ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8C428 | MSEGSAGDPGHGSSRQRAVHPENLSLGSSCFSPPVNFLQELPSYRSVARRRTNILSRDKQSGTLLKPTDSFSCQLDGGITENLNSQSIRKYALNISEKRRLRDIQETQMKYLSEWDQWKRYSSKSWKRFLEKAREMTTHLELWRKDIRSIEGKFGTGIQSYFSFLRFLVVLNLVIFLIIFMLVLLPILLTKYKITNSTFVLIPFKDMDIQCTLYPISSSGLIYFYSYIIDLLSGTGFLEETSLFYGHYTIDGVKFQSFTYDLPLAYLISTIAYLALSLLWIVKRSVEGFKINLIRSEEHFQSYCNKIFAGWDFCITNRSM... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83337
Sequence Length: 726
Subcellular Location: Membrane
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Q8IU68 | MLLPRSVSSERAPGVPEPEELWEAEMERLRGSGTPVRGLPYAMMDKRLIWQLREPAGVQTLRWQRWQRRRQTVERRLREAAQRLARGLGLWEGALYEIGGLFGTGIRSYFTFLRFLLLLNLLSLLLTASFVLLPLVWLRPPDPGPTLNLTLQCPGSRQSPPGVLRFHNQLWHVLTGRAFTNTYLFYGAYRVGPESSSVYSIRLAYLLSPLACLLLCFCGTLRRMVKGLPQKTLLGQGYQAPLSAKVFSSWDFCIRVQEAATIKKHEISNEFKVELEEGRRFQLMQQQTRAQTACRLLSYLRVNVLNGLLVVGAISAIFWA... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81641
Sequence Length: 726
Subcellular Location: Endoplasmic reticulum membrane
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Q7TN58 | MFRQWSVQSGPAPRRPESQAASEELWEQEVERLCASRTPVRMLPYAMADKRFIRELREPEGVKTTFWQRWHRPRRVARQHLREAEQRLARGFGLWEGALYEIGGLFGTGIQSYFTFLRFLLLLNLLTMLLTACFVLLPLVWLRPPELGPALKLRLQCSSSPLPQSDIPRFHNPLWNILTGRAFNNTYLFYGAYRAGPESSSEYSIRLAYLLSPMVCLLLCFCGILQRMAEGLPQQTLLGQRYRTPLSAKVFSSWDFCIRVWEAATIKKHEISNELKMELEEGRRVELAQQQTRAQKACRLLTYLRTNILIVLLVVGAISA... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82329
Sequence Length: 722
Subcellular Location: Endoplasmic reticulum membrane
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A3DF04 | MKVLGLIVEYNPFHNGHLYHLEESKKISGADFVVCVMSGNFIQRGEPAIVNKWARTKMALSAGADLVIELPLSCAMASAEYFASGAVRILNDIGIVDYICFGSEHGDVKTLDYIAQILVEEPESYKSFLKEELDNGLSYPAARESALKKYTAHSINIPQIISSSNNILGIEYLKALRRIKSSIIPLTIKRINNDYNTENITGSISSASSIRKYISTSNSTSFDDVLAMTMPKTSVDILFEEFSAGRGPVFKEDFYPVVTSLIRKMTPEQIRNFAYVSEGLENRIKSAADTAGTYEELVESICTRRYTKTRVQRILMGILM... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
C4Z916 | MKVAGVITEYNPFHNGHKYQLEQIKRQTSADYIVVVMSGDFVQRGEPAIIDKYERTRMALLSGADLVLELPSVFATASAEFFAGGGVSVLKNTGVVDMLCYGVESVDHELTKLVAGVLKNPPSEYSASLARLIQGGMSFPAARSRALCEYFRDTYDSASEKLDAFIASPNNILAIEYEKALMDCDITGFPIQRVGEGYHSTDSTSEFSSATAVRGVISTLIDIDKHNTITNMQLDNSWISTKFSQLIPSACADILVNCILGGHIVFPDDISEMLYYRLLTGKDKGFAQYADCTKELSAKIVKNIYKYEGFTQFCNLLKSK... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
Q5WFF2 | MRALGLVVEYNPFHNGHLHHLTQAKQQTGADVVVAVMSGTFLQRGEPALLSRWYRAEMALAAGADLVVELPYAYSVQTAERFAEGAVTILAALRCSVLNFGSEKGEIAPFYALAEFMNDHQVAFNHHVKQFLKDGVSYPKASAQAFSMLSGHEKLLPLDQPNNILGYHYVKAIQRLGISMEATTTLRIQAGYHDKEFAGPIASATAIRKALLSGENIETAVPAHTARLIQMYKRRYRLLHTWEHYFPFLQHKVLTTPLAELAKTAECSEGLEHRLRDSLFSASSFQGWLSATKSKRYTQTRLQRLFAHLLTGTTAEENAA... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
Q5E971 | MSGSSGPQAQRGPCPFALLLLLLLGPSSVLAISFHLPVNSRKCLREEIHKDLLVTGAYEITDQSGGAGGLRTHLKITDSAGHILYSKEDATKGKFAFTTEDYDMFEVCFESKGTGRIPDQLVILDMKHGVEAKNYEEIAKVEKLKPLEVELRRLEDLSESIVNDFAYMKKREEEMRDTNESTNTRVLYFSIFSMFCLIGLATWQVFYLRRFFKAKKLIE | Function: Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi. The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes.... |
Q6FRZ3 | MKFLLLLLLAPFISALRFDLKAESKPEQMCIRDFVSEGELVVINIDTDGSLNDGNVLNLYVHDSNGNEYRRLKNFVGEQRIAFTAPATTSFDVCFENTLDSNRGNRNAKRAIELDIESGSQARDWNKISATEKLRPIELELRKIEELTDEIVDELNYLKNREERLRNTNESTNERVRNFSVLVIIVLTSLGAWQVNYLKNYFKSKHII | Function: Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (By similarity).
Location Topology: Single-pass type I membrane protein
Se... |
P0CN72 | MILRIPSLLYLFTLLTAVYAVKFDLTSDRNPKPKCIWNFASAHSLVIVTANVPGEPDQQVDIQILDGSERGNVYLSKKDVRGEARLAVTTHESADVGVCLTNRYTGSGNPRVVRSVELDVDIGADAIDYNAIANQESLSILEVEMRKLEAVTKEIVEEMGYLQRREMRMRDTNESTNQRVKVFSVLIICCTIGLGVWQLLHLRSFFKRKYLID | Function: Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (By similarity).
