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P47068 (BBC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Myosin tail region-interacting protein MTI1
Alternative name(s):
Protein BBC1
Gene names
Name:BBC1
Synonyms:MTI1
Ordered Locus Names:YJL020C
ORF Names:J1286, J1305, YJL021C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of actin cytoskeleton. Ref.3

Subunit structure

Binds to the SH3 domains of the type I myosins MYO3 and MYO5. Ref.3

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: Colocalizes with cortical actin patches. Ref.3

Sequence similarities

Contains 1 SH3 domain.

Sequence caution

The sequence CAA89311.1 differs from that shown. Reason: Frameshift at positions 729 and 732.

The sequence CAA89312.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11571157Myosin tail region-interacting protein MTI1
PRO_0000064839

Regions

Domain5 – 6965SH3
Coiled coil234 – 30168 Potential
Coiled coil356 – 43075 Potential
Compositional bias278 – 412135Glu-rich
Compositional bias674 – 830157Pro-rich

Amino acid modifications

Modified residue1031Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
Modified residue1581Phosphoserine Ref.6 Ref.7 Ref.9
Modified residue1661Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue5651Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue6211Phosphoserine Ref.6 Ref.9
Modified residue6311Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue6341Phosphoserine Ref.6 Ref.9
Modified residue6361Phosphothreonine Ref.9
Modified residue6381Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue6471Phosphoserine Ref.8 Ref.9
Modified residue8501Phosphothreonine Ref.9
Modified residue8891Phosphoserine Ref.7
Modified residue8941Phosphothreonine Ref.6 Ref.9
Modified residue8951Phosphothreonine Ref.6 Ref.9

Secondary structure

............. 1157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47068 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: 88A5899B89CCE8ED

FASTA1,157128,297
        10         20         30         40         50         60 
MSEPEVPFKV VAQFPYKSDY EDDLNFEKDQ EIIVTSVEDA EWYFGEYQDS NGDVIEGIFP 

        70         80         90        100        110        120 
KSFVAVQGSE VGKEAESSPN TGSTEQRTIQ PEVEQKDLPE PISPETKKET LSGPVPVPAA 

       130        140        150        160        170        180 
TVPVPAATVP VPAATAVSAQ VQHDSSSGNG ERKVPMDSPK LKARLSMFNQ DITEQVPLPK 

       190        200        210        220        230        240 
STHLDLENIP VKKTIVADAP KYYVPPGIPT NDTSNLERKK SLKENEKKIV PEPINRAQVE 

       250        260        270        280        290        300 
SGRIETENDQ LKKDLPQMSL KERIALLQEQ QRLQAAREEE LLRKKAKLEQ EHERSAVNKN 

       310        320        330        340        350        360 
EPYTETEEAE ENEKTEPKPE FTPETEHNEE PQMELLAHKE ITKTSREADE GTNDIEKEQF 

       370        380        390        400        410        420 
LDEYTKENQK VEESQADEAR GENVAEESEI GYGHEDREGD NDEEKEEEDS EENRRAALRE 

       430        440        450        460        470        480 
RMAKLSGASR FGAPVGFNPF GMASGVGNKP SEEPKKKQHK EKEEEEPEQL QELPRAIPVM 

       490        500        510        520        530        540 
PFVDPSSNPF FRKSNLSEKN QPTETKTLDP HATTEHEQKQ EHGTHAYHNL AAVDNAHPEY 

       550        560        570        580        590        600 
SDHDSDEDTD DHEFEDANDG LRKHSMVEQA FQIGNNESEN VNSGEKIYPQ EPPISHRTAE 

       610        620        630        640        650        660 
VSHDIENSSQ NTTGNVLPVS SPQTRVARNG SINSLTKSIS GENRRKSINE YHDTVSTNSS 

       670        680        690        700        710        720 
ALTETAQDIS MAAPAAPVLS KVSHPEDKVP PHPVPSAPSA PPVPSAPSVP SAPPVPPAPP 

       730        740        750        760        770        780 
ALSAPSVPPV PPVPPVSSAP PALSAPSIPP VPPTPPAPPA PPAPLALPKH NEVEEHVKSS 

       790        800        810        820        830        840 
APLPPVSEEY HPMPNTAPPL PRAPPVPPAT FEFDSEPTAT HSHTAPSPPP HQNVTASTPS 

       850        860        870        880        890        900 
MMSTQQRVPT SVLSGAEKES RTLPPHVPSL TNRPVDSFHE SDTTPKVASI RRSTTHDVGE 

       910        920        930        940        950        960 
ISNNVKIEFN AQERWWINKS APPAISNLKL NFLMEIDDHF ISKRLHQKWV VRDFYFLFEN 

       970        980        990       1000       1010       1020 
YSQLRFSLTF NSTSPEKTVT TLQERFPSPV ETQSARILDE YAQRFNAKVV EKSHSLINSH 

      1030       1040       1050       1060       1070       1080 
IGAKNFVSQI VSEFKDEVIQ PIGARTFGAT ILSYKPEEGI EQLMKSLQKI KPGDILVIRK 

      1090       1100       1110       1120       1130       1140 
AKFEAHKKIG KNEIINVGMD SAAPYSSVVT DYDFTKNKFR VIENHEGKII QNSYKLSHMK 

      1150 
SGKLKVFRIV ARGYVGW 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae."
Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.
Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-765, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[4]Pohl T.M., Aljinovic G.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1157.
[5]"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 SER-631 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[6]"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-103; SER-158; SER-166; SER-565; SER-621; SER-631; SER-634; SER-638; THR-894 AND THR-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-158 AND SER-889, IDENTIFICATION BY MASS SPECTROMETRY [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-166; SER-565 AND SER-647, 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-103; SER-158; SER-166; SER-565; SER-621; SER-631; SER-634; THR-636; SER-638; SER-647; THR-850; THR-894 AND THR-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49295 Genomic DNA. Translation: CAA89311.1. Frameshift.
Z49296 Genomic DNA. Translation: CAA89312.1. Different initiation.
AF373805 Genomic DNA. Translation: AAL57239.1.
BK006943 Genomic DNA. Translation: DAA08776.1.
PIRS56791.
S56792.
RefSeqNP_012514.2. NM_001181454.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TG0X-ray0.97A1-68[»]
1WDXX-ray2.50A/B/C/D1-68[»]
1ZUKX-ray1.90A/B1-68[»]
2DYFNMR-B796-802[»]
ProteinModelPortalP47068.
SMRP47068. Positions 3-68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33738. 127 interactions.
DIPDIP-2614N.
DIP-6279N.
IntActP47068. 71 interactions.
MINTMINT-553243.

Proteomic databases

MaxQBP47068.
PaxDbP47068.
PeptideAtlasP47068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL020C; YJL020C; YJL020C.
GeneID853433.
KEGGsce:YJL020C.

Organism-specific databases

CYGDYJL020c.
SGDS000003557. BBC1.

Phylogenomic databases

eggNOGNOG12793.
OMARTESHEE.
OrthoDBEOG7FBRS6.

Enzyme and pathway databases

BioCycYEAST:G3O-31492-MONOMER.

Gene expression databases

GenevestigatorP47068.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
PfamPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP47068.
NextBio973976.
PROP47068.

Entry information

Entry nameBBC1_YEAST
AccessionPrimary (citable) accession number: P47068
Secondary accession number(s): D6VWG0, P47067, Q8X1F4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 17, 2003
Last modified: June 11, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references