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P38167

- ECM21_YEAST

UniProt

P38167 - ECM21_YEAST

Protein

Protein ECM21

Gene

ECM21

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (01 Mar 2005)
      Previous versions | rss
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    Functioni

    May be involved in cell wall organization and biogenesis.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin protein ligase binding Source: SGD

    GO - Biological processi

    1. ubiquitin-dependent endocytosis Source: SGD

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28985-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein ECM21
    Alternative name(s):
    Extracellular mutant protein 21
    Gene namesi
    Name:ECM21
    Ordered Locus Names:YBL101C
    ORF Names:YBL0814
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL101c.
    SGDiS000000197. ECM21.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11171117Protein ECM21PRO_0000086917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphoserine1 Publication
    Modified residuei115 – 1151Phosphoserine1 Publication
    Modified residuei140 – 1401Phosphoserine2 Publications
    Modified residuei286 – 2861Phosphoserine1 Publication
    Modified residuei527 – 5271Phosphoserine1 Publication
    Modified residuei550 – 5501Phosphoserine1 Publication
    Cross-linki577 – 577Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki651 – 651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki712 – 712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei775 – 7751Phosphoserine2 Publications
    Cross-linki794 – 794Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki807 – 807Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki1024 – 1024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei1035 – 10351Phosphoserine1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP38167.
    PaxDbiP38167.

    Expressioni

    Gene expression databases

    GenevestigatoriP38167.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-21359,EBI-16219

    Protein-protein interaction databases

    BioGridi32602. 41 interactions.
    DIPiDIP-791N.
    IntActiP38167. 7 interactions.
    MINTiMINT-628659.
    STRINGi4932.YBL101C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi490 – 51122Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CSR2 family.Curated

    Phylogenomic databases

    eggNOGiNOG258346.
    GeneTreeiENSGT00530000067002.
    HOGENOMiHOG000000708.
    OMAiGNMELPT.
    OrthoDBiEOG7SBNZM.

    Family and domain databases

    InterProiIPR011022. Arrestin_C-like.
    [Graphical view]
    PfamiPF02752. Arrestin_C. 1 hit.
    [Graphical view]
    SMARTiSM01017. Arrestin_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38167-1 [UniParc]FASTAAdd to Basket

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    MPFITSRPVA KNSSHSLSET DLNQSKGQPF QPSPTKKLGS MQQRRRSSTI     50
    RHALSSLLGG ANVHSPAVLN NTTKGGNNNG NIRSSNTDAQ LLGKKQNKQP 100
    PPNARRHSTT AIQGSISDSA TTTPRSSTSD TNRRTSGRLS VDQEPRISGG 150
    RYSQIEEDST VLDFDDDHNS SAVVSSDLSS TSLTRLANSK KFNEQFLIEY 200
    LTARGLLGPK TVLSNEYLKI SISTSGESVF LPTISSNDDE YLSRLNGLND 250
    GTDDAEADFF MDGIDQQEGN TPSLATTAAA TESGGSINEN RDTLLRENNS 300
    GDHPGSGSEL NTRSVEIDSS MVSYSIAVIV SVKKPTRFTD MQLELCSRVK 350
    VFWNTGVPPT KTFNEEFYNA ASMKWNLNDE NFDLFVPLSI SPDDQMIENN 400
    SNDRQMRLFK NIPTEERLYL DKTKTKASLL NAIDVNKTHL YQPGDYVFLV 450
    PVVFSNHIPE TIYLPSARVS YRLRLATKAI NRKGFYRQDS NSPQPIVSPD 500
    SSSSLSSTTS SLKLTETESA QAHRRISNTL FSKVKNHLHM SSHQLKNEES 550
    GEEDIFAEYP IKVIRTPPPV AVSTANKPIY INRVWTDSLS YEISFAQKYV 600
    SLNSEVPIKI KLAPICKNVC VKRIHVSITE RVTFVSKGYE YEYDQTDPVA 650
    KDPYNPYYLD FASKRRKERS VSLFEIRTKE KGTRALREEI VENSFNDNLL 700
    SYSPFDDDSD SKGNPKERLG ITEPIIIETK LKFPKYEDLD KRTAKIIPPY 750
    GIDAYTSIPN PEHAVANGPS HRRPSVIGFL SGHKGSKSHE ENEKPVYDPK 800
    FHQTIIKSNS GLPVKTHTRL NTPKRGLYLD SLHFSNVYCR HKLEIMLRIS 850
    KPDPECPSKL RHYEVLIDTP IFLVSEQCNS GNMELPTYDM ATMEGKGNQV 900
    PLSMNSDFFG NTCPPPPTFE EAISVPASPI VSPMGSPNIM ASYDPDLLSI 950
    QQLNLSRTTS VSGPSGYSDD AGVPNVNRNS ISNANAMNGS ISNSAFVSGN 1000
    SGQGVARARA TSVNDRSRFN NLDKLLSTPS PVNRSHNSSP TNGLSQANGT 1050
    VRIPNATTEN SKDKQNEFFK KGYTLANVKD DEEQEGIVSS SSADSLLSHG 1100
    NEPPRYDEIV PLMSDEE 1117
    Length:1,117
    Mass (Da):123,610
    Last modified:March 1, 2005 - v2
    Checksum:i7DE365C1625B8BA9
    GO