Location Topology: Single-pass type I membrane protein
Se... |
Q769F9 | MMNNKLLLLVIALLCIASNSIVESFSFKVSAKVEECIYEEIGVDLSFTAMFQVIQGGFNDIDFTIISPDKRIVYSGQRESEGTKTLRSSFAGVYSFCFSNKMSSLTDKTVSFILSVGESSPIREIAKKKDLTPIERSIMTLSDGVIAVKNEQNYFKMREAAHRNTAESTNSRVLWWSVFEAFVLIALSIWQIYYLRRFFEVKRAV | Function: Could have a role in the budding of coatomer-coated and other species of coated vesicles.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 23297
Sequence Length: 205
Subcellular Location: Cytoplasmic vesicle membrane
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B4JYU5 | MLKSLLCILLIFGCLCRIHGVMFHLTPNTQKCLKEDIQANQLVMGEYEVSDVPGQIIDYIARDTKGHILSQKEHITKGKFSFTSEVFDAYEICFISKVPPHQRGISQEVSLVTKKGVETKNYEGIGEASKLKPLEVDLKRLEDLSDSIVRDFAVMRKREEEMRDTNEKTNSRVLFFSIFSMCCLLGLATWQVLYLRRYFKAKKLIE | Function: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 23734... |
Q8SXY6 | MARAAFIVCLLMACAWSSHAVMFKLSPNTQKCLKEDIQANQLVMGEFEVSDVPGQIIDYIARDTKGHILSQKEHITKGKFSFMSEVYDTYEICFISKVPAHQRGVIQEVSLLTKKGVETKSYEGIGEASKLKPLEVDLKRLEDLSDSIVRDFVLMRKREEEMRDTNEKTNSRVLFFSIFSMCCLLGLATWQVLYLRRYFKAKKLIE | Function: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 23692
Sequence Length... |
P49755 | MSGLSGPPARRGPFPLALLLLFLLGPRLVLAISFHLPINSRKCLREEIHKDLLVTGAYEISDQSGGAGGLRSHLKITDSAGHILYSKEDATKGKFAFTTEDYDMFEVCFESKGTGRIPDQLVILDMKHGVEAKNYEEIAKVEKLKPLEVELRRLEDLSESIVNDFAYMKKREEEMRDTNESTNTRVLYFSIFSMFCLIGLATWQVFYLRRFFKAKKLIE | Function: Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi . The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes... |
Q6PFT6 | MASSVSGAEEVRVSALTPLKLVGLVCVFLALCLDVGAVLSPAWVTADDQYHLSLWKSCSKPAASATWRCNSTLGTDWQIATLALLLGGAFLILLSFLVALVSVCIRSRRRFYRPVAIMLFAAVVLQACCLVLYPIKFIETISLRIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY | Function: Regulates cell junction organization in epithelial cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19947
Sequence Length: 181
Subcellular Location: Membrane
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Q9BQJ4 | MASAGSGMEEVRVSVLTPLKLVGLVCIFLALCLDLGAVLSPAWVTADHQYYLSLWESCRKPASLDIWHCESTLSSDWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQVCSLVLYPIKFIETVSLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY | Function: Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B. During podocyte differentiati... |
Q9JJG6 | MASAGSGMEEVRVSVLTPLKLVGLVCIFLALCLDLGAVLSPAWVTADHQYYLSLWESCRKPANLDIWHCESTLGSDWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQVCSLVLYPIKFIETVSLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY | Function: Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B . During podocyte differentiat... |
Q6PBE5 | MASSASGMEEVRSSVLTPLKLVGLVCIFLALCLDIGAVLSPAWVTADNQYYLSLWESCKKAENLWICDSTLESDWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQVCGLVLYPIKFIETVTLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY | Function: Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19783
Sequence Length: 179
Subcellular Location: Membrane
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Q2TBP5 | MASAQLDYTIEIPDQPCRSQENSPDQGGKEAGTRLPLVILLGWGGCSDKNLAKYSAIYHKRGCIVIRYTAPWHMVFFSETLGIPSLRVLAQKLLELLFDYEVEKEPLLFHVFSNAGVMLYRYVLELLQTHQRFCHLRVVGTIFDSGPGDSNLLGALRALAVVLEHRPAALRLLLLVAFTLVAFLFHVLLAPLTALFHTHFYDRLLDAASRWPELYLYSRADEVVLARDVERMVEARLAHQVLVRSVDFVSSAHVSHLRDYPTYYTTLCINFMHSCVHCSGPCPPHLTSAPEINA | Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD1/5/9 proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33161
Sequence Length: ... |
Q6DHN0 | MGDDDLDYNIVFSEALISEKHWRGSKEPVVILLGWAGSRDKHLAKYSSIYNEQGCTTLRYTAPLKTVFISESLGYKELRSTAHKLLELLYDYEVENNPIFFHVFSNGGFMLYRYMVELLHSHKQFSTLCVVGTVVDSAPGSQNVVGALRALKTTLGPKVNVLLQYFLLALFAVAVFLLRIVLYPLTKYFHRNHYDAMMEHPAPWPQMYLYSRADRVIRYRDVEKMVKGLQEKGLMVESFDFITPAHVSLFRDCPEDYSNRCRTFLSHCMTTSEEILMKKHH | Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32512
Sequence Length: 281
S... |
Q9D0Z3 | MASAELDYSIEIPDQPCWSQKNRQGGKEAGKQQPVVILLGWGGCRDKNLAKYSAIYHKRGCIVIRYTAPWHMVFFSESLGIPSLRVIAQKLLELLFDYEIEREPLLFHVFSNAGVMLYRYVLELLQTHQRFRHLHVVGTIFDSGPGDSNLIGALRALATILERRPAVLRLLLLAAFALVVILFHFLLAPFTALFHTHFYDRLQDSGSCWPELYLYSRADKVVSARDVERMVEARLAHQVMVRGVDFVSSAHVSHLRDYPTYYTSLCVDFMHNCVQC | Function: Negatively regulates bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD1/5/9 proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31589
Sequence Length: 276
Subcellular Location: Nucleus outer membr... |
Q5U405 | MDRGSHRNSSPARTPPQASPARTSPARAPPQASPARTPPQASPARTPPQASPARAPPPQASPARASPARAPPSRSSSGRSSSARSASTTSSPTRVYLVRATPVGAVPIRASPARSAPATRATRESPGLSFPKFSWQETQRQLPLIGCVILLISLVISLILLFYFWRGHTGIKYKEPLESCPIHAVRCDGVVDCKMKSDELGCVRFDWDKSLLKVYSGSSGEWLPVCSSSWNDTDSKRTCQQLGFDSAYRTTEVAHRDITSSFLLSEYNTTIQESLYRSQCSSRRYVSLQCSHCGLRAMTGRIVGGALTSESKWPWQVSLH... | Function: Serine protease (By similarity). Cleaves the proform of PRSS8/prostasin to form the active protein (By similarity). Cleaves the proform of HGF to form the active protein which promotes MAPK signaling (By similarity). Promotes the formation of the stratum corneum and subsequently the epidermal barrier in embry... |
Q58167 | MVLNINSFYKNCRGEFMRAVFIYHKNNQRMEKFYKNLLNEPDFCRICDDCYNCRGNWTFKNNVKNIVIEEVYEEFVDNPYDYLPELPEGDICIAQLHEDLLYELPLLLKEKGYKALIVPSETPHDLSLALRRDLKRVCSNYNIEFENPKPFCSLEKKEGNEYINKFIDYFKIGKPELEIEVENGLIKDVKVKISAPCGETYYIAKRLKGKAIDDLKEEIANAHHNYPCLASMEMDKELGDTILHKAGYIAFEVVEKALKK | Function: Is able to catalyze the biosynthesis of dTMP using dUMP, tetrahydrofolate and formaldehyde in vitro, i.e. a reaction equivalent to that catalyzed by bacterial thymidylate synthases (EC 2.1.1.45). However, M.jannaschii like most methanogenic Archaea lacks folates, thus the physiological cosubstrate is unknown ... |
Q8XB34 | MENFKHLPEPFRIRVIEPVKRTTRAYREEAIIKSGMNPFLLDSEDVFIDLLTDSGTGAVTQSMQAAMMRGDEAYSGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQEKGLDRSKMVAFSNYFFDTTQGHSQINGCTVRNVYIKEAFDTGVRYDFKGNFDLEGLERGIEEVGPNNVPYIVATITSNSAGGQPVSLANLKAMYSIAKKYDIPVVMDSARFAENAYFIKQREAEYKDWTIEQITRETYKYADMLAMSAKKDAMVPMGGLLCMKDDSFFDVYTECRTLCVVQEGFPTYGGLEGGAMERLAV... | Catalytic Activity: H2O + L-tryptophan = indole + NH4(+) + pyruvate
Sequence Mass (Da): 52789
Sequence Length: 471
Pathway: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1.
