| UniProt ID | RAX2_SCHPO | |
|---|---|---|
| UniProt AC | O14239 | |
| Protein Name | Polarized growth protein rax2 | |
| Gene Name | rax2 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 1155 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Localizes at the cell cortex of the 'old' growing cell tips. |
|
| Protein Description | Controls cell polarity, through the G1 phase of mitosis, via regulation of for3 localization. Required for actin cable formation where it directs the spatial distribution of the actin cables.. | |
| Protein Sequence | MAIYSSFWIRLYFTFRFFCYFLTSVVASDVSFLGDFSGFNVLSNSSANTDLSSQFFEQTNNGSLSSLIDTSYSNSQICYSSWQGDLYVIVLDSEQQTVLLQSNFTSNPTSLEIFSSQNTSFFGNISAIFCDDKFPYAYATFTFSDKPSFTSIYRWNVTNSNVTIEHFYNVKGNVDSLFFLNNDSVAISGNFTEISPFSSSNGPQIAKLAFRSNNSFSQNSLNRNLSSVSCDLTDSYSLWDPSSSGLVSIYAWAPYLIDFNRIRFYNYESSENSVAFFSAINPADGTVLPLTHYDLETGLSSTCDVNCSLQNFANYQDFYFSKGYNSYQIEIQMFGNGEATENSAFGLSSLQFFETNQNSYFDDSYNQESCGFPGLNSLSSYEGNFEASFSNASMPYWIQTIAGEQASVSFFPNITVPTNGTVQLLIPGCTYDNTCSQRGSVIANVYFAKNKQPATKLVQQASDFDQYVSLYSGYLQGFSDNFRPYVELLPYKNSRMVTHSIRFLEQSYTNVSNGLVFVNTTTDVNKLPSIIEFPAASKLRGTAISQIKSLSNGNFSLYMTGNFSDNYGNNVVYMDSLNHLHSFPNNGLNGWVSYIYVSGDSSYFGGNFTHTGDGSIKLNYIAMYSETSRNWSSLGLGTNGPVTHIGSTSLFIDGKIESFISFQGDFNEVYTSEGYAISTSGFSLWNPSSKSWVSMEKLGFYMSGYLFDIPGFNSTQRIYSGNLSAIASYSTRNIAHFSSDSLNDTFIPCYVNAFPSYIRLEDIAYPFANNSMIAILGSEEMEDKCTAAVYFANSTEPIYPKRILSANCSSKFIVLEDCLIIYSNDTDESDIVKNTFVSFNTTSNSLGNTTALSQLKGHINSVIVDDSYNNIFFGGNLSEQSSGCVGFCIFEYNSSSWRNISHNLISAEVQSILWVNETYSSMYLAGKFVWDTSDVDYLLMYNFDNNTIMSCKGSSSIPGPVLLASLKSQSKDEYSVLLYGTEVSSSDTYLNVLNSEGAINSYSLDIHLNQSTINSIDFFESNQISQIPINDSIIVLSGLIVLDDSSKASAVYCVNKSCLPLLTAFKDNGEAGIVRKVVQQKSFSSSASKMIPVTTKYDHIGQPRYVVIISLGISIGVMFLIMSGSIVVEIIHWFFSEHVETLHDYSNFLKELKTQ | |
| 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 |
|---|---|---|---|---|---|
| 44 | N-linked_Glycosylation | SGFNVLSNSSANTDL CCCEECCCCCCCCCH | 35.50 | - | |
| 61 | N-linked_Glycosylation | QFFEQTNNGSLSSLI HHHHHCCCCCHHHHE | 44.83 | - | |
| 103 | N-linked_Glycosylation | QTVLLQSNFTSNPTS CEEEEECCCCCCCCC | 31.11 | - | |
| 118 | N-linked_Glycosylation | LEIFSSQNTSFFGNI EEEEECCCCCCCCCE | 39.37 | - | |
| 124 | N-linked_Glycosylation | QNTSFFGNISAIFCD CCCCCCCCEEEEECC | 21.64 | - | |
| 156 | N-linked_Glycosylation | FTSIYRWNVTNSNVT CEEEEEEEECCCCEE | 23.03 | - | |
| 161 | N-linked_Glycosylation | RWNVTNSNVTIEHFY EEEECCCCEEEEEEE | 36.70 | - | |
| 182 | N-linked_Glycosylation | DSLFFLNNDSVAISG CEEEEECCCEEEEEC | 45.11 | - | |
| 190 | N-linked_Glycosylation | DSVAISGNFTEISPF CEEEEECCCEEEECC | 33.60 | - | |
| 213 | N-linked_Glycosylation | AKLAFRSNNSFSQNS HHHHHHCCCCCCCCC | 43.86 | - | |
