UniProt ID | SIP3_YEAST | |
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UniProt AC | P38717 | |
Protein Name | Membrane-anchored lipid-binding protein SIP3 {ECO:0000303|PubMed:26001273} | |
Gene Name | SIP3 {ECO:0000303|PubMed:8127709} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1229 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass membrane protein . Localizes to puncta in the cell periphery representing cortical endoplasmic reticulum (cER)-plasma membrane (PM) membrane contact sites. |
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Protein Description | May be involved in sterol transfer between intracellular membranes.. | |
Protein Sequence | MSVHGRDPKKRQLRLISVAFKEASIDSPSFRASVNFFQTRVDALEDWIEKTVDFFDQKYKVSFEDFRRAKETLLSQLLPPPALLSNGFVSNQSFTPRLIDSFNKDYYDFSMKLLQIVKGDDSSHSTALLELMTTAIEPYRNVRKNFDFYQGKYDSMLASYQAIRISKTSLEPSSIKSDALQLFEVQKNYLKASLDLISAISAVKLSLDKFILESMKVLKSRSIFITKDSGRKIDLSPCINEYLDNYAIWVENSIEGSKVLDSDISNAKKQAYRYTLKRITPSSDTSDYNIRSIHSSKLLSKDTQVPPKSPEKSGWLYMKTQVGKPTREIWVRRWCFLKNAVFGMFLLSPSKTYVEETDKFGVFLTNVRYDPEEDRKFCFEVKIFGNKVTEAHDNMSKDITLVFQTSNYLDLKSWLIAFEATKKYVMSIQHDSLEYELAFKRFSPKFFEFASSTTTSIDQLITTFDKETESLYETLNCSISEYDILTLGEEKVFQFQMPTTPISTKMTQLAILSNFLTKGSWFPNAVLANIWGTTDWSEYTILPGKGKKPSSLLTIDGKRLPIRNSTIYPQYYSNELKVLDLQFKSLVFSPDQRLEKLPEELLLFKFEALWCPNKKQKFSATCFCTKDYIYCYMNSMEFICLTKISLSEIVSVEADRSSKKTLKLYDASGLQMKAIVLFSDYKLIASKLQYLLENKAIKNPNSNEEILVKFEQMEKESQEKKQEELYKIEQENSFDRKATSVSKIIKSRVTFWEMSDDASTLLNRLKKLQTEYSITYNHEYEISSKGLAHILFGDKSNAFPKCLFLARKDGEEHGKRFWYKNKDINGKSQLVRKIPFRLDMTGNFLNTGKYHRDKESKMIFATQRIVKIVDNKYYEVDLDPFFVKVPFCHLLKLSIKFVITESYDVDNHLEIKLNMTASSSSLHVLYKLEYIDSRTGKTIEKLSLAEIICQTWALKFAHSEFLLIRRVLRYYLEKIGKHGKVIKAIKLCGILGVLSNKSEEPATEKNGNSKESESMQYDIRYSCTILFLVFIKLMVYRVTNLTFVFFRILIGILLLCAEKFSRINRMMVVGLLASIMINILLSEKASVPYWSIKRAEKLFHDRLGSDKFTMQRAIYISDSDLLSSQLSVPSNNPIFEKFSEDNFNKDYQYSETRKQLAMRRNELLIELRILQDMEKQLVHDDYEKFLLEEVNKCSMVSIEMTDLWFNDTQLQNYCSICNEELEKLRPPIT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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2 | Phosphorylation | ------MSVHGRDPK ------CCCCCCCHH | 33.84 | 28889911 | |
153 | Phosphorylation | FDFYQGKYDSMLASY CCCCCCCHHHHHHHH | 21.78 | 30377154 | |
155 | Phosphorylation | FYQGKYDSMLASYQA CCCCCHHHHHHHHHC | 16.77 | 30377154 | |
159 | Phosphorylation | KYDSMLASYQAIRIS CHHHHHHHHHCCEEE | 17.51 | 30377154 | |
160 | Phosphorylation | YDSMLASYQAIRISK HHHHHHHHHCCEEEC | 9.07 | 30377154 | |
166 | Phosphorylation | SYQAIRISKTSLEPS HHHCCEEECCCCCCC | 21.74 | 30377154 | |
201 | Phosphorylation | LDLISAISAVKLSLD HHHHHHHHHHHHHHH | 27.07 | 27017623 | |
277 | Ubiquitination | QAYRYTLKRITPSSD HHHHHEEECCCCCCC | 33.67 | 17644757 | |
286 | Phosphorylation | ITPSSDTSDYNIRSI CCCCCCCCCCCCCCH | 42.99 | 27214570 | |
288 | Phosphorylation | PSSDTSDYNIRSIHS CCCCCCCCCCCCHHH | 16.56 | 21440633 | |
295 | Phosphorylation | YNIRSIHSSKLLSKD CCCCCHHHHCCCCCC | 27.74 | 21440633 | |
348 | Phosphorylation | VFGMFLLSPSKTYVE HHHHHHCCCCCCEEE | 29.31 | 21551504 | |
389 | Phosphorylation | KIFGNKVTEAHDNMS EEECCCCEECCHHCC | 29.12 | 27017623 | |
733 | Phosphorylation | YKIEQENSFDRKATS HHHHHHCCCCCHHHH | 27.98 | 27717283 | |
760 | Phosphorylation | EMSDDASTLLNRLKK ECCCCHHHHHHHHHH | 36.66 | 28889911 | |
1206 | N-linked_Glycosylation | EMTDLWFNDTQLQNY EEECCCCCCHHHHHH | 39.58 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of SIP3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of SIP3_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of SIP3_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-286, AND MASSSPECTROMETRY. |