EC: 4.1.99.1
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Q8JFG3 | MGAYTTAPCDLEMGPEERTVVLIEKKSSTGWMWKVSVALLIAALCFAGVLLFAWYWNGKPEILIHSGQSEALTKKDHAEKTDPHSTLKRISSKAKAAIHLEGSYDEDEGLKDQVEWKNGQGQAFAQGGFRLVDNKIVIPHTGLYFVYSQASFRVSCSDGDEEGAGRHLTPLSHRISRYSESMGSDVSLMSAVRSACQNTAQEDSYSDGRGWYNTIYLGAVFQLNRGDKLETETNQLSELETDEGKTFFGVFAL | Function: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27978
Sequence Length: 253
Subcellular Location: Membrane
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P13453 | MSIQRLGYLGFEVADVRSWRTFATTRLGMMEASASETEATFRIDSRAWRLSVSRGPADDYLFAGFEVDSEQGLQEVKESLQAHGVTVKVEGGELIAKRGVLGLISCTDPFGNRVEIYYGATELFERPFASPTGVSGFQTGDQGLGHYVLSVADVDAALAFYTKALGFQLADVIDWTIGDGLSVTLYFLYCNGRHHSFAFAKLPGSKRLHHFMLQANGMDDVGLAYDKFDAERAVVMSLGRHTNDHMISFYGATPSGFAVEYGWGAREVTRHWSVVRYDRISIWGHKFQAPA | Catalytic Activity: 3-methylcatechol + O2 = 2-hydroxy-6-oxo-2,4-heptadienoate + H(+)
Sequence Mass (Da): 32209
Sequence Length: 291
Pathway: Xenobiotic degradation; toluene degradation.
EC: 1.13.11.-
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P23149 | MSELDTARTGAVRKAADLLYEATRSGVAVVPVRNLIGETDLEAAYAVQEVNTQRALVAGRRLVGRKIGLTSVAVQKQLGVEQPDYGMLFADMARTEGEEIALDDVLQPKVEAEIAFVLGRDLDGDQLTVADLFRAIEFAVPAIEIVGSRITNWDIRITDTIADNASSGLYVLGSTPKRLCDFDSRQAGMVMERQGIPVSSGVGAACLGAPLNAVLWLARVMARAGRPLRTGDTVLSGALGPMVPVAGGDVFDVRIAGLGSVTAAFAKA | Function: Converts the product of 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase.
Sequence Mass (Da): 28239
Sequence Length: 268
Pathway: Xenobiotic degradation; toluene degradation.
EC: 4.2.-.-
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E0X9C7 | MSSLDRKKPQNRSKNNYYNICLKEKGSEELTCEEHARIIFDGLYEFVGLLDAHGNVLEVNQVALEGAGITLEEIRGKPFWKARWWQISKKTEATQKRLVETASSGEFVRCDVEILGKSGGREVIAVDFSLLPICNEEGSIVYLLAEGRNITDKKKAEAMLALKNQELEQSVERIRKLDNAKSDFFAKVSHELRTPLSLILGPLEAVMAAEAGRESPYWKQFEVIQRNAMTLLKQVNTLLDLAKMDARQMGLSYRRANLSQLTRTISSNFEGIAQQKSITFDTKLPVQMVAEVDCEKYERIILNLLSNAFKFTPDGGLIRC... | Function: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylates TodT via a four-step phosphorelay in response to toluene. Can also be induced by benzene and ethylbenzene.
PTM: Autophosphorylated. Activation requires a sequential transfer of a phosphate... |
A5W4E2 | MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE | Function: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to a 6-bp palindromic DNA structure in the tod promoter region.
PTM: Phosphorylated by TodS.
Sequence ... |
H2KZH5 | MSSSRHFSIPYDEDVVHSVILENTPSPPPKPPRGILRKEAPMKPQRSALKIEPARDDDKENNSQPQARSQFKAKDTMEQMQSYFKRSISVLRKSEEHFTGAEAADILTAYIETHRNEFPRDNIGRSNAVKLLEIWLESNTIQSVESHQKKFVDSERTFYRLGGDSESLYIVNTPIASRNHDDSASVSRSESSRRSNSIKRLFSPFVRRNRSNSRGRDKDKDNLKDGSSTNLKSTWSLFSSSSEKNEKKLKKAEQQLIKEEEAEVYELSLFHLLSLIDVEFLEDVALPVQDSKNNASFLSSILGKVGLGASEERLDPHQED... | Function: Involved in promoting a consistent pattern of asymmetric cell division and fate assignment, perhaps by regulating apoptosis of specific cells, including in the Q neuroblast lineage . Downstream target of MAP kinase mpk-1 .
