ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q91VM4 | MMCLECASAAAGGAEEEEADAERRRRRRGAQPGAGGSACCGARGVGGAGVVSADEEVQTLSGSVRRVPSGLPSIPSTPGCAAAAKGPSAPQPKPASLGRGRGAAAAILSLGNVLNYLDRYTVAGVLLDIQQHFGVKDRGAGLLQSVFICSFMVAAPIFGYLGDRFNRKVILSCGIFFWSAVTFSSSFIPQQYFWLLVLSRGLVGIGEASYSTIAPTIIGDLFTKNTRTLMLSVFYFAIPLGSGLGYITGSSVKQAAGDWHWALRVSPVLGMITGTLILILVPATKRGHADQLGGQLKARTSWLRDMKALIRNRSYVFSSL... | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate in the lymph, thereby playing a role in lymphocyte trafficking . S1P is a bioactive signaling molecule that regulates many physiological processes important for the deve... |
B0JZE1 | MCLESDGVGTVSNSQGCIPGAEERGLETLPGRMNPTSLDVKAVELESSSSKPDKAYNWKRASVAAAGILSVGNVLNYLDRYTVAGVLLDIQQHFEVKDSGAGLLQTVFICSFMVAAPIFGYLGDRFNRKVILSSGIFFWSAITFSSSFIPKKYFWLLVLSRGLVGIGEASYSTIAPTIIGDLFTKNTRTLMLSVFYFAIPLGSGLGYITGSSVKQVAGDWRWALRVSPVLGVITGTLLLIFVPTAKRGHAEQLKGSSWIRDMRGLIKNRSYVFSSLATSTVSFATGALGMWIPLYLYRAQVVQKSVEPCNIPPCSTKDSL... | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate.
Catalytic Activity: sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55447
Sequence L... |
F4IKF6 | MVTKEEDCLPPVTETTSRCYSTSSSTPLAELETVRSLEIVESSSSLSPVWLLVIFCIINLLNYMDRGAIASNGVNGSTRSCNDKGKCTLATGIQGHFNLSNFEDGVLSSSFMVGLLIASPIFASLAKRLIGVGLTVWTIAVLGCGSSFAFWFIVLCRMFVGVGEASFISLAAPFIDDNAPQEQKAAWLGLFYMCIPSGVALGYVYGGYVGKHFSWRYAFWGEAVLMAPFAVLGFLMKPLQLKGSETLKNNNRLQVDNEIEHDQFEVSIETSKSSYANAVFKSFTGFAKDMKVLYKEKVFVVNVLGYVSYNFVIGAYSYWG... | Function: Probable sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55667
Sequence Length: 510
Subcellular Location: Mitochondrion inner membrane
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Q6ZMD2 | MAGGMSAECPEPGPGGLQGQSPGPGRQCPPPITPTSWSLPPWRAYVAAAVLCYINLLNYMNWFIIAGVLLDIQEVFQISDNHAGLLQTVFVSCLLLSAPVFGYLGDRHSRKATMSFGILLWSGAGLSSSFISPRYSWLFFLSRGIVGTGSASYSTIAPTVLGDLFVRDQRTRVLAVFYIFIPVGSGLGYVLGSAVTMLTGNWRWALRVMPCLEAVALILLILLVPDPPRGAAETQGEGAVGGFRSSWCEDVRYLGKNWSFVWSTLGVTAMAFVTGALGFWAPKFLLEARVVHGLQPPCFQEPCSNPDSLIFGALTIMTGV... | Function: Sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54769
Sequence Length: 512
Subcellular Location: Membrane
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Q9D232 | MSTECLKPQTGGPQSQSLSQGGQYGALASGTCLPPSTPVPWSLPRWRAYLAAAVLCYINLLNYMNWFIIPGVLLDVQKYFHISDSHAGLLQTVFISCLLVSAPVFGYLGDRYNRKAILSFGILLWSGAGLSSSFISYQYSWLFFLSRGFVGTGAASYSTIAPTVLGDLFVKDQRTCALAVFYIFIPVGSGLGYVLGSTVAELTGNWRWALRLMPCLDAMALALLILLVPDVPRGAAEKQGEVAVRAPRSSWCEDVRYLGRNWSFVFSTLGVTAIAFVTGALGFWAPKFLFEARVVHGLQLPCFQEQCHSQDSLIFGALTV... | Function: Sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55456
Sequence Length: 514
Subcellular Location: Membrane
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Q9ALP0 | MSRVSDTFAETSSVYSPDHADIYDAIHSARGRDWAAEAGEVVQLVRTRLPEAQSLLDVACGTGAHLERFRAEYAKVAGLELSDAMREIAIRRVPEVPIHIGDIRDFDLGEPFDVITCLCFTAAYMRTVDDLRRVTRNMARHLAPGGVAVIEPWWFPDKFIDGFVTGAVAHHGERVISRLSHSVLEGRTSRMTVRYTVAEPTGIRDFTEFEILSLFTEDEYTAALEDAGIRAEYLPGAPNGRGLFVGIRN | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . Catalyzes the dimethylation of the C-4 amino group from dTDP-4-amino-2,3,4,6-te... |
Q9M4A2 | MEGKFAISESTNLLQRIKDFTQSVVVDLAEGRSPKISINQFRNYCMNPEADCLCSSDKPKGQEIFTLKKEPQTYRIDMLLRVLLIVQQLLQENRHASKRDIYYMHPSAFKAQSIVDRAIGDICILFQCSRYNLNVVSVGNGLVMGWLKFREAGRKFDCLNSLNTAYPVPVLVEEVEDIVSLAEYILVVEKETVFQRLANDMFCKTNRCIVITGRGYPDVSTRRFLRLLMEKLHLPVHCLVDCDPYGFEILATYRFGSMQMAYDIESLRAPDMKWLGAFPSDSEVYSVPKQCLLPLTEEDKKRTEAMLLRCYLKREMPQWR... | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination . Together with MTOPVIB, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination . The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation th... |
Q22236 | MYEYSFNPNIDHEPGSVESQQSTIYSDSDDSDDSFLDDEVIPPKEQAMRKIEFALADIKRQMDNKEKSLTLRISTSKSHFCLRYTAKRKGKLDRDLHCLHQVYDLLENDKRSTKRELYYEHKAVYGNQKYLDSSIKSICELLNESRANLNILSCGRGIIRGAITFLVENVGVIDARVQEVLITDALLFSNIISEADFILVVEKDTTFQKLMDENFQAMFPRGILATSKGYPDIATRNVLKMLSEKRKFPIYGLFDADPHGIEIYLTYKYGPTKEFAEGRGAFVPTIEWIGLFPTDFHRFTIDQSQCLPLVRTDFVKIEKM... | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 49169
Sequence Length: 425
Subcellular Location: Nucleus
EC: 5.... |
Q7KPA5 | MDEFSENIERIALELLSNLVHGNATLSVPRNSSGNVISEYRRVSYNNRGSRHSFCVLIYMLSRVHRLQVRGGSFTVRGLYYDNPLLVRSQSRIAEARLDVCRMLRTSPLSLGILAASKGLVAGDLRLLMTNGDVLDSSLYGGPLTLPTDPEKIDRIETLAEFVLIVEKESVFESLLSRNVFGTFERRFILITGKGYPDCCTRRIVHRLTEENQLAAYILVDADPFGVEIMLVYRHGSKSMSFSSQGLTTPALRWIGLHPSEIPALGTGAVALVAGDNKKINDLLARHDLEPGVRQELRMLQDVQLKAEIESVIDFLTDDY... | Function: Required for meiotic recombination . Together with mei-P22, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 37064
Sequence Length: ... |
Q8SVS9 | MALAPTSSAISGSLRSSMLKLLMRLKSRTLATRLRLYEIIIEMQELGITRNEREIFYMDVNVFRTQSVVRRLVSSIASELQISKHDLGVRNTLKGIFIGRLGFVRHHGLGMVEMSSKGGCPQLIPDMSDIAEVLCDYKKTVVVEKDTVLQRIASEIEREKCLEEILFVCGKGYPCKNTVLLLKMIEHKTAVAGLFDLDPFGIHIFCIYKYGSKETPDIRVETIMRIGVCMEDVLEKNAYKDVFVKLNVHDLKMINRLVRFGELSADLLFLRKIDGKVEMEALFSKEPRRLRYFLFRMLERISS | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 34749
Sequence Length: 303
Subcellular Location... |
Q9Y5K1 | MAFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASSSEVLASIENIIQDIITSLARNEAPAFTIDNRSSWENIKFEDSVGLQMVSHCTTRKIKSDSPKSAQKFSLILKILSMIYKLVQSNTYATKRDIYYTDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEEDGTKVNCTCGATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSPCIMITGKGVPDLNTRLLVKKLWDTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKR... | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation throu... |
Q9WTK8 | MAFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVASSSEVLTAIENIIQDIIKSLARNEVPAFTIDNRSSWENIMFDDSVGLRMIPQCTTRKIRSDSPKSVKKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIAGNLRYMEEDGTRVQCTCSATATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQR... | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination . The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation thro... |
C4VB43 | MKNNLKVKLEELVIYILKNIKRYPNIIQRLKFYEQIHLGLTLNKIKNKREIYYNSVSIFKKQSIVDMLIKDTCNKLKCTQSDLLISTTLKGVFYGNITFYKNNKLVHVNLKGTSLIPDMNQIDRIEYTQKKCLIIEKDTIFSKTVREYISNDILFICGKGYPCRNTLLLVNKLNIRKYGIFDFDPYGLEICTKYPSIKKIGIDIKDINLIDKQHFMILNKYDIRKINTLLKQKVYEIELFYMLKNNIKIEIEGLFSAKGFDINNYFYTKII | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 32095
