ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P36988 | AVKCIGWQETCNGKLPCCDGCVMCECNIMGQNCRCNHPKATSECES | Function: Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
Sequence Mass (Da): 4999
Sequence Length: 46
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellu... |
P36983 | MKHLIFSSALVCALVVCTFAEEQVNVPFLPDERAVKCIGWQETCNGNLPCCNECVMCECNIMGQNCRCNHPKATNECESRRR | Function: Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
PTM: Plectoxin-5 presumably undergoes post-translational modification to give rise to plectoxin-6.
Sequence Mass (Da): 9241
Sequence Length: 82
Domain: The presen... |
P83998 | MPCPKILKQCKSDEDCCRGWKCFGFSIKDKMCISR | Function: Neurotoxin.
Sequence Mass (Da): 4086
Sequence Length: 35
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P30288 | KKKCIAKDYGRCKWGGTPCCRGRGCICSIMGTNCECKPRLIMEGLGLA | Function: Omega-agatoxins inhibit neuronal voltage-gated calcium channels. This toxin acts by modifying the gating of the high voltage activated P-type Cav2.1/CACNA1A channel. Is a potent blocker in both insect and mammalian central neurons.
Sequence Mass (Da): 5210
Sequence Length: 48
Domain: The presence of a 'disulf... |
P37045 | MKLCMTLLITAIAVVTFVVATQEESAEFNEVEESREDNCIAEDYGKCTWGGTKCCRGRPCRCSMIGTNCECTPRLIMEGLSFA | Function: Antagonist of voltage-gated Cav2.1/CACNA1A (P-type) calcium channels. Paralyzes insect by blocking neuromuscular transmission.
PTM: The toxin with D-Ser (named omega-aga IVC) is 80-90 fold more potent than that with L-Ser (omega-aga IVB) against Cav2.1/CACNA1A (P-type) channels in rat cerebellar Purkinje neur... |
I6R1R5 | MPSLCIIALFGTLTFYTLIPSIHTLKCVRCDGPMSNYDCKTTYPAAEECPSLSGGSSNYCSKKETFTSNGNLEQTRRYCNSVAAPSTACTDLKTGGKLCEYSCNTDGCNSVAGMEPTRAVYFIAILMLA | Function: Toxin that increase voltage-gated calcium channel (Cav) currents in DRG neurons by 70% and 120%, when 1 uM and 10 uM are tested, respectively.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 13873
Sequence Length: 129
Subcellular Location: Secreted
|
P0DSL6 | MNIRLMFTLIALLVLTVSFSGANSCFKRNRQCKGSFLKSACCEGLKCVNGRCT | Function: May have neurotoxic activity.
Sequence Mass (Da): 5835
Sequence Length: 53
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P61789 | DDDCGWIMDDCTSDSDCCPNWVCSKTGFVKNICKYEM | Function: Blocks calcium channels (Cav).
Sequence Mass (Da): 4229
Sequence Length: 37
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P61790 | ADCGWLFHSCESNADCCENWACATTGRFRYLCKYQI | Function: Blocks calcium channels (Cav).
Sequence Mass (Da): 4167
Sequence Length: 36
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
Q5Y4U2 | MCVATCLCTFAYVLAKSDEGENLISKVEETQRGCIEIGGDCDGYLDKSYCQCCRNNGFCSCYKVPEWFGYKVGCKCSVDWNFVGWCRLKQFCPGGSQNPSLCKDPNPRRRRHGK | Function: Inhibits voltage-gated calcium channels (Cav).
Sequence Mass (Da): 12862
Sequence Length: 114
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
B3A0P0 | IIECFFSCEIEKDGKSKEGKPCKPKGDKDKDKKCGGWRCKIKMCIKI | Function: Is toxic to insects. Reduces amplitude and frequency of spontaneous firing and inhibits voltage-gated sodium current (Nav) in the dorsal unpaired median (DUM) neurons of P.americana.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 5380
Sequence Length: 47
Subcellular Location: Secreted
|
P0C2A1 | ADVPGNYPLDSYGNCYPCTILGDNQYCI | Function: Binds to sodium channels (Nav) and affects the channel activation process.
Sequence Mass (Da): 3069
Sequence Length: 28
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
|
A0A088BP94 | MKFAIVITLLLVAFSAVALADKSIERAVMDLITARDDDCGKLFADCTSDSDCCENWVCSKTGFVKNICKYNFG | Function: Insecticidal toxin that potently and irreversibly blocks voltage-gated sodium channels (Nav) in cockroach dorsal unpaired median (DUM) neurons (IC(50)=833.7 nM) . It does not change both the steady-state activation and inactivation curves, suggesting it acts as a pore blocker (possibly at Nav site 1) . Does n... |
P55816 | AKDGDVKGPAGCMKYKSGDCRGKTCCDQQYLWYKWRNLACRCFTVEVFKKDCWCNDIS | Function: Acts by delaying the inactivation of presynaptic voltage-sensitive sodium channels (Nav). Acts against insects and cause a progressive spastic paralysis.
Sequence Mass (Da): 6724
Sequence Length: 58
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Su... |
P55817 | AKDGDFEGPPGCLKMGELCKGGTCCTKVYKYWKWRKLECLGKNDGWFKKKFICDEPCNPXX | Function: Acts by delaying the inactivation of presynaptic voltage-sensitive sodium channels (Nav). Acts against insects and causes a progressive spastic paralysis.
Sequence Mass (Da): 6975
Sequence Length: 61
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
S... |
O46166 | MKLQLMICLVLLPCFFCEPDEICRARMTHKEFNYKSNVCNGCGDQVAACEAECFRNDVYTACHEAQKG | Function: Toxin that paralyzes insects. May have a direct effect on the insect central nervous system.
Sequence Mass (Da): 7741
Sequence Length: 68
Domain: Is exclusively composed of 4 tightly packed alpha helices (no beta strand is present).