Sequence Mass (Da): 71255
Sequence Length: 621
Domain: DEP domain is required for funct... |
O88746 | MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELAT... | Function: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By ... |
Q402F4 | MTRLPLGSSSIDIAGPTTNWWDQINESVQWQDGIFYSLCASYALVSAVALIQLIRIELRVPEYGWTTQKVFHLMNFVVNGVRAIVFGFHKQVFLFHPKVLSLAILDLPGLLFFSTFTLLVLFWAEIYHQARSLPTDKLRISYISINGAIYFIQACIWVYLWSNDNSTVEFIGKIFIAVVSFIAALGFLLYGGRLFLMLRRFPIESKGRRKKLHEVGSVTAICFTCFLISCFVVVLSAFDPDASLDVLDHPVLNLIYYLLVEILPSALVLYILRKLPPKRVSAQYHPIS | Function: Necessary for the efficient intracellular multiplication of tobamoviruses, probably being a membrane anchor promoting the formation of the replication complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32748
Sequence Length: 288
Subcellular Location: Vacuole membrane
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Q19766 | MSDTILGFNKSNVVLAAGIAGAAFLGYCIYFDHKRINAPDYKDKIRQKRRAQAGAGGMAPRRPAAAGNDAAPDVTDPSQMQRFFLQEVQLGEELMAAGNVDEGAVHIANAVMLCGESQQLLSIFQQTLSEDQFRAVVQQLPSTRERLAEMFGAKADEAENEPPMVQYLGDGPPPAQIQELIDDTDDLE | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (By similarity). Together with tomm-22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of... |
Q9DCC8 | MVGRNSAIAAGVCGALFIGYCIYFDRKRRSDPNFKNRLRERRKKQKLAKERAGLSKLPDLKDAEAVQKFFLEEIQLGEELLAQGDYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLPTISQRIVSAQSLAEDDVE | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into ... |
P35848 | MPSQAVTYTTAAVAAVATGFLAYAVYFDYKRRNDPEFRRQLRRSARRQARQEKEYAELSQQAQRQRIRQMVDEAKEEGFPTTSDEKEAYFLEQVQAGEILGQDPTKAIDASLAFYKALKVYPTPGDLISIYDKTVAKPILDILAEMIAYDPSLKIGTNYTGGVDVAELMREMASAPGVGLD | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into ... |
Q5JJI4 | MDMGAMSDPERMFFFDLACQNAKVTYEQNPHDADNLTRWGGALLELSQMRNGPESLKCLEDAESKLEEALKIDPMKADALWCLGNAQTSHGFFTSDTVKANEFFEKATQCFQKAVDVEPANDLYRKSLDLSSKAPELHMEIHRQMASQASQAASSTSNTRQSRKKKKDSDFWYDVFGWVVLGVGMVVWVGLAKSNAPPQAPR | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into ... |
O14225 | MRRSVIIGSLLATAAVGYAIYFDYKRRNDPHFRKTLKRRYKKVHEAKKQEEKLATKKFDITVEEALQVVASTPVPSSAEEKELFFMQQVARGEQLFQQQPDNIKESAACFYSALKVYPQPVELFAIYERTVPEPIMNLLRAMQAKESIPSVE | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into ... |
P92792 | MEMQSEFDRLLFFEHARKSAETTYAQNPLDADNLTRWGGALLELSQFQPVAESKQMISDATSKLEEALTVNPEKHDALWCLGNAHTSHVFLTPDMDEAKVYFEKATQCFQQAFDADPSNDLYRKSLEVTAKAPELHMEIHRHGPMQQTMAAEPSTSTSTKSSKKTKSSDLKYDIFGWVILAVGIVAWVGFAKSNMPPPPPPPPQ | Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into ... |
P35180 | MSQSNPILRGLAITTAIAALSATGYAIYFDYQRRNSPQFRKVLRQRAKEQAKMEEQAKTHAKEVKLQKVTEFLSMELAKDPIPSDPSEREATFTTNVENGERLSMQQGKELEAASKFYKALTVYPQPADLLGIYQRSIPEAIYEYIILMIAILPPANVASFVKGVVGSKAESDAVAEANDIDD | Function: Central component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitat... |
A6QPI6 | MAAAAAGPGAPLSADELLPKGDAEKPEEELEEEDDEELDETLSERLWGLTEMFPERVRSAAGATFDLSLFVAQKMYRFSRAALWIGTTSFMILVLPVVFETEKLQMEQQQQLQQRQILLGPNTGLSGGMPGALPSLPGKI | Function: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the ... |
Q9WUL0 | MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKDKDKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSDKHKDKHKDRDKEKRKEEKIRAAGDAKIKKEKENGFSSPPRIKDEPEDDGYFAPPKEDIKPLKRPRDEDDADYKPKKIKTEDIKKEKKRKLEEEEDGKLKKPKNKDKDKKVAEPDNKKKKAKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPEGVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNDEKNTITNLSKCDFTQMSQYFKAQSEARKQ... | Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... |
Q9ZDK2 | MKLVIVESPAKAKTINKYLGDEFKVIASFGHIRDLPSKKGSVLPDKNFLMEYDISDKAGKYVDAIVKEARKAEVVYLATDPDREGESISWHVAEVIKEKNKVESDDFFKRVAFNEITKKAIMNAVANPRKLDTNLVNAQQARRALDYLVGFTLSPLLWRKLPGCKSAGRVQSVALRLICDREDEIERFKSEEYWDISLKMQNSNNDLFTAKLTHVNDQKLKKFSIINEKEAKDLTQKLKLQKFYVEKIEKKQQKRQPQPPFITSSLQQEAARKLGFSAKKTMQIAQKLYEGVDIGKETIGLITYMRTDGVTLSNDAIADI... | Cofactor: Binds two Mg(2+) per subunit.
Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in dup... |
P07799 | MSSSDSDSVSLSIRRRQRRGSSKRISMKESDEESDSSENHPLSESLNKKSKSESDEDDIPIRKRRASSKKNMSNSSSKKRAKVMGNGGLKNGKKTAVVKEEEDFNEIAKPSPKHKRVSKANGSKNGAKSAVKKEESDTDDSVPLRAVSTVSLTPYKSELPSGASTTQNRSPNDEEDEDEDYKWWTSENIDDTQKWTTLEHNGVIFAPPYEPLPKNVKLIYDGNPVNLPPEAEEVAGFYAAMLETDHAKNPVFQDNFFRDFLKVCDECNFNHNIKEFSKCDFTQMFHHFEQKREEKKSMPKEQKKAIKQKKDEEEEKYKWC... | Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... |
Q2FHI8 | MADNLVIVESPAKAKTIEKYLGKKYKVIASMGHVRDLPRSQMGVDTEDNYEPKYITIRGKGPVVKELKKHAKKAKNVFLASDPDREGEAIAWHLSKILELEDSKENRVVFNEITKDAVKESFKNPREIEMNLVDAQQARRILDRLVGYNISPVLWKKVKKGLSAGRVQSVALRLVIDRENEIRNFKPEEYWTIEGEFRYKKSKFNAKFLHYKNKPFKLKTKKDVEKITAALDGDQFEITNVTKKEKTRNPANPFTTSTLQQEAARKLNFKARKTMMVAQQLYEGIDLKKQGTIGLITYMRTDSTRISDTAKVEAKQYITD... | Cofactor: Binds two Mg(2+) per subunit.
Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in dup... |
Q5JH81 | MAEANQLFKEFKIQSVSEFFRRNAAMLGYTGKVRSLTTLVHEAVTNSLDACEEAGIPPYVRVEIEELGNEHYKVVVEDNGPGIPEKYITHVFGKMLAGTKAHRNIQSRGQQGIGISGAVMFAQITSGKATRVITSTGNDEIIEAWVKIDVDKNEGKIVKKEKHPNPKGWRGTRIELEVKNVKYMRSKQGVFWYLKLTAIANPHAHIELIEPDGKLIVFPRSSDYIPEPPVEMKPHPKGVLTDDVYRLAKKTRRNTVRRFLIGEFSRISDKKVDELIEYIAALRLIKTVEDKKLQEQYYQKLMEGHVKAVLRAFKGYTKVV... | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 64233
Sequence Length: 567
EC: 5.6.2.2
|
P84093 | GNCIELNNDCDGSKDDCQCCRDNAYCSCYNFFGIKSGCKCSVGNSGTGYSVCLKKLECPNRRAWTSWKKECTKPCIGKRC | Function: Omega-agatoxin are antagonists of voltage-gated calcium channels (Cav). Induces rapid general flaccid paralysis followed by death when injected into the cerebral ventricle of mice at dose levels of 3 ug per mouse.
