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Protein

Intracellular protein transport protein USO1

Gene

USO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein transporter activity Source: InterPro

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: SGD
  • Golgi vesicle docking Source: SGD
  • intracellular protein transport Source: InterPro
  • SNARE complex assembly Source: SGD
  • vesicle fusion with Golgi apparatus Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29474-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Intracellular protein transport protein USO1
Short name:
Int-1
Gene namesi
Name:USO1
Synonyms:INT1
Ordered Locus Names:YDL058W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL058W.
SGDiS000002216. USO1.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • ER to Golgi transport vesicle membrane Source: SGD
  • Golgi membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17901790Intracellular protein transport protein USO1PRO_0000065730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1770 – 17701PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25386.
PeptideAtlasiP25386.

PTM databases

iPTMnetiP25386.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-20157,EBI-20157

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32000. 85 interactions.
DIPiDIP-6815N.
IntActiP25386. 6 interactions.
MINTiMINT-660998.

Structurei

3D structure databases

ProteinModelPortaliP25386.
SMRiP25386. Positions 18-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati45 – 8945ARM 1Add
BLAST
Repeati127 – 17044ARM 2Add
BLAST
Repeati173 – 21341ARM 3Add
BLAST
Repeati215 – 26046ARM 4Add
BLAST
Repeati261 – 31252ARM 5Add
BLAST
Repeati314 – 36249ARM 6Add
BLAST
Repeati363 – 42967ARM 7Add
BLAST
Repeati431 – 51282ARM 8Add
BLAST
Repeati543 – 58442ARM 9Add
BLAST
Repeati586 – 63045ARM 10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 724724Globular headAdd
BLAST
Regioni465 – 48723Charged (hyper-hydrophilic)Add
BLAST
Regioni991 – 1790800Dispensable for the protein functionAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili725 – 17901066Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1172 – 1786615Asp/Glu-rich (acidic)Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the VDP/USO1/EDE1 family.Curated
Contains 10 ARM repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00390000017018.
HOGENOMiHOG000094118.
InParanoidiP25386.
OMAiTIPTLCD.
OrthoDBiEOG735458.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006955. Uso1_p115_C.
IPR024095. Vesicle_P115-like.
IPR006953. Vesicle_Uso1_P115_head.
[Graphical view]
PANTHERiPTHR10013. PTHR10013. 5 hits.
PfamiPF04871. Uso1_p115_C. 1 hit.
PF04869. Uso1_p115_head. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

