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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.
Subcellular Location: Secreted
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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 presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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
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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 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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 neurons and is more resistant to proteases. The epimerization is done by the venom peptide isomerase heterodimer.
Sequence Mass (Da): 9167
Sequence Length: 83
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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
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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
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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
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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
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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
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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
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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
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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 not show toxicity when intraperitoneally injected into mouse .
Sequence Mass (Da): 8006
Sequence Length: 73
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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.
Subcellular Location: Secreted
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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.
Subcellular Location: Secreted
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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
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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 within the domain II S1-S2 loop. In vivo, paralyzes lepidopteran and dipteran larvae. Paralyzed insects ultimately die from secondary effects of starvation and dehydration .
Sequence Mass (Da): 10672
Sequence Length: 94
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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
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B6DD61 | MFSTSDQVSKMNSRILSALLILGIATCVIAGGFCPKSRHPQCNLSYKINDCCAQSDCRVGSVCCVEGCGNVCRAESDTPLGEKFVDGSECKHGHVFPKKWYQFWWRV | Function: Has antibacterial activity.
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 11842
Sequence Length: 107
Subcellular Location: Secreted
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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 knottin.
Subcellular Location: Secreted
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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
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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 Mass (Da): 6739
Sequence Length: 59
Subcellular Location: Cell membrane
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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 disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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(50)=51-95 nM), and Nav1.8/SCN10A) as well as the nociceptor cation channel TRPA1 (IC(50)=389 nM) (By similarity) . Acts as a potent and selective blocker of voltage-gated calcium channel Cav3.1/CACNA1G, but not of Cav3.2/CACNA1H, and Cav3.3/CACNA1I (By similarity). On Nav1.7/SCN9A, primarily interacts with the DII and DIV voltage-sensor domains . Also acts as an inhibitor of nociceptor cation channel TRPA1 (IC(50)~389 nM) by binding to the S1-S4 gating domain of TRPA1 (By similarity). It shows moderate affinity for lipid bilayers (By similarity).
PTM: An unnatural amidation at Ser-35 provokes a 14-fold increased toxin ability to inhibit Nav1.2/SCN2A and a ~2-fold decreased toxin ability to inhibit both Nav1.5/SCN5A and Nav1.7/SCN9A.
Sequence Mass (Da): 3994
Sequence Length: 35
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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 composed of 2 domains: a highly rigid N-terminal inhibitor cystine knot (knottin) domain and a rather flexible C-terminal linear cationic cytotoxin domain that forms amphiphilic alpha-helices.
Subcellular Location: Secreted
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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/SCN2A (IC(50)=40-540 nM), Nav1.3/SCN3A (IC(50)=102 nM), Nav1.4/SCN4A (IC(50)=30-39 nM), Nav1.5/SCN5A (IC(50)=19-90 nM), Nav1.6/SCN8A (IC(50)=26 nM), and Nav1.8/SCN10A (IC(50)=146 nM)) . For inhibition of inactivation, it is 20-fold more potent in inhibiting inactivation on Nav1.7/SCN9A (IC(50)=250 nM) than other channels (about 4.6 uM for all channels) . It also weakly inhibits Cav1.2/CACNA1C and Cav3.2/CACNA1H (29% block at 1 uM) . It inhibits Nav1.7/SCN9A activation by interacting with DII and impairs Nav1.7/SCN9A inactivation by interacting with DIV . It docks on top of the DII S3 helix Nav1.7/SCN9A . It is about 60-fold less active on Nav1.7/SCN9A at depolarized potential (0 mV; IC(50)=15 nM), compared to -120 mV potential (IC(50)=0.26 nM) . This toxin binds to lipid membrane . This ability correlates with hNav1.7/SCN9A inhibition, showing that membrane binding is the first step in the inhibitory mechanism of this toxin . It inhibits Nav1.2/SCN2A less potently when it is coexpressed with SCN2B or SCN4B than when it is expressed alone, showing that beta subunits (SCN2B and SCN4B) have a protective effect .
Sequence Mass (Da): 3833
Sequence Length: 30
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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-amino-3,6-dideoxy-alpha-D-glucose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-mycaminose + 2 H(+) + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 27428
Sequence Length: 255
Domain: His-123 is a strong candicate for an active site that hydrogen bonds to a water molecule which in turn hydrogen bonds to the C-3' amino group. However, it is not conserved in related S.venezuelae DesVI methyltransferase and its mutagenesis does not completely abolish catalytic activity .
Pathway: Antibiotic biosynthesis; tylosin biosynthesis.