Sequence Mass (Da): 8869
Sequence Length: 80
Domain: The presence of a 'disulfide through disulf... |
Q6DHU8 | MEASKESPSAFKTPCKPAKVKSPVNACGTPVTIPASPFMKKLGCGTGVNVYLMNRMGKQTHSPWAIKKINSKCAQGQVSVYQKRLCEEAKILKDLKHPNIVGFRAFTTAKDGSKCLAMEFGGEQSLNDLIEKRREEGLQAFPVDTIEKVALHVARGLLYLHNEKKLLHGDMKSCNVVIKGDFESIKICDVGVSLPLDENMQVSDPKAHYIGTEPWKPKEALEDGVITDKADIFAYGLTLWEMMTLSVPHLEMLDTEGDEDDDDESFEEDFDEDAYYERLGSRPALDAVTLGGSYQRMVELFCLCTEEDPQKRPSAAHIVQ... | PTM: Phosphorylated; in a cell-cycle dependent manner at mitosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 37664
Sequence Length: 339
EC: 2.7.12.2
|
Q96KB5 | MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALET... | Function: Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.
PTM: Phosphorylated; in a cell-... |
P09176 | MIKNEIKILSDIEHIKKRSGMYIGSSANETHERFMFGKWESVQYVPGLVKLIDEIIDNSVDEGIRTKFKFANKINVTIKNNQVTVEDNGRGIPQAMVKTPTGEEIPGPVAAWTIPKAGGNFGDDKERVTGGMNGVGSSLTNIFSVMFVGETGDGQNNIVVRCSNGMENKSWEDIPGKWKGTRVTFIPDFMSFETNELSQVYLDITLDRLQTLAVVYPDIQFTFNGKKVQGNFKKYARQYDEHAIVQEQENCSIAVGRSPDGFRQLTYVNNIHTKNGGHHIDCAMDDICEDLIPQIKRKFKIDVTKARVKECLTIVMFVRD... | Function: Large subunit of the DNA topoisomerase that untwists superhelical DNA. Controls of topological states of double-stranded DNA by transient breakage and subsequent rejoining of DNA strands.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 57977
Sequen... |
A0QPN1 | MTATLDVPEQNPDLVLDQSADDYWNHYQLTFALYSVSDRAIPSAYDGLKPGQRRLLYQMHDSKLLPGNKPQKSSKVCSAVTGNLHPHGGASMYGAAALMAADFQRVKVIDGQGAFPRIQGDIPAADRYTEMRLSAPGAALTAELNDHAVPMVPTFDGEWVEPTVLPAQWPVLLCNGAVGIAEGWATKVPAHNPREVMAACRALLKTPNMTDDRLCKLIPGPDWGSGASVVGTAGLREYITTGRGHFTVRGTISVEGKNCIITELPPGVASNTVQDRIRALVESGEMSGVADMSDLTDRRNGLRIVVTAKRGHNAEQIRDQ... | Cofactor: Maximal DNA relaxation at 5.0 mM MgCl(2) .
Function: Catalyzes the relaxation of negatively supercoiled DNA in the presence of ATP or dATP but not other nucleotides. Individual subunits have no activity. Not able to negatively supercoil DNA, it can however introduce positive supercoils in DNA. Relaxes positiv... |
A0QPN2 | MSDPASTIPPAHHPTFWRERAVSYTAADITELDDVQHTRLRPAVNLGLDVLNTALREIVDNAIEEVADPGHGGSTVTITLHADGSVSVADDGRGLPVDTDPTTGKNGIVKTLGTARAGGKFSAHKDATSTGAGLNGIGAAAAVFISARTDVTVRRDGKTFLQSFGRGYPGVFEGKEFDPEAPFTRNDTQKLRGVSNRKPDLHGTEVRILFDPAIAPDSTLDIGEVLLRAHAAARMSPGVHLVVVDEGWPGEEVPPAVLEPFSGPWGTDTLLDLMCTAAGTPLPEVRAVVEGRGEYTTGRGPTPFRWSLTAGPAEPATVAA... | Cofactor: Maximal DNA relaxation at 5.0 mM MgCl(2).
Function: Catalyzes the relaxation of negatively supercoiled DNA in the presence of ATP or dATP but not other nucleotides. Individual subunits have no activity. Not able to negatively supercoil DNA, it can however introduce positive supercoils in DNA. Relaxes positive... |
Q5R7J8 | MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTALVEKEGIHVLDWPFDDGAPPSNQIVDGWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ | Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues (By similarity).
PTM: Farnesylated. Farnesylation is required for membrane targeting (By similarity).
Location Topology: Lipid... |
Q12974 | MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ | Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.
PTM: Farnesylated. Farnesylation is required for membrane targeting and for interaction ... |
O75365 | MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM | Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in respons... |
Q9D658 | MARMNRPAPVEVSYRHMRFLITHNPSNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM | Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in respons... |
Q54DU9 | MTGIRSALPNPASLVESSTHRFLIFDAPNDDNLPLYINELKKYNVSHLVRACDPTYSTEPLQAIGIQVHDMPFADGGSPPDAVVNNWIKILGESYKKDSKETIGIHCVAGLGRAPVLVAIALIEGGMNPLQAVEYIRERRRGSINIKQIQYLKNYKSKKKSSCRIM | Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 18422
Sequence Length: 166
Subcellular Location: Membrane
EC: 3.1.3.48
|
Q86IL4 | MDPGRSHIETIIESSTHKFILFDEPTEETIPYFKDLMKKNSCINIVRCCEINYDASLFEGVKIHELCFKDGNVPPKDIIERWLEILKQAFIENGKQKTTVGIHCIAGLGRTPLLVCIALIEDGMKPLQAVEFVRSKRKNAINSPQIKFLKEYKASKKAGCKIM | Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 18542
Sequence Length: 163
Subcellular Location: Membrane
EC: 3.1.3.48
|
Q8TEL6 | MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLKLHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQ... | Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control . The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway . The DesCEND ... |
Q9JLV2 | MAAAPAAAGAGASRGRRLAATAAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKLSKWSGIPQLLLKLYATSHLHSDFVECQSILKEISPLLSMEAMAFVTEDRKFTQEATYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQ... | Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway. The DesCEND (d... |
A5FXW5 | MPQLIAGNWKMNGTLAGIAAYAAALRPASPGAELLVCPPAPLIAPLRAALDGAPVALGAQDCAVKRSGAHTGDLSADLLAELGATHVILGHSERRADHAESSATVREKARTAIAAGLVPIICVGETEAERDSGEAETVVRAQLAGSLPEELAGQTVPGVVAPGIIAYEPVWAIGTGRTPTEEDVAAMHASIRAALRRQLGAAGATMPILYGGSVKPSNAASLLALPEVGGALVGGASLKAEDFLAIASAAARD | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 25333
Sequence Length: 253
Pathway: Carbohydrate biosynthes... |
Q9YBR1 | MKPVLAVNMKTYSSAFGEGARRLARDAARVAREVDVRVILVAPLINASSLAGVYGDVYIQHADPVDLGAHTGYTPVEAAAAEGLRGVMVNHSEHKVTYRHLQAVVSKARSLGLEVLACADTPEEAAAAALLRPSMVALEPPELIGTGIPVSQAKPEVITRGVEAVARVAPGVAVLAGAGITAGEDARRAVELGAQGVLVASAVMKAKDPHGKMLELAEAMAKP | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 23020