Sequence Length: 271
Subcellular Location... |
Q5ZPV8 | MAGREKRRRVAALDGEERRRRQEEAATLLHRIRGLVRWVVAEVAAGRSPTVALHRYQNYCSSASAAAASPCACSYDVPVGTDVLSLLHRGSHASRLNVLLRVLLVVQQLLQQNKHCSKRDIYYMYPSIFQEQAVVDRAINDICVLFKCSRHNLNVVPVAKGLVMGWIRFLEGEKEVYCVTNVNAAFSIPVSIEAIKDVVSVADYILIVEKETVFQRLANDKFCERNRCIVITGRGYPDIPTRRFLRYLVEQLHLPVYCLVDADPYGFDILATYKFGSLQLAYDANFLRVPDIRWLGVFTSDFEDYRLPDCCLLHLSSEDR... | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity). May be involved in plant growth and development, and stress tolerance.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded D... |
Q8BWU1 | MNWTAATCWALLLAAAFLCDSCSAKGGRGGARGSARGVRGGARGASRVRVRPAPRYGSSLRVAAAGAAAGAAAGVAAGLATGSGWRRTSGPGELGLEDDENGAMGGNGTDRGVYSYWAWTSGSGSVHSPRICLLLGGTLGALELLRP | Function: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14591
Sequence Length: 147
Subcellular Location: Cell membrane
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Q5BIV7 | MNWTTATCWALLLATAFLCDSCSAKGGRGGARGSARGVRGGARGASRVRVRPAPRYSSSLRVAAAGAAAGAAAGVAAGLATGSGWRRTSGPGELGLEDDENGAMGGNGTDRGVYSYWAWTSGSGSVHSPRICLLLSGTLGALELLRP | Function: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP (By similarity).
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14712
Sequence Length: 147
Subcellular Location: Cell membrane
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A2BDG5 | MRGTSAVCWSLLLLIALLSQNVTAKGGRGGARGGARGASRGASRVRLKTSSRYGSLRVASQAAAAGAAARAAARLSENTWRNNDHSGMDTQFGNSTNEGMYSYRAWTSGTCPLSSHLSFRLIISIGAILTCSSSSIYVSTKINLGK | Function: Prion-like protein that has PrP(C)-like neuroprotective activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15246
Sequence Length: 146
Subcellular Location: Cell membrane
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Q93704 | MNYEVYCGNAHAEPNSSAVQQLAEACVEQDASYFDGCSRTCVKDKYLLPLTQFDNLEIVVYGQIFPILVLFAVFANAAVALVLSKKHMITPTNVVLKYMAIAELLVGLVPLPWTLFFFSMGNIKETHRLELWWCYLQKYSMDAFPPVFHMIAMWLTVLLAAQRYVSISHPLHSRSACNVKNVRLATMIITVTSFLCGLPKSFDYEYETVHGWIYSHGNWTYASSCVMMPTAILTNMGQTVYFNIYFWTRALGFIILPSFLLVLLNGLLIKGIRRAQRRKLRLLREKRSEEAARQRDSNSTSLMLVAIVSIFLIVNLPQAI... | Function: G-protein coupled receptor for the neuropeptide like protein nlp-38 . Plays a role in several types of aversive gustatory associative learning including gustatory plasticity and salt avoidance learning . Its role in salt avoidance learning may be through activation of the transcription factor crh-1/CREB and d... |
Q96PI1 | MSSQQQQRQQQQCPPQRAQQQQVKQPCQPPPVKCQETCAPKTKDPCAPQVKKQCPPKGTIIPAQQKCPSAQQASKSKQK | Function: Cross-linked envelope protein of keratinocytes. Involved in UV-induced cornification.
PTM: Cross-linked to membrane proteins by transglutaminase.
Sequence Mass (Da): 8793
Sequence Length: 79
Subcellular Location: Cytoplasm
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A6LKE9 | MKIAFFNPQGNFDKKDSHLTEHPDFGGQLIYVKELAKAMGKMGNKVDIITRKIIDKKWPEFSGDFDYYPDAENVRIVRIAFGGDKFLNKERLWDFLGEYVKNIYRFYQKEGFPDFVTTHYGDGGIAGAMFKKLTHIPYSFTAHSLGAQKKDKFKNAKDAEERYRFSIRISAEKVAMKYASFIVTSTQQEKEEQYSHNEYIDVYPEIKDKIFVIPPGVNTNIFYPDDTDEYKFSKLPIIVSSRLDPKKNIEFVIESFNKYLKDGFELIIVLRKKPEEYTGYERQLIEKAKKAKGKFLVITSQKELAKLYNSAAKHRGIFAL... | Function: Plays a role in sucrose synthesis by catalyzing the first step of sucrose biosynthesis from UDP-glucose and fructose-6-phosphate.
Catalytic Activity: beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) + sucrose 6(F)-phosphate + UDP
Sequence Mass (Da): 49174
Sequence Length: 423
EC: 2.4.1.14
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Q96N96 | MTSASPEDQNAPVGCPKGARRRRPISVIGGVSLYGTNQTEELDNLLTQPASRPPMPAHQVPPYKAVSARFRPFTFSQSTPIGLDRVGRRRQMRASNVSSDGGTEPSALVDDNGSEEDFSYEDLCQASPRYLQPGGEQLAINELISDGNVVCAEALWDHVTMDDQELGFKAGDVIQVLEASNKDWWWGRSEDKEAWFPASFVRLRVNQEELSENSSSTPSEEQDEEASQSRHRHCENKQQMRTNVIREIMDTERVYIKHLRDICEGYIRQCRKHTGMFTVAQLATIFGNIEDIYKFQRKFLKDLEKQYNKEEPHLSEIGSC... | Function: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent mechanism. Increases both RAC1 and CDC42 activity, but decreases the amount of active RHOA. Required for MMP9 up-regul... |
P21454 | MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALPYSSGGGNGPFGVGWSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTESSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLAENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAFTAQNSWLARQDPFSLYNYGFEIRLLRLCRQVLMFHHFPDE... | Function: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. ADP-ribosylation prevents the polymerization of G-actin to F... |
P0DPK6 | MTVNEIDLPPIFCPLESARHPRAHLVDERAREWIRTSPMCTTDEERTWVAASCSTDFFARFAPDAATDDRLLWTSLWVYWGFAFDDHRCDNGPFSNRPAAFSALAGRVQRALEAPSARDESDGFIPALQEIAAQFRSFGTPLQVRRFAAAHRAWLSGVTWQIGNAAAGRMPGLDEYVAMRLLSAGGEPPFAMLELATGLEVPAQDLERPAVRALTEMAIMVAALDNDRHSLRKELARGQTDQNVYSVLMQETGLPLQEAVAAATRLRDRVLLRFMAVHDRVRPGAGLELSTYLQGLRYGIRGNAEWGLRVPRYLSLGRVP... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the formation of (3R,6R,10S,11R,14R)-spiroviolene from geranylgeranyl diphosphate (GGPP) via a 1,11-cyclization and a 10Re,14Si-cyclization.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (-)-spiroviolene + diphosphate
Sequence Mass (Da): 3996... |
O82422 | MESLQGKESNGAVPVCNGGGGAAAPPAKQQLPEGTDALRYANILRSRNKFADALQLYTTVLDKDGANVEALIGKGICLQAQSLPRQALDCFTEAVKVDPKNACALTHCGMIYKDEGHLVEAAEAYQKARSADPSYKAASEFLAIVLTDLGTSLKLAGNTEDGIQKYCEALEVDSHYAPAYYNLGVVYSEMMQFDVALTCYEKAALERPLYAEAYCNMGVIYKNRGELDAAIACYDRCLTISPNFEIAKNNMAIALTDLGTKVKIEGDINQGVAYYKKALFYNWHYADAMYNLGVAYGEMLNFEMAIVFYELALHFNPRCA... | Function: Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by addi... |
Q32L17 | MEVPTLSKTRKPPDLNEESLDLGIMIALFEIGSIPPVSCSSLPSLKSSDHEATEQRIAKKFESLLKEIKDIVKHVTSYEQKVTETKEPFKETNMFEVSELREKIIELDEINKELVKKLLASLDLGKKENAKKQEMRLDNQNSEDTVQDCSGDLVNCSKGQKALPETQLSKEKAKHGFPHIQEENIRLRNNMERLLQEAEHWSVEHTELSKLIKSYQKSQNDIKTLKNNGTHSPTQTNNESAKQELEEQVKRLKEDTYSLHLIATLLENECQILEQRVELLDELHHQKEEPLQGEPMQINHEQSDKEQKLPEAEKVKIHEK... | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity).
PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1.
Sequence Mass (Da): 42777
Sequence Lengt... |
Q9BXG8 | MASSAKSAEMPTISKTVNPTPDPHQEYLDPRITIALFEIGSHSPSSWGSLPFLKNSSHQVTEQQTAQKFNNLLKEIKDILKNMAGFEEKITEAKELFEETNITEDVSAHKENIRGLDKINEMLSTNLPVSLAPEKEDNEKKQEMILETNITEDVSAHKENIRGLDKINEMLSTNLPVSLAPEKEDNEKKQQMIMENQNSENTAQVFARDLVNRLEEKKVLNETQQSQEKAKNRLNVQEETMKIRNNMEQLLQEAEHWSKQHTELSKLIKSYQKSQKDISETLGNNGVGFQTQPNNEVSAKHELEEQVKKLSHDTYSLQLM... | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity).
PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1.
Sequence Mass (Da): 49445
Sequence Lengt... |
Q99MY0 | MSDTDNSAEMPARCPSPNPAPGAKQEPPNSGITISLLEIGSLPTVCYHSFPPPKNSICPVEKRGRVQKFSNLLKDVKDVLKNIAGVEEKSTVGEPFDDAYIPEDLSELNVRGVEKKNKIRFKDDLFIHFDPEREQNTMKQMLLKNQSAKNMVPKFARDLCNAEETRGFDGMLLSVKRPRNGSLHLRGEYRKLRNNMEQLLQEADHWSKQHNELSELMRSYQECQNETQETTDKDRACLQNQPNNGLSTKQKLEEQVKKLSHDTHALHLIAALLENECQVLQQRVDILKDFHLHEAGLGHEKPLQMSCEQDKKCPKLAEAD... | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. Directly binds to a guanine-rich region of the PCNA promoter and up-regulates its expression which in turn induces cell transformation and tumor formation. May play an important role in the regulation of cell prolifer... |
Q96JX3 | MSLAAYCVICCRRIGTSTSPPKSGTHWRDIRNIIKFTGSLILGGSLFLTYEVLALKKAVTLDTQVVEREKMKSYIYVHTVSLDKGENHGIAWQARKELHKAVRKVLATSAKILRNPFADPFSTVDIEDHECAVWLLLRKSKSDDKTTRLEAVREMSETHHWHDYQYRIIAQACDPKTLIGLARSEESDLRFFLLPPPLPSLKEDSSTEEELRQLLASLPQTELDECIQYFTSLALSESSQSLAAQKGGLWCFGGNGLPYAESFGEVPSATVEMFCLEAIVKHSEISTHCDKIEANGGLQLLQRLYRLHKDCPKVQRNIMR... | Function: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be ... |
Q60598 | MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKN... | Function: Contributes to the organization of the actin cytoskeleton and cell shape . Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with ... |
Q66HL2 | MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENL... | Function: Contributes to the organization of the actin cytoskeleton and cell shape . Plays a role in the formation of lamellipodia and in cell migration . Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones . Through its interaction with CTTNBP2, involved in the regul... |
Q4WND5 | MNNEALAEDPPTPLWELVLEQFKDQLVLILLGSAAVSFVLALFEEGDDWTAFVDPVVILTILILNAVVGVTQESSAEKAIAALQEYSANEATVVRDGKTQRIKAEDLVPGDIIHIGVGDRVPADCRLLAIQSNSFRVDQAVLTGESESVSKDTRSIKDEQAVKQDQTNILFSGTSVVNGHATAIVVLTGASTAIGGIHESITSQISEPTPLKQKLNDFGDMLAKVITVICVLVWLINVEHFNDPAHGGWAKGAIYYLKIAVSLGVAAIPEGLAVVITTCLALGTRKMAAKNAVVRSLPSVETLGSCSVICSDKTGTLTTN... | Function: Magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the endoplasmic reticulum lumen (Probable). Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the endoplasmioc reticulum is important for redox homeostas... |
Q86TD4 | MRALVLLGCLLASLLFSGQAEETEDANEEAPLRDRSHIEKTLMLNEDKPSDDYSAVLQRLRKIYHSSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLENTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQEYKPDTHQELFLQEEISLLEDLNQ... | PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54431
Sequence Length: 473
Subcellular Location: Sarcoplasmic reticulum lumen
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Q7TQ48 | MKALLLLCCFLASLLLSGQAEVEDASEEAPLRDRSHIDKTLMLNEDKPADDYSAVLQRLRKIYHTSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLEDTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRELFLKEEISLLEDLNQV... | PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54287
Sequence Length: 472
Subcellular Location: Sarcoplasmic reticulum lumen
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Q55025 | MIRIRNRWFRWLAIALASLVASIGIATVGFAATGVTPDQVLSAIEGTFGVNVGQRRNHIKGTCAVGNFVATTEAKTYSRSPLFSGQSIPVVARFSLAGGNPKAPDTAKNPRGLGLQFQLPNNRFLNMALLNTPVFGVASPEGFYENILAIRPDPTTGKPDPEKVKAFREKYPENKAQAAFLASNNPPTSYANTSYFGLHAFKFINQTNQTRLVRWQFVPQDGEKRLTDAELQAAPANFLEQKLIERTQDSPVKWDFWITLGQPGDAEDNPTIAWPSDRQQVKVGTLTLTAASPQPGAACEGINYDPLVLSDGIEPTNDPV... | Function: Has an organic peroxide-dependent peroxidase activity.
Sequence Mass (Da): 37055
Sequence Length: 339
Subcellular Location: Periplasm
EC: 1.11.1.-
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O13950 | MDGTSQAFKIIVATIIIGAIISTLGIFFTRKTIQKKLPAVFLIGPSDSGKTSLFCELIYKEKKTTVPSIEPNEAVWKYGAWLVDLPGHPRAKRWITTKFSGNYNVKAVVFVLNSATIDRDVHEVGLMLFDTILKCRKHHVPHLLIACNKFDLFTAQPAEKIQQLLKAELHNILEEKNLQLESIVSEDVDWESVADQIEDTDLKFLPGSVAKMSNIEEWISWMESALQ | Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarit... |
P36057 | MLSNTLIIACLLVIGTTIALIAVQKASSKTGIKQKSYQPSIIIAGPQNSGKTSLLTLLTTDSVRPTVVSQEPLSAADYDGSGVTLVDFPGHVKLRYKLSDYLKTRAKFVKGLIFMVDSTVDPKKLTTTAEFLVDILSITESSCENGIDILIACNKSELFTARPPSKIKDALESEIQKVIERRKKSLNEVERKINEEDYAENTLDVLQSTDGFKFANLEASVVAFEGSINKRKISQWREWIDEKL | Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarit... |
Q59967 | MSLSPRSDRTEIRRSWGLDSIVSALSQASTDPLPHHLLSDQFYPLPSRESLGLILHGLRSVLFPRHFGDPELSVETTHYFIGNTLDKTLNLLNEQIRRELWLQHVTQGTPEATPAVLSQHASELTQAFAQALPEIKRLLDSDVNAAYLGDPAAQSISEILFCYPGITAITFHRLAHRLYQLGLPLLARITAEVSHSETGIDIHPGAAIGGSFFIDHGTGVVIGETCVIGDRVRIYQAVTLGAKSFPRDETGALIKGQARHPVIEDDVVIYAGATLLGRITVGRGSTIGGNVWLTRSVPAGSFISQAQIRSDNFESGGGI | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 34570
Sequence Length: 319
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.30
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Q96SB4 | MERKVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKEN... | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the ... |
O70551 | MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDIPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNGEMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVDRPLTEN... | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the ... |
P78362 | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYC... | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing . Promotes neuronal apoptosis... |
O54781 | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPE... | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing . Promotes neuronal apoptosis... |
Q05738 | MEGHVKRPMNAFMVWSRGERHKLAQQNPSMQNTEISKQLGCRWKSLTEAEKRPFFQEAQRLKILHREKYPNYKYQPHRRAKVSQRSGILQPAVASTKLYNLLQWDRNPHAITYRQDWSRAAHLYSKNQQSFYWQPVDIPTGHLQQQQQQQQQQQFHNHHQQQQQFYDHHQQQQQQQQQQQQFHDHHQQKQQFHDHHQQQQQFHDHHHHHQEQQFHDHHQQQQQFHDHQQQQQQQQQQQFHDHHQQKQQFHDHHHHQQQQQFHDHQQQQQQFHDHQQQQHQFHDHPQQKQQFHDHPQQQQQFHDHHHQQQQKQQFHDHHQQ... | Function: Transcriptional regulator that controls a genetic switch in male development . It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells . Involved in different aspects of gene regu... |
Q8ZNG2 | MNICVNSLYRLSIPQFHSLYTEEVSDEALTLLFSAVENGDQNCIDLLCNLALRNDDLGHRVEKFLFDLFSGKRTGSSDIDKKINQACLVLHQIANNDITKDNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSDELAAATQGLVQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLVNTGDHWLLCLFYKLAEKIKCLIFNTYYDLNENTKQEIIEAAKIAGISESDEVNFIEMNLQNNVPNGCGLFCYHTIQLLSNAGQNDPATTLREFAENFLTLSV... | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease targets the host cell ubiquitin pathway by acting as a deubiquitinase in infected host cells. Specifically hydrolyzes mono- and polyubiquitin substrates in vitro with a preference for 'Lys-63... |
P84766 | ATGSGGMNLVFVGAEMAPXXX | Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 2043
Sequence Length: 21
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.242
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Q9MAQ0 | MATVTASSNFVSRTSLFNNHGASSCSDVAQITLKGQSLTHCGLRSFNMVDNLQRRSQAKPVSAKSSKRSSKVKTAGKIVCEKGMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAWDTCVVVQIKVGDKVENVRFFHCYKRGVDRVFVDHPIFLAKVVGKTGSKIYGPITGVDYNDNQLRFSLLCQAALEAPQVLNLNSSKYFSGPYGEDVVFVANDWHTALLPCYLKSMYQSRGVYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSSFDFMDGYEKPVKGRKINWMKAAILEAHRVL... | Function: Required for the synthesis of amylose . Destroyed as it is released from the starch granules during the night . The circadian expression is controlled by CCA1 and LHY transcription factors .
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucl... |
P84633 | GMNLVFVGAEVAPWSKTGGLGDVLA | Function: Required for the synthesis of amylose in endosperm.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 2489
Sequence Length: 25
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Lo... |
P09842 | MAALATSQLATSGTVLGVTDRFRRPGFQGLRPRNPADAALGMRTIGASAAPKQSRKAHRGSRRCLSVVVSATGSGMNLVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVVSPRYDQYKDAWDTSVISEIKVADEYERVRFFHCYKRGVDRVFIDHPWFLEKVRGKTKEKIYGPDAGTDYEDNQQRFSLLCQAALEAPRILNLNNNPYFSGPYGEDVVFVCNDWHTGLLACYLKSNYQSNGIYRTAKVAFCIHNISYQGRFSFDDFAQLNLPDRFKSSFDFIDGYDKPVEGRKINWMKAGILQADKVLTVSPYYAE... | Function: Required for the synthesis of amylose in endosperm.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 66211
Sequence Length: 603
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular ... |
Q5AHK2 | MSYSSASFRKLNNVGISQPSQTTTTTTSANQPQSQSQQQPLQQSQQQHLHMKPNPHIPHHQLPGTVGTRTSIPQPALMASNSILTLGPFKHRKDLTRESVLSTYQIMGYIAAGTYGKVYKAKLKSNKLNKTDDDSGIDGINNKDIFSESMNDLHHDNSSSIMINTTTNITINNSLPQFFAIKKFKSDNHHHHINNNNNGGNHLSKGNNSIHQDEVLHYTGISQSAIREMSLCRELNNKNITKLVDIILENKSIYMVFEFCEHDLLQIIHYQSHPDFKPIPCPTIKSLIWQILNGVTFLHKNWILHRDLKPANIMVSSQGV... | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... |
P0CS77 | MATIPGGGTIMDPMHLYRARRDKERRGVLKTYKILGFISSGTYGRVYKAVLLPPPKTASAKSALPSSTRAALSLPKDKLPSPSFTEDSDPLNNPEMCMRPGDRPAKRGDVFAIKKFKPDKEGDVLTYAGISQSGAREIMLNRELHHRNLVSLREVILEDKSIYMVFEYAEHDFLQIIHYHSQTARASIPPSTLRRLLHQLLCGVHFLHSNFVLHRDLKPANILVTSQGVVKIGDLGLARLWHKPLAQQGLYGGDKVVVTIWYRAPELILGAKHYTAAVDIWAVGCIYAELLSLRPIFKGDEAKMDGKKSLPFQRDQMGKI... | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... |
Q6BM25 | MNSGYNPGNANHITSHSNRTKNGVPTIPQPALMASNAILTIGPYKHRKDLIRESVLTKYQIIGYIAAGTYGKVYKAKSKTNGNSNSNSALMNDNVISIGNGQKEAGLQKTNNESMEDKNQLFAIKKFKSDNHSNKNNHDINGNEVIHYTGISQSAIREMSLCRELSNKNITKVVDILLENKSIYMVFEYCEHDLLQIIQYHSHPDVKPIPDFTIKSITWQILNGVTFLHKNWIFHRDLKPANIMVSSSGVVKIGDLGLARKFNNPLQSLYTGDKVVVTIWYRAPELLLGARHYTPSIDLWAVGCILAELLSLRPIFKGEE... | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... |
Q4FCZ5 | MPLRPHIGLGFPAHAYQKRHVEPHDRSTGYQPKVRITDRYRIIGFISSGTYGRVYKAVGRNGKPVGEFAIKKFKPDKEGEQISYTGISQSAIREMSLCSELHHINVIRLCEIVLEDKCIFMVFEYAEHDLLQIIHHHTQQPRHPIPPATIKSIMFQLLNGCQYLHINWVLHRDLKPANIMVTSSGEVKIGDLGLARRFDKPLHSLFSGDKVVVTIWYRAPELILGSYHYTPAIDMWAVGCIFAELLSLRPIFKGEEAKMDSKKTVPFRRNQMQKIIEIMGVPTKDKWPLLSTMPEYNQLNTLANSMASSHHNHHSHHHPH... | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... |
A4QXX4 | MSHSNPPTGASGGPGSASASAAPARGYYSLKRSIQTAFNDPLDRGLGPPAYQSKVRVMDKYQVIGFISSGTYGRVYKARGRQGQPGEFAIKKFKPDKEGEQITYTGISQSAIREMALCSELRHPNVIRLVETILEDKAIFMVFEYAEHDLLQIIHHHTQQPKHPIPPQTIKSIMFQLLNGCQYLHTNWVLHRDLKPANIMVTSSGEVKVGDLGLARIFWKPVRTLMQGDKVVVTIWYRAPELLMGSHHYTPAVDMWAVGCIFAELLSLRPIFKGEEAKMDNTKKGGSRDMPFQRHQMQKIVDIMGMPTKERWPLLTSMPD... | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... |
Q0TWJ7 | MERKRGREMNPPSADPPSATPVARANLPGSVAAAFHGRPCSQGTTTLKRVNERYKIVGFISSGTYGRVYKAEGKNGRTGEFAIKKFKPDKEGELQYSGISQSAIREMALCTELAHPNVVHTVEIILEEKCIFIVFEYAEHDLLQIIHHHNQPQRQAIPARTIKSILYQLLQGLVYLHRNWVMHRDLKPANIMVTSAGKVKIGDLGLARLFYKPLQSLFSGDKVVVTIWYRAPELLLGSRHYTPAVDLWAVGCIFAELLSLRPIFKGEEAKMDSKKTVPFQRNQMQKIVEIMGMPSKDRWPLLTAMPEYPQLSSLIAGNAA... | Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex... |
A3LUB9 | MASNSILTLGPFKHRKDLTRESVLSTYQIIGYIAAGTYGKVYKAKLKNTASAEQLFAIKKFKSDNHSSNRSHHNHDINGNEIVHYTGISQSAIREMSLCRELNNKNITKLVDIILENKSIYMIFEFCEHDLLQIIHYHSHPEVKPIPQATVKSLIWQILNGVTFLHQNWIFHRDLKPANIMVSSSGVVKIGDLGLARKFNNPLQSLYTGDKVVVTIWYRAPELLLGARHYTPAIDLWAVGCILAELLSLRPIFKGEEAKIDINNKKSVPFQKNQFQKIVEVLGTPSMKNWPALNKYPEFISFQQQLTTNYPPNLVNWYKM... | Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex... |
Q14714 | MGKNKQPRGQQRQGGPPAADAAGPDDMEPKKGTGAPKECGEEEPRTCCGCRFPLLLALLQLALGIAVTVVGFLMASISSSLLVRDTPFWAGIIVCLVAYLGLFMLCVSYQVDERTCIQFSMKLLYFLLSALGLTVCVLAVAFAAHHYSQLTQFTCETTLDSCQCKLPSSEPLSRTFVYRDVTDCTSVTGTFKLFLLIQMILNLVCGLVCLLACFVMWKHRYQVFYVGVRICSLTASEGPQQKI | Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC.
Location Topology: Multi-pass membrane protein
Sequence ... |
Q62147 | MGRKPSPRAQELPEEEARTCCGCRFPLLLALLQLALGIAVTVLGFLMASISPSLLVRDTPFWAGSIVCVVAYLGLFMLCVSYQVDERTCVQFSMKVFYFLLSALGLMVCMLAVAFAAHHYSLLAQFTCETSLDSCQCKLPSSEPLSRAFVYRDVTDCTSVTGTFKLFLIIQMVLNLVCGLVCLLACFVMWKHRYQVFYVGVGLRSLMASDGQLPKA | Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC (By similarity).
Location Topology: Multi-pass membrane p... |
Q1C1S0 | MTTLTHIPQGTPITLESIGKRYGNRTVLDNLQLRITAGQFVAVVGRSGCGKSTLLRLLAGLEAASDGTLLSGNALLSHAKDETRLMFQEARLLPWKKVIDNVGLGLRGHWRDEALQVLDTVGLADRANEWPAALSGGQKQRVALARALIHRPRLLLLDEPLGALDALTRIEMQGLIERLWQQHGFTVLLVTHDVSEAIALADRVLLIEEGRIGLDLAIDLPRPRRKGSAKLAALEAEVLERVLSPPQGIEASRQGIKASRQGTATSRRVAN | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
P40401 | MMKAEAAGSLPKTNAEAVRKKPGRKRYGWMKGLLLPAVIIAIWQVIGGLGVVSATVLPTPVTIVLTFKELILSGELFGHLQISIYRAALGFLLGAGLGLMIGILAGFSKRTELYLDPSLQMLRTVPHLAVTPLFILWFGFDEVSKILLIALGAFFPVYINTFNGIRGVDAKLFEVARVLEFKWHQQISKVILPAALPNILLGIRLSLGIAWLGLVVAELMGSSSGVGYMIMDARQFSQTNKVFAGIIIFAVVGKLTDSFVRLLERKLLKWRNSYEG | Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30240
Sequence Length: 276
Subcellular Location: Cell membrane
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P75851 | MATPVKKWLLRVAPWFLPVGIVAVWQLASSVGWLSTRILPSPEGVVTAFWTLSASGELWQHLAISSWRALIGFSIGGSLGLILGLISGLSRWGERLLDTSIQMLRNVPHLALIPLVILWFGIDESAKIFLVALGTLFPIYINTWHGIRNIDRGLVEMARSYGLSGIPLFIHVILPGALPSIMVGVRFALGLMWLTLIVAETISANSGIGYLAMNAREFLQTDVVVVAIILYALLGKLADVSAQLLERLWLRWNPAYHLKEATV | Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28925
Sequence Length: 263
Subcellular Location: Cell inner membrane
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P40402 | MEILWFIPTHGDARYLGSESDGRTADHLYFKQVAQAADRLGYTGVLLPTGRSCEDPWLTASALAGETKDLKFLVAVRPGLMQPSLAARMTSTLDRISDGRLLINVVAGGDPYELAGDGLFISHDERYEATDEFLTVWRRLLQGETVSYEGKHIKVENSNLLFPPQQEPHPPIYFGGSSQAGIEAAAKHTDVYLTWGEPPEQVKEKIERVKKQAAKEGRSVRFGIRLHVIARETEQEAWEAAERLISHLDDDTIAKAQAALSRYDSSGQQRMAVLHQGDRTKLEISPNLWAGIGLVRGGAGTALVGDPQTIADRIAEYQAL... | Function: Catalyzes the desulfonation of aliphatic sulfonates.
Catalytic Activity: an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) + H2O + sulfite
Sequence Mass (Da): 41802
Sequence Length: 376
EC: 1.14.14.5
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Q9LDU6 | MAETVHSPIVTYASMLSLLAFCPPFVILLWYTMVHQDGSVTQTFGFFWENGVQGLINIWPRPTLIAWKIIFCYGAFEAILQLLLPGKRVEGPISPAGNRPVYKANGLAAYFVTLATYLGLWWFGIFNPAIVYDHLGEIFSALIFGSFIFCVLLYIKGHVAPSSSDSGSCGNLIIDFYWGMELYPRIGKSFDIKVFTNCRFGMMSWAVLAVTYCIKQYEINGKVSDSMLVNTILMLVYVTKFFWWEAGYWNTMDIAHDRAGFYICWGCLVWVPSVYTSPGMYLVNHPVELGTQLAIYILVAGILCIYINYDCDRQRQEFRR... | Function: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the enzyme cause dwarfism.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49591
Sequen... |
Q9M881 | MALLLNSTITVAMKQNPLVAVSFPRTTCLGSSFSPPRLLRVSCVATNPSKTSEETDKKKFRPIKEVPNQVTHTITQEKLEIFKSMENWAQENLLSYLKPVEASWQPQDFLPETNDEDRFYEQVKELRDRTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLTPWAVWVRAWTAEENRHGDLLNKYLYLSGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTAKLATTYGDTTLAKICGTIAADEKRHETAYTRIVEKLFEIDPDGTVQALASMMRKRITMPAHLMHDGRDDD... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain (By similarity). Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity. Involved in omega-7 monounsaturated fatty acid biosynthes... |
E3PZS2 | MELHLALRASPLPAADPGRRPPPPRGNFATNCTAAINSTHISQEKFRSLDSWVEHNMLTFLKPVEKCWQPQDFLPDPSHLSAEELGDAVREIHERAAEIPDEVWVCMVGNMVTEEALPTYQSLISSVLGGTVAGSTPWDRWIRGWSAEENRHGDLLNKYLYLTGRLDMRQVEKTIQYLIGSGMDVGVGNSILCGFIYTCFQEKATFISHGNTARLAKHHGDTTLAKICGLVAADEKRHAVAYTNLMKKLFEVAPNESMLAFAHIMRAHVTMPASRMFDGRDPRLFTHFSAVTQKIGVYTVRDYGEMLDFFLKEWEISAVV... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. Catalyzes the desat... |
Q9LF05 | MSMALLLTSPAMKQKPAVITSPRRGSSPSRRLRVSCVTTNPARKKNETCNHFRPIKEVNNQLTHTIPQEKLEIFKSMENWAEQKLLPYLKPVEDSWQPQDFLPAPENDDEFYDRVKEIRERTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLSPWAVWIRAWTAEENRHGDLLNKYLYLTGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTARLATTYGDVTLAKICGTIAADEKRHETAYTKIVEKLFEIDPDGSVQALASMMKKRITMPAHLMHDGRDNDLFDHYAAV... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Also able to convert palmitoyl-ACP to palmitoleoyl-ACP at the C9 position. Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity... |
B9F058 | MSLTGCLPPRPPCSMRRRTSGGGASVSPVVAMASTAGVGGIGNPTPRGKKPFAPWREVPPQVTHTLPPEKKEVFDSLEGWAADTILPYLKPVEESWQPQDHLPDPRSPSFGDEVAALRERAAGLPDDHLVCLVGDMVTEEALPTYQTMLNTMDGGVRDETGAGGSAWAVWTRAWAAEENRHGDLMNKYLYLTGRVDMRQVEKTIQYLIGSGMDPRTENDPYMGFIYTTFQERATSISHGNTARHAGRHGDAALARVCGTVAADEKRHEAAYAAIVAKLFEVDPDYTVRAFARMMRRKVAMPARLMYDGADDRLFARFAAV... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Sequence Mass (Da): 43956
Sequence Length: 402
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.-
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Q9M879 | MAMAMDRIVFSPSSYVYRPCQARGSRSSRVSMASTIRSATTEVTNGRKLYIPPREVHVQVKHSMPPQKLEIFKSLEGWADETLLTYLKPVEKSWQPTDFLPEPESEGFYDQVKELRERCKELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTPWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPKTENNPYLGFIYTSFQERATFISHGNTARLAKDRGDLKLAQICGTIAADERRHETAYTKIVEKLFEIDPDGTILGLADMMKKKISMPAHLMYDGQDDNLFEHFSTVAQR... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferred... |
