UniProt ID | AXL2_YEAST | |
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UniProt AC | P38928 | |
Protein Name | Axial budding pattern protein 2 | |
Gene Name | AXL2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 823 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . In small buds, localizes to incipient bud sites, emerging buds and to the bud periphery. In large buds, localizes as a ring at the bud neck. Requires ERV14 to be efficiently delivered to the cell |
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Protein Description | Required for haploid cells axial budding pattern. Acts as an anchor to help direct new growth components and/or polarity establishment components like the BUD5 GTP/GDP exchange factor to localize at the cortical axial budding site. Regulates septin organization in late G1 independently of its role in polarity-axis determination.. | |
Protein Sequence | MTQLQISLLLTATISLLHLVVATPYEAYPIGKQYPPVARVNESFTFQISNDTYKSSVDKTAQITYNCFDLPSWLSFDSSSRTFSGEPSSDLLSDANTTLYFNVILEGTDSADSTSLNNTYQFVVTNRPSISLSSDFNLLALLKNYGYTNGKNALKLDPNEVFNVTFDRSMFTNEESIVSYYGRSQLYNAPLPNWLFFDSGELKFTGTAPVINSAIAPETSYSFVIIATDIEGFSAVEVEFELVIGAHQLTTSIQNSLIINVTDTGNVSYDLPLNYVYLDDDPISSDKLGSINLLDAPDWVALDNATISGSVPDELLGKNSNPANFSVSIYDTYGDVIYFNFEVVSTTDLFAISSLPNINATRGEWFSYYFLPSQFTDYVNTNVSLEFTNSSQDHDWVKFQSSNLTLAGEVPKNFDKLSLGLKANQGSQSQELYFNIIGMDSKITHSNHSANATSTRSSHHSTSTSSYTSSTYTAKISSTSAAATSSAPAALPAANKTSSHNKKAVAIACGVAIPLGVILVALICFLIFWRRRRENPDDENLPHAISGPDLNNPANKPNQENATPLNNPFDDDASSYDDTSIARRLAALNTLKLDNHSATESDISSVDEKRDSLSGMNTYNDQFQSQSKEELLAKPPVQPPESPFFDPQNRSSSVYMDSEPAVNKSWRYTGNLSPVSDIVRDSYGSQKTVDTEKLFDLEAPEKEKRTSRDVTMSSLDPWNSNISPSPVRKSVTPSPYNVTKHRNRHLQNIQDSQSGKNGITPTTMSTSSSDDFVPVKDGENFCWVHSMEPDRRPSKKRLVDFSNKSNVNVGQVKDIHGRIPEML | |
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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41 | N-linked_Glycosylation | YPPVARVNESFTFQI CCCCEEECCCEEEEE | 33.37 | - | |
50 | N-linked_Glycosylation | SFTFQISNDTYKSSV CEEEEECCCCCCCCC | 47.47 | - | |
96 | N-linked_Glycosylation | SDLLSDANTTLYFNV HHHHCCCCCEEEEEE | 38.29 | - | |
117 | N-linked_Glycosylation | SADSTSLNNTYQFVV CCCCCCCCCEEEEEE | 38.27 | - | |
163 | N-linked_Glycosylation | LDPNEVFNVTFDRSM CCCCCCEEEEEEHHH | 36.77 | - | |
260 | N-linked_Glycosylation | IQNSLIINVTDTGNV EECCEEEEEECCCCE | 24.52 | - | |
266 | N-linked_Glycosylation | INVTDTGNVSYDLPL EEEECCCCEEEEECC | 22.96 | - | |
304 | N-linked_Glycosylation | PDWVALDNATISGSV CCEEEECCCEEECCC | 39.57 | - | |
324 | N-linked_Glycosylation | GKNSNPANFSVSIYD CCCCCCCCEEEEEEE | 30.86 | - | |
