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P38167

- ECM21_YEAST

UniProt

P38167 - ECM21_YEAST

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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

Functioni

May be involved in cell wall organization and biogenesis.

GO - Molecular functioni

  1. ubiquitin protein ligase binding Source: SGD

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. ubiquitin-dependent endocytosis Source: SGD
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiP38167.
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

« Hide

        10         20         30         40         50
MPFITSRPVA KNSSHSLSET DLNQSKGQPF QPSPTKKLGS MQQRRRSSTI
60 70 80 90 100
RHALSSLLGG ANVHSPAVLN NTTKGGNNNG NIRSSNTDAQ LLGKKQNKQP
110 120 130 140 150
PPNARRHSTT AIQGSISDSA TTTPRSSTSD TNRRTSGRLS VDQEPRISGG
160 170 180 190 200
RYSQIEEDST VLDFDDDHNS SAVVSSDLSS TSLTRLANSK KFNEQFLIEY
210 220 230 240 250
LTARGLLGPK TVLSNEYLKI SISTSGESVF LPTISSNDDE YLSRLNGLND
260 270 280 290 300
GTDDAEADFF MDGIDQQEGN TPSLATTAAA TESGGSINEN RDTLLRENNS
310 320 330 340 350
GDHPGSGSEL NTRSVEIDSS MVSYSIAVIV SVKKPTRFTD MQLELCSRVK
360 370 380 390 400
VFWNTGVPPT KTFNEEFYNA ASMKWNLNDE NFDLFVPLSI SPDDQMIENN
410 420 430 440 450
SNDRQMRLFK NIPTEERLYL DKTKTKASLL NAIDVNKTHL YQPGDYVFLV
460 470 480 490 500
PVVFSNHIPE TIYLPSARVS YRLRLATKAI NRKGFYRQDS NSPQPIVSPD
510 520 530 540 550
SSSSLSSTTS SLKLTETESA QAHRRISNTL FSKVKNHLHM SSHQLKNEES
560 570 580 590 600
GEEDIFAEYP IKVIRTPPPV AVSTANKPIY INRVWTDSLS YEISFAQKYV
610 620 630 640 650
SLNSEVPIKI KLAPICKNVC VKRIHVSITE RVTFVSKGYE YEYDQTDPVA
660 670 680 690 700
KDPYNPYYLD FASKRRKERS VSLFEIRTKE KGTRALREEI VENSFNDNLL
710 720 730 740 750
SYSPFDDDSD SKGNPKERLG ITEPIIIETK LKFPKYEDLD KRTAKIIPPY
760 770 780 790 800
GIDAYTSIPN PEHAVANGPS HRRPSVIGFL SGHKGSKSHE ENEKPVYDPK
810 820 830 840 850
FHQTIIKSNS GLPVKTHTRL NTPKRGLYLD SLHFSNVYCR HKLEIMLRIS
860 870 880 890 900
KPDPECPSKL RHYEVLIDTP IFLVSEQCNS GNMELPTYDM ATMEGKGNQV
910 920 930 940 950
PLSMNSDFFG NTCPPPPTFE EAISVPASPI VSPMGSPNIM ASYDPDLLSI
960 970 980 990 1000
QQLNLSRTTS VSGPSGYSDD AGVPNVNRNS ISNANAMNGS ISNSAFVSGN
1010 1020 1030 1040 1050
SGQGVARARA TSVNDRSRFN NLDKLLSTPS PVNRSHNSSP TNGLSQANGT
1060 1070 1080 1090 1100
VRIPNATTEN SKDKQNEFFK KGYTLANVKD DEEQEGIVSS SSADSLLSHG
1110
NEPPRYDEIV PLMSDEE
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. Curated
The sequence CAB39760.1 differs from that shown. Reason: Frameshift at positions 8, 964 and 967. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P38167.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 113 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