Q84VY3 | MLAHKSLLSFTTQWATLMPSPSTFLASRPRGPAKISAVAAPVRPALKHQNKIHTMPPEKMEIFKSLDGWAKDQILPLLKPVDQCWQPASFLPDPALPFSEFTDQVRELRERTASLPDEYFVVLVGDMITEDALPTYQTMINTLDGVRDETGASESAWASWTRAWTAEENRHGDLLRTYLYLSGRVDMLMVERTVQHLIGSGMDPGTENNPYLGFVYTSFQERATFVSHGNTARLAKSAGDPVLARICGTIAADEKRHENAYVRIVEKLLEIDPNGAVSAVADMMRKKITMPAHLMTDGRDPMLFEHFSAVAQRLEVYTAD... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferred... |
Q0J7E4 | MAATATMAMPLANRLRCKPNTNSSSPSRTLFGRRVTMISSSRWGSAVSGSAIMSAAADVAAAVRREEDEEMRSYLSPEKLEVLTQMEPWVEEHVLPLLKPVEAAWQPSDLLPDPAVLGGEGFHAACAELRERAAGVPDLLLVCLVANMVTEEALPTYQSSLNRVRAVGDLTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRFDMAEVERAVHRLIRSGMAVDPPCSPYHAFVYTAFQERATAVAHGNTARLVGARGHGDAALARVCGTVAADEKRHEAAYTRIVSRLLEADPDAGVRAVARMLRRGVAMPTSPISD... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Sequence Mass (Da): 46101
Sequence Length: 419
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.-
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O22832 | MALKFNPLVASQPYKFPSSTRPPTPSFRSPKFLCLASSSPALSSGPKEVESLKKPFTPPREVHVQVLHSMPPQKIEIFKSMENWAEENLLIHLKDVEKSWQPQDFLPDPASDGFEDQVRELRERARELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVMAFADMMRKKISMPAHLMYDGRNDNLFDNF... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Required for the activation of certain jasmonic acid (JA)-mediated responses and the repression of the salicylic acid (SA) signaling pathway.
Catalyti... |
P13018 | MKISVIPEQVAETLDAENHFIVREVFDVHLSDQGFELSTRSVSPYRKDYISDDDSDEDSACYGAFIDQELVGKIELNSTWNDLASIEHIVVSHTHRGKGVAHSLIEFAKKWALSRQLLGIRLETQTNNVPACNLYAKCGFTLGGIDLFTYKTRPQVSNETAMYWYWFSGAQDDA | Function: Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes . Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin (By similarity).
Catalytic Activity: acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-acetyl... |
P08457 | MTTTHGSTYEFRSARPGDAEAIEGLDGSFTTSTVFEVDVTGDGFALREVPADPPLVKVFPDDGGSDGEDGAEGEDADSRTFVAVGADGDLAGFAAVSYSAWNQRLTIEDIEVAPGHRGKGIGRVLMRHAADFARERGAGHLWLEVTNVNAPAIHAYRRMGFAFCGLDSALYQGTASEGEHALYMSMPCP | Function: Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin.
Catalytic Activity: acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-acetylstreptothricin F
... |
P42845 | MSQPQMSPEKEQELASKILHRAELAQMTRQLKLGLSNVPSTKRKQDSTTKKRSGEDAEDVDEDHKTLLEAISPAKKPLHDDTNKMTVISPVKFVEKPNTPPSSRQRKAEDRSQQIKPRKEDTPSTPRASATPIILPHASSHYQRPHDKNFMTPKRNNNNSSNHSNNNNNIKKKAAGSKDAPQDSDNTAGADLLMYLATSPYNKSSHHGTPMAVRMPTTPRSYHYASQLSLNGNTASTSNDAVRFSHIKPSASSPQSTFKSNLLPNFPDESLMDSPSLYLSNNNGSVQATLSPQQRRKPTTNTLHPPSNVPTTPSRELNGT... | Function: Involved in the regulation and timing of MBF-dependent transcription in late G1 of the cell cycle.
PTM: Phosphorylated by CDC28 in a cell cycle-dependent manner, inhibiting the interaction with SWI6.
Sequence Mass (Da): 45684
Sequence Length: 420
Subcellular Location: Cytoplasm
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Q0UK53 | MMNPFFQNTSCSPYYRTDQPCSLGNYVSYAIPVAGVADIVAAINFTQTHNVRLVIKNTGHDYMGKSTGRGALSLWTHNLKSRQLVNYSSAHYTGPAIKVGAGVTGGEALVHASASGYRIVSGDCPTVGYSGGYSSGGGHSILNSVHGLAADNVLEWEVVTADGRHVVASPDQNSDLYWAMSGGGGGTFAVALSMTSRVHADSIIGAASLSFNATSAPSNDSFVSALNAWWAFLPSLVDVGATPSWNIFAGNFLVPNTTAPGRTAADMDTLYSPFLSELKRLGIPYAFESFSAPNYLQHYNDTDGPLPDGPLAAWA | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 mal... |
Q0UK52 | MAPAETTGNVQRPEAGKQSMGSFWTQMFPPKPTYTEEQVPDLTGKIFIVTGSSSGVGKEAARMLYAKNAKVYMAARPGPKLPAAINSVQEAVPKSGGALIPLELDLADLAVVKKAVEKFTSLETKLHGLINNAAVQALKDTDGDARTAQGHEIHMGVNVLAPFLFTRLLTGVLTATARQEPPGTVRVVWVSSMGTETIGEKRRGLSPDYVDYWPLMSPLERYGLSKAGNWLHGVEFARRYAADGIASFPINPGHLKSDLYREGGALFKFALKPVLYPPTYGAYVELFAALSPTLTLKDSGAWSKYVEMVYFPDC | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit ... |
Q0UK51 | MAAYFLLGLYGSTLVYRLIFHPLNRFPGPLAARISDLWLCTQLGGHDMHHLSERLSKRYGEFVRIGSSTLMLTHPKAVAAIYGPGSPCRKGTFYDLEQPNRGIATRDESLHAGRRRVWSRGFGDKALRTYEPRVAAYVHMLLGRLADARGKPVDMARLAEAFAFDTMGDLGLGADFGMLRQARTHEAVEQLVQGMTIMGRRLPMWLMRLLIDVAQALVPTAATTGFLGFCHHHLDRFMADPRRSERPSLMAPLLSHYEKQNIADRDLSILRNDCRFIIIAGSDTVAATLTFAFFYLAKHPGHVTRLREELFPLRAADGTF... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7... |
Q0UK49 | MGLQFLAPGEKVFPSLHRIIISTFALIAAYIFIVRPLRNILFHPLKKYPGPKLFGASSIPYGFYYMTGKWHLKIRNLHATYGPIVRIGPDELSYACPEAWEDIYGRYVPTKRRENPKPVWYCSPDAHDMVGASLGDHGRMRRVMAPGFTYSAMCKQEPLIKGHVDMFLSKLCSLCGDGRAEVNILDWLTYCTFDLIGDLSFGEPFGCMENNMLHPWLQLVFANIYITHIILLCQRIPFFYLFLPIKTTYQLWRDFRRHVVLLREVVERRLSLSTPRDDFLDVMTTKQTSTLYMTKEEIFKNAILLTGGGAETTSSSLSGM... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7... |
P15705 | MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDALNDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRTQQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAPQKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNNRAAAEYEKGEYETAISTLND... | Function: May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature.
PTM: N-glycosylated.
