLLPVVV NRCIFLARNF RIFKCMDWAE KVRLLWEFVN TCINVLYKNG
610 620 630 640 650
DSLELCLALY LSAAEMADQE NYPDFAYEFF TQAFSIYEES VLDSELQYQQ
660 670 680 690 700
LLMIIGKLQK TRNFSVDDYD TLITKCTLYA SKLLKKPDQC CGIYLASHLW
710 720 730 740 750
WQVASGEDSR PFQDPKRVLE CLQKSLKIAD ACMDQLTSLK LFINILERYF
760 770 780 790 800
YYYDQHCESI IAKHISGLID LTEQNMRSIL ISSPADLIAS DPRAYASSIW
810 820 830
EVANVSVIDS LKNHLERATA YAEKRSEDER WSSIFQ
Length:836
Mass (Da):96,408
Last modified:July 11, 2012 - v2
Checksum:iFBB26C7CABF7DADB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881S → P in BAA13840 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20717.2.
D89178 mRNA. Translation: BAA13840.1.
PIRiT11719.
RefSeqiNP_588260.2. NM_001023250.2.

Genome annotation databases

EnsemblFungiiSPCC777.13.1; SPCC777.13.1:pep; SPCC777.13.
GeneIDi2539462.
KEGGispo:SPCC777.13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20717.2.
D89178 mRNA. Translation: BAA13840.1.
PIRiT11719.
RefSeqiNP_588260.2. NM_001023250.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276025. 283 interactions.
MINTiMINT-4680031.

PTM databases

iPTMnetiO74552.

Proteomic databases

MaxQBiO74552.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC777.13.1; SPCC777.13.1:pep; SPCC777.13.
GeneIDi2539462.
KEGGispo:SPCC777.13.

Organism-specific databases

EuPathDBiFungiDB:SPCC777.13.
PomBaseiSPCC777.13. vps35.

Phylogenomic databases

HOGENOMiHOG000196946.
InParanoidiO74552.
KOiK18468.
OMAiRIRYTTP.
OrthoDBiEOG761C34.

Enzyme and pathway databases

ReactomeiR-SPO-3238698. WNT ligand biogenesis and trafficking.

Miscellaneous databases

PROiO74552.

Family and domain databases

InterProiIPR005378. Vps35.
[Graphical view]
PANTHERiPTHR11099. PTHR11099. 3 hits.
PfamiPF03635. Vps35. 1 hit.
[Graphical view]
PIRSFiPIRSF009375. Retromer_Vps35. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-836.
    Strain: PR745.
  4. "Sorting nexin homologues are targets of phosphatidylinositol 3-phosphate in sporulation of Schizosaccharomyces pombe."
    Koga T., Onishi M., Nakamura Y., Hirata A., Nakamura T., Shimoda C., Iwaki T., Takegawa K., Fukui Y.
    Genes Cells 9:561-574(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: FUNCTION.
  6. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-318 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Global fitness profiling of fission yeast deletion strains by barcode sequencing."
    Han T.X., Xu X.Y., Zhang M.J., Peng X., Du L.L.
    Genome Biol. 11:R60.1-R60.13(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiVPS35_SCHPO
AccessioniPrimary (citable) accession number: O74552
Secondary accession number(s): P78830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: July 11, 2012
Last modified: June 8, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.