Sequence Length: 223
Pathway: Carbohydrate biosynthes... |
B6JFZ2 | MPGKIRPLIAGNWKMNGLKASLGELAAIGKGAGEVWRRVDLLICPPATLIFPAAAAMIGSKVAIGGQDCHAEASGANTGDISAEMLADAGATYVIVGHSERRTDHGETDAVVRAKAEAAWRAGLVAIVCVGETRAERDAGRAAEVVGRQLDGSVPDGARAANLVVAYEPVWAIGTGLTPTSQDIEEIHAVIRQNLTGRFKAEGEGVRLLYGGSLKPANAAEILALANVNGGLIGGASLKAADFLAIAEACP | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 25678
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
Q2GGH7 | MSLLIVANWKMYGDFLTFSSFTKELSANLVNVKADVEVVLCPPFIACSKIVDCAPNIKLGAQNCFYESEGKYTGEVSAKMLYSCGCSYVIVGHYERRSIFYESDYCVQLKAKSAIDAGLIPIICIGETLLDRENGMLKNALLDQCYNSFPKHGEFVIAYEPVWAIGSNTIPSIDMITESLDIIRSYDSKSNIIYGGAVNQSNIKDVIAINQLSGVLVGSASLKVSSFCDIIYGAVNVRQN | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26330
Sequence Length: 240
Pathway: Carbohydrate biosynthes... |
P04828 | MPRKFFVGGNFKMNGNAESTTSIIKNLNSANLDKSVEVVVSPPALYLLQAREVANKEIGVAAQNVFDKPNGAFTGEISVQQLREANIDWTILGHSERRVILKETDEFIARKTKAAIEGGLQVIFCIGETLEEREANKTIDVVTRQLNAAAKELSKEQWAKVVIAYEPVWAIGTGKVATTEQAQEVHSAIRKWLKDAISAEAAENTRIIYGGSVSEKNCKDLAKEADIDGFLVGGASLKPAFVDIVNARL | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27157
Sequence Length: 249
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
|
B4SBF7 | MRRKIVVGNWKMNNSVAESVQLATDVLAALGEGFSGCEVGIAPTYLALDATEKVIAESEVQLVAQNCHYENDGAFTGEVSARMILAVGCSSVIIGHSERRQYFGETNATVNLRIKKALSEGLNVILCVGETLAERESGVMETVISSQVREGLDGIIDISAIVIAYEPVWAIGTGKTASSAQAEEVHLFIRTLVTGLYGQTASEKVRIQYGGSVKPSNAAELFAMPNIDGGLIGGASLNADDFAAIVKAASV | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26425
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
P48495 | MGRKFFVGGNWKCNGTAEEVKKILATLNAADVPSQDVVEVVVSPPYVFLPLVKNELRPDFHVAAQNCWVKKGGAFTGEVSAEMLVNLSIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEERESGSTMDVVAAQTKAIADRVKDWTNVVVAYEPVWAIGTGKVASPAQAQEVHAELRKWLAANVSPEVAASTRIIYGGSVNGANCKELGGQPDVDGFLVGGASLKPEFIDIIKAAEVKRNA | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27132
Sequence Length: 254
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
Q29371 | MAPARKFFVGGNWKMNGRKNNLGELINTLNAAKLPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVANGAFTGEIGPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWNKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVPEAVAHSTRIIYGGSVTGATCKELASQPDVDGFRVSGASLKPEFVDIINAK | Function: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (... |
P81666 | TFDVCYEQLFFVGGNWK | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 2053
Sequence Length: 17
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
Q7KQM0 | MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM | Function: Catalyzes the interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic and gluconeogenic pathways.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27935
Sequence Length: 248
Pathway: Carbohydrate biosynthesis; gluconeogene... |
P85814 | MAATSLTAPPSFSGLRASRAVVAMAGTGKGGAFTGEISVEQLKDIGRWVILGHSERIVVAYEPVWAIGTGKVATPDQAQEVHGLCR | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 8935
Sequence Length: 86
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
|
A4SXQ5 | MRPLIVIGNWKMNGNLASNQDWVKTVARGMESGMPAGRKFAVCPSFPYLSQCSTLIKEHSLAFLSLGAQDVSAHGAGAYTGEVGASMLKEMGCEYVIVGHSERRQMHQEADESVAAKALQALDSGMTPVICVGETADERNSGRAEEIVCSQVAKQVSVLQDRLADCLIAYEPVWAIGTGKVASAQVAQDMHRAIRMQLAEFDEDVASHVGILYGGSVKPDNAVELFAMPDIDGGLVGGASLNPQDFLAICQA | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26816
Sequence Length: 252
Pathway: Carbohydrate biosynthes... |
B2RII9 | MRKNIVAGNWKMNKTLQEGLALAKELDAALKGRTISCDVIIGTPFIHLASIAAAIDTTRIGVAAENCADKESGAYTGEVSAAMVASTGARYVIIGHSERRAYYHETSPILMEKVKLALSNGLTPIFCVGEVLEEREAGKHFEVVARQVEEALFTLDQTDFAKLILAYEPVWAIGTGKTATADQAQEMHAHIRKSIAAKYGKEVANGCSILYGGSCNAANAKELFSRADVDGGLIGGASLSVDKFLPIIEAF | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26793
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
Q978V5 | MFTVIVNLKNYAEANGKNFVEFVSKLPKYDSVRLIIAPAILDLHNAHEFRNVEFFSQHVDDVGYGPYTGHIAIESLMNYGIIGSLLNHSERRLGEDKIISTVKKAQMLGFEIALCVESMEEAKRYSALKPSFIAYEPKELIGGNVSVSTAKPEIISEIVDICGTEGVPVLVGAGIKNRQDVRKSLDLGAQGILVSSGVVKSPDPVRSLNSLIK | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 23290
Sequence Length: 213
Pathway: Carbohydrate biosynthes... |
B5YL53 | MPKKFIVANWKMHKTVREALAFLDEFIPITKGLNGREIGIAPTFICIESVGKVLINTSIKLCAQNAFYENKGAYTGEVSPAMLKDCGVEYVIIGHSERRKYFYENDDIINKKIHACIKEGLKVIFCIGETFEDRQNNKTMEILKTQIRNGLLEINSPEALTIAYEPVWAIGTGVVATEEQIKQSHLFIRNQLKEIYGERANEVRILYGGSVTPENIKSIMAIDNVEGVLVGGASLDPLKFAKIVKY | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27602
Sequence Length: 246
Pathway: Carbohydrate biosynthes... |
O83548 | MRGYFIAGNWKMHKTCAEAVALAQELVRELRGGPHTYMIAPSFTALDAVGKVLRGSNVLLGAQDVSSEEWGAHTGEVSVLQLEDLGVQVVIVGHSERRHGRGENDKLINQKVRRVLESGLRVILCVGERLQEYEAGCTNEVVGTQVRAGMADVCGSLMHNVTVAYEPVWAIGTGKTATPAQANAVHAHIRSVVREMYGAAIAEALCIQYGGSMKAENARALLAEEHIDGGLIGGASLEAASFVPIARSV | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26540
Sequence Length: 249
Pathway: Carbohydrate biosynthes... |
Q83GI1 | MLPKRAYPVQDSNVHSQEKKIIAGNWKMNINHSQAVSYLQELNWRLIDNGHDFDSCEIAVFPPFTDLRSVQTLVASDDIQISYGAQDVSAFSDGAHTGQISAQFLKDLDCKYVLIGHSEQRCLPCYPGNNSAINELNNKHDGLIANKLLRSFAAGICPILCIGDISPGDHFDATLSRFRSVLSHLKAISDKKHSIGYALGSKTHFLDSDQLHMLVAYEPSSAINSGNCANSGDIVRMAAAIKDIVNVRVLYGGGVNLFNASAVFNEDLLDGILVGRASLNASDFASLIKTCCL | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 31858