Sequence Mass (Da): 66265
Sequence Length: 589
Subcellular Location: Cytoplasm
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Q7FA29 | MKRRHWSHPSCGLLLLVAVFCLLLVFRCSQLRHSGDGAAAAAPDGGAGRNDGDDVDERLVELAAVDPAAMAVLQAAKRLLEGNLARAPERHRDVALRGLREWVGKQERFDPGVMSELVELIKRPIDRYNGDGGGGGEGEGRRYASCAVVGNSGILLAAEHGELIDGHELVVRLNNAPAGDGRYARHVGARTGLAFLNSNVLSQCAVPRRGACFCRAYGEGVPILTYMCNAAHFVEHAVCNNASSSSSGAADATAAAPVIVTDPRLDALCARIVKYYSLRRFARETGRPAEEWARRHEEGMFHYSSGMQAVVAAAGVCDRV... | Function: Possesses sialyltransferase-like activity in vitro. Transfers sialic acid to the glycoprotein asialofetuin. The transferred sialic acid is linked to galactose of Gal-beta-1,3-GalNAc through alpha-2,6-linkage.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41999
Sequence Length: 38... |
A0A0P0ZEA9 | MEGSINDARRTNYLVLLRTCYEIYGIYEPLLALFAVYSVAVVVYRLYLHPLARFPGPKLAAATGWYEFYHDVFRGGQYLYEIESMHRKYGPIIRINPHELVVNDPDFYNTVFVAANTRRTDKWSGLEGIGLRGSLAFTRDHDLHRIRRKRYEPFFSRLSVSRIEPIIVDEAKLLAKQLEASSKTGRVIELEHVMSAFTGDVITTLCSEKSPDMIRHPEFGKGWHTSLYNFPSCFRAGAFNSFLEYSTDHINTAKREMLSVDKLEQNNKSSVFRYVLSTDMPQAERDTERLAREAALLFGAGSVTTTRFFSVTIYYTLRNR... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid . The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dim... |
Q6ZH45 | MRVLPLALAAAIFSGVTAILVYLSGLSSYGGARVSDADLAALGALQSGFSKCVDANGLGLKAIPGEDYCRVVIQYPSDTDSKWKDPKTGEPEGLSFEFNLCEAVASWEQVRNSTTILTKEYIDALPNGWEEYAWRRINKGIHLNKCQNRTLCMEKLSLVLPETPPYVPRQFGRCAVVGNSGDLLKTKFGDEIDSYDVVIRENGAPIQNYTEYVGTKSTFRLLNRGSAKALDKVVELDETKKEALIVKTTIHDIMNQMIREIPITNPVYLMLGTSFGSSAKGTGLKALEFALSMCDSVDMYGFTVDPGYKEWTRYFSESRK... | Function: May possess sialyltransferase-like activity in vitro.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48577
Sequence Length: 439
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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A0A0P0ZEM1 | MEYKFSTVVDPGTYETHGLCEGYEVRYHKNAELEDIGCLRCQEHWRQSVGPLGAFKGTLGNPFNLLSLVIPECLPDRLSIVGFANELAFIHDDVTDIVQYGDAHNNDFKEAFNSMATTGSMENAASGKRALQAYIAREMVRIDKERAIPTIKAWAKFVDYGGRQETTRFTSEKEYTEYRIQDIGLWFWYGLLSFAMALDVPEHEREMCHEVCRTAYVQIMLVHDLASWEKEKLNAAALGKDVITNIIFVLMEEHGISEEEAKERCRETAKTLAADYLKIVEEYKARDDISLDSRKYIESWLYTISGNTVWSFICPRYNSS... | Function: Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid . The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate an... |
Q09006 | MCDSDIKVKQLEKRASGQAFELILSPPSMDAAPDLSITSPKKKECSLEEIQKKLEAAEERRKLHEAEILKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTTKMETIKENREAQIAAKLERLREKDKKVEEIRKGKECKEPSEK | Function: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules (By similarity).
PTM: Different phosphorylated forms, from unphosphorylated to highly phosphorylated, are found in the mature egg. Progressive dephosp... |
Q09005 | KREHEKEVLQKAIEENNNFSKMAEEKLTTKMEAIKENREAQMAAKLERLREKDKKLEEIRKGKECKEPSED | Function: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules (By similarity).
PTM: From unphosphorylated forms to highly phosphorylated ones in the mature egg, followed by progressive dephosphorylation from the ... |
A0A1D8PK71 | MSFQNKNLYDLLGNDVEEDAAPSAPSREVVKKNTSSKKSDAAPASADPAKAKKKKSPTGNEAALKNKNFNKDVAPPQSTATKHSKKPFDRHSRTGKTDSKKKLQQGWGQSDKRELEGEVEGTEDAEAELEAEAEENDESANAIPKKSLQEYLAELELSKQELEGSKKLRQANEGAEQKWTAEEKIEKQQEVFFASTHTKKAKSKAQKEKVFLDIDANFGDEQPQTTRGGFRGGKRGGARGGSRGGAKRGGARGAAKPEVNDKNFPSL | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradat... |
P39015 | MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradat... |
Q9UBI4 | MLGRSGYRALPLGDFDRFQQSSFGFLGSQKGCLSPERGGVGTGADVPQSWPSCLCHGLISFLGFLLLLVTFPISGWFALKIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQPPQDSPAGPNLDSTLQQLALHFLGGSMNSMAGGAPSPGPADTVEMVSEVEPPAPQVGARSSPKQPLAEGLLTALQPFLSEALVSQVGACYQFNVVL... | Function: May play a role in cholesterol transfer to late endosomes . May play a role in modulating membrane acid-sensing ion channels. Can specifically inhibit proton-gated current of ASIC1 isoform 1. Can increase inactivation speed of ASIC3. May be involved in regulation of proton sensing in dorsal root ganglions (By... |
Q9UJZ1 | MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALT... | Function: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in m... |
F1BVB6 | MSKMASSIFATFSLLSSLLPTSLASSDANYEDFLQCLDLYSQNSIPVYTRNTSSYTSILESTIKNLVFLSPTTPKPNFIVTPMQESHVQTSVICCRMHGLQMRIRSGGHDFEGLSYVSNVPFVVLDLIHLKTINVDIEENSAWVQTGATIGELYYRIAEKVGVHAFPAGLCPTVGVGGHISGAGYGVLMRKYGVSADHVIDARIVNVDGEILDRESMGEDLFWAIRGGGGASFGVILAWKIRLVPVPPTVTIFIVPKTLEEGATALLHKWQFIGDNVHEDLFIGLSMRSVIISPKGDKTILVSFIGLFLGGSDKLVQHME... | Cofactor: Binds 1 FAD per subunit in a bicovalent manner.
Function: Catalyzes the oxidation of different tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and (S)-corypalmine . Catalyzes the oxidation of (S)-coreximine and (S)-tetrahydropalmatine . Catalyzes the oxidation of different 1-benzylisoquinoline... |
Q9LT15 | MAGGAFVSEGGGGGRSYEGGVTAFVIMTCIVAAMGGLLFGYDLGISGGVTSMEEFLTKFFPQVESQMKKAKHDTAYCKFDNQMLQLFTSSLYLAALVASFMASVITRKHGRKVSMFIGGLAFLIGALFNAFAVNVSMLIIGRLLLGVGVGFANQSTPVYLSEMAPAKIRGALNIGFQMAITIGILVANLINYGTSKMAQHGWRVSLGLAAVPAVVMVIGSFILPDTPNSMLERGKNEEAKQMLKKIRGADNVDHEFQDLIDAVEAAKKVENPWKNIMESKYRPALIFCSAIPFFQQITGINVIMFYAPVLFKTLGFGDDA... | Function: Hexose-H(+) symporter that catalyzes the high-affinity uptake of glucose, galactose and mannose . Proton-coupled symporter responsible for the uptake of glucose from the apoplast into the cells (Probable).