P25386-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIIQGLIQQ PKIQSVDETI PTLCDRVENS TLISDRRSAV LGLKAFSRQY
60 70 80 90 100
RESVIASGLK PLLNTLKRDY MDEDSVKAIL ETILILFIRG DGHDDLTRGW
110 120 130 140 150
ISQQSRLQNG KYPSPLVMKQ EKEQVDQFSL WIADALTQSE DLIHLLVEFW
160 170 180 190 200
EIDNFHIRLY TIQLLEAVMA TRPLKARSAL ISLPTSISTM VSLLDDMHEP
210 220 230 240 250
IRDEAILLLM AVVNDSPHVQ KLVAFENIFE RLFSIIEEEG GLRGSLVVND
260 270 280 290 300
CLSLINNILK YNTSNQTLFL ETGNLPKLAH LLSEPISQDE VFFWNDQRIV
310 320 330 340 350
NINTALDIVS LTVEPGNTVT TKHQNALLDS SVLMVVLRLA FFHNIPKKVR
360 370 380 390 400
PVALLTAANM VRSNEHAQLE FSKIDVPYFD PSLPVNSTAN GGPIKLIPVV
410 420 430 440 450
SILINWMLYA NSVHTFDTRV ACSRLLKAYF MDNFDLQRDF LLKQVQLCNN
460 470 480 490 500
STNNVGDNAK ENGGSNKSDK ESDSDKDTDG KDGTEYEGSF KANLFEVLLN
510 520 530 540 550
YDAELNLNPF KLFFTTDIFM FFFQQDHKYS EELREITRNV TTGNDLEDEE
560 570 580 590 600
PLKAIQTISE LLTTSLTAAD IRIPISYLTF LIYWLFGDFK ATNDFLSDKS
610 620 630 640 650
VIKSLLSFSY QIQDEDVTIK CLVTMLLGVA YEFSSKESPF PRKEYFEFIT
660 670 680 690 700
KTLGKDNYAS RIKQFKKDSY FSKVDMNEDS ILTPELDETG LPKVYFSTYF
710 720 730 740 750
IQLFNENIYR IRTALSHDPD EEPINKISFE EVEKLQRQCT KLKGEITSLQ
760 770 780 790 800
TETESTHENL TEKLIALTNE HKELDEKYQI LNSSHSSLKE NFSILETELK
810 820 830 840 850
NVRDSLDEMT QLRDVLETKD KENQTALLEY KSTIHKQEDS IKTLEKGLET
860 870 880 890 900
ILSQKKKAED GINKMGKDLF ALSREMQAVE ENCKNLQKEK DKSNVNHQKE
910 920 930 940 950
TKSLKEDIAA KITEIKAINE NLEEMKIQCN NLSKEKEHIS KELVEYKSRF
960 970 980 990 1000
QSHDNLVAKL TEKLKSLANN YKDMQAENES LIKAVEESKN ESSIQLSNLQ
1010 1020 1030 1040 1050
NKIDSMSQEK ENFQIERGSI EKNIEQLKKT ISDLEQTKEE IISKSDSSKD
1060 1070 1080 1090 1100
EYESQISLLK EKLETATTAN DENVNKISEL TKTREELEAE LAAYKNLKNE
1110 1120 1130 1140 1150
LETKLETSEK ALKEVKENEE HLKEEKIQLE KEATETKQQL NSLRANLESL
1160 1170 1180 1190 1200
EKEHEDLAAQ LKKYEEQIAN KERQYNEEIS QLNDEITSTQ QENESIKKKN
1210 1220 1230 1240 1250
DELEGEVKAM KSTSEEQSNL KKSEIDALNL QIKELKKKNE TNEASLLESI
1260 1270 1280 1290 1300
KSVESETVKI KELQDECNFK EKEVSELEDK LKASEDKNSK YLELQKESEK
1310 1320 1330 1340 1350
IKEELDAKTT ELKIQLEKIT NLSKAKEKSE SELSRLKKTS SEERKNAEEQ
1360 1370 1380 1390 1400
LEKLKNEIQI KNQAFEKERK LLNEGSSTIT QEYSEKINTL EDELIRLQNE
1410 1420 1430 1440 1450
NELKAKEIDN TRSELEKVSL SNDELLEEKQ NTIKSLQDEI LSYKDKITRN
1460 1470 1480 1490 1500
DEKLLSIERD NKRDLESLKE QLRAAQESKA KVEEGLKKLE EESSKEKAEL
1510 1520 1530 1540 1550
EKSKEMMKKL ESTIESNETE LKSSMETIRK SDEKLEQSKK SAEEDIKNLQ
1560 1570 1580 1590 1600
HEKSDLISRI NESEKDIEEL KSKLRIEAKS GSELETVKQE LNNAQEKIRI
1610 1620 1630 1640 1650
NAEENTVLKS KLEDIERELK DKQAEIKSNQ EEKELLTSRL KELEQELDST
1660 1670 1680 1690 1700
QQKAQKSEEE RRAEVRKFQV EKSQLDEKAM LLETKYNDLV NKEQAWKRDE
1710 1720 1730 1740 1750
DTVKKTTDSQ RQEIEKLAKE LDNLKAENSK LKEANEDRSE IDDLMLLVTD
1760 1770 1780 1790
LDEKNAKYRS KLKDLGVEIS SDEEDDEEDD EEDEEEGQVA
Length:1,790
Mass (Da):206,452
Last modified:December 21, 2004 - v2
Checksum:i90062544F55A52EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3912NG → TA in CAA38253 (PubMed:2010462).Curated
Sequence conflicti725 – 7251N → S in CAA38253 (PubMed:2010462).Curated
Sequence conflicti847 – 8471G → E in AAB00143 (PubMed:7582869).Curated
Sequence conflicti924 – 9241E → K in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1253 – 12531V → I in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1319 – 13191I → V in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1461 – 14611N → S in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1581 – 15811G → S in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1600 – 16001I → V in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1661 – 16611R → S in AAB00143 (PubMed:7582869).Curated
Sequence conflicti1772 – 17721D → DEEDDEE in AAB00143 (PubMed:7582869).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54378 Genomic DNA. Translation: CAA38253.1.
Z74105 Genomic DNA. Translation: CAA98620.1.
Z74106 Genomic DNA. Translation: CAA98621.1.
U53668 Genomic DNA. Translation: AAB66659.1.
L03188 Genomic DNA. Translation: AAB00143.1.
BK006938 Genomic DNA. Translation: DAA11798.1.
PIRiS67593.
RefSeqiNP_010225.1. NM_001180117.1.