Subcellular Location: Secreted
|
P49126 | MKVFVVLLCLSLAAVYALEERLDKDADIMLDSPADMERAKDGDVEGPAGCKKYDVECDSGECCQKQYLWYKWRPLDCRCLKSGFFSSKCVCRDV | Function: Insecticidal toxin . This toxin promotes opening of insect Nav channels. The toxin binds to the S1-S2 and S3-S4 loops in the domain II voltage-sensor of insect Nav channels (i.e., receptor site 4). The American cockroach P.americana is largely resistant to the effects of this toxin due to an unusual sequence ... |
P61791 | DDCGTLFSGCDTSKDCCEGYVCHLWCKYK | Function: Inhibitor of voltage-gated potassium channels of the Kv4/KCND family (By similarity). Blocks calcium channels (Cav).
Sequence Mass (Da): 3281
Sequence Length: 29
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
B6DD61 | MFSTSDQVSKMNSRILSALLILGIATCVIAGGFCPKSRHPQCNLSYKINDCCAQSDCRVGSVCCVEGCGNVCRAESDTPLGEKFVDGSECKHGHVFPKKWYQFWWRV | Function: Has antibacterial activity.
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 11842
Sequence Length: 107
Subcellular Location: Secreted
|
P49271 | WLGCARVKEACGPWEWPCCSGLKCDGSECHPQ | Function: Is both paralytic and lethal, when injected into lepidopteran larvae. Is a slower acting toxin, being lethal at 24 hours, but not paralytic at 1 hour post-injection.
Sequence Mass (Da): 3537
Sequence Length: 32
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a... |
P36989 | CAKHSETCKNGNCCTCTQYRGKDEPMACRRGTHGQRCQCVMKIMKH | Function: Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 5234
Sequence Length: 46
Subcellular Location: Secreted
|
P54373 | MSTYESLMVMIGFANLIGGIMTWVISLLTLLFMLRKKDTHPIYITVKEKCLHEDPPIKG | Function: Toxic component of a type I toxin-antitoxin (TA) system . Overexpression of txpA causes cell lysis; the TxpA protein has been suggested to act on the cell membrane or might possibly block cell wall synthesis . Overexpression in E.coli is not toxic .
Location Topology: Single-pass membrane protein
Sequence Mas... |
P86269 | GYCAEKGIRCDDIHCCTGLKCKCNASGYNCVCRKK | Function: Inhibits P2RX3 receptors. Has an analgesic effect in rat. Enhances the high-affinity desensitization of P2RX3 purinoceptors. At 50 nM, decreases the IC(50) for ambient ATP from 46.5 nM to 12.7 nM in mouse P2RX3.
Sequence Mass (Da): 3845
Sequence Length: 35
Domain: The presence of a 'disulfide through disulfid... |
P0DQN3 | ECRYWLGGCSAGQTCCKHLVCSRRHGWCVWDGTFS | Function: Ion channel impairing toxin that inhibits voltage-gated calcium channel Cav3.1/CACNA1G (IC(50)=53 nM), voltage-gated potassium channels Kv2.1/KCNB1 (IC(50)=411 nM), all sodium channels tested (Nav1.2/SCN2A (IC(50)=60-104 nM), Nav1.5/SCN5A (IC(50)=76-358 nM), Nav1.6/SCN8A (IC(50)=21-133 nM), Nav1.7/SCN9A (IC(5... |
B3EWH0 | AKACTPLLHDCSHDRHSCCRGDMFKYVCDCFYPEGEDKTEVCSCQQPKSHKIAEKIIDKAKTTL | Function: Enhances the high-affinity desensitization of human P2RX3 purinoceptors . At 50 nM, the toxin decreases the IC(50) for ambient ATP from 2.67 nM to 0.77 nM in human P2RX3 .
PTM: Amidation at Leu-64 is not mandatory for activity on P2RX3.
Sequence Mass (Da): 7264
Sequence Length: 64
Domain: The toxin is compose... |
P83476 | YCQKWMWTCDSERKCCEGMVCRLWCKKKLW | Function: Gating-modifier toxin that targets voltage-gated sodium channels with a selective activity on Nav1.7/SCN9A (IC(50)=1-1.5 nM) . It inhibits both activation and inactivation . For inhibition of activation, it is 100-fold more selective for Nav1.7/SCN9A (IC(50)=0.26-3) than for other sodium channels (Nav1.2/SCN2... |
P61233 | CGTNRAWCRNAKDHCCCGYSCVKPIWASKPEDDGYCWKKFGGC | Function: This toxin blocks the neuromuscular transmission, and also acts on muscle. It exerts an effect of first exciting and then inhibiting the contraction of muscle. This toxin is active only against mammals.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 4849
Sequence Length: 43
Domain: The presence of a 'di... |
P95748 | MAHSSATAGPQADYSGEIAELYDLVHQGKGKDYHREAADLAALVRRHSPKAASLLDVACGTGMHLRHLADSFGTVEGLELSADMLAIARRRNPDAVLHHGDMRDFSLGRRFSAVTCMFSSIGHLAGQAELDAALERFAAHVLPDGVVVVEPWWFPENFTPGYVAAGTVEAGGTTVTRVSHSSREGEATRIEVHYLVAGPDRGITHHEESHRITLFTREQYERAFTAAGLSVEFMPGGPSGRGLFTGLPGAKGETR | Function: S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.
Catalytic Activity: dTDP-3-amin... |
O70023 | MRIALLTMGSRGDVQPFVALGTGLRARGHEVVLGAPEALRPLVEQAGLEYRATPGDPDGFFTMPEVVETLRRGPAMRDLMKALPPAPEEYDQEVLDRIERAGEGVDLVVHAPLTVTTALGEPSTPWLSVNWWPNTSTWTFPAVESGQRRMGPLTPLYNRLTHWRAEREDWGWRRAEVNEFRGRRGLPPFGKSSPLRRLGHPRPHLYPFSPSVLPKPRDWPGQCHVTGYWFWDQPGWRPSPELEDFLADGEPPVLLTLGSTWPVHRQEEMVEYAVAAARGARRRLLLVGGPEGALPGDALRVPSADYSWLMPRTAAVVHHG... | Function: Involved in the biosynthesis of the macrolide antibiotic tylosin derived from the polyketide lactone tylactone. Catalyzes the transfer of 6-deoxy-alpha-D-allose from dTDP-6-deoxy-alpha-D-allose to O-mycaminosyltylonolide (OMT) to yield demethyllactenocin.