Catalytic Activity: D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in)
Location Topology: Multi-pass ... |
O65413 | MPSVGIVIGDGKKEYPGKLTLYVTVTCIVAAMGGLIFGYDIGISGGVTTMDSFQQKFFPSVYEKQKKDHDSNQYCRFDSVSLTLFTSSLYLAALCSSLVASYVTRQFGRKISMLLGGVLFCAGALLNGFATAVWMLIVGRLLLGFGIGFTNQSVPLYLSEMAPYKYRGALNIGFQLSITIGILVANVLNFFFSKISWGWRLSLGGAVVPALIITVGSLILPDTPNSMIERGQFRLAEAKLRKIRGVDDIDDEINDLIIASEASKLVEHPWRNLLQRKYRPHLTMAILIPAFQQLTGINVIMFYAPVLFQTIGFGSDAALI... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56166
Sequence Length: 508
Subcellular Location: Membrane
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Q94AZ2 | MTGGGFATSANGVEFEAKITPIVIISCIMAATGGLMFGYDVGVSGGVTSMPDFLEKFFPVVYRKVVAGADKDSNYCKYDNQGLQLFTSSLYLAGLTATFFASYTTRTLGRRLTMLIAGVFFIIGVALNAGAQDLAMLIAGRILLGCGVGFANQAVPLFLSEIAPTRIRGGLNILFQLNVTIGILFANLVNYGTAKIKGGWGWRLSLGLAGIPALLLTVGALLVTETPNSLVERGRLDEGKAVLRRIRGTDNVEPEFADLLEASRLAKEVKHPFRNLLQRRNRPQLVIAVALQIFQQCTGINAIMFYAPVLFSTLGFGSDA... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57419
Sequence Length: 526
Subcellular Location: Cell membrane
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Q8GW61 | MAGGALTDEGGLKRAHLYEHRITSYFIFACIVGSMGGSLFGYDLGVSGGVTSMDDFLKEFFPGIYKRKQMHLNETDYCKYDNQILTLFTSSLYFAGLISTFGASYVTRIYGRRGSILVGSVSFFLGGVINAAAKNILMLILGRIFLGIGIGFGNQAVPLYLSEMAPAKIRGTVNQLFQLTTCIGILVANLINYKTEQIHPWGWRLSLGLATVPAILMFLGGLVLPETPNSLVEQGKLEKAKAVLIKVRGTNNIEAEFQDLVEASDAARAVKNPFRNLLARRNRPQLVIGAIGLPAFQQLTGMNSILFYAPVMFQSLGFGG... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55386
Sequence Length: 504
Subcellular Location: Membrane
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P23586 | MPAGGFVVGDGQKAYPGKLTPFVLFTCVVAAMGGLIFGYDIGISGGVTSMPSFLKRFFPSVYRKQQEDASTNQYCQYDSPTLTMFTSSLYLAALISSLVASTVTRKFGRRLSMLFGGILFCAGALINGFAKHVWMLIVGRILLGFGIGFANQAVPLYLSEMAPYKYRGALNIGFQLSITIGILVAEVLNYFFAKIKGGWGWRLSLGGAVVPALIITIGSLVLPDTPNSMIERGQHEEAKTKLRRIRGVDDVSQEFDDLVAASKESQSIEHPWRNLLRRKYRPHLTMAVMIPFFQQLTGINVIMFYAPVLFNTIGFTTDAS... | Function: Major hexose transporter. Mediates an active uptake of hexoses, by sugar/hydrogen symport. Can transport glucose, 3-O-methylglucose, fructose, xylose, mannose, galactose, fucose, 2-deoxyglucose and arabinose. Confers sensitivity to galactose in seedlings.
Location Topology: Multi-pass membrane protein
Sequenc... |
Q8Y678 | MHAEFRTDRGRIRHHNEDNGGVFENKDNQPIVIVADGMGGHRAGDVASEMAVRLLSDAWKETTALLTAEEIETWLRKTIQEVNKEIVLYAESEMDLNGMGTTLVAAIMAQSQVVIANVGDSRGYLLQNHVLRQLTEDHSLVHELLRTGEISKEDAMNHPRKNILLRALGVEGKVEVDTFVVPFQTSDTLLLCSDGLTNMVPETEMEEILKSKRTLSEKADVFITKANSYGGEDNITVLLVERDLTQKGRDAS | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that dephosphorylates EF-Tu.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28026
Sequence Length: 252
Subcellular Location: Cytoplasm
EC:... |
B3LFK1 | MPSTTLLFPQKHIRAIPGKIYAFFRELVSGVIISKPDLSHHYSCENATKEEGKDAADEEKTTTSLFPESNNIDRSLNGGCSVIPCSMDVSDLNTPISITLSPENRIKSEVNAKSLLGSRPEQDTGAPIKMSTGVTSSPLSPSGSTPEHSTKVLNNGEEEFICHYCDATFRIRGYLTRHIKKHAIEKAYHCPFFNSATPPDLRCHNSGGFSRRDTYKTHLKARHVLYPKGVKPQDRNKSSGHCAQCGEYFSTIENFVENHIESGDCKALPQGYTKKNEKRSGKLRKIKTSNGHSRFISTSQSVVEPKVLFNKDAVEAMTIV... | Function: Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates t... |
A0A384XLH1 | MIPNRWRDLARRDIFEPLGLNGSYFIPNAHNRAHVAVASKYSDEVDIDFLDVMACSGGQMSSLSDYIKLMQTFLDPTLPQSLLPAHIMREWMTPVFGFNDDETEVGLLWEIVKIQDSYCRPVRVYEKNGVLGASRSVFAIHREMAFGVALLNTGTATVTGNIALEIFRIMQPYLDKLQERKVKERFAGHWRLPLQTNATSGSMVDISVSDGSLWITRLVLNGTDVLSLTEAMPAFGGARSRRVALWSMRRDEFRMVLGAGAATSCMSSWTAMDSGFSRGYPMDLVYFKGGRLHIPSAGVVLVRA | Function: Beta-lactamase-like protein; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of b... |
A0A3B1EFQ1 | MPLPTRKIGQSLVSEIGFGSMGIARLGPSGFYGVVESDDERFKVLDAAHAAGCTFWDSAHLYGDSEELIGKWLKRTGKRNDIFLATKFGITPQGVRGDPDFVKEQCATSLERLGVDCIDLFYQHRVDPKTPIEITVGAMAELVKEGKVKYLGLSECSAKALRRAHAVHPIAALQIEYSPFVLDIEDPKIALLETARELGVTIVAYSPLGRGLLTGQYKSPDDFEPNDFRRTIPKFSADNFPKILDVVAQLKKIGEKHNATPGQVTLAWILAQGPEFIVIPGTKKIKYLEENVGAASIKLTEEEVAAVRKLAEESEIPGDR... | Function: Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl C... |
A0A384XR80 | MSRLLCPSSSTSVVRRARPTFVLGNLSIKQAQGTGASSALARRRRSTFAATADGLHVIPLEQKYPFPWLRDACRCPDCVHPSTRQKLFCTSDIPVDIQPATNGVEEVGEGVKIRWSNGHESLYDWDFLKEHSSSVSRSEANKDLPRVGWTRASIAKERDLYLEYEELKTKEGLRKAIDHTCRFGLLFIRNVPNVETSTASCSLRTLAHYFGDIRTTFYGELWDVKNVSNSRNIAYTNLGLGLHMDLLYFQHPPQFQFLHCLRNRVQGGSSIFSDALHAAETLRIQDAASYSVLTDVQVPFFYVNDGHHLYHTHPTIEVSA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis beg... |
A0A3B1EFQ2 | MAVDRKIRIAVVGGGPGGVIAALALSKSPNVEIDLYEAATAFGDIGLSLGMPWRPWRILRLLGLQGYLAALLPPDQIPKEDVTVPTIHYRKSDQAVGEDIFTCTSLSGYTRFRRSHFHAALLPHLPSNCKTYTSKRLVSYAEPSNASDPIVITFADGTTAECDVLVGADGIKSPTRASMYNYAADEAEKAGRSAEANDLRSKIRAKFSGVEVYRSVISAEQLRAAAPDHHAFRCPTQFLGKEKVRMPTYPIQSENSQFLNCALYICDYSREGEDYPEPWVTDVEAKDLRSSLPDWEPEAQAAVSCMGEVVSRWAICTLSP... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of b... |
Q0V8E7 | MSTQAAGNQTSSGATDSEDSYDSWYIDEPQGGQELQPEGLVPSCQPNVPPSLYHTCLAVLSILVLFLLAMLVRRRQLWPRCGHGRPGLPSPVDFLTGDRPRTVPAAVFMVLFSSLCLLLPTEDPLPFLSLASPPGRDGEAETSRGPWKILALLYYPALYYPLAACATVRHGAAHLLGSLLSWAHLGVQVWQRAECPESPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFGHGAATGSKGLQSSYSEEYLRTLLCQKKLKSSSHTCKRGFASQAWMYFRHSVYIPQRGFRLPLKLVLSVTLTGTAIYQVALLLLVGVV... | Function: Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1 . Retinol uptake is enhanced by LRAT, an enzyme that converts reti... |
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