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P38968

- SEC31_YEAST

UniProt

P38968 - SEC31_YEAST

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Protein

Protein transport protein SEC31

Gene
SEC31, WEB1, YDL195W, D1229
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side 5 Publications

GO - Cellular componenti

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

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 – 3491Phosphoserine2 Publications
Modified residuei836 – 8361Phosphoserine1 Publication
Modified residuei974 – 9741Phosphoserine1 Publication
Modified residuei977 – 9771Phosphoserine1 Publication
Modified residuei980 – 9801Phosphoserine2 Publications
Modified residuei988 – 9881Phosphoserine1 Publication
Modified residuei992 – 9921Phosphoserine3 Publications
Modified residuei999 – 9991Phosphoserine3 Publications
Modified residuei1050 – 10501Phosphothreonine4 Publications
Modified residuei1053 – 10531Phosphoserine2 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 SHR3.7 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.

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.
Contains 8 WD repeats.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti317 – 3171A → T in AAA50367. 1 Publication
Sequence conflicti367 – 3671T → S in CAA58252. 1 Publication
Sequence conflicti367 – 3671T → S in CAA98772. 1 Publication
Sequence conflicti691 – 6911S → N in AAA50367. 1 Publication
Sequence conflicti754 – 7541A → V in AAA50367. 1 Publication
Sequence conflicti877 – 8771T → A in AAA50367. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 136 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.

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

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