Sequence Length: 293
Pathway: Carbohydrate biosynthes... |
P04789 | MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26835
Sequence Length: 250
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Glycosome
EC: 5.3.1.1
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B1AIG9 | MKYIIANFKMNATQELINHFLNNLTLFDEQKIIIGLAPGDLYLKTFVNLAEIKKVNLYAQNPSLHNKGPYTGQISCLQLLDINIKNALVGHSEIRIDFSQSIIDQKIKISMDLLEQVIICVGETFDAYKQNKSLNFVLNQLANIINYKGLKKIIIAYEPIWAIGTDLELDFKHINYMIEGIKTYLYNCTGINIPILYGGSVNDNNINELCNQKLIDGFLIGNASLDVNVFNKIIDKCK | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26978
Sequence Length: 238
Pathway: Carbohydrate biosynthes... |
Q9KNR1 | MRRPVVMGNWKLNGSKAMVTDLLNGLNAELEGVEGVDVVVAPPAMYLDLAERLIKEGGNKLILGAQNTDTHNSGAYTGDMSPAMLKDFGASHIIIGHSERRDYHKESDEFVAKKFAFLKENGLTPVFCIGETEAQNEAGETEAVCARQINAVIDAYGVEALNGAIIAYEPIWAIGTGKAATADDAQRIHASIRALIAAKDAAVAEQVIIQYGGSVKPENAASYFAQPDIDGALVGGASLDAKGFAAIAKAAAEAKKA | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27001
Sequence Length: 257
Pathway: Carbohydrate biosynthes... |
Q56738 | MRQALVMGNWKLNATKGSVEALINGLVDAAKDNATVEVAVCPPAVFIPQVEALTADTAITYGAQDCDVNTSGAFTGENSAVMLKEFGCKYTLVGHSERRVIHGESSEVVADKFAVTPENGLVPVLCIGETLEQFEAGETKAVVEAQLQAVVTKSGITSLNNAVIGYEPVWAIGTGKTATPEIAQEIPAHIRSWLAEQDAAVANKVQILYGGSVKPANSAELFGQADIDGGLVGGASLDAVEFSKVISGASA | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26018
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
Q8EJ86 | MEPGFWHEKWQQQQIGFHQQDVNPFLVTYWHQLALPADAKIFVPLCGKSLDMCFLAEQGHQVIGCELNELAVQQFFSDNQLPMQQSAEGEHQHYQTEQISLYQGDIFTLPQSITAEVSGFYDRAALIAWPESMRAQYAKQLAYLLPQGSVGLLVTLDYPQEVLSGPPFAVSPTWVETHLSEDFEIQPLACQDVLADNPRFVKKAVPWLNEAVYLLKRR | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Sequence Mass (Da): 24894
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.1.1.67
|
Q93JT2 | MTDHDNQRWLQLWRERRTDFHQHGVNLLLSRFWPAFAPATPSRVFVPLCGKSLDMLWLAEQGHDVIGVELSPLAIEAFFRENHLPPSKRRQGRFTLWRHGRIGILCGDYFALSEADLGPVDSVYDRAALTALPPILRSRYVAQLRRIVPDTARVFLLTLEDAEADATLQQALGVDEELAALYTAGFEIALAHVESLFEPDPQNGAPRRVEHKVYQLTGKRPASPEADGRAAETED | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Sequence Mass (Da): 26502
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.67
|
C5BIS1 | MKASFWHEKWKKREIGFHESVVNPALTDHWHALSAAGGSVFVPLCGKSLDLGWLLSQGVSVIGVELSEIAVQELFVSLDIEPSVSDVENFKLYSAENIAIWVGDIFNLNKAWLGVITAIYDRAALVALPESMRLEYAGKLIELSNCATQLLVTFEYDQSLHQGPPFSVPESAVQKCYGTRYQLQCLERKAVAGGLKGRIAATESVWKLSRNINS | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Sequence Mass (Da): 23655
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.1.1.67
|
Q9KSN0 | MRDPEFWHNKWAANQIGFHLEDVNPLLIRFWSDLAPKRSEKVLVPLCGKSEDLIWLANQHDSVQGVELSQIAVRSFFAEHFYTPTVTRLNAQHELYQFDELTLFTGDFFTAPVESVDLVYDRAALVALPEEMRAEYAQRVLQLLKPGGRILLVSMDYVQTELSGPPFSVPEAEIRTLFMGCEVRRVYQDTSIDPHLNKRTQAGLSRFAEEVWVIEKSE | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Sequence Mass (Da): 25114
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.1.1.67
|
F4KFG5 | MSASQNIVVSETTMSSIIPNNNNNNNNSSSQKLPPCLISISKKKLLKNIDIINGGGQRINAWVDSMRASSPTHLKSLPSSISTQQQLNSWIMQHPSALEKFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFCASVHFRCVDEKKWSELVLQVRSVLKKFPTLQLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDEDAFK... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 41974
Sequence Length: 369
Pathw... |
Q5HZ05 | MVSQNVVVSDAKTGIITVSTVSNSSVFTPTAQKPPTAPGYISVSKKKLLKNLEINGADQSQRLNSWVDSMRASSPTHLKSLSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDED... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 41758
Sequence Length: 370
Pathw... |
Q27957 | MADSRPKPANKTPPKSPGEPAKDKAAKRLSLEAEGAGEGAAAAGAELSALEEAFRKFAVHGDARASGREMHGKNWSKLCRDCQVIDGRSVTVTDVDIVFSKIKGKSCRTITFEQFKEALEELAKKRFKDKSAEEAVREVHKLIEGKAPIISGVTKAISSPTVSRLTDTSKFTGSHKERFDPSGRGKGRAGRVDLVDESGYVPGYKHAGTYDQKVQGGK | Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (By similarity). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubul... |
O94811 | MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK | Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath . Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, a... |
Q7TQD2 | MADSKAKPAKAANKTPPKSPGDPARAAKRLSLESEGANEGATAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK | Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath . Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, a... |
F0ZDD0 | MKQHILWDLNNYINQDYTLPKINCTFDIKTNINSSVKEDQEKWILEFFGNSIEKSKKYLGQQTFLIYMFSFPFASPDELKCIFKIMDWAFIIDDFYFESKAKGMSYLEKLFKTNKDKSKDKFIKLFWEIINEYKQIGKKDSIDVLINEIYSWAKSAVQCSKNDQISSNSTLAEYMESRYYDIGIIMALASSTTLISIPKEIRESKIFKQLEYWFVVCNTLINDCYSFNKEKNEPVLTNYVKIKTLQCGSIQTSLDFVAETIENSLTEINNHSNQLIQQYPNNINLKQYIKSLKYLTSGHLHVSSICNRYK | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpenes beta-elemene, (E)-beta-farnesene and (E,E)-alpha-farnesene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate
Sequence Mass (Da): 36478
Sequence Length: 310
Domain: Contains severa... |
Q9LMI0 | MISRSYTNLLDLASGNFPVMGRERRRLPRVMTVPGNVSEFDEDQAYSVSSDNPSSVSSDRMIIVANRLPLKAEKRNGSWSFSWDQDSLYLQLKDGLPEDMEILYVGSLSVDVDSNEQDDVAQILLDKFKCVPTFFPPDLQSKFYDGFCKRQIWPLFHYMLPFSADHGGRFDRSLWEAYVATNKLFFQKVIEVINPDDDFVWIHDYHLMVLPTFLRRRFNRIRMGFFLHSPFPSSEIYRSLPVREEILKALLNSDLIGFHTFDYARHFLTCCSRMLGLEYQSKRGYIGLEYYGRTVGIKIMPVGINMGRIQSVMRYSEEEG... | PTM: Phosphorylated.