EC: 2.1.1.235
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O70023 | MRIALLTMGSRGDVQPFVALGTGLRARGHEVVLGAPEALRPLVEQAGLEYRATPGDPDGFFTMPEVVETLRRGPAMRDLMKALPPAPEEYDQEVLDRIERAGEGVDLVVHAPLTVTTALGEPSTPWLSVNWWPNTSTWTFPAVESGQRRMGPLTPLYNRLTHWRAEREDWGWRRAEVNEFRGRRGLPPFGKSSPLRRLGHPRPHLYPFSPSVLPKPRDWPGQCHVTGYWFWDQPGWRPSPELEDFLADGEPPVLLTLGSTWPVHRQEEMVEYAVAAARGARRRLLLVGGPEGALPGDALRVPSADYSWLMPRTAAVVHHGGFGTTADAVRAGVPQVLVPVFADHPFWAARLRRMGTAARPVPLARMNREALAASVRTAVTDPAMAVRARRLGEAVAAERGVENACVLIEEWAETRTTAHTPG | 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 + dTDP-6-deoxy-alpha-D-allose = demethyllactenocin + dTDP + H(+)
Sequence Mass (Da): 46635
Sequence Length: 422
EC: 2.4.1.317
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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 receptors which leads to activation of additional tyrosine kinases and subsequent cell activation . Also has an inhibitory role in some cells . Non-covalently associates with activating receptors of the CD300 family to mediate cell activation . Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor . Associates with natural killer (NK) cell receptors such as KIR2DS2 and the KLRD1/KLRC2 heterodimer to mediate NK cell activation . Also enhances trafficking and cell surface expression of NK cell receptors KIR2DS1, KIR2DS2 and KIR2DS4 and ensures their stability at the cell surface . Associates with SIRPB1 to mediate activation of myeloid cells such as monocytes and dendritic cells . Associates with TREM1 to mediate activation of neutrophils and monocytes . Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival . Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages . Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines . In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability (By similarity). Negatively regulates B cell proliferation . Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity).
PTM: Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12179
Sequence Length: 113
Subcellular Location: Cell membrane
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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 associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity).
PTM: Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12131
Sequence Length: 113
Subcellular Location: Cell membrane
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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 receptors which leads to activation of additional tyrosine kinases and subsequent cell activation . Also has an inhibitory role in some cells . Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family . Required for neutrophil activation mediated by integrin . Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Also associates non-covalently with the NK cell receptors KLRA4/LY49D and KLRA8/LY49H which leads to NK cell activation . Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages . Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) which is produced by TREM2 ectodomain shedding (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons . Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development . Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons . Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability . Negatively regulates B cell proliferation . Required for CSF1-mediated osteoclast cytoskeletal organization . Positively regulates multinucleation during osteoclast development .
PTM: Tyrosine phosphorylated . Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12367
Sequence Length: 114
Subcellular Location: Cell membrane
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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 associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity).
PTM: Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 11617
Sequence Length: 108
Subcellular Location: Cell membrane
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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
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Q2T9J0 | MRRQWGSAMRAAEQAGCMVSASRAGQPEAGPWSCSGVILSRSPGLVLCHGGIFVPFLRAGSEVLTAAGAVFLPGDSCRDDLRLHVQWAPTAAGPGGGAERGRPGLCTPQCASLEPGPPAPSRGRPLQPRLPAELLLLLSCPAFWAHFARLFGDEAAEQWRFSSAARDDEVSEDEEADQLRALGWFALLGVRLGQEEVEEERGPAMAVSPLGAVPKGAPLLVCGSPFGAFCPDIFLNTLSCGVLSNVAGPLLLTDARCLPGTEGGGVFTARPAGALVALVVAPLCWKAGEWVGFTLLCAAAPLFRAARDALHRLPHSTAALAALLPPEVGVPWGLPLRDSGPLWAAAAVLVECGTVWGSGVAVAPRLVVTCRHVSPREAARVLVRSTTPKSVAIWGRVVFATQETCPYDIAVVSLEEDLDDVPIPVPAEHFHEGEAVSVVGFGVFGQSCGPSVTSGILSAVVQVNGTPVMLQTTCAVHSGSSGGPLFSNHSGNLLGIITSNTRDNNTGATYPHLNFSIPITVLQPALQQYSQTQDLGGLRELDRAAEPVRVVWRLQRPLAEAPRSKL | 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-terminal 15-kDa fragment and C-terminal 45-kDa fragment upon import into the peroxisomes. The full-lengh TYSND1 is the active the proteolytic processing of PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-cleavage of TYSND1 down-regulates its protease activity.