359 | N-linked_Glycosylation | ISSLPNINATRGEWF ECCCCCCCCCCCCCE | 41.73 | - | |
382 | N-linked_Glycosylation | FTDYVNTNVSLEFTN HHCCCCCCEEEEEEC | 19.04 | - | |
389 | N-linked_Glycosylation | NVSLEFTNSSQDHDW CEEEEEECCCCCCCE | 45.01 | - | |
403 | N-linked_Glycosylation | WVKFQSSNLTLAGEV EEEEECCCEEEEEEC | 42.14 | - | |
416 | Acetylation | EVPKNFDKLSLGLKA ECCCCCCCEEEEEEC | 35.52 | 24489116 | |
447 | N-linked_Glycosylation | DSKITHSNHSANATS CCCCCCCCCCCCCCC | 26.06 | - | |
451 | N-linked_Glycosylation | THSNHSANATSTRSS CCCCCCCCCCCCCCC | 46.92 | - | |
495 | N-linked_Glycosylation | PAALPAANKTSSHNK CCCCCCCCCCCCCCH | 50.69 | - | |
597 | Phosphorylation | TLKLDNHSATESDIS CCCCCCCCCCHHHCC | 43.04 | 23749301 | |
599 | Phosphorylation | KLDNHSATESDISSV CCCCCCCCHHHCCCH | 38.75 | 23749301 | |
601 | Phosphorylation | DNHSATESDISSVDE CCCCCCHHHCCCHHH | 35.57 | 23749301 | |
604 | Phosphorylation | SATESDISSVDEKRD CCCHHHCCCHHHHHH | 29.33 | 23749301 | |
605 | Phosphorylation | ATESDISSVDEKRDS CCHHHCCCHHHHHHC | 33.64 | 23749301 | |
609 | Ubiquitination | DISSVDEKRDSLSGM HCCCHHHHHHCCCCC | 57.98 | 23749301 | |
612 | Phosphorylation | SVDEKRDSLSGMNTY CHHHHHHCCCCCCCC | 28.59 | 20377248 | |
614 | Phosphorylation | DEKRDSLSGMNTYND HHHHHCCCCCCCCCH | 39.69 | 22369663 | |
618 | Phosphorylation | DSLSGMNTYNDQFQS HCCCCCCCCCHHHHH | 18.14 | 29734811 | |
619 | Phosphorylation | SLSGMNTYNDQFQSQ CCCCCCCCCHHHHHC | 16.25 | 28889911 | |
625 | Phosphorylation | TYNDQFQSQSKEELL CCCHHHHHCCHHHHH | 37.40 | 20377248 | |
627 | Phosphorylation | NDQFQSQSKEELLAK CHHHHHCCHHHHHCC | 47.48 | 20377248 | |
634 | Ubiquitination | SKEELLAKPPVQPPE CHHHHHCCCCCCCCC | 50.23 | 23749301 | |
642 | Phosphorylation | PPVQPPESPFFDPQN CCCCCCCCCCCCCCC | 32.55 | 24909858 | |
651 | Phosphorylation | FFDPQNRSSSVYMDS CCCCCCCCCCEECCC | 34.22 | 20377248 | |
652 | Phosphorylation | FDPQNRSSSVYMDSE CCCCCCCCCEECCCC | 22.15 | 28889911 | |
653 | Phosphorylation | DPQNRSSSVYMDSEP CCCCCCCCEECCCCC | 20.65 | 24961812 | |
655 | Phosphorylation | QNRSSSVYMDSEPAV CCCCCCEECCCCCCC | 9.35 | 20377248 | |
664 | Ubiquitination | DSEPAVNKSWRYTGN CCCCCCCCCCCCCCC | 44.81 | 23749301 | |
665 | Phosphorylation | SEPAVNKSWRYTGNL CCCCCCCCCCCCCCC | 16.16 | 23749301 | |
668 | Phosphorylation | AVNKSWRYTGNLSPV CCCCCCCCCCCCCCH | 16.85 | 21440633 | |
669 | Phosphorylation | VNKSWRYTGNLSPVS CCCCCCCCCCCCCHH | 15.83 | 28132839 | |
673 | Phosphorylation | WRYTGNLSPVSDIVR CCCCCCCCCHHHHHH | 27.53 | 17330950 | |
676 | Phosphorylation | TGNLSPVSDIVRDSY CCCCCCHHHHHHHCC | 25.63 | 17330950 | |
682 | Phosphorylation | VSDIVRDSYGSQKTV HHHHHHHCCCCCCEE | 22.34 | 21440633 | |