Catalytic Activity: D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP
Sequence Mass (Da): 96688
Sequence Length: 851
EC: 2.4.1.15
|
W6HUT3 | MSVSLSFAASATFGFRGGLGGFSRPAAAIKQWRCLPRIQCHSAEQSQSPLRRSGNYQPSIWTHDRIQSLTLSHTADEDDHGERIKLLKCQTNKLMEEKKGEVGEQLQLIDHLQQLGVAYHFKDEIKDTLRGFYASFEDISLQFKDNLHASALLFRLLRENGFSVSEDIFKKFKDDQKGQFEDRLQSQAEGLLSLYEASYLEKDGEELLHEAREFTTKHLKNLLEEEGSLKPGLIREQVAYALELPLNRRFQRLHTKWFIGAWQRDPTMDPALLLLAKLDFNALQNMYKRELNEVSRWWTDLGLPQKLPFFRDRLTENYLW... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Monoterpene synthase involved in the biosynthesis of volatile compounds present in floral scent . Mediates the conversion of (2E)-geranyl diphosphate (GPP) into sabinene and sub-products such as alpha-thujene, alpha-pinene, beta-pinene, myrcene, alpha-phell... |
Q5GJ59 | MATTGTTSMPAPVFHPTVWGDYFIKFVPEPLQVSDETMAERIRHLREEVSGMFQACKNVVDKTNLVDVVQRLGIDHHFEEQIATALASIHSAGLFNSSSLHEAALRFRLLRQQGFWVPADELVKFIKNEDGSFIDGITNDPKGLLSLYNAAHLVTHDEGTTTLEDAIAFARQHLEAARRCSLKSPLAEQVGRALGIPLPRTLKREEAIAFIPEYSSQQDQQVYSPVILELAKLDFNLLQHLHQEELKEISQWWKDLSGEIGLGYVRDRIVECYFWSYTVHYERGQARARMILAKVFMLTSLLDDTYDVHATLEEARELNK... | Function: Sesquiterpene synthase that catalyzes the formation of a blend of sesquiterpenes and sesquiterpenoid alcohols . Converts farnesyl diphosphate to tau-cadinol .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + tau-cadinol
Sequence Mass (Da): 62575
Sequence Length: 548
Domain: The Asp-Asp-X... |
J7LQ09 | MEARRSGNFKASIWDDDFLQSLTSPYTAKEYLKQADKLKWQVKVIIKETKQRLDQLDLIDNIQRLGISHHFRDEIQRVLQNIYEKMRVECPDRMLMEKDLYSTSLQFRLLRQHGYHVSQDVFCSFMDGAGNFQAVDDLKGILALYEASFLSREGENILGSARDFSTRHLKQKLEEITDPILAEKIRRALELPLHWRLQKLEAIWFINIYESRFDANLILLQLAKLEFNMVQAQYQEDLKWLSRWYKETGLPEKMNFARDRLAECFLWALGFIPEAHLGQARKILTKIAVLIVIMDDFYDIYGTLDEIKVFTEELQRWDIN... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene synthase converting farnesyl diphosphate to trans-alpha-bergamotene as the major product.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene + diphosphate
Sequence Mass (Da): 63549
Sequence Length: 542
Domain: The Asp-Asp-Xa... |
B9RXW0 | MKVGQPVLQCQTNSEAFGMMQERRSGNYKPNIWKYDFLQSLSSKYDEEKYKTQAERLKEDAKHLFIEAVDLQGKLELVDCIIKVGLASHFKDEIKKALDTIASSIKNDKSDAIKNRYVTALCFRLLRQHGYEVSQAKKSDFLDENGTFLKAKSMDVKGVLELFEASYLALESENILDDAKAFSTTILKDINSATTESNLYKQVVHALELPFHWRVRWFDVKWHIKTFQKDKSINKTLLDLAKVNFNVVQATLQNDLKEISRWWRNLGLIENLKFSRDRLVESFLCTVGLVFEPQYSSFRRWLTKVVIMILVIDDVYDIYG... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the cyclization of farnesyl diphosphate to (E,E)-alpha-farnesene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate
Sequence Mass (Da): 65793
Sequence Length: 564
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is ... |
G1DGI7 | MIEEMRKLLATLDDGEISPSAYDTAWVARIPSQSNATCPEFPETLEWIAHNQLPDGSWGDRNHFQIYDRVLSTVSCLVALKTWNLGHDNINKGERFLKQNIYKLTKDKGDLLCGFELIFMTMLEEAKQKGLDIPIDIPALKILQGYRQKKLQKIPLEMVHSIPTTILYSLEGLQDHINWEKILQFIGTDGSFLSSPSATACVYMHTKDPRCLEYLKGVVKKVKNSVPCQYAIDLFERLWIVDTLERLGIDRYFQPEIKNILDYVYKYWSDKKGIGWGRESYLKDIDDTSMGFRLLRLHGYKVTPDVFLNFMSSEDKFFCF... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Bifunctional diterpene synthase that directly generates the endocyclic double bond, as well as the hydroxyl group: produces an endocyclic double bond isomer of copalyl diphosphate (CPP), and carries out subsequent replacement of the diphosphate