Sequence Mass (Da): 59309
Sequence Length: 566
Subcellular Location: Peroxisome
EC: 3.4.21.-
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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 intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 32807
Sequence Length: 279
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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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 intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 30538
Sequence Length: 264
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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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 intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 31978
Sequence Length: 279
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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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
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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 intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 36580
Sequence Length: 316
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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Q6R6M4 | MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ | 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 deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors RIGI and IFIH1 stimulates the cellular response to viral infection.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 59619
Sequence Length: 530
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q6QN14 | MEDDSLYLRGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGSED | 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 apoptosis.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 44690
Sequence Length: 398
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q8VXY9 | MESLKRFLCSIALLLISLLLPSSLAQQQQHESIRTMEDFSGYPIHEPGQFGSINLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKRSLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLELHIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAGLAAAELALAVEKHVLESESIDTVGTVGILELHPGAINSIPSKSHLEIDTRDIDEARRNTVIKKIQESANTIAKKRKVKLSEFKIVNQDPPALSDKLVIKKMAEAATELNLSHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEYSSPEDMANGVKVLSLTLAKLSLD | 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 breakdown without the intermediate generation of urea.
Catalytic Activity: (S)-ureidoglycolate + 2 H(+) + H2O = CO2 + glyoxylate + 2 NH4(+)
Sequence Mass (Da): 51487
Sequence Length: 476
Pathway: Nitrogen metabolism; (S)-allantoin degradation; glyoxylate from (S)-ureidoglycolate: step 1/1.
Subcellular Location: Endoplasmic reticulum
EC: 3.5.1.116
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Q940S3 | MIEPSMERENGALTAATTTTTAVTSPPPMASSPRQALVERLKDYGQEDIFSLWDELSPDEKDFLVRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENWVSTVDGRTMEDREKWWKMGLKTIYEGKLGVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQIQAERILCVQRLAAQVVSEGPIRPVTIHWYIMTSPFTDEATRKYFSSHKYFGLEPDQISFFQQGTLPCVTKDGKFIMETPFSLAKAPDGNGGVYAALKCSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKGAASAAKVVRKAYPQEQVGVFVRRGKGGPLTVVEYSELDQSMASAINQRTGRLQYCWSNVCLHMFTLDFLNQVATGLEKDSVYHLAEKKIPSMNGYTMGLKLEQFIFDSFPYAPSTALFEVLREEEFAPVKNVNGSNFDTPESARLLVLRLHTRWVIAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCEISL | 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 embryo development .
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 55992
Sequence Length: 505
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
EC: 2.7.7.23