683 | Phosphorylation | SDIVRDSYGSQKTVD HHHHHHCCCCCCEEC | 25.70 | 19779198 | |
685 | Phosphorylation | IVRDSYGSQKTVDTE HHHHCCCCCCEECHH | 21.92 | 21440633 | |
687 | Ubiquitination | RDSYGSQKTVDTEKL HHCCCCCCEECHHHH | 52.81 | 23749301 | |
688 | Phosphorylation | DSYGSQKTVDTEKLF HCCCCCCEECHHHHH | 18.90 | 23749301 | |
691 | Phosphorylation | GSQKTVDTEKLFDLE CCCCEECHHHHHCCC | 30.59 | 21440633 | |
693 | Ubiquitination | QKTVDTEKLFDLEAP CCEECHHHHHCCCCC | 57.45 | 23749301 | |
706 | Phosphorylation | APEKEKRTSRDVTMS CCHHHCCCCCCCCHH | 38.90 | 21440633 | |
707 | Phosphorylation | PEKEKRTSRDVTMSS CHHHCCCCCCCCHHH | 30.43 | 20377248 | |
711 | Phosphorylation | KRTSRDVTMSSLDPW CCCCCCCCHHHCCCC | 18.67 | 22369663 | |
713 | Phosphorylation | TSRDVTMSSLDPWNS CCCCCCHHHCCCCCC | 20.55 | 22369663 | |
714 | Phosphorylation | SRDVTMSSLDPWNSN CCCCCHHHCCCCCCC | 26.43 | 23749301 | |
720 | Phosphorylation | SSLDPWNSNISPSPV HHCCCCCCCCCCCCC | 31.50 | 22369663 | |
723 | Phosphorylation | DPWNSNISPSPVRKS CCCCCCCCCCCCCCC | 24.47 | 22369663 | |
725 | Phosphorylation | WNSNISPSPVRKSVT CCCCCCCCCCCCCCC | 29.27 | 22369663 | |
730 | Phosphorylation | SPSPVRKSVTPSPYN CCCCCCCCCCCCCCC | 22.21 | 22369663 | |
732 | Phosphorylation | SPVRKSVTPSPYNVT CCCCCCCCCCCCCCH | 25.74 | 20377248 | |
734 | Phosphorylation | VRKSVTPSPYNVTKH CCCCCCCCCCCCHHH | 30.56 | 20377248 | |
736 | Phosphorylation | KSVTPSPYNVTKHRN CCCCCCCCCCHHHHH | 26.97 | 21440633 | |
739 | Phosphorylation | TPSPYNVTKHRNRHL CCCCCCCHHHHHHHH | 19.93 | 24961812 | |
752 | Phosphorylation | HLQNIQDSQSGKNGI HHHHHCCCCCCCCCC | 15.18 | 24909858 | |
754 | Phosphorylation | QNIQDSQSGKNGITP HHHCCCCCCCCCCCC | 56.54 | 25533186 | |
763 | Phosphorylation | KNGITPTTMSTSSSD CCCCCCCCEECCCCC | 15.44 | 21440633 | |
765 | Phosphorylation | GITPTTMSTSSSDDF CCCCCCEECCCCCCE | 24.05 | 21440633 | |
766 | Phosphorylation | ITPTTMSTSSSDDFV CCCCCEECCCCCCEE | 23.08 | 21440633 | |
767 | Phosphorylation | TPTTMSTSSSDDFVP CCCCEECCCCCCEEE | 22.12 | 20377248 | |
768 | Phosphorylation | PTTMSTSSSDDFVPV CCCEECCCCCCEEEC | 37.56 | 20377248 | |
769 | Phosphorylation | TTMSTSSSDDFVPVK CCEECCCCCCEEECC | 40.75 | 20377248 | |
802 | Phosphorylation | KKRLVDFSNKSNVNV CCCEEECCCCCCCCH | 38.59 | 28889911 | |
805 | Phosphorylation | LVDFSNKSNVNVGQV EEECCCCCCCCHHHH | 50.70 | 22369663 |
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 AXL2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of AXL2_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 AXL2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673 AND SER-676, ANDMASS SPECTROMETRY. |