| Tag | Content |
|---|
| CPLM ID | CPLM-008004 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tricalbin-2 |
Protein Synonyms/Alias | |
Gene Name | TCB2 |
Gene Synonyms/Alias | YNL087W; N2250 |
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 |
|---|
| 229 | PPRIDAIKTFQNTKS | ubiquitination | [1] | | 1068 | NSNRSIGKAVVPLST | ubiquitination | [1] |
|
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, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | May play a role in membrane trafficking. |
Sequence Annotation | DOMAIN 365 463 C2 1.
DOMAIN 637 733 C2 2.
DOMAIN 970 1070 C2 3. |
Keyword | Cell membrane; Coiled coil; Complete proteome; Lipid-binding; Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1178 AA |
Protein Sequence | MSPNSSKTRT DQISSMPGIN EATKVESKNV VKDAVPIKSE VETNGTSIVR EKQDPSYVGW 60
KQVGGWEEKD ELTSEDLLVD VNKDTFLGNL LPDKFYGDWY HEVAILIIAG LCSFVLGYFK 120
FSLASVLIVM LTTGMLYRTS SKKYRESLRD LAQKEQTVEK ITSDYESVEW LNTFLDKYWP 180
IIEPSVSQQI VDGTNTALSE NVAIPKFIKA IWLDQFTLGV KPPRIDAIKT FQNTKSDVVV 240
MDVCLSFTPH DMSDLDAKQC RNYVNSNVVL KAKIFGMDIP VSVADIFFQV FVRFRFQLMT 300
TLPLVETINI QLLEVPEVDF ISRLLGNSVF NWEILAIPGL MRLIQKMAFK YLSPVLLPPF 360
SLQLNIPQLL SKTGLPIGVL EIKVKNAHGL RKLVGMIKKT VDPYLTFELS GKIVGKTKVF 420
KNSANPVWNE SIYILLQSFT DPLTIAVYDK RETLSDKKMG TVIFNLNKLH ANHYHKNEKV 480
HFLRNSKPVG ELTFDLRFFP TIEPKKLLNG DEEPLPDMNT GITKITIREL KGLDELSDKK 540
FVFAELYVNA ELVMTTKKEK RTAHLKWNSD YYSVVTDRRK TICRFVLKDQ SGKVISSSVQ 600
PLNHLIDRTE VNKEWIPLRN GKGELKVTTY WRPVDIDLGL KSVGYTTPIG MLRVFINKAE 660
NLRNPDSLGK ISPYAKVSVN GVARGRTNER IETLNPIWNQ SIYVSVTSPL QKVSIDCFGI 720
DTNGDDHNLG SLNIQTQNIY HKDNDDKYTI FIDNAPRTGN LIGKKGVKGT VTYYLSFYPV 780
VPVLSLEEAK EVDEINEKKD KLEKQKSTLD DKNISKEEKE RIKKEEFRLT EKYDMYSYKM 840
KLDLDELLQY NAGVLGVTVL GGELPQPGLY VQTFFDSCGY AAITSAKNAI RTIKTGWSGD 900
FMIKELEWSV TTFRVTKTKD ANKAENFICE VNIPTIELVR NCYYKPSVLN LIGKKSAKLL 960
VQVSWFPVTA TELPQSDLIT NSGDLKITAK SAENLIGVNK NGYSDPYVEF FLNEKSTSPF 1020
FKTAVQKKTL NPTWNESKTI EVSNRVNDYL TINVKDYEST NSNRSIGKAV VPLSTIDPES 1080
DTTFNIPLVG PKGEDGGVLH LEFEFEPRYT TNVVKREAGL GNFATKGLGT GIKAGSTVFA 1140
LGTNVVSTGL GTIDKVKAGV FGGKKSTTTG DKKSEEKQ 1178 |
Gene Ontology | GO:0005933; C:cellular bud; IDA:SGD. GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0008289; F:lipid binding; IDA:SGD. GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD. GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |