UniProt ID | LCB5_YEAST | |
---|---|---|
UniProt AC | Q06147 | |
Protein Name | Sphingoid long chain base kinase 5 | |
Gene Name | LCB5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 687 | |
Subcellular Localization |
Golgi apparatus membrane Peripheral membrane protein . |
|
Protein Description | Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Redundant to LCB4, is only responsible for few percent of the total activity. Involved in the biosynthesis of sphingolipids and ceramides. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance.. | |
Protein Sequence | MTLKPSKRRKGRSRHSRKKQITSAILTEEGIMIKAKPSSPYTYANRMADKRSRSSIDNISRTSFQSNISRTSFQSNSDNNSIFETASLISCVTCLSDTDTIDRSETSTTDTSKDDLSANPKLHYPSVNGQLPANTVIPYGRILDARYIEKEPLHYYDANSSPSSPLSSSMSNISEKCDLDELESSQKKERKGNSLSRGSNSSSSLLTSRSPFTKLVEVIFARPRRHDVVPKRVSLYIDYKPHSSSHLKEEDDLVEEILKRSYKNTRRNKSIFVIINPFGGKGKAKKLFMTKAKPLLLASRCSIEVVYTKYPGHAIEIAREMDIDKYDTIACASGDGIPHEVINGLYQRPDHVKAFNNIAITEIPCGSGNAMSVSCHWTNNPSYSTLCLIKSIETRIDLMCCSQPSYAREHPKLSFLSQTYGLIAETDINTEFIRWMGPARFELGVAFNIIQKKKYPCEIYVKYAAKSKNELKNHYLEHKNKGSLEFQHITMNKDNEDCDNYNYENEYETENEDEDEDADADDEDSHLISRDLADSSADQIKEEDFKIKYPLDEGIPSDWERLDPNISNNLGIFYTGKMPYVAADTKFFPAALPSDGTMDMVITDARTSLTRMAPILLGLDKGSHVLQPEVLHSKILAYKIIPKLGNGLFSVDGEKFPLEPLQVEIMPRLCKTLLRNGRYVDTDFDSM | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
38 | Phosphorylation | IMIKAKPSSPYTYAN CEEEECCCCCCHHHH | 43.15 | 27017623 | |
39 | Phosphorylation | MIKAKPSSPYTYANR EEEECCCCCCHHHHH | 30.38 | 21440633 | |
52 | Phosphorylation | NRMADKRSRSSIDNI HHHCCCCCHHHHCHH | 42.10 | 22369663 | |
54 | Phosphorylation | MADKRSRSSIDNISR HCCCCCHHHHCHHHH | 32.65 | 22369663 | |
55 | Phosphorylation | ADKRSRSSIDNISRT CCCCCHHHHCHHHHH | 32.62 | 22369663 | |
60 | Phosphorylation | RSSIDNISRTSFQSN HHHHCHHHHHHHHCC | 35.44 | 23749301 | |
62 | Phosphorylation | SIDNISRTSFQSNIS HHCHHHHHHHHCCCC | 27.40 | 22369663 | |
63 | Phosphorylation | IDNISRTSFQSNISR HCHHHHHHHHCCCCC | 21.85 | 22369663 | |
66 | Phosphorylation | ISRTSFQSNISRTSF HHHHHHHCCCCCCCC | 33.83 | 22369663 | |
69 | Phosphorylation | TSFQSNISRTSFQSN HHHHCCCCCCCCCCC | 33.48 | 22369663 | |
91 | S-palmitoylation | ETASLISCVTCLSDT HHHHHHHHHHHCCCC | 2.02 | - | |
94 | S-palmitoylation | SLISCVTCLSDTDTI HHHHHHHHCCCCCCC | 1.38 | - | |
106 | Phosphorylation | DTIDRSETSTTDTSK CCCCCCCCCCCCCCH | 32.40 | 28889911 | |
107 | Phosphorylation | TIDRSETSTTDTSKD CCCCCCCCCCCCCHH | 25.84 | 28889911 | |
109 | Phosphorylation | DRSETSTTDTSKDDL CCCCCCCCCCCHHHC | 36.73 | 19779198 | |
111 | Phosphorylation | SETSTTDTSKDDLSA CCCCCCCCCHHHCCC | 35.27 | 28889911 | |
112 | Phosphorylation | ETSTTDTSKDDLSAN CCCCCCCCHHHCCCC | 36.58 | 28889911 | |
