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P38968

- SEC31_YEAST

UniProt

P38968 - SEC31_YEAST

Protein

Protein transport protein SEC31

Gene

SEC31

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.6 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural molecule activity Source: SGD

    GO - Biological processi

    1. COPII-coated vesicle budding Source: SGD
    2. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29580-MONOMER.
    ReactomeiREACT_188969. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein SEC31
    Alternative name(s):
    Protein WEB1
    Gene namesi
    Name:SEC31
    Synonyms:WEB1
    Ordered Locus Names:YDL195W
    ORF Names:D1229
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL195w.
    SGDiS000002354. SEC31.

    Subcellular locationi

    GO - Cellular componenti

    1. COPII vesicle coat Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: GOC

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12731273Protein transport protein SEC31PRO_0000051436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei349 – 3491Phosphoserine3 Publications
    Modified residuei836 – 8361Phosphoserine2 Publications
    Modified residuei974 – 9741Phosphoserine2 Publications
    Modified residuei977 – 9771Phosphoserine2 Publications
    Modified residuei980 – 9801Phosphoserine3 Publications
    Modified residuei988 – 9881Phosphoserine2 Publications
    Modified residuei992 – 9921Phosphoserine4 Publications
    Modified residuei999 – 9991Phosphoserine4 Publications
    Modified residuei1050 – 10501Phosphothreonine5 Publications
    Modified residuei1053 – 10531Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38968.
    PaxDbiP38968.
    PeptideAtlasiP38968.

    Expressioni

    Gene expression databases

    GenevestigatoriP38968.

    Interactioni

    Subunit structurei

    The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13. Interacts with EMP24, ERV25, SEC16 and SHR3.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SEC13Q044918EBI-20524,EBI-16529
    SEC16P484153EBI-20524,EBI-16551
    SEC23P153034EBI-20524,EBI-16584
    SEC24P404824EBI-20524,EBI-16592

    Protein-protein interaction databases

    BioGridi31850. 65 interactions.
    DIPiDIP-4792N.
    IntActiP38968. 51 interactions.
    MINTiMINT-567140.
    STRINGi4932.YDL195W.

    Structurei

    Secondary structure

    1
    1273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Beta strandi17 – 204
    Beta strandi22 – 265
    Beta strandi28 – 303
    Beta strandi43 – 497
    Helixi50 – 523
    Beta strandi65 – 706
    Beta strandi72 – 754
    Beta strandi77 – 848
    Beta strandi86 – 894
    Beta strandi100 – 1034
    Beta strandi107 – 1093
    Beta strandi113 – 1164
    Beta strandi118 – 1203
    Beta strandi123 – 1275
    Beta strandi129 – 1313
    Beta strandi133 – 1353
    Turni138 – 1414
    Turni145 – 1473
    Beta strandi165 – 1684
    Beta strandi175 – 1839
    Beta strandi185 – 1895
    Turni190 – 1934
    Beta strandi194 – 1996
    Beta strandi212 – 2176
    Beta strandi224 – 2296
    Beta strandi232 – 2343
    Beta strandi239 – 2413
    Beta strandi260 – 2656
    Beta strandi273 – 28513
    Beta strandi287 – 2893
    Beta strandi292 – 2976
    Beta strandi299 – 3013
    Beta strandi306 – 3083
    Beta strandi315 – 3184
    Beta strandi321 – 33010
    Beta strandi385 – 3873
    Turni388 – 3903
    Beta strandi391 – 3955
    Beta strandi402 – 4054
    Helixi416 – 4249
    Helixi428 – 4369
    Helixi441 – 45616
    Helixi458 – 4669
    Helixi509 – 51911
    Helixi523 – 5319
    Turni532 – 5343
    Helixi536 – 5438
    Helixi549 – 56315
    Helixi568 – 57710
    Helixi582 – 5876
    Helixi590 – 5923
    Helixi593 – 60311
    Helixi608 – 62316
    Turni624 – 6263
    Helixi628 – 63710
    Helixi641 – 65010
    Helixi652 – 66110
    Helixi666 – 68520
    Helixi697 – 71115
    Turni712 – 7143
    Helixi716 – 72510
    Helixi731 – 74414
    Beta strandi909 – 9113
    Helixi916 – 9194

