P25386 · USO1_YEAST

Function

function

Required for protein transport from the ER to the Golgi complex.

Miscellaneous

Present with 2330 molecules/cell in log phase SD medium.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoskeleton
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentER to Golgi transport vesicle membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
Biological Processendoplasmic reticulum to Golgi vesicle-mediated transport
Biological ProcessGolgi vesicle docking
Biological Processintracellular protein transport
Biological Processmembrane fusion
Biological ProcessSNARE complex assembly
Biological Processvesicle fusion with Golgi apparatus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Intracellular protein transport protein USO1
  • Short names
    Int-1

Gene names

    • Name
      USO1
    • Synonyms
      INT1
    • Ordered locus names
      YDL058W

Organism names

Accessions

  • Primary accession
    P25386
  • Secondary accessions
    • D6VRT8
    • E9PAG8
    • P89892
    • Q07380

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasmic vesicle membrane
; Peripheral membrane protein
Endoplasmic reticulum membrane
; Peripheral membrane protein
Golgi apparatus membrane
; Peripheral membrane protein
Note: Probably present on vesicles operational between the ER and the Golgi complex.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000657301-1790Intracellular protein transport protein USO1
Modified residue1770Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer. Dimerizes by parallel association of the tails, resulting in an elongated structure with two globular head domains side by side, and a long rod-like tail structure.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region1-724Globular head
Repeat45-89ARM 1
Repeat127-170ARM 2
Repeat173-213ARM 3
Repeat215-260ARM 4
Repeat261-312ARM 5
Repeat314-362ARM 6
Repeat363-429ARM 7
Repeat431-512ARM 8
Region452-484Disordered
Compositional bias463-484Basic and acidic residues
Region465-487Charged (hyper-hydrophilic)
Repeat543-584ARM 9
Repeat586-630ARM 10
Coiled coil725-1790
Region991-1790Dispensable for the protein function
Region1185-1221Disordered
Compositional bias1191-1221Basic and acidic residues
Region1326-1351Disordered
Region1485-1547Disordered
Region1645-1667Disordered
Region1722-1742Disordered
Region1762-1790Disordered
Compositional bias1769-1790Acidic residues

Domain

Composed of a globular head region and a rod-like C-terminal coiled coil domain. The rodlike tail sequence is highly repetitive, composed of a heptapeptide repeat pattern characteristic of alpha-helical coiled coils. May form filamentous structures in the cell.