Genome annotation databases

EnsemblFungiiYDL058W; YDL058W; YDL058W.
GeneIDi851501.
KEGGisce:YDL058W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54378 Genomic DNA. Translation: CAA38253.1.
Z74105 Genomic DNA. Translation: CAA98620.1.
Z74106 Genomic DNA. Translation: CAA98621.1.
U53668 Genomic DNA. Translation: AAB66659.1.
L03188 Genomic DNA. Translation: AAB00143.1.
BK006938 Genomic DNA. Translation: DAA11798.1.
PIRiS67593.
RefSeqiNP_010225.1. NM_001180117.1.

3D structure databases

ProteinModelPortaliP25386.
SMRiP25386. Positions 18-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32000. 85 interactions.
DIPiDIP-6815N.
IntActiP25386. 6 interactions.
MINTiMINT-660998.

PTM databases

iPTMnetiP25386.

Proteomic databases

MaxQBiP25386.
PeptideAtlasiP25386.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL058W; YDL058W; YDL058W.
GeneIDi851501.
KEGGisce:YDL058W.

Organism-specific databases

EuPathDBiFungiDB:YDL058W.
SGDiS000002216. USO1.

Phylogenomic databases

GeneTreeiENSGT00390000017018.
HOGENOMiHOG000094118.
InParanoidiP25386.
OMAiTIPTLCD.
OrthoDBiEOG735458.

Enzyme and pathway databases

BioCyciYEAST:G3O-29474-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

PROiP25386.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006955. Uso1_p115_C.
IPR024095. Vesicle_P115-like.
IPR006953. Vesicle_Uso1_P115_head.
[Graphical view]
PANTHERiPTHR10013. PTHR10013. 5 hits.
PfamiPF04871. Uso1_p115_C. 1 hit.
PF04869. Uso1_p115_head. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae."
    Nakajima H., Hirata A., Ogawa Y., Yonehara T., Yoda K., Yamasaki M.
    J. Cell Biol. 113:245-260(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Bai Y., Symington L.S.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
  5. "Antigenic and functional conservation of an integrin I-domain in Saccharomyces cerevisiae."
    Hostetter M.K., Tao N.J., Gale C., Herman D.J., McClellan M., Sharp R.L., Kendrick K.E.
    Biochem. Mol. Med. 55:122-130(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 782-1790.
  6. "Uso1 protein is a dimer with two globular heads and a long coiled-coil tail."
    Yamakawa H., Seog D.H., Yoda K., Yamasaki M., Wakabayashi T.
    J. Struct. Biol. 116:356-365(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SUBUNIT, DOMAIN.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1770, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUSO1_YEAST
AccessioniPrimary (citable) accession number: P25386
Secondary accession number(s): D6VRT8
, E9PAG8, P89892, Q07380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.