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PM6X-ray2.45A/C370-763[»]
    2PM7X-ray2.35A/C370-763[»]
    2PM9X-ray3.30A1-411[»]
    2QTVX-ray2.50D899-947[»]
    3MZLX-ray2.80B/D/F/H370-746[»]
    4BZJelectron microscopy40.00A/C1-1273[»]
    4BZKelectron microscopy40.00A/C1-1273[»]
    ProteinModelPortaliP38968.
    SMRiP38968. Positions 5-745, 907-942, 1172-1273.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38968.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati6 – 4641WD 1Add
    BLAST
    Repeati60 – 9940WD 2Add
    BLAST
    Repeati106 – 14641WD 3Add
    BLAST
    Repeati158 – 19841WD 4Add
    BLAST
    Repeati207 – 25044WD 5Add
    BLAST
    Repeati255 – 29541WD 6Add
    BLAST
    Repeati298 – 33841WD 7Add
    BLAST
    Repeati385 – 40521WD 8; interaction with SEC13Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi773 – 1149377Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat SEC31 family.Curated
    Contains 8 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG248389.
    GeneTreeiENSGT00390000003175.
    HOGENOMiHOG000048339.
    KOiK14005.
    OMAiCSGNIEK.
    OrthoDBiEOG79GTFQ.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR021614. Sec31.
    IPR009917. SRA1-protein/COPII_Sec31.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF11549. Sec31. 1 hit.
    PF07304. SRA1. 1 hit.
    PF00400. WD40. 2 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 2 hits.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38968-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLAEFSRT ATFAWSHDKI PLLVSGTVSG TVDANFSTDS SLELWSLLAA     50
    DSEKPIASLQ VDSKFNDLDW SHNNKIIAGA LDNGSLELYS TNEANNAINS 100
    MARFSNHSSS VKTVKFNAKQ DNVLASGGNN GEIFIWDMNK CTESPSNYTP 150
    LTPGQSMSSV DEVISLAWNQ SLAHVFASAG SSNFASIWDL KAKKEVIHLS 200
    YTSPNSGIKQ QLSVVEWHPK NSTRVATATG SDNDPSILIW DLRNANTPLQ 250
    TLNQGHQKGI LSLDWCHQDE HLLLSSGRDN TVLLWNPESA EQLSQFPARG 300
    NWCFKTKFAP EAPDLFACAS FDNKIEVQTL QNLTNTLDEQ ETETKQQESE 350
    TDFWNNVSRE ESKEKPTVFH LQAPTWYGEP SPAAHWAFGG KLVQITPDGK 400
    GVSITNPKIS GLESNTTLSE ALKTKDFKPL INQRLVKVID DVNEEDWNLL 450
    EKLSMDGTEE FLKEALAFDN DESDAQDDAN NEKEDDGEEF FQQIETNFQP 500
    EGDFSLSGNI EQTISKNLVS GNIKSAVKNS LENDLLMEAM VIALDSNNER 550
    LKESVKNAYF AKYGSKSSLS RILYSISKRE VDDLVENLDV SQWKFISKAI 600
    QNLYPNDIAQ RNEMLIKLGD RLKENGHRQD SLTLYLAAGS LDKVASIWLS 650
    EFPDLEDKLK KDNKTIYEAH SECLTEFIER FTVFSNFING SSTINNEQLI 700
    AKFLEFINLT TSTGNFELAT EFLNSLPSDN EEVKTEKARV LIASGKSLPA 750
    QNPATATTSK AKYTNAKTNK NVPVLPTPGM PSTTSIPSMQ APFYGMTPGA 800
    SANALPPKPY VPATTTSAPV HTEGKYAPPS QPSMASPFVN KTNSSTRLNS 850
    FAPPPNPYAT ATVPATNVST TSIPQNTFAP IQPGMPIMGD YNAQSSSIPS 900
    QPPINAVSGQ TPHLNRKAND GWNDLPLKVK EKPSRAKAVS VAPPNILSTP 950
    TPLNGIPANA ASTMPPPPLS RAPSSVSMVS PPPLHKNSRV PSLVATSESP 1000
    RASISNPYAP PQSSQQFPIG TISTANQTSN TAQVASSNPY APPPQQRVAT 1050
    PLSGGVPPAP LPKASNPYAP TATTQPNGSS YPPTGPYTNN HTMTSPPPVF 1100
    NKPPTGPPPI SMKKRSNKLA SIEQNPSQGA TYPPTLSSSA SPLQPSQPPT 1150
    LASQVNTSAE NVSHEIPADQ QPIVDFLKEE LARVTPLTPK EYSKQLKDCD 1200
    KRLKILFYHL EKQDLLTQPT IDCLHDLVAL MKEKKYKEAM VIHANIATNH 1250
    AQEGGNWLTG VKRLIGIAEA TLN 1273
    Length:1,273
    Mass (Da):138,717
    Last modified:July 27, 2011 - v3
    Checksum:i87F192E4B10E7571
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti317 – 3171A → T in AAA50367. (PubMed:7760818)Curated
    Sequence conflicti367 – 3671T → S in CAA58252. (PubMed:8896272)Curated
    Sequence conflicti367 – 3671T → S in CAA98772. (PubMed:9169867)Curated
    Sequence conflicti691 – 6911S → N in AAA50367. (PubMed:7760818)Curated
    Sequence conflicti754 – 7541A → V in AAA50367. (PubMed:7760818)Curated
    Sequence conflicti877 – 8771T → A in AAA50367. (PubMed:7760818)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15219 Genomic DNA. Translation: AAA50367.1.
    X83276 Genomic DNA. Translation: CAA58252.1.
    Z74243 Genomic DNA. Translation: CAA98772.1.
    BK006938 Genomic DNA. Translation: DAA11668.2.
    PIRiS58782.
    RefSeqiNP_010086.2. NM_001180255.2.

