UniProt ID | KAR3_YEAST | |
---|---|---|
UniProt AC | P17119 | |
Protein Name | Kinesin-like protein KAR3 | |
Gene Name | KAR3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 729 | |
Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus. Cytoplasm, cytoskeleton. Cytoplasmic microtubules. | |
Protein Description | Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule's minus end.. | |
Protein Sequence | MESLPRTPTKGRSTQHLSTPSPKNDILAMNGHKRRNTTTPPPKHTLLKPQRTDIHRHSLASQSRISMSPNRELLKNYKGTANLIYGNQKSNSGVTSFYKENVNELNRTQAILFEKKATLDLLKDELTETKEKINAVNLKFETLREEKIKIEQQLNLKNNELISIKEEFLSKKQFMNEGHEIHLKQLAASNKKELKQMENEYKTKIEKLKFMKIKQFENERASLLDKIEEVRNKITMNPSTLQEMLNDVEQKHMLEKEEWLTEYQSQWKKDIELNNKHMQEIESIKKEIENTLKPELAEKKKLLTEKRNAYEAIKVKVKEKEEETTRLRDEVALKQKTNLETLEKIKELEEYIKDTELGMKELNEILIKEETVRRTLHNELQELRGNIRVYCRIRPALKNLENSDTSLINVNEFDDNSGVQSMEVTKIQNTAQVHEFKFDKIFDQQDTNVDVFKEVGQLVQSSLDGYNVCIFAYGQTGSGKTFTMLNPGDGIIPSTISHIFNWINKLKTKGWDYKVNCEFIEIYNENIVDLLRSDNNNKEDTSIGLKHEIRHDQETKTTTITNVTSCKLESEEMVEIILKKANKLRSTASTASNEHSSRSHSIFIIHLSGSNAKTGAHSYGTLNLVDLAGSERINVSQVVGDRLRETQNINKSLSCLGDVIHALGQPDSTKRHIPFRNSKLTYLLQYSLTGDSKTLMFVNISPSSSHINETLNSLRFASKVNSTRLVSRK | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MESLPRTPTK -----CCCCCCCCCC | 42.23 | 22369663 | |
7 | Phosphorylation | -MESLPRTPTKGRST -CCCCCCCCCCCCCC | 33.11 | 22369663 | |
9 | Phosphorylation | ESLPRTPTKGRSTQH CCCCCCCCCCCCCCC | 45.58 | 22369663 | |
13 | Phosphorylation | RTPTKGRSTQHLSTP CCCCCCCCCCCCCCC | 40.88 | 21440633 | |
14 | Phosphorylation | TPTKGRSTQHLSTPS CCCCCCCCCCCCCCC | 20.74 | 19823750 | |
18 | Phosphorylation | GRSTQHLSTPSPKND CCCCCCCCCCCCCCC | 35.83 | 22369663 | |
19 | Phosphorylation | RSTQHLSTPSPKNDI CCCCCCCCCCCCCCE | 33.86 | 22369663 | |
21 | Phosphorylation | TQHLSTPSPKNDILA CCCCCCCCCCCCEEC | 48.90 | 22369663 | |
37 | Phosphorylation | NGHKRRNTTTPPPKH CCCCCCCCCCCCCCC | 30.18 | 28889911 | |
38 | Phosphorylation | GHKRRNTTTPPPKHT CCCCCCCCCCCCCCC | 40.63 | 29734811 | |
39 | Phosphorylation | HKRRNTTTPPPKHTL CCCCCCCCCCCCCCC | 31.59 | 21440633 | |
52 | Phosphorylation | TLLKPQRTDIHRHSL CCCCCCCCCHHHHCH | 33.77 | 24961812 | |
58 | Phosphorylation | RTDIHRHSLASQSRI CCCHHHHCHHHHCCC | 26.11 | 28889911 | |
61 | Phosphorylation | IHRHSLASQSRISMS HHHHCHHHHCCCCCC | 33.70 | 24961812 | |
63 | Phosphorylation | RHSLASQSRISMSPN HHCHHHHCCCCCCCC | 29.14 | 24961812 | |
66 | Phosphorylation | LASQSRISMSPNREL HHHHCCCCCCCCHHH | 16.46 | 22369663 | |
68 | Phosphorylation | SQSRISMSPNRELLK HHCCCCCCCCHHHHH | 16.54 | 22369663 | |
92 | Phosphorylation | YGNQKSNSGVTSFYK ECCCCCCCCCCCHHH | 41.55 | 30377154 | |
96 | Phosphorylation | KSNSGVTSFYKENVN CCCCCCCCHHHHCHH | 24.95 | 27017623 | |
118 | Phosphorylation | ILFEKKATLDLLKDE HHHCCHHHHHHHHHH | 29.68 | 21126336 | |
226 | Acetylation | ERASLLDKIEEVRNK HHHHHHHHHHHHHHH | 52.57 | 24489116 | |
304 | Phosphorylation | AEKKKLLTEKRNAYE HHHHHHHHHHHHHHH | 50.31 | 17287358 | |
447 | Phosphorylation | KIFDQQDTNVDVFKE HHCCCCCCCCHHHHH | 32.57 | 28889911 | |
570 | Phosphorylation | VTSCKLESEEMVEII CCCCCCCCHHHHHHH | 49.66 | 28889911 | |
586 | Phosphorylation | KKANKLRSTASTASN HHHHHHHHCCCCCCC | 38.47 | 27017623 | |
589 | Phosphorylation | NKLRSTASTASNEHS HHHHHCCCCCCCCCC | 25.29 | 27017623 | |
596 | Phosphorylation | STASNEHSSRSHSIF CCCCCCCCCCCEEEE | 22.67 | 27017623 | |
681 | Phosphorylation | PFRNSKLTYLLQYSL CCCCCHHEEEEEEEE | 18.83 | 27017623 | |
686 | Phosphorylation | KLTYLLQYSLTGDSK HHEEEEEEEECCCCC | 12.96 | 27017623 | |
687 | Phosphorylation | LTYLLQYSLTGDSKT HEEEEEEEECCCCCE | 13.39 | 27017623 | |
689 | Phosphorylation | YLLQYSLTGDSKTLM EEEEEEECCCCCEEE | 32.76 | 27017623 |
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 KAR3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAR3_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 KAR3_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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 THR-19; SER-21 AND SER-68,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 THR-19 AND SER-21, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, AND MASSSPECTROMETRY. |