Catalytic Activity: 5-O-beta-D-mycaminosyltylonolide +... |
O43914 | MGGLEPCSRLLLLPLLLAVSGLRPVQAQAQSDCSCSTVSPGVLAGIVMGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK | Function: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors . TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated recep... |
Q8WNQ8 | MGGLEPCSRLLLLPLLLAVGGLRPVQAQAQSDCSCSTVSPGVLAGIVLGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK | Function: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the a... |
O54885 | MGALEPSWCLLFLPVLLTVGGLSPVQAQSDTFPRCDCSSVSPGVLAGIVLGDLVLTLLIALAVYSLGRLVSRGQGTAEGTRKQHIAETESPYQELQGQRPEVYSDLNTQRQYYR | Function: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors . TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated recep... |
Q9TU45 | MGRLGPSNGLLPLLLAVGGFSLVQAQRECSCSAVSPGILAGIVLGDLVLTLLIALAVYSLGRLVPRTRGAVDVTRKQHIAETESAYQELQGQRSDVYSDLNTQRQYYK | Function: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the a... |
O62584 | MPQDPRHPEHQYLDLVKHILENGARRMDRTGTGTLSVFGATMRFSLEDNTFPLLTTRRVFYRGVVEELLFFLRGETDSKVLEKKGVRIWEKNGAKQFLQSVGIDREEGDLGPIYGFQWRHFGARYETSASSYEGKGVDQIASAIAAIRANPASRRIVVSAWNPTDLGSMALPPCHVLFQFNVTDGKLSCAMYQRSGDMGLGVPFNIASYSLLTILVAHLTGLQPGEFVHFLGDAHVYLDHVDSLRQQIQRPPRAFPKLFVSPKGPRTEPEHFQYEDFELVGYDPHPAIKMNMSA | Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 33112
Sequence Length: 294
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.45
|
Q2T9J0 | MRRQWGSAMRAAEQAGCMVSASRAGQPEAGPWSCSGVILSRSPGLVLCHGGIFVPFLRAGSEVLTAAGAVFLPGDSCRDDLRLHVQWAPTAAGPGGGAERGRPGLCTPQCASLEPGPPAPSRGRPLQPRLPAELLLLLSCPAFWAHFARLFGDEAAEQWRFSSAARDDEVSEDEEADQLRALGWFALLGVRLGQEEVEEERGPAMAVSPLGAVPKGAPLLVCGSPFGAFCPDIFLNTLSCGVLSNVAGPLLLTDARCLPGTEGGGVFTARPAGALVALVVAPLCWKAGEWVGFTLLCAAAPLFRAARDALHRLPHSTAAL... | Function: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids.
PTM: Self-cleavage gives rise to an N-t... |
P0CI79 | MTQFDKQYNSIIKDIINNGISDEEFDVRTKWDSDGTPAHTLSVISKQMRFDNSEVPILTTKKVAWKTAIKELLWIWQLKSNDVNDLNMMGVHIWDQWKQEDGTIGHAYGFQLGKKNRSLNGEKVDQVDYLLHQLKNNPSSRRHITMLWNPDELDAMALTPCVYETQWYVKHGKLHLEVRARSNDMALGNPFNVFQYNVLQRMIAQVTGYELGEYIFNIGDCHVYTRHIDNLKIQMEREQFEAPELWINPEVKDFYDFTIDDFKLINYKHGDKLLFEVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
P11044 | MKQYKDFCRHVLEHGEKKGDRTGTGTISTFGYQMRFNLREGFPMLTTKKLHFKSIAHELLWFLKGDTNVRYLQENGVRIWNEWADENGELGPVYGSQWRSWRGADGETIDQISRLIEDIKTNPNSRRLIVSAWNVGEIDKMALPPCHCLFQFYVSDGKLSCQLYQRSADVFLGVPFNIASYALLTMIIAHVTGLEPGEFIHTFGDVHIYQNHIEQVNLQLERDVRPLPQLRFARKVDSIFNFAFEDFIIEDYDPHPHIKGAVSV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
A1TM53 | MNAPARPVRSQYEDFMRHVYTHGVAKGDRTGTGTRSVFGYQMRFDLNEGFPLVTTKKVHLKSIITELLWFLTGSSSNHWLKERGVTIWDEWAREDGDLGPVYGVQWRSWPTPDGGHIDQISQVVETLRTHPDSRRIIVSAWNVADLDKMALMPCHAFFQFYVAPPQAAGERGKLSCQLYQRSADIFLGVPFNIASYALLTHMMAQQCNLEVGDFIWTGGDCHIYSNHFEQVELQLSRAPHPYPTLHILRRPDSLFDYRFEDFEVRDYAHHPAIKAPVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
Q9WBI3 | MDINNEEKQYLNLLEKVLFQGEDRDDRTGIGTKNVFGEQLKFNLRTSFPLLTTKKVFWKGVVEELLWFISGSTDVSVLNQKGVKIWNKNAESFYTQQNLFKKNDLGPIYGFQWRHYGENYIGCDNKYGGIDQLKNIITTIQNEPWDRRMILLAWNPKDNSKMALPPCHCIAHFDVSSKINGKRELSCHLFQRSADMGLGVPFNIASYALLTHIIAHVSSTNTELIVPGDFVHTLSNVHIYKNHIKALTEQISRIPRKFPTLEIINKNKNIDAFSSKDFVLKDYNPYPALEMEMAL | Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 33961
Sequence Length: 295
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.45
|
P00469 | MLEQPYLDLAKKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTKKVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPDMTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQWRAWHTSKGDTIDQLGDVIEQIKTHPYSRRLIVSAWNPEDVPTMALPPCHTLYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGEFIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIKLLNYDPYPAIKAPVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
Q6R6M4 | MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLY... | Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitinatio... |
Q6QN14 | MEDDSLYLRGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLY... | Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, cell migration, and the cellular response to viral infection. Seems to be non-functional in the regulation of apopt... |
Q8VXY9 | MESLKRFLCSIALLLISLLLPSSLAQQQQHESIRTMEDFSGYPIHEPGQFGSINLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKRSLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLELHIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAGLAAAELALAVEKHVLES... | Cofactor: Binds 2 manganese ions per subunit. Can also use nickel and cobalt with lower activity.