113 | Ubiquitination | TSTTDTSKDDLSANP CCCCCCCHHHCCCCC | 58.30 | 23749301 | |
147 | Phosphorylation | GRILDARYIEKEPLH CEEEEEEEEECCCCC | 18.36 | 17330950 | |
155 | Phosphorylation | IEKEPLHYYDANSSP EECCCCCEECCCCCC | 15.66 | 22369663 | |
156 | Phosphorylation | EKEPLHYYDANSSPS ECCCCCEECCCCCCC | 9.61 | 22369663 | |
160 | Phosphorylation | LHYYDANSSPSSPLS CCEECCCCCCCCCCH | 45.40 | 20377248 | |
161 | Phosphorylation | HYYDANSSPSSPLSS CEECCCCCCCCCCHH | 28.71 | 20377248 | |
163 | Phosphorylation | YDANSSPSSPLSSSM ECCCCCCCCCCHHHC | 46.68 | 20377248 | |
164 | Phosphorylation | DANSSPSSPLSSSMS CCCCCCCCCCHHHCC | 32.99 | 22369663 | |
167 | Phosphorylation | SSPSSPLSSSMSNIS CCCCCCCHHHCCCHH | 24.61 | 22369663 | |
168 | Phosphorylation | SPSSPLSSSMSNISE CCCCCCHHHCCCHHH | 37.43 | 20377248 | |
169 | Phosphorylation | PSSPLSSSMSNISEK CCCCCHHHCCCHHHH | 23.89 | 20377248 | |
171 | Phosphorylation | SPLSSSMSNISEKCD CCCHHHCCCHHHHCC | 32.72 | 22369663 | |
174 | Phosphorylation | SSSMSNISEKCDLDE HHHCCCHHHHCCHHH | 34.94 | 22369663 | |
184 | Phosphorylation | CDLDELESSQKKERK CCHHHHHHHHHHHHC | 51.17 | 30377154 | |
194 | Phosphorylation | KKERKGNSLSRGSNS HHHHCCCCCCCCCCC | 36.07 | 21440633 | |
196 | Phosphorylation | ERKGNSLSRGSNSSS HHCCCCCCCCCCCCH | 34.12 | 24961812 | |
199 | Phosphorylation | GNSLSRGSNSSSSLL CCCCCCCCCCCHHHH | 32.21 | 22369663 | |
201 | Phosphorylation | SLSRGSNSSSSLLTS CCCCCCCCCHHHHHC | 33.04 | 22369663 | |
202 | Phosphorylation | LSRGSNSSSSLLTSR CCCCCCCCHHHHHCC | 28.35 | 22369663 | |
203 | Phosphorylation | SRGSNSSSSLLTSRS CCCCCCCHHHHHCCC | 25.48 | 22369663 | |
204 | Phosphorylation | RGSNSSSSLLTSRSP CCCCCCHHHHHCCCC | 29.37 | 22369663 | |
207 | Phosphorylation | NSSSSLLTSRSPFTK CCCHHHHHCCCCCHH | 27.64 | 22369663 | |
208 | Phosphorylation | SSSSLLTSRSPFTKL CCHHHHHCCCCCHHH | 30.63 | 22369663 | |
503 | Phosphorylation | EDCDNYNYENEYETE CCCCCCCCCCCCCCC | 15.12 | 26447709 | |
507 | Phosphorylation | NYNYENEYETENEDE CCCCCCCCCCCCCCC | 39.47 | 19779198 | |
509 | Phosphorylation | NYENEYETENEDEDE CCCCCCCCCCCCCCC | 43.11 | 28889911 | |
535 | Phosphorylation | ISRDLADSSADQIKE HHHHHCCCCCHHHHH | 23.09 | 28889911 | |
686 | Phosphorylation | YVDTDFDSM------ CCCCCCCCC------ | 26.78 | 21440633 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of LCB5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LCB5_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of LCB5_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-168; SER-169;SER-171; SER-201; SER-202 AND SER-204, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASSSPECTROMETRY. |