CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011864
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tricalbin-1 
Protein Synonyms/Alias
  
Gene Name
 TCB1 
Gene Synonyms/Alias
 YOR086C; YOR3141c 
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
480NLNTLHDKTTQRNLKacetylation[1]
566KLVLTTGKATDTGTLubiquitination[2]
666AIRVFIEKANDLRNLubiquitination[2]
692VLVNGLSKGRTDFKSubiquitination[2]
1061LNDVLRIKVMDWDSTubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 May play a role in membrane trafficking. 
Sequence Annotation
 DOMAIN 373 471 C2 1.
 DOMAIN 645 741 C2 2.
 DOMAIN 979 1078 C2 3.
 METAL 1008 1008 Calcium 1 (By similarity).
 METAL 1008 1008 Calcium 2 (By similarity).
 METAL 1014 1014 Calcium 1 (By similarity).
 METAL 1064 1064 Calcium 1 (By similarity).
 METAL 1064 1064 Calcium 2 (By similarity).
 METAL 1066 1066 Calcium 1 (By similarity).
 METAL 1066 1066 Calcium 2 (By similarity).
 METAL 1066 1066 Calcium 3 (By similarity).
 METAL 1069 1069 Calcium 3 (By similarity).
 METAL 1072 1072 Calcium 2 (By similarity).
 METAL 1072 1072 Calcium 3 (By similarity).
 MOD_RES 1000 1000 Phosphoserine.  
Keyword
 Calcium; Calcium/phospholipid-binding; Cell membrane; Coiled coil; Complete proteome; Lipid-binding; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1186 AA 
Protein Sequence
MAKEDTGVTA PKKPETAQVA NINGIDKLEP PKTKEETESS KSVSSEKAAH ASDESFKRSI 60
HEASYVGWKQ IGGWEDKDEL TLDDELMDMT RETFLDNIIP DSLYGDWYHS VAIFFIGGVA 120
SFALGHYKFS MGSAFFVIVI TSLLYRTSAK KYRGSIRELV QKEFTVQKVE NDYESLEWLN 180
AFLDKYWPIL EPSVSQLIVQ QANEQMATNE AIPKFITQLW IDELTLGVKP PRVDLVKTFQ 240
NTASDVVVMD WGISFTPHDL CDMSAKQVRN YVNELAVVKA KIFGITIPVS VSDIAFKAHA 300
RVKFKLMTPF PHVETVNIQL LKVPDFDFVA TLFGRSIFNW EILAIPGLMT LIQKMAKKYM 360
GPILLPPFSL QLNIPQLLSG SNLSIGILEI TVKNAKGLKR TSSILNESID PYLSFEFNDI 420
SIAKTRTVRD TLNPVWDETL YVLLNSFTDP LTISVYDKRA KLKDKVLGRI QYNLNTLHDK 480
TTQRNLKAQF LRNSKPVGEL TFDLRFFPTL EEKKLPDGSV EELPDLNTGI AKVVVEEGSR 540
FAEEEQKVTA YVEVYLNAKL VLTTGKATDT GTLKWNSDYE AVIADRRKTR YKFVVKDGKG 600
EEIGSTIQTL NDLIDRSQVN KNLIPLKNQK GDIKITTYWR PVRLEIGSNS VAYTPPIGAI 660
RVFIEKANDL RNLEKFGTID PYCKVLVNGL SKGRTDFKSQ TLNPVWNQVI YVAVTSPNQR 720
ITLQCMDVET VNKDRSLGEF NVNVQDLFKK DENDKYEETI DEKAKVGRLV MPKKKPKGTI 780
TYYTSFYPAL PVLTLEEIQD LDKVNKKKKA LELRKSAIDE KKISKEDKAK FDQEWNEVKE 840
LEDMYSNRQK LDLPELLQYN QGVLAVTVLN GELPDSGLYV QAFFDDNGHP RFVSPRIPSR 900
IVKNGWSGDV IIKELDKSIT TFRVAKNKNY NRVEKCVCEV ELPTQELVKN CYYKPSILHL 960
SGEGSAKLML QISWFPIDTK QLPANDLITN SGDLTIMSRS AENLIASDLN GYSDPYLKYY 1020
INNEEDCAYK TKVVKKTLNP KWNDEGTIQI NNRLNDVLRI KVMDWDSTSA DDTIGTAEIP 1080
LNKVKVEGTT ELDVPVEGLE NAGQDGGMLH LAFSFKPRYT ISVSKREKKV GDIASKGLGT 1140
GLKAGTTVIG GGVGAIGKIK KGVFGGLGSL TNHKKNHEMG EEETKF 1186 
Gene Ontology
 GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
 GO:0008289; F:lipid binding; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD.
 GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR020477; C2_dom.
 IPR018029; C2_membr_targeting.
 IPR017147; Tricalbin. 
Pfam
 PF00168; C2 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2 
PRINTS
 PR00360; C2DOMAIN.