Function: Involved in the catabolism of purine nucleotides. Can use (S)-ureidoglycolate as substrate, but not (R)-ureidoglycolate or allantoate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine break... |
Q940S3 | MIEPSMERENGALTAATTTTTAVTSPPPMASSPRQALVERLKDYGQEDIFSLWDELSPDEKDFLVRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENWVSTVDGRTMEDREKWWKMGLKTIYEGKLGVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQIQAERILCVQRLAAQVVSEGPIRPVTIHWYIMTSPFTDEATRKYFSSHKYFGLEPDQISFFQQGTLPCVTKDGKFIMETPFSLAKAPDGNGGVYAALKCSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKGAASAAKVVRKAYPQEQVG... | Function: Uridylyltransferase involved in the biosynthesis of UDP-glucosamine, an essential precursor for glycoprotein and glycolipid synthesis. Can use both UDP-glucosamine and the 4-epimer UDP-galactosamine as substrates, but no other sugars or NTPs . Acts redundantly with GLCNAC1PUT2. Required for gametogenesis and ... |
Q18493 | MTITAPPKDEIISKFPGSEPLLNFYNELSDAEKSKLFHQISTLNLSEAHQWFIDSADQRAPSTAEDLKPVLDSQHFVQAELHQVILDGLWNKGMDAIGRGEVCAIVLAGGQATRLGSSQPKGTIPLGINASFGDSLLGIQAAKIALLQALAGEREHQNPGKIHWAVMTSPGTEEATREHVKKLAAHHGFDFDEQITIFSQDEIAAYDEQGNFLLGTKGSVVAAPNGNGGLYSAISAHLPRLRAKGIKYFHVYCVDNILCKVADPHFIGFAISNEADVATKCVPKQKGELVGSVCLDRGLPRVVEYSELGAELAEQKTPDG... | Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 53497
Sequence Length: 484
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosam... |
O74933 | MTVKSQQQIIDSFKQANQDQLFQYYDSLTIDQQQEFIDQLSTIEEPAKLISTVEQAIQFSQTNSTSRNFTQLPNEQTASTLDLSKDILQNWTELGLKAIGNGEVAVLLMAGGQGTRLGSSAPKGCFNIELPSQKSLFQIQAEKILKIEQLAQQYLKSTKKPIINWYIMTSGPTRNATESFFIENNYFGLNSHQVIFFNQGTLPCFNLQGNKILLESKNSICQSPDGNGGLYKALKDNGILDDLNSKGIKHIHMYCVDNCLVKVADPIFIGFAIAKKFDLATKVVRKRDANESVGLIVLDQDNQKPCVIEYSEISQELANK... | Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 54644
Sequence Length: 486
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosam... |
Q54GN5 | MDTTNFEDIRNEWIEQGQGHVFNWFDKLSNEEKLNFENDIRKINVKEVNKDYKNVLLNKDEQKIMKYEHFENVMTLNKIKEQDKKKWEDIGYELISKGEVAVLLLAGGQATRLGTTFPKGFYDVGLPSKKSLFQLQAERIYRLQQLVSERYNGSYDQDSKPIQWYIMTSEATHSETIKFFENKNYFGLKKSAFFFFSQAMIPCITPEDGKIISESGSKLSLSPNGNGGLFKALSTSGAIDDMRKKGIKYVTQYCVDNILINMADPVFVGYMHDQSADCGAKVVSKSDPKEPVGVMALNGDGKPFVLEYSEIDEQSKFKKD... | Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 55431
Sequence Length: 487
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosam... |
Q8SQS1 | MGYISMNSTNLIRPYEGTELNDAGRKYKKIGERLLREKKLGVVILSGGQGTRLGSDEPKGLFKIKGKTLFEWHMETIKELISKYNADIAVFIMTSSFTDEAVRKYFQSTDFGLKIQFFKQRNSLCVGTDGKPLEWYDGHAESPYGNGDIFNAIQQVNLEGIEALNVICIDNVLAKILDPVFVGAFYSDDYDILSKSVTKEEKESVGAFLMDERLKIKEYSENDAKGEGIQGNICNHIFKTSFIKKMKNINLPEHKAFKKIPYTISGKLIKPVKPNGFKKETFIFDSFEYTQKNGVMNVPREKEFSPLKNGMDSSVDNPVT... | Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 37953
Sequence Length: 335
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosam... |
Q16222 | MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGR... | Function: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
Catalytic Activity: H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP = diphosphate + UD... |
Q91YN5 | MNVNDLKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEFDRSSHQEKVDARMEPVPRQVLGSATRDQEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGR... | Function: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P (By similarity).
Catalytic Activity: H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP = ... |
O94617 | MDDKELFDRSIFEETNQLHLYDQLNYLKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPLSIVDTSDSSWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFPDQEASISIPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEACKATENVDGHK... | Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 53121
Sequence Length: 475
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosam... |
P43123 | MTDTKQLFIEAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLL... | Function: UDP-N-acetylglucosamine pyrophosphorylase that utilizes N-acetylglucosamine-1-phosphate as substrate . Together with AGM1, is involved in the production of UDP-N-acetylglucosamine from N-acetylglucosamine-6-phosphate .
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + U... |
O64765 | MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFV... | Function: Uridylyltransferase involved in the biosynthesis of UDP-glucosamine, an essential precursor for glycoprotein and glycolipid synthesis. Can use UDP-glucosamine, the 4-epimer UDP-galactosamine and UDP-glucose as substrates . Acts redundantly with GLCNAC1PUT1. Required for gametogenesis and embryo development .