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Q18493 | MTITAPPKDEIISKFPGSEPLLNFYNELSDAEKSKLFHQISTLNLSEAHQWFIDSADQRAPSTAEDLKPVLDSQHFVQAELHQVILDGLWNKGMDAIGRGEVCAIVLAGGQATRLGSSQPKGTIPLGINASFGDSLLGIQAAKIALLQALAGEREHQNPGKIHWAVMTSPGTEEATREHVKKLAAHHGFDFDEQITIFSQDEIAAYDEQGNFLLGTKGSVVAAPNGNGGLYSAISAHLPRLRAKGIKYFHVYCVDNILCKVADPHFIGFAISNEADVATKCVPKQKGELVGSVCLDRGLPRVVEYSELGAELAEQKTPDGKYLFGAGSIANHFFTMDFMDRVCSPSSRLPYHRAHKKISYVNEQGTIVKPEKPNGIKLEQFIFDVFELSKRFFIWEVARNEEFSPLKNAQSVGTDCLSTCQRDLSNVNKLWLERVQAKVTATEKPIYLKTIVSYNGENLQELRHREISDSALESDHSINKFFVV | 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-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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O74933 | MTVKSQQQIIDSFKQANQDQLFQYYDSLTIDQQQEFIDQLSTIEEPAKLISTVEQAIQFSQTNSTSRNFTQLPNEQTASTLDLSKDILQNWTELGLKAIGNGEVAVLLMAGGQGTRLGSSAPKGCFNIELPSQKSLFQIQAEKILKIEQLAQQYLKSTKKPIINWYIMTSGPTRNATESFFIENNYFGLNSHQVIFFNQGTLPCFNLQGNKILLESKNSICQSPDGNGGLYKALKDNGILDDLNSKGIKHIHMYCVDNCLVKVADPIFIGFAIAKKFDLATKVVRKRDANESVGLIVLDQDNQKPCVIEYSEISQELANKKDPQDSSKLFLRAANIVNHYYSVEFLNKMIPKWISSQKYLPFHIAKKKIPSLNLENGEFYKPTEPNGIKLEQFIFDVFPSVELNKFGCLEVDRLDEFSPLKNADGAKNDTPTTCRNHYLERSSKWVIQNGGVIDNQGLVEVDSKTSYGGEGLEFVNGKHFKNGDII | 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-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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Q54GN5 | MDTTNFEDIRNEWIEQGQGHVFNWFDKLSNEEKLNFENDIRKINVKEVNKDYKNVLLNKDEQKIMKYEHFENVMTLNKIKEQDKKKWEDIGYELISKGEVAVLLLAGGQATRLGTTFPKGFYDVGLPSKKSLFQLQAERIYRLQQLVSERYNGSYDQDSKPIQWYIMTSEATHSETIKFFENKNYFGLKKSAFFFFSQAMIPCITPEDGKIISESGSKLSLSPNGNGGLFKALSTSGAIDDMRKKGIKYVTQYCVDNILINMADPVFVGYMHDQSADCGAKVVSKSDPKEPVGVMALNGDGKPFVLEYSEIDEQSKFKKDQNGQLVFNYAHICINAFSFDFLDRIAKNHLDHLKYHVAFKKIPSAHPISGERQSPSSPNGWKLEKFIFDVFPFSKKMVCLEIERSKEFSPLKNCGGMNLPDSPETCLRDISNLHKSFIENSGGKIDSSNSTICEVSPLVSLNGENLKNFVNDKTFILPIEINQNLNN | 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-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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Q8SQS1 | MGYISMNSTNLIRPYEGTELNDAGRKYKKIGERLLREKKLGVVILSGGQGTRLGSDEPKGLFKIKGKTLFEWHMETIKELISKYNADIAVFIMTSSFTDEAVRKYFQSTDFGLKIQFFKQRNSLCVGTDGKPLEWYDGHAESPYGNGDIFNAIQQVNLEGIEALNVICIDNVLAKILDPVFVGAFYSDDYDILSKSVTKEEKESVGAFLMDERLKIKEYSENDAKGEGIQGNICNHIFKTSFIKKMKNINLPEHKAFKKIPYTISGKLIKPVKPNGFKKETFIFDSFEYTQKNGVMNVPREKEFSPLKNGMDSSVDNPVTCTIAVERHRIKTTIQ | 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-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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Q16222 | MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI | 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 + UDP-N-acetyl-alpha-D-galactosamine
Sequence Mass (Da): 58769
Sequence Length: 522
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
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Q91YN5 | MNVNDLKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEFDRSSHQEKVDARMEPVPRQVLGSATRDQEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGYFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSEAITADVNHNLKDANDVPIQCEISPLISYAGEGLEGYVADKEFHAPLIIDENGVHELVKNGI | 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 = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
Sequence Mass (Da): 58609
Sequence Length: 522
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
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O94617 | MDDKELFDRSIFEETNQLHLYDQLNYLKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPLSIVDTSDSSWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFPDQEASISIPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEACKATENVDGHKHLLLRAANIAYHYFSFDFLQKASLHSSTLPIHLACKKIPFYDVTSHHYTTPLNPNGYKLESFIFDLFPSVSVENFGCFQVPRRTSFSPLKNSSKSPNDNHETCVNDILSLGKSWILKNGGILSPSDCTYVSPECSLQGESLEWIKGKQVSNCKLY | 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-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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P43123 | MTDTKQLFIEAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTGKYTKPTEPNGIKLEQFIFDVFDTVPLNKFGCLEVDRCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVLVEVSSKLSYAGENLSQFKGKVFDRSGIVLEK | 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 + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 53476
Sequence Length: 477
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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O64765 | MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFVRRGKGGPLTVVEYTELDQSMASATNQQTGRLQYCWSNVCLHMFTLDFLNQVANGLEKDSVYHLAEKKIPSINGDIVGLKLEQFIFDCFPYAPSTALFEVLREEEFAPVKNANGSNYDTPESARLLVLRLHTRWVIAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCEISL | 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 .