    Sequence cautioni

    The sequence CAA55995.1 differs from that shown. Reason: Frameshift at positions 8, 964 and 967.
    The sequence CAB39760.1 differs from that shown. Reason: Frameshift at positions 8, 964 and 967.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti964 – 9674PSGY → HPDT(PubMed:7502586)Curated
    Sequence conflicti964 – 9674PSGY → HPDT(PubMed:7813418)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79489 Genomic DNA. Translation: CAA55995.1. Frameshift.
    Z35862 Genomic DNA. Translation: CAB39760.1. Frameshift.
    BK006936 Genomic DNA. Translation: DAA07022.1.
    PIRiS45395.
    RefSeqiNP_009449.1. NM_001178341.1.

    Genome annotation databases

    EnsemblFungiiYBL101C; YBL101C; YBL101C.
    GeneIDi852173.
    KEGGisce:YBL101C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79489 Genomic DNA. Translation: CAA55995.1 . Frameshift.
    Z35862 Genomic DNA. Translation: CAB39760.1 . Frameshift.
    BK006936 Genomic DNA. Translation: DAA07022.1 .
    PIRi S45395.
    RefSeqi NP_009449.1. NM_001178341.1.

    3D structure databases

    ProteinModelPortali P38167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32602. 41 interactions.
    DIPi DIP-791N.
    IntActi P38167. 7 interactions.
    MINTi MINT-628659.
    STRINGi 4932.YBL101C.

    Proteomic databases

    MaxQBi P38167.
    PaxDbi P38167.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL101C ; YBL101C ; YBL101C .
    GeneIDi 852173.
    KEGGi sce:YBL101C.

    Organism-specific databases

    CYGDi YBL101c.
    SGDi S000000197. ECM21.

    Phylogenomic databases

    eggNOGi NOG258346.
    GeneTreei ENSGT00530000067002.
    HOGENOMi HOG000000708.
    OMAi GNMELPT.
    OrthoDBi EOG7SBNZM.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28985-MONOMER.

    Miscellaneous databases

    NextBioi 970626.

    Gene expression databases

    Genevestigatori P38167.

    Family and domain databases

    InterProi IPR011022. Arrestin_C-like.
    [Graphical view ]
    Pfami PF02752. Arrestin_C. 1 hit.
    [Graphical view ]
    SMARTi SM01017. Arrestin_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
      Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
      Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [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. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
      Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
      Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577; LYS-651; LYS-712; LYS-794; LYS-807 AND LYS-1024.
      Strain: SUB592.
    8. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577.
    9. "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-140; SER-527 AND SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "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-140; SER-286 AND SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-18; SER-115; SER-775 AND SER-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiECM21_YEAST
    AccessioniPrimary (citable) accession number: P38167
    Secondary accession number(s): D6VPQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 112 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 799 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3