Sequence similarities

Belongs to the VDP/USO1/EDE1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,790
  • Mass (Da)
    206,452
  • Last updated
    2004-12-21 v2
  • Checksum
    90062544F55A52EE
MDIIQGLIQQPKIQSVDETIPTLCDRVENSTLISDRRSAVLGLKAFSRQYRESVIASGLKPLLNTLKRDYMDEDSVKAILETILILFIRGDGHDDLTRGWISQQSRLQNGKYPSPLVMKQEKEQVDQFSLWIADALTQSEDLIHLLVEFWEIDNFHIRLYTIQLLEAVMATRPLKARSALISLPTSISTMVSLLDDMHEPIRDEAILLLMAVVNDSPHVQKLVAFENIFERLFSIIEEEGGLRGSLVVNDCLSLINNILKYNTSNQTLFLETGNLPKLAHLLSEPISQDEVFFWNDQRIVNINTALDIVSLTVEPGNTVTTKHQNALLDSSVLMVVLRLAFFHNIPKKVRPVALLTAANMVRSNEHAQLEFSKIDVPYFDPSLPVNSTANGGPIKLIPVVSILINWMLYANSVHTFDTRVACSRLLKAYFMDNFDLQRDFLLKQVQLCNNSTNNVGDNAKENGGSNKSDKESDSDKDTDGKDGTEYEGSFKANLFEVLLNYDAELNLNPFKLFFTTDIFMFFFQQDHKYSEELREITRNVTTGNDLEDEEPLKAIQTISELLTTSLTAADIRIPISYLTFLIYWLFGDFKATNDFLSDKSVIKSLLSFSYQIQDEDVTIKCLVTMLLGVAYEFSSKESPFPRKEYFEFITKTLGKDNYASRIKQFKKDSYFSKVDMNEDSILTPELDETGLPKVYFSTYFIQLFNENIYRIRTALSHDPDEEPINKISFEEVEKLQRQCTKLKGEITSLQTETESTHENLTEKLIALTNEHKELDEKYQILNSSHSSLKENFSILETELKNVRDSLDEMTQLRDVLETKDKENQTALLEYKSTIHKQEDSIKTLEKGLETILSQKKKAEDGINKMGKDLFALSREMQAVEENCKNLQKEKDKSNVNHQKETKSLKEDIAAKITEIKAINENLEEMKIQCNNLSKEKEHISKELVEYKSRFQSHDNLVAKLTEKLKSLANNYKDMQAENESLIKAVEESKNESSIQLSNLQNKIDSMSQEKENFQIERGSIEKNIEQLKKTISDLEQTKEEIISKSDSSKDEYESQISLLKEKLETATTANDENVNKISELTKTREELEAELAAYKNLKNELETKLETSEKALKEVKENEEHLKEEKIQLEKEATETKQQLNSLRANLESLEKEHEDLAAQLKKYEEQIANKERQYNEEISQLNDEITSTQQENESIKKKNDELEGEVKAMKSTSEEQSNLKKSEIDALNLQIKELKKKNETNEASLLESIKSVESETVKIKELQDECNFKEKEVSELEDKLKASEDKNSKYLELQKESEKIKEELDAKTTELKIQLEKITNLSKAKEKSESELSRLKKTSSEERKNAEEQLEKLKNEIQIKNQAFEKERKLLNEGSSTITQEYSEKINTLEDELIRLQNENELKAKEIDNTRSELEKVSLSNDELLEEKQNTIKSLQDEILSYKDKITRNDEKLLSIERDNKRDLESLKEQLRAAQESKAKVEEGLKKLEEESSKEKAELEKSKEMMKKLESTIESNETELKSSMETIRKSDEKLEQSKKSAEEDIKNLQHEKSDLISRINESEKDIEELKSKLRIEAKSGSELETVKQELNNAQEKIRINAEENTVLKSKLEDIERELKDKQAEIKSNQEEKELLTSRLKELEQELDSTQQKAQKSEEERRAEVRKFQVEKSQLDEKAMLLETKYNDLVNKEQAWKRDEDTVKKTTDSQRQEIEKLAKELDNLKAENSKLKEANEDRSEIDDLMLLVTDLDEKNAKYRSKLKDLGVEISSDEEDDEEDDEEDEEEGQVA

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict390-391in Ref. 1; CAA38253
Compositional bias463-484Basic and acidic residues
Sequence conflict725in Ref. 1; CAA38253
Sequence conflict847in Ref. 5; AAB00143
Sequence conflict924in Ref. 5; AAB00143
Compositional bias1191-1221Basic and acidic residues
Sequence conflict1253in Ref. 5; AAB00143
Sequence conflict1319in Ref. 5; AAB00143
Sequence conflict1461in Ref. 5; AAB00143
Sequence conflict1581in Ref. 5; AAB00143
Sequence conflict1600in Ref. 5; AAB00143
Sequence conflict1661in Ref. 5; AAB00143
Compositional bias1769-1790Acidic residues
Sequence conflict1772in Ref. 5; AAB00143

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X54378
EMBL· GenBank· DDBJ
CAA38253.1
EMBL· GenBank· DDBJ
Genomic DNA
Z74105
EMBL· GenBank· DDBJ
CAA98620.1
EMBL· GenBank· DDBJ
Genomic DNA
Z74106
EMBL· GenBank· DDBJ
CAA98621.1
EMBL· GenBank· DDBJ
Genomic DNA
U53668
EMBL· GenBank· DDBJ
AAB66659.1
EMBL· GenBank· DDBJ
Genomic DNA
L03188
EMBL· GenBank· DDBJ
AAB00143.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA11798.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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