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Mass (Da): 55760
Sequence Length: 502
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.23
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Q07307 | MDNSIHSTDGPDSVIPNSNPKKTVRQRVRLLARHLTTREGLIGDYDYGFLFRPELPFMKKDPRAPPFFGLNEKIPVLLAFILGLQHALAMLAGVVTPPLIISSSLSLPSDLQQYLVSTSLIVCGLLSMVQITRFHIYKTPYYIGSGVLSVMGVSFSIISVASGAFNQMYSNGFCQLDEAGNRLPCPEAYGALIGTSACCALVEILLAFVPPKVIQKIFPPIVTGPTVMLIGISLIGTGFKDWAGGSACMDDGMLCPSATAPRPLPWGSPEFIGLGFLVFVSIILCERFGAPIMKSCSVVIGLLVGCIVAAACGYFSHADIDAAPAASFIWVKTFPLSVYGPMVLPIIAVFIICACECIGDVTATCDVSRLEVRGGTFESRIQGAVLADGINSVVAALATMTPMTTFAQNNGVIALTRCANRWAGYCCCLILIVAGIFAKFAAAIVAIPNSVMGGMKTFLFASVVISGQAIVAKAPFTRRNRFILTASMALGYGATLVPTWFGNVFPQTENRDLEGFENAIELVLETGFAVTAFVAMLLNAIMPAEVEEIGAVTPMPVSAHDNRDGEAEYQSKQA | 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: Cell membrane
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Q9GZZ9 | MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELVSEVSEEELKNFSGPVPDLPEGITVAYTIPKKQEDSVTELTVEDSGESLEDLMAKMKNM | 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-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer . Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding . Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism . Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress . Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes (By similarity).
Sequence Mass (Da): 44863
Sequence Length: 404
Domain: The UFM1-interacting sequence (UIS) motif mediates interaction with both UFM1 and LC3/GABARAP proteins (GABARAP, GABARAPL1 and GABARAPL2).
Subcellular Location: Cytoplasm
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Q8VE47 | MADSVERLRQRVEELEQELARERTRRSGGDGHCGRTRIQEMSDEVLDSNPYSRLMALKRMGIVSDYKKIRTYAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITTVEHFEHFMNRISNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTWMESGVSENAVSGHIQLMIPGESACFACAPPLVVASNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLKFGTVSFYLGYNAMQDFFPTMFMKPNPQCDDKNCRKQQEEYKKRAAALPTQEAEPQEEAEVVHEDNEWGIELVSEVSEEELKNSSGPVPTLPEGITVAYTVPKKTEDSASEVTVEDSGESLEDLMARMKNM | 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 via a trans-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer (By similarity). Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding (By similarity). Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism (By similarity). Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (By similarity). Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes .
Sequence Mass (Da): 44790
Sequence Length: 403
Domain: The UFM1-interacting sequence (UIS) motif mediates interaction with both UFM1 and LC3/GABARAP proteins (GABARAP, GABARAPL1 and GABARAPL2).
Subcellular Location: Cytoplasm
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Q8VY10 | MEMSLTDSDWDSSSDSGSSEHEEVEFSYGGRAQNIFSNLEETIGKIDEFLSFERGFMYGDIVRSATEPSGQSGRVINIDMFVNLESTHGKIMKEVDTKRLQKLRSISLSDYVINGPWVGRVDKIVERVSVTLDDGTNYEVLVDGQDKLVAIPPNLLEDSQYSYYPGQRVQVKLAHAPRSTTWLCGTWRGTQVMGTVCTVEAGLVYVDWVASIVMEGDRNLTAPQALQNPESLTLLPCVSHASWQLGDWCILPGSSHCDIAERQTPNVAAYNLNECHKTFQKGFNRNMQNSGLDELFVITKTKMKVAVMWQDGSCSLGVDSQQLLPVGAVNAHDFWPEQFVVEKETCNSKKWGVVKAVNAKEQTVKVQWTIQVEKEATGCVDEVMEEIVSAYELLEHPDFGFCFSDVVVKLLPEGKFDPNADTIVATEAKHLLTESDYSGAYFLSSIGVVTGFKNGSVKVKWANGSTSKVAPCEIWKMERSEYSNSSTVSSEGSVQDLSQKISQSDEASSNHQETGLVKLYSVGESCNENIPECSSFFLPKAAIGFITNLASSLFGYQGSTSVISSHSRCNDSEDQSDSEVLVQETAESYDNSETNSGEVDMTTTMVNIPIEGKGINKTLDSTLLENSRNQVRFRQFDMVNDCSDHHFLSSDKGLAQSQVTKSWVKKVQQEWSNLEANLPNTIYVRVCEERMDLLRAALVGAPGTPYHDGLFFFDIMLPPQYPHEPPMVHYHSGGMRLNPNLYESGRVCLSLLNTWSGSGTEVWNAGSSSILQLLLSFQALVLNEKPYFNEAGYDKQLGRAEGEKNSVSYNENAFLITCKSMISMLRKPPKHFEMLVKDHFTHRAQHVLAACKAYMEGVPVGSSANLQGNSTTNSTGFKIMLSKLYPKLLEAFSEIGVDCVQEIGPES | 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 by facilitating the degradation of PHT1 proteins at the endomembrane . Functions cooperatively with NLA to regulate the abundance of the inorganic phosphate (Pi) transporters PHT1-1, PHT1-2 and PHT1-3 in different subcellular compartments . Regulates Pi homeostasis by mediating, cooperatively with NLA, polyubiquitination of PHT1-4 and its targeting for degradation .
