CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007897
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myosin tail region-interacting protein MTI1 
Protein Synonyms/Alias
 Protein BBC1 
Gene Name
 BBC1 
Gene Synonyms/Alias
 MTI1; YJL020C; J1286; J1305; YJL021C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
73VQGSEVGKEAESSPNubiquitination[1]
357EGTNDIEKEQFLDEYubiquitination[1]
424ALRERMAKLSGASRFubiquitination[1]
499RKSNLSEKNQPTETKubiquitination[1]
858SVLSGAEKESRTLPPubiquitination[1]
1012FNAKVVEKSHSLINSubiquitination[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 Involved in the regulation of actin cytoskeleton. 
Sequence Annotation
 DOMAIN 5 69 SH3.
 MOD_RES 103 103 Phosphoserine.
 MOD_RES 158 158 Phosphoserine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 565 565 Phosphoserine.
 MOD_RES 621 621 Phosphoserine.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 634 634 Phosphoserine.
 MOD_RES 636 636 Phosphothreonine.
 MOD_RES 638 638 Phosphoserine.
 MOD_RES 647 647 Phosphoserine.
 MOD_RES 850 850 Phosphothreonine.
 MOD_RES 889 889 Phosphoserine.
 MOD_RES 894 894 Phosphothreonine.
 MOD_RES 895 895 Phosphothreonine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1157 AA 
Protein Sequence
MSEPEVPFKV VAQFPYKSDY EDDLNFEKDQ EIIVTSVEDA EWYFGEYQDS NGDVIEGIFP 60
KSFVAVQGSE VGKEAESSPN TGSTEQRTIQ PEVEQKDLPE PISPETKKET LSGPVPVPAA 120
TVPVPAATVP VPAATAVSAQ VQHDSSSGNG ERKVPMDSPK LKARLSMFNQ DITEQVPLPK 180
STHLDLENIP VKKTIVADAP KYYVPPGIPT NDTSNLERKK SLKENEKKIV PEPINRAQVE 240
SGRIETENDQ LKKDLPQMSL KERIALLQEQ QRLQAAREEE LLRKKAKLEQ EHERSAVNKN 300
EPYTETEEAE ENEKTEPKPE FTPETEHNEE PQMELLAHKE ITKTSREADE GTNDIEKEQF 360
LDEYTKENQK VEESQADEAR GENVAEESEI GYGHEDREGD NDEEKEEEDS EENRRAALRE 420
RMAKLSGASR FGAPVGFNPF GMASGVGNKP SEEPKKKQHK EKEEEEPEQL QELPRAIPVM 480
PFVDPSSNPF FRKSNLSEKN QPTETKTLDP HATTEHEQKQ EHGTHAYHNL AAVDNAHPEY 540
SDHDSDEDTD DHEFEDANDG LRKHSMVEQA FQIGNNESEN VNSGEKIYPQ EPPISHRTAE 600
VSHDIENSSQ NTTGNVLPVS SPQTRVARNG SINSLTKSIS GENRRKSINE YHDTVSTNSS 660
ALTETAQDIS MAAPAAPVLS KVSHPEDKVP PHPVPSAPSA PPVPSAPSVP SAPPVPPAPP 720
ALSAPSVPPV PPVPPVSSAP PALSAPSIPP VPPTPPAPPA PPAPLALPKH NEVEEHVKSS 780
APLPPVSEEY HPMPNTAPPL PRAPPVPPAT FEFDSEPTAT HSHTAPSPPP HQNVTASTPS 840
MMSTQQRVPT SVLSGAEKES RTLPPHVPSL TNRPVDSFHE SDTTPKVASI RRSTTHDVGE 900
ISNNVKIEFN AQERWWINKS APPAISNLKL NFLMEIDDHF ISKRLHQKWV VRDFYFLFEN 960
YSQLRFSLTF NSTSPEKTVT TLQERFPSPV ETQSARILDE YAQRFNAKVV EKSHSLINSH 1020
IGAKNFVSQI VSEFKDEVIQ PIGARTFGAT ILSYKPEEGI EQLMKSLQKI KPGDILVIRK 1080
AKFEAHKKIG KNEIINVGMD SAAPYSSVVT DYDFTKNKFR VIENHEGKII QNSYKLSHMK 1140
SGKLKVFRIV ARGYVGW 1157 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0030036; P:actin cytoskeleton organization; IPI:SGD. 
Interpro
 IPR001452; SH3_domain. 
Pfam
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS50002; SH3 
PRINTS