| 224 | N-linked_Glycosylation | SQNSLNRNLSSVSCD CCCCCCCCCCEEECC | 43.11 | - | |
| 306 | N-linked_Glycosylation | LSSTCDVNCSLQNFA CCCCCCCCCEECCCC | 9.08 | - | |
| 391 | N-linked_Glycosylation | NFEASFSNASMPYWI CCEECCCCCCCCEEE | 33.74 | - | |
| 413 | N-linked_Glycosylation | ASVSFFPNITVPTNG CEEEECCCEECCCCC | 37.09 | - | |
| 419 | N-linked_Glycosylation | PNITVPTNGTVQLLI CCEECCCCCEEEEEC | 37.76 | - | |
| 510 | N-linked_Glycosylation | FLEQSYTNVSNGLVF HHHHCEEECCCCEEE | 27.30 | - | |
| 519 | N-linked_Glycosylation | SNGLVFVNTTTDVNK CCCEEEEECCCCHHH | 21.90 | - | |
| 554 | N-linked_Glycosylation | IKSLSNGNFSLYMTG EEECCCCCEEEEEEC | 27.81 | - | |
| 562 | N-linked_Glycosylation | FSLYMTGNFSDNYGN EEEEEECCCCCCCCC | 24.88 | - | |
| 607 | N-linked_Glycosylation | DSSYFGGNFTHTGDG CCCEECCCCEECCCC | 38.74 | - | |
| 630 | N-linked_Glycosylation | MYSETSRNWSSLGLG EEECCCCCHHHCCCC | 42.63 | - | |
| 713 | N-linked_Glycosylation | LFDIPGFNSTQRIYS EEECCCCCCCCEEEC | 50.49 | - | |
| 722 | N-linked_Glycosylation | TQRIYSGNLSAIASY CCEEECCCHHHEEEE | 25.53 | - | |
| 743 | N-linked_Glycosylation | HFSSDSLNDTFIPCY CCCCCCCCCCCEEEE | 50.67 | - | |
| 769 | N-linked_Glycosylation | DIAYPFANNSMIAIL HCCCCCCCCCEEEEE | 41.30 | - | |
| 793 | N-linked_Glycosylation | TAAVYFANSTEPIYP CEEEEECCCCCCCCC | 39.30 | - | |
| 807 | N-linked_Glycosylation | PKRILSANCSSKFIV CHHHEECCCCCCEEE | 23.87 | - | |
| 824 | N-linked_Glycosylation | DCLIIYSNDTDESDI CEEEEEECCCCHHHH | 38.95 | - | |
| 840 | N-linked_Glycosylation | KNTFVSFNTTSNSLG HCEEEEEECCCCCCC | 34.63 | - | |
| 848 | N-linked_Glycosylation | TTSNSLGNTTALSQL CCCCCCCCHHHHHHH | 39.28 | - | |
| 876 | N-linked_Glycosylation | NNIFFGGNLSEQSSG CCEEECCCCCCCCCC | 40.55 | - | |
| 893 | N-linked_Glycosylation | GFCIFEYNSSSWRNI EEEEEEECCCCCCCC | 28.37 | - | |
| 899 | N-linked_Glycosylation | YNSSSWRNISHNLIS ECCCCCCCCCHHHHH | 33.58 | - | |
| 916 | N-linked_Glycosylation | VQSILWVNETYSSMY HHHHHEECCCCCCCC | 25.06 | - | |
| 945 | N-linked_Glycosylation | LLMYNFDNNTIMSCK EEEEECCCCEEEECC | 43.33 | - | |
| 1009 | N-linked_Glycosylation | YSLDIHLNQSTINSI EEEEEEECCCCCCEE | 21.42 | - | |
| 1030 | N-linked_Glycosylation | QISQIPINDSIIVLS CCCCCCCCCEEEEEE | 31.46 | - | |
| 1055 | N-linked_Glycosylation | ASAVYCVNKSCLPLL CCEEEEECHHHHHHH | 27.28 | - |
| 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 RAX2_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAX2_SCHPO !! | ||||||
* 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 RAX2_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of RAX2_SCHPO !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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