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 Mass (Da): 100484
Sequence Length: 907
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.2.23
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Q9LUQ5 | MEPNVVEIATPPAASCSRIRTPTKAETPEVIDVEEYDLQNGGVPNGNNVDYKNKGKAIDFDSMSYGDYGEEDEYAVGSPGDDYGYPESSPLSNSLLDPESLIYEDDENYSEQYDFEMEAEPDNYSMYQDLFDGKDIPTGVEVSMDWFPNSADKESASSSKSSHANNGNNSSKKATKASGIHSQFSSDMETPVAQPWNALPHKAEGVIPNSAYALPQNSKAFQPPYAVHYSALKTAFSNYLQPQTPDTVLGEAPAPAAGSSGLLPPNTPGFKSNAARFKEEPPILPPDDSRVKRNMEDYLGLYLFFKRFDIVEDFSDHHYASKGTTSKQHSKDWAKRIQDEWRILEKDLPEMIFVRAYESRMDLLRAVIIGAQGTPYHDGLFFFDIFFPDTYPSTPPIVHYHSGGLRINPNLYNCGKVCLSLLGTWSGNQREKWIPNTSTMLQVLVSIQGLILNQKPYFNEPGYERSAGSAHGESTSKAYSENTFILSLKTMVYTMRRPPKYFEDFAYGHFFSCAHDVLKACNAYRNGATPGYLVKGAPDVEENSAGMSSLKFRTDVATFVETVLLKEFILLGVLGLEPEEEEKTPETIIVAESSKCTRSRSKRDRVSSS | 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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 67769
Sequence Length: 609
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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Q93571 | MACLRKLKEDIQVLEKLFPKNHNRFQILSASVDELSMKFINAENKGIIVTANIQENYPRQPPIWFSESDDVPVIGMSLQRLTETEESTNILHQVHRLVSDLCSFYNLQMPCELPQIAPPVRDDIDEGRGSDISDTTSEPIDDDMAGDGEVDDDDEEEEDDEDADGDIEIVEMAEEDPTSQHDVGVSKEGLDMLDKVSKINRQQHLDGKVQGSITATDRLMKEIRDIHRSEHFKNGIYTFELEKEENLYQWWIKLHKVDEDSPLFEDMKKLKKDHNQDHLLFSFTFNEKFPCDPPFVRVVAPHINQGFVLGGGAICMELLTKQGWSSAYSIESCILQIAATLVKGRARISFDAKHTSTYSMARAQQSFKSLQQIHAKSGWYTPPKTEG | 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-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 44061
Sequence Length: 387
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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Q8GY87 | MEPDVVEIPPPPLIASGSRTRKPRKAVPEVIDVESYEFRNVGVVKDNNVVDKKNKGKAIQVDSFSFNNVQSHHHGSSLLNLETFQDYYGHKNIPFSEFANQPIDVDDYSMYQDVLDPKDVPAGAEVTVPWGLNSSSKGTAKSSISIMRSQSMKGYGTVSLATTNVPQLWDYTLPQQNQAIYSSVSFSAVQPQTPDVVMVTNPTPNPFSYDASASSSHPIAAEPISSVQDSSNARKLKEEFLRDFKRFDTVEDFSDHHYASKGKSSKQHSKNWVKKVQADWKILENDLPEAISVRACESRMDLLRAVIIGAEGTPYHDGLFFFDIQFPDTYPSVPPNVHYHSGGLRINPNLYNCGKVCLSLLGTWAGSAREKWLPNESTMLQLLVSIQALILNEKPYFNEPGYVQSAGTASGESKSKVYSENVFLLSLKTMVYSIRRPPQHFEEYVQNHYFVRSHDIVKACNAYKAGAPLGSMVKGGVQDLEEARQSGSKKFKTDVASFMQTVVDEFVKLGVKELAEKPEPPMSNANTENQSKKKTRKRSRSSR | 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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 60552
Sequence Length: 543
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 21254
Sequence Length: 192
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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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-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine.