... |
Q07307 | MDNSIHSTDGPDSVIPNSNPKKTVRQRVRLLARHLTTREGLIGDYDYGFLFRPELPFMKKDPRAPPFFGLNEKIPVLLAFILGLQHALAMLAGVVTPPLIISSSLSLPSDLQQYLVSTSLIVCGLLSMVQITRFHIYKTPYYIGSGVLSVMGVSFSIISVASGAFNQMYSNGFCQLDEAGNRLPCPEAYGALIGTSACCALVEILLAFVPPKVIQKIFPPIVTGPTVMLIGISLIGTGFKDWAGGSACMDDGMLCPSATAPRPLPWGSPEFIGLGFLVFVSIILCERFGAPIMKSCSVVIGLLVGCIVAAACGYFSHADI... | Function: Uric acid-xanthine transporter.
PTM: Ubiquitinated by hulA. Ubiquitination leads to internalization, sorting into the endosomal pathway to the vacuolar lumen where uapA is eventually degraded.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61121
Sequence Length: 574
Subcellular Location: C... |
Q9GZZ9 | MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVA... | Function: E1-like enzyme which specifically catalyzes the first step in ufmylation . Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP . Activates UFM1 via a trans-bind... |
Q8VE47 | MADSVERLRQRVEELEQELARERTRRSGGDGHCGRTRIQEMSDEVLDSNPYSRLMALKRMGIVSDYKKIRTYAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITTVEHFEHFMNRISNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTWMESGVSENAVSGHIQLMIPGESACFACAPPLVVASNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLKFGTVSFYLGYNAMQDFFPTMFMKPNPQCDDKNCRKQQEEYKKRAAAL... | Function: E1-like enzyme which specifically catalyzes the first step in ufmylation . Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP (By similarity). Activates UFM1 v... |
Q8VY10 | MEMSLTDSDWDSSSDSGSSEHEEVEFSYGGRAQNIFSNLEETIGKIDEFLSFERGFMYGDIVRSATEPSGQSGRVINIDMFVNLESTHGKIMKEVDTKRLQKLRSISLSDYVINGPWVGRVDKIVERVSVTLDDGTNYEVLVDGQDKLVAIPPNLLEDSQYSYYPGQRVQVKLAHAPRSTTWLCGTWRGTQVMGTVCTVEAGLVYVDWVASIVMEGDRNLTAPQALQNPESLTLLPCVSHASWQLGDWCILPGSSHCDIAERQTPNVAAYNLNECHKTFQKGFNRNMQNSGLDELFVITKTKMKVAVMWQDGSCSLGVDS... | Function: E2 ubiquitin-protein ligase that mediates E1-dependent protein ubiquitination . Mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability . Negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions... |
Q9LUQ5 | MEPNVVEIATPPAASCSRIRTPTKAETPEVIDVEEYDLQNGGVPNGNNVDYKNKGKAIDFDSMSYGDYGEEDEYAVGSPGDDYGYPESSPLSNSLLDPESLIYEDDENYSEQYDFEMEAEPDNYSMYQDLFDGKDIPTGVEVSMDWFPNSADKESASSSKSSHANNGNNSSKKATKASGIHSQFSSDMETPVAQPWNALPHKAEGVIPNSAYALPQNSKAFQPPYAVHYSALKTAFSNYLQPQTPDTVLGEAPAPAAGSSGLLPPNTPGFKSNAARFKEEPPILPPDDSRVKRNMEDYLGLYLFFKRFDIVEDFSDHHYA... | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugatin... |
Q93571 | MACLRKLKEDIQVLEKLFPKNHNRFQILSASVDELSMKFINAENKGIIVTANIQENYPRQPPIWFSESDDVPVIGMSLQRLTETEESTNILHQVHRLVSDLCSFYNLQMPCELPQIAPPVRDDIDEGRGSDISDTTSEPIDDDMAGDGEVDDDDEEEEDDEDADGDIEIVEMAEEDPTSQHDVGVSKEGLDMLDKVSKINRQQHLDGKVQGSITATDRLMKEIRDIHRSEHFKNGIYTFELEKEENLYQWWIKLHKVDEDSPLFEDMKKLKKDHNQDHLLFSFTFNEKFPCDPPFVRVVAPHINQGFVLGGGAICMELLT... | Function: Catalyzes the covalent attachment of ubiquitin to other proteins (Potential). Required for the maintenance of neuromuscular function .
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-... |
Q8GY87 | MEPDVVEIPPPPLIASGSRTRKPRKAVPEVIDVESYEFRNVGVVKDNNVVDKKNKGKAIQVDSFSFNNVQSHHHGSSLLNLETFQDYYGHKNIPFSEFANQPIDVDDYSMYQDVLDPKDVPAGAEVTVPWGLNSSSKGTAKSSISIMRSQSMKGYGTVSLATTNVPQLWDYTLPQQNQAIYSSVSFSAVQPQTPDVVMVTNPTPNPFSYDASASSSHPIAAEPISSVQDSSNARKLKEEFLRDFKRFDTVEDFSDHHYASKGKSSKQHSKNWVKKVQADWKILENDLPEAISVRACESRMDLLRAVIIGAEGTPYHDGLF... | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugatin... |
Q9FI61 | MIDFSRIQKELQDCERNQDSSGIRVCPKSDNLTRLTGTIPGPIGTPYEGGTFQIDITMPDGYPFEPPKMQFSTKVWHPNISSQSGAICLDILKDQWSPALTLKTALVSIQALLSAPEPKDPQDAVVAEQYMKNYQVFVSTARYWTETFAKKSSLEEKVKRLVEMGFGDAQVRSAIESSGGDENLALEKLCSA | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugatin... |
Q9VSF3 | MIKLFTLKQQKKDGEQKGSQQKKASAAQLRIQKDINELNLPNTCATDFPDPNDLLNFKLIISPDEGFYRDGRFVFNFRVGSNYPHEPPKVKCATQVYHPNIDLDGNVCLNILREDWNPVLNINSIVYGLQFLFLEPNPEDPLNKEAADVLQTNRRQFENNVKKAMRGGCVGETYFECCLLK | Function: Accepts the ubiquitin-like protein Nedd8 from the Uba3-APP-BP1 E1 complex and catalyzes its covalent attachment to other proteins. Required for Cul1 and Cul3 neddylation. Negatively regulates full-length ci stability and hedgehog signaling.