    Genome annotation databases

    EnsemblFungiiYDL195W; YDL195W; YDL195W.
    GeneIDi851332.
    KEGGisce:YDL195W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15219 Genomic DNA. Translation: AAA50367.1 .
    X83276 Genomic DNA. Translation: CAA58252.1 .
    Z74243 Genomic DNA. Translation: CAA98772.1 .
    BK006938 Genomic DNA. Translation: DAA11668.2 .
    PIRi S58782.
    RefSeqi NP_010086.2. NM_001180255.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PM6 X-ray 2.45 A/C 370-763 [» ]
    2PM7 X-ray 2.35 A/C 370-763 [» ]
    2PM9 X-ray 3.30 A 1-411 [» ]
    2QTV X-ray 2.50 D 899-947 [» ]
    3MZL X-ray 2.80 B/D/F/H 370-746 [» ]
    4BZJ electron microscopy 40.00 A/C 1-1273 [» ]
    4BZK electron microscopy 40.00 A/C 1-1273 [» ]
    ProteinModelPortali P38968.
    SMRi P38968. Positions 5-745, 907-942, 1172-1273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31850. 65 interactions.
    DIPi DIP-4792N.
    IntActi P38968. 51 interactions.
    MINTi MINT-567140.
    STRINGi 4932.YDL195W.

    Proteomic databases

    MaxQBi P38968.
    PaxDbi P38968.
    PeptideAtlasi P38968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL195W ; YDL195W ; YDL195W .
    GeneIDi 851332.
    KEGGi sce:YDL195W.

    Organism-specific databases

    CYGDi YDL195w.
    SGDi S000002354. SEC31.

    Phylogenomic databases

    eggNOGi NOG248389.
    GeneTreei ENSGT00390000003175.
    HOGENOMi HOG000048339.
    KOi K14005.
    OMAi CSGNIEK.
    OrthoDBi EOG79GTFQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29580-MONOMER.
    Reactomei REACT_188969. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    EvolutionaryTracei P38968.
    NextBioi 968393.
    PROi P38968.

    Gene expression databases

    Genevestigatori P38968.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR021614. Sec31.
    IPR009917. SRA1-protein/COPII_Sec31.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF11549. Sec31. 1 hit.
    PF07304. SRA1. 1 hit.
    PF00400. WD40. 2 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 2 hits.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Suppression of mutations in two Saccharomyces cerevisiae genes by the adenovirus E1A protein."
      Zieler H.A., Walberg M., Berg P.
      Mol. Cell. Biol. 15:3227-3237(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / SNY243.
    2. "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast chromosome IV reveals the location of five known genes and characterizes at least six new open reading frames including putative genes for ribosomal protein L35 and a sugar transport protein."
      Verhasselt P., Voet M., Mathys J., Volckaert G.
      Yeast 12:1065-1070(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "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.
    4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 367.
      Strain: ATCC 204508 / S288c.
    5. "COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast."
      Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L.
      Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex."
      Wuestehube L.J., Duden R., Eun A., Hamamoto S., Korn P., Ram R., Schekman R.W.
      Genetics 142:393-406(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "COPII subunit interactions in the assembly of the vesicle coat."
      Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.
      J. Biol. Chem. 272:25413-25416(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE COPII COAT, INTERACTION WITH SEC16.
    8. "Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum."
      Salama N.R., Chuang J.S., Schekman R.W.
      Mol. Biol. Cell 8:205-217(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SEC13.
    9. "Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles."
      Campbell J.L., Schekman R.W.
      Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes."
      Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T.
      Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    11. "Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles."
      Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.
      Mol. Biol. Cell 10:3549-3565(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHR3.
    12. "The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting."
      Matsuoka K., Schekman R.W.
      Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex."
      Belden W.J., Barlowe C.
      J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMP24 AND ERV25.
    14. "Dynamics of the COPII coat with GTP and stable analogues."
      Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
      Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE COPII COAT.
    15. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    16. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-999; THR-1050 AND SER-1053, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-836; SER-980; SER-992; SER-999; THR-1050 AND SER-1053, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-349; SER-974; SER-977; SER-980; SER-988; SER-992; SER-999 AND THR-1050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
    21. Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
    22. "Sec16p potentiates the action of COPII proteins to bud transport vesicles."
      Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
      J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    23. Cited for: STRUCTURE OF THE COPII COMPLEX.
    24. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    25. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    26. "Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
      Sato K., Nakano A.
      J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
    27. "Structure and organization of coat proteins in the COPII cage."
      Fath S., Mancias J.D., Bi X., Goldberg J.
      Cell 129:1325-1336(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-763 IN COMPLEX WITH SEC13, SUBUNIT.
    28. "Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31."
      Bi X., Mancias J.D., Goldberg J.
      Dev. Cell 13:635-645(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 899-947 IN COMPLEX WITH SEC23 AND SAR1.
    29. "Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat."
      Whittle J.R., Schwartz T.U.
      J. Cell Biol. 190:347-361(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 370-746 IN COMPLEX WITH SEC13.

    Entry informationi

    Entry nameiSEC31_YEAST
    AccessioniPrimary (citable) accession number: P38968
    Secondary accession number(s): D6VRF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1840 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3