Sequence Mass (Da): 20738
Sequence Length: 181
Domain: Both the N-terminal docking peptide and the catalytic core domain must bind the Uba3-Ula1 complex simultaneously for optimal transfer of Nedd8.
Pathway: Protein modification; protein neddylation.
EC: 2.3.2.34
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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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 17279
Sequence Length: 152
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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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 heterodimer on chromatin to activate E3-ubiquitin ligase activity of the heterodimer, and thus its DNA damage repair mechanisms . Required, cell autonomously, for death of the linker cell, a male-specific cell which guides the elongation of the gonad; perhaps acting as part of the ubiquitin proteasome system (UPS) and modulated by heat shock transcription factor hsf-1 .
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 Mass (Da): 16705
Sequence Length: 147
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.23
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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 formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation.
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 Mass (Da): 18847
Sequence Length: 169
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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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 Mass (Da): 16818
Sequence Length: 149
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
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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 misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway . In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate .
PTM: Autoubiquitinated at Met-1.
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 Mass (Da): 17331
Sequence Length: 151
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.23
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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 misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3 . After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway . In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate (By similarity).
PTM: Autoubiquitinated at Met-1.
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 Mass (Da): 17345
Sequence Length: 151
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.23
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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]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 17331
Sequence Length: 151
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.23
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Q6DG60 | MAHTITPAVESGLGVLTHAVSSTVPVAVLPSLPPGIGSGVPAGAGLLSQIHATSWDPTLSTDWDNEKASQQCILRIKRDIMSIYKEPPPGMFVVPDPHDMTKIHALITGPFDTPYEGGFFLFLFRCPPDYPIHPPRVKLITTGHNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETMRVAVCDMLEGKVSCPEALWSVMEKSFLEYYDFYEGVCKERLHLQGQNMQDPFGEKRGRFDYQGLLTRLRAIQRRLREKCPPEDNDGDSDSDTSSSGTDPDSQGSSQP | 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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 36451
Sequence Length: 328
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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Q9H832 | MAESPTEEAATAGAGAAGPGASSVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV | 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-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 38210
Sequence Length: 354
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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Q3UE37 | MAESPTEEAATATAGAGAAGPGSSGVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV | 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 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 38368
Sequence Length: 356
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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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-conjugating enzyme]-L-cysteine.
Sequence Mass (Da): 35077
Sequence Length: 313
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.23
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Q05086 | MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML | 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 PML tumor suppressor, and the cell cycle regulator CDKN1B . Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins . Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation . Acts as transcriptional coactivator of progesterone receptor PGR upon progesterone hormone activation . Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (By similarity). Required for synaptic remodeling in neurons by mediating ubiquitination and degradation of LAMTOR1, thereby limiting mTORC1 signaling and activity-dependent synaptic remodeling (By similarity). Synergizes with WBP2 in enhancing PGR activity .
PTM: Phosphorylation at Tyr-659 by ABL1 impairs E3 ligase activity and protects p53/TP53 from degradation in (HPV)-infected cells.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 100688
Sequence Length: 875
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.26
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Q1JQA1 | MAAVAAEARVFLEVRRRLQSALLILGDSKEGGLPMAVSVTPSSLRMQSPGGCTELRLPAGVRLAPSTCRGLQHVPGDGLHLRLHARAESRPELISVFNQSSQDQECCTFYCQSCGEVIIRDRMLLRVLPLPGDNWGALVDEWCCHPDPFANKPLHPRENDCFTGDCFYLVNLKSDLWQPRPEGAPVETHHLSSENHLKLKPKANTKVICKRCKVMLGETVSSETTKFYMTEIIILPSERNFPIIPRSQFVQSVLAQCVVELSSARSTFRFTIQGHDDKVYILLWLLNSDSLVIESLGQYTNIKKFPVLEDVLKPDSNSACNAVKVLYQPCIKSRNAELSSLWENDLSVHSLTLPSTTCLELLLILSKSNATLPPSLRCMNSFQVAFLKM | 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-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 43392
