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Protein

AP-1 complex subunit sigma-1

Gene

vas2

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

Functioni

Component of the AP-1 complex which links clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.1 Publication

GO - Molecular functioni

GO - Biological processi

  • endosomal transport Source: PomBase
  • intracellular protein transport Source: PomBase
  • vesicle-mediated transport Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit sigma-1
Alternative name(s):
Sigma1-adaptin
Valproic acid-sensitive protein 2
Gene namesi
Name:vas2
Synonyms:aps1
ORF Names:SPAP27G11.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAP27G11.06c.
PomBaseiSPAP27G11.06c. vas2.

Subcellular locationi

GO - Cellular componenti

  • AP-1 adaptor complex Source: PomBase
  • cytosol Source: PomBase
  • endosome Source: PomBase
  • Golgi apparatus Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to hypersensitivity to valproic acid.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162AP-1 complex subunit sigma-1PRO_0000316201Add
BLAST

Proteomic databases

MaxQBiQ9P7N2.

Interactioni

Subunit structurei

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit apl4 and beta-type subunit apl2), a medium adaptin (mu-type subunit apm1) and a small adaptin (sigma-type subunit aps1). AP-1 interacts with clathrin (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

MINTiMINT-4705913.

Structurei

3D structure databases

ProteinModelPortaliQ9P7N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000185227.
OMAiKICRELI.
PhylomeDBiQ9P7N2.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P7N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIKFFLLVS RQGKVRLAKW FNTLSIKERA KIIRDVSSLV ITRKPKMCNF
60 70 80 90 100
VEYKGEKIVY RRYASLFFVC GIEQDDNELI ILEVIHKFVE CLDKYFGNVC
110 120 130 140 150
ELDLIFNFEK AYYVMEELLL AGELQESSKT NVLSAVLAGD AESEADAQQD
160
SLQKLVGSVK KR
Length:162
Mass (Da):18,647
Last modified:October 1, 2000 - v1
Checksum:i9616603E7EF51C7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB76027.1.
RefSeqiNP_593410.1. NM_001018843.2.

Genome annotation databases

EnsemblFungiiSPAP27G11.06c.1; SPAP27G11.06c.1:pep; SPAP27G11.06c.
GeneIDi2542885.
KEGGispo:SPAP27G11.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB76027.1.
RefSeqiNP_593410.1. NM_001018843.2.

3D structure databases

ProteinModelPortaliQ9P7N2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4705913.

Proteomic databases

MaxQBiQ9P7N2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAP27G11.06c.1; SPAP27G11.06c.1:pep; SPAP27G11.06c.
GeneIDi2542885.
KEGGispo:SPAP27G11.06c.

Organism-specific databases

EuPathDBiFungiDB:SPAP27G11.06c.
PomBaseiSPAP27G11.06c. vas2.

Phylogenomic databases

HOGENOMiHOG000185227.
OMAiKICRELI.
PhylomeDBiQ9P7N2.

Miscellaneous databases

NextBioi20803925.
PROiQ9P7N2.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 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. "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].
  3. "Deletion mutants of AP-1 adaptin subunits display distinct phenotypes in fission yeast."
    Ma Y., Takeuchi M., Sugiura R., Sio S.O., Kuno T.
    Genes Cells 14:1015-1028(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, IDENTIFICATION IN THE AP-1 COMPLEX, SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiAP1S1_SCHPO
AccessioniPrimary (citable) accession number: Q9P7N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2000
Last modified: January 20, 2016
This is version 82 of the entry and version 1 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.