Catalytic Activity: [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl... |
P42745 | MSTPARKRLMRDFKRLQQDPPAGISGAPQDNNIMLWNAVIFGPDDTPWDGGTFKLSLQFSEDYPNKPPTVRFVSRMFHPNIYADGSICLDILQNQWSPIYDVAAILTSIQSLLCDPNPNSPANSEAARMFSESKREYNRRVREVVEQSWTAD | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugatin... |
P35129 | MALKRIQKELQDLGRDPPAQCSAGPVGDDLFHWQATIMGPPESPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRERYNQLAREWTQKYAM | Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Mediates the selective degradation of short-lived and abnormal proteins . Plays a role in the DNA damage response . In particular, in response to ionizing radiation, associates with the E3 ubiquitin-protein ligase brc-1-brd-1 he... |
P0CS17 | MSTAAKRRLIRDFKRLTSDAPIGISGSPNPDNIMVWNAVIFGPPETPFEDGSFRLTLTFTDAYPNKPPTVRFISKMFHPNIYANGELCLDILQNRWSPTYDVAAILTSVQSLLNDPNPASPANVDAAQLFKENLKEYERRVKKTVELSWVDNADEIEAEVVEADEGSSS | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formati... |
Q55EY8 | MTSRYAKRLQKELLDLKTNPPPCISITEGDNLDKWVIAVDGTEGSIYQGEHFKLQFKFSSGYPLDSPEVIFIGTPPIHPHIYSNGHICLSILYDNWSPALTVSSVCLSILSMLSGCTEKIRPTDDSKYVSRVLNKSPKEVRWMFHDDTV | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
Q96B02 | MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins . Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini . Involved in degradation of misfold... |
Q8VDW4 | MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPIHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini . Involved in degradation of misfolde... |
Q28FC1 | MASMQKRLQKELLALQNEPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGDNIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrate and DNA repair.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme... |
Q6DG60 | MAHTITPAVESGLGVLTHAVSSTVPVAVLPSLPPGIGSGVPAGAGLLSQIHATSWDPTLSTDWDNEKASQQCILRIKRDIMSIYKEPPPGMFVVPDPHDMTKIHALITGPFDTPYEGGFFLFLFRCPPDYPIHPPRVKLITTGHNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETMRVAVCDMLEGKVSCPEALWSVMEKSFLEYYDFYEGVCKERLHLQGQNMQDPFGEKRGRFDYQGLLTRLRAIQRRLREKCPPEDNDGDSDSDTSSSGTDP... | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. May be involved in apoptosis regulation.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-co... |
Q9H832 | MAESPTEEAATAGAGAAGPGASSVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLI... | Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cystei... |
Q3UE37 | MAESPTEEAATATAGAGAAGPGSSGVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLG... | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquit... |
Q66KB0 | MAESPAAEAIILPGAAAGGGVLPHLSGLQAPGTSPLTTSSVWDPTASADWDNERASNQCVLRIKRDIMSIYKEPPPGMFVVPDPHDMTKIHALITGPFDTPYEGGFFLFLFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSLSSVLISIQSLMTENPYHNEPGFEQERHSGDSKNYNECIRHETIRVAVCEMLEGKCQCPDALRSVMEKSFMEYYDFYEAVCKDRFHLQGQNMQDPFGEKRGHFDYQSLLSRLQTIHQRVREKHRKETVDIDSDSSSSETETDTQGSSNP | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. May be involved in apoptosis regulation.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-co... |
Q05086 | MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAA... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates . Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the... |
Q1JQA1 | MAAVAAEARVFLEVRRRLQSALLILGDSKEGGLPMAVSVTPSSLRMQSPGGCTELRLPAGVRLAPSTCRGLQHVPGDGLHLRLHARAESRPELISVFNQSSQDQECCTFYCQSCGEVIIRDRMLLRVLPLPGDNWGALVDEWCCHPDPFANKPLHPRENDCFTGDCFYLVNLKSDLWQPRPEGAPVETHHLSSENHLKLKPKANTKVICKRCKVMLGETVSSETTKFYMTEIIILPSERNFPIIPRSQFVQSVLAQCVVELSSARSTFRFTIQGHDDKVYILLWLLNSDSLVIESLGQYTNIKKFPVLEDVLKPDSNSAC... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugati... |
Q7Z6J8 | MAASAAETRVFLEVRGQLQSALLILGEPKEGGMPMNISIMPSSLQMKTPEGCTEIQLPAEVRLVPSSCRGLQFVVGDGLHLRLQTQAKLGTKLISMFNQSSQTQECCTFYCQSCGEVIIKDRKLLRVLPLPSENWGALVGEWCCHPDPFANKSLHPQENDCFIGDSFFLVNLRTSLWQQRPELSPVEMCCVSSDNHCKLEPKANTKVICKRCKVMLGETVSSETTKFYMTEIIIQSSERSFPIIPRSWFVQSVIAQCLVQLSSARSTFRFTIQGQDDKVYILLWLLNSDSLVIESLRNSKYIKKFPLLENTFKADSSSAW... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugati... |
A8GKB7 | MEGSVNQSKWQAYSHLMRINKPIGTLLLLWPTLWALWLAGKGVPSLSILVVFVVGVFLMRAAGCVVNDYADRAVDGHVKRTAARPMPSGRVSEKEAKVLFVVLVLVSFGLVLTLNAMTIWLSLAALALAWAYPFMKRVTHLPQFVLGAAFGWGIPMAYAAVSESLPLSCWLLLLANICWTVAYDTLYAMVDRDDDLKIGIKSTAILFGRYDKLIVGLLQFATLLLMLWVGYLTQMSGAFYWSLLLAGALFIHQQKQIATRERDACFKAFMDNNYVGLVLFIGIALSYWQG | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q12S01 | MTAQTQQSIMAKLALYAQLSRIDRPIGTLLLLWPCLMALLFAAKGMPDIKVLLIFILGVVIMRACGCIINDYADRNLDAHVERTKQRPLASGAISSKEALSLFALLGLLAFALVLLLNPLVVKLSVVGIVLTIMYPFMKRVTNMPQMFLGIVWSWSIPMAYAAQLGEVPVEAWWLFAANWCWTVAYDTMYAMIDRDDDLKVGIKSSAILFGRFDRQWIAVFQLMAFGCFLMAGLSAEREFIYALGLLGFIAFSVYQQRLIFSRERPACFKAFLNNNWVGMLLFLTLAADYLLY | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q3JJ81 | MNTSSGWSRQPPASLSELEIHWLFAPGSLTERLSALGEYSLEPVDQRHAAACAADASLLGVEPDSPIWVREVVMRLDAQPCVTARSIASAHALETQWKPLTGYGSLPLGHILYDDPAIVRAPFECALLMPDDPLDAISRRYARAAAPPRARRSAFVRNGATLVVSECFLPQFWSGFAQARLAGA | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19954
Sequence Length: 184
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q1I4M5 | MDNLWTSLPLPGLSDDQRHWLFAPGSLTLRLKALGRFSLEVTQQRIDFPEPGEAHALGCTTDSPAWIREVALKIDDQVMVCARSLTPMRERRPAWPELAGYGGEPLGSMLYNTPDIHRGAFECQRPQADDPLSRLATSLGQPSGKLLARRSRFLRDGQPLLIAECFVEGFWALLQERSAPLKLAI | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20648
Sequence Length: 185
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q3KIF2 | MDTSHYWSSRPLSELTGSEHHWLFLPGALTPRLKAMGDYSIEVVEQSHGPLNPEEAQALNVSPNTIGWVREVVMKLDGEACVTARSLTSVPALNGDWADLNGYGRRPLAEILYTSEQTLREPFQCALLPPGAPLAALSYRYAPQAERLLARRSRFTRNGSALLVSECFLPAFWARVEYAQALKSA | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20500
Sequence Length: 185
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q3JUM4 | MRFDAADAHWRETPRPGASSAQKDWLTRGGSLTAHLARLGRVTVRVTRETVAAPWADEHRALSCASRAPVWVREVVLAVDGAPFVAAHSIAPLAASKGVWQAMRRLRTRPLAELLYSDPEVTRSALVSRRVLAGHPLFSLASLALARAYATEHAFAARRSVFERRGTPLMVTECMLPALWRHLDAHGERRARGLEQT | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 21770
Sequence Length: 197
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q6F9N7 | MQKIQSNQIQEQDLTPELKKWLYASGSLTQQLTDLADGLFTVEPIQEKYQRMSFMDSRWMRMPAYHVAWVRESLLYGCEQQPWVKAKSIFPVLSLQKKARIFKHIGKKPIGRFLFQRTTPLCERRVIRLEEGWTRQSCYTWHGCKFIVQETFLASFEQYIQHHSHSI | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19927
Sequence Length: 167
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
A0KEP8 | MKSELTVPLARLVPWQTPAQCEPPEALLPWLLEADSMTRRLRRHNRHFSVQLFGNRSVALDADEQQLVVAEQPMGLCREVILHGDHGPAVLGWTLFAEAALQESGLRELGEQPLGERIFGDEPARRDHLQLACFEIASNPWCPAGTVWGRRSRLFLGQWPLLVHELFLPSLSCNKELE | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20132
Sequence Length: 178
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q21U27 | MKVWSKRNVQRGNRKRWVGATGSLSARLAAAGQRFSVQVLSQGLQALDPDEASALGLSRLKVGYVREVLLRVDEVAVVFARSVTAHPHSQGPWRSIRGLGTRPLADVLFGQHGIARTPLQFASLQVASSLHRHVAHAWLGATGAALASRVLPARRSVFTRGAAPLLVMEVFAAPHAPWGWLTTKTRRGPPALPRTKP | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 21319
Sequence Length: 197
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q0VTA8 | MLPAALHPDSLWRPLEQLVLPPIIRDWMADPDSLTRRLKRYGHFSVVPGLHAIALPRADERRLLSLPVRRAALIREVTLHLDDTPVVAARSVLPLTSLAGANRSLGHMGSRSLGLELYNRPICQRDQVWARLASTDQHHSLCWGRQSRFIKRGAPLLVAEYFLPALWEKLHVARCVQASWLHDKAYLYASIRGEPTDAVRLSRF | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 23167
Sequence Length: 204
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q5E206 | MSDINSWCASVLKRVQWQEADTFECSNDLQRYWLLGLDSLSRRLEQHCNVLSVSVLDNTHVNPDKLTVEEEALLSGEVCLRRKVILKGDQQSWVYGRTLIPLSSLQDQPHDLTRQGHTPLGITVFSAQSAHRDKLQVGTIMTERGELFARRSRLWMNNKPMLVAELFLPEAPIYSKEVES | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20606
Sequence Length: 180
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q9ZCP3 | MYNTNFGFKKVDYTKKQWLINNIFSRVADKYDLMNDLMSIGLHRLWKDEFIMQIPNLNSNILDVASGSGDIALKLAKKAKDRGNNISLILSDINEEMLNNAKKKSIDLNLFQNIKFIVANAEELPFSDNSFDYYTIAFGIRNVPDINKALKEAYRVLKPMGKFVCLEFSKVKEGILKDFYKFYSFNIIPSIGQIIAGNKEAYEYLVESIALFPSQDDFRIMIKESGFEEVHYKNLSGGIVAIHSAYKI | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