Sequence Length: 389
Domain: The C-terminal half (AA 188-389) is able to bind cyclin-B and shows a self-ubiquitination activity (mono-, poly, or multi-ubiquitination) in a HECT-like sequence dependent manner.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.26
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Q7Z6J8 | MAASAAETRVFLEVRGQLQSALLILGEPKEGGMPMNISIMPSSLQMKTPEGCTEIQLPAEVRLVPSSCRGLQFVVGDGLHLRLQTQAKLGTKLISMFNQSSQTQECCTFYCQSCGEVIIKDRKLLRVLPLPSENWGALVGEWCCHPDPFANKSLHPQENDCFIGDSFFLVNLRTSLWQQRPELSPVEMCCVSSDNHCKLEPKANTKVICKRCKVMLGETVSSETTKFYMTEIIIQSSERSFPIIPRSWFVQSVIAQCLVQLSSARSTFRFTIQGQDDKVYILLWLLNSDSLVIESLRNSKYIKKFPLLENTFKADSSSAWSAVKVLYQPCIKSRNEKLVSLWESDISVHPLTLPSATCLELLLILSKSNANLPSSLRRVNSFQVAFLKM | 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-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 43657
Sequence Length: 389
Domain: The C-terminal half (AA 188-389) is able to bind cyclin-B and shows a self-ubiquitination activity (mono-, poly, or multi-ubiquitination) in a HECT-like sequence dependent manner.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.26
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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-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32235
Sequence Length: 290
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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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-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33001
Sequence Length: 293
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.39
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.3.40
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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 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28434
Sequence Length: 248
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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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 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27792
Sequence Length: 251
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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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 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28152
Sequence Length: 250
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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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 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27407
Sequence Length: 249
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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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 biosynthesis.
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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 biosynthesis.
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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 biosynthesis.
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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.
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Mass (Da): 21185
Sequence Length: 197
EC: 2.5.1.129
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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.
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Mass (Da): 22233
Sequence Length: 200
EC: 2.5.1.129
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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.
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Mass (Da): 21256
Sequence Length: 189
EC: 2.5.1.129
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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.
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Mass (Da): 19968
Sequence Length: 182
EC: 2.5.1.129
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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.
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Mass (Da): 20890
Sequence Length: 187
EC: 2.5.1.129
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Q9SB51 | MLLVLDLGISSLVLVVSLVLPLIGLFVRHKWRVAAQRREEIRRLLIHASEEAARAELEASVEFSSVAVSNVFHCPVCYCLATTRCSRCKAVRYCSGKCQIIHWRQGHKDECHPASIVYDSEDESDSDLRLGEENGQNTPEETLLVGPEPVTIPIGESLLSNRARSPEDGNGDIADNKDDLIDKEEAVSVAETSGSSFSGFSSSPRNDSGDEISRCESFSSSESERSESLLDAHVSVEPEDTCFSTIEDAPSKLLSPKFVHLVESVDNLANLPKLSVHKPEDDAGQNQSQSRSLHSLVTDRHPVSADPSLKSSDFWGTALGSAERVSDSCVKSKSGRPGNSSLHFSFGSGSSRDTSAAKVSEQRSSILKEAPRGTGYISDGVNLRERNAKRFDEAEIALPISSSTDALSPLDSSNLSHVTLPKSKSASSENGSMLAPLKVGEVQLLASKASNTKKCADLMKHSPLGAKSVRVLDHQKQNGAVVQHINSLHGRSGLKASVLKVVDQWTRPKSENEMAGRHGHKGLFPYEVFAKLYTYKIEFQPCGLINVGNSCFANVVFQCLMFTPPLTTYFLQQFHSRACTKKEQCFTCGFEKLVVKAKEEKSPLSPNGLLSQLQNIGIFLGNGKEEDAHEFLRFVVDTMQSVCIKASEYDMTKSSKLEDTTLIGLTFGGYLRSKIKCMKCQVKSELREKMMDLTVEIDGDISTLDDALRRFTRTEILDGENKYRCGSCKSYERAKKKLKITEPPNVLTIALKRFQAGKFGKLNKLIRFPETLDLAPYVSGGSEKSHDYKLYGVIVHLDVMNAAFSGHYVCYIRNQNKWYKADDSTVVTSDVERILTKGAYMLFYARCTPTPPRLAVCTKTEASNKKSRVPLPKANEKSTISRSVSTSSPELSSNTPGGGRSGNIQSFYSSFQRLQKILEEDSASDSSSLFDSNSDECSCSTDSTSMDDFADFIFGDHQGRAHGQSETPSPTSSSSSSSPPFTRRSPLSRSSPETYGTSRHQLPLGGER | 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 SHM1 stability and activity . Involved in cadmium tolerance by interacting with HIPP27 and probably modulating its stability .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 110600
Sequence Length: 1008
Subcellular Location: Membrane
EC: 3.4.19.12
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