Q9JPD1 | MNEPTPLSRSFGYQSVDEREREQRIRRVFSAVAARYDLMNDLMSFGIHRLWKRRFVRMAAPQAGQHIVDLAGGTGDVAALMAAADRRVTVVDPSAEMMAVGQARGHAHVDWQVGSAEQLPLADASVDTLTISFGIRNATRIDVALREIHRVLKPGGRFLCLEFSTPAWWLRPFYNLFSFTVIPRLGAWIANSPEAYTYLVESIRRFPDQRGFAAMISAAGFESVRWHDLSFGIACVHVGTRAAAATPAGTA | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
Q1GC56 | MTEKSDSTTHFGFETVPEHEKAGRVQGVFNSVASKYDIMNDVMSVGIHRIWKDAMMDWLAPRPGQRLLDVAGGTGDISFRFLKRAGHGHSTVLDLTTPMLEEGRKRAEAEQMAECLDWVTGDAMALPFKDNTFDVYTISFGIRNVTRPQEALNEAYRVLKPGGRLMVLEFSQLPNDGLQKLYDLYSFNVIPRMGQMIAGDYDSYQYLVESIRNFPDQETFLGMVKSAGFENAKHRNLSMGIAALHSGWKI | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
Q21H69 | MSDEQTTHFGYEKVDVKDKARRVAGVFHSVAAKYDIMNDVMSGGIHRIWKQFTIELSGVRSGHKVLDIAGGTGDLTKKFSRIVGPTGQVVLADINESMLNVGRDKLIDSGVAGNVVYTQADAQYLPFPDNTFDCITIAFGLRNVTDKDLAIASMLRVLKPGGRLLILEFTKPQNALVEKAYDFYSFKILPTMGQIIAQDADSYRYLAESIRMHPDQETLKGMMDAAGFAQTKYHNMTGGIVALHTGIKP | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
B8F4B1 | MNNIDQQEVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDKTNGLFGKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNICYQQITVEDFLKQHCITDTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKAYMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCNYIAVLQNS | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26863
Sequence Length: 236
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q31GD8 | MSQADLNKHKNADPSELNNFNQLANTWWDESGEFGALHKINPLRIEFIKQFQSIENKTILDVGCGGGILSESLAKAGGNVTGIDLAEDVLTIARLHSLDTETKVNYHLISAEDHAQTHEEEYDIVTCMEMLEHVPDPASIIHAAAKAVKPGGWVFFSTLNRNYKSYLLAIFAAEQVLNLVPKGTHTHDKFIQPSELDAMARQAGLFLKEGAGIDFNPLLKRYRLTDRLDVNYLLAYQKSAV | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26834
Sequence Length: 241
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q2W6W0 | MELKFMDHVGTASPEEIARFTAMAEAWWDPQGKFKPLHRFNPVRLAFMRRHFAAHFGRDESLMRPFEGLTLLDVGSGGGLLSEPLARMGFAVTGIDAGDKNVAVARLHAEQTGVPVDYRVSTPEQLDPNEAFDVVLSMEVVEHVPDVSAFLGHATARLKPGGVFMGATLNRTAKAWALAVVGAEYVLGWLPKGTHDWNKFVRPSEFAAMLRDRGITVRQMAGMAFNPLSDTWRETDNLDVNYMLFGVKG | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27531
Sequence Length: 249
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q9YBF0 | MSCRPSSVSIAVTGSSGVRVALRLLEALKGEVEIRGIILTRGAEEVARYEEGIEPEDLRRLLRSYAPLYMENDMSSPLASSSNQPDAMAIVPASMKTVGLIARGIPSSLPARAALAVLRLGRRLVVAPRETPLGVVELENMLAIARMGGIVVPLTLSFYIKPSSVEDLVDFAAGKVLDALGVKVDVYRRWRGPEEGD | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
P94300 | MSERIEKIMTVGITGASGGMYGVRLTQELLRQEYKVHLVLTEAAWQVFKEELLLDTTDRQKVIHELFGDLPGELHTHDLHDYAAPIASGSYRSAGMVIIPCSMGTLSGMAHGASGNLLERTADVMLKEKRKLVIVPRETPLHDIHLENMLKLSKMGATILPAMPGYYHLPKTIDDLINFLVGKALDSLGVEHTLFTRWGE | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
O66811 | MQKIALCITGASGVIYGIKLLQVLEELDFSVDLVISRNAKVVLKEEHSLTFEEVLKGLKNVRIHEENDFTSPLASGSRLVHYRGVYVVPCSTNTLSCIANGINKNLIHRVGEVALKERVPLVLLVREAPYNEIHLENMLKITRMGGVVVPASPAFYHKPQSIDDMINFVVGKLLDVLRIEHNLYKRWRG | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
O29054 | MRFVVALTGASGQILGIRLIEKLTELGAEVYAVASRAAKITLKAETDYDEGYVREIATKYYDEDEIAAPFASGSFRHDGMAVVPCSIKTASSIAYGIADNLIARAADVTLKEKRRLVLAIREAPLHSGHLKTLARLAEMGAVIFPPVLSFYTRPKSVDDLIEHTVSRIAEQLGVEVDYRRWG | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
Q9PPF1 | MKVLLGISGSSSVNLGLKLLKNLENQCELYCILTQGAKLNFKTENQANLEEICQENFKYTHFLDDKNLSLSVASGSFGIEKTIIAPCSISSLAKIHAGFADTLLMRAAAVALKERKKLILGVREMPFSTLNLEHMLKLSQMGVIIAPPIIASYSKANNLEQMENFIAGKWLDLLEIKHNLYEKWQNF | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
Q9SB51 | MLLVLDLGISSLVLVVSLVLPLIGLFVRHKWRVAAQRREEIRRLLIHASEEAARAELEASVEFSSVAVSNVFHCPVCYCLATTRCSRCKAVRYCSGKCQIIHWRQGHKDECHPASIVYDSEDESDSDLRLGEENGQNTPEETLLVGPEPVTIPIGESLLSNRARSPEDGNGDIADNKDDLIDKEEAVSVAETSGSSFSGFSSSPRNDSGDEISRCESFSSSESERSESLLDAHVSVEPEDTCFSTIEDAPSKLLSPKFVHLVESVDNLANLPKLSVHKPEDDAGQNQSQSRSLHSLVTDRHPVSADPSLKSSDFWGTALG... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Involved in salt tolerance by modulating sodium transport activity and repressing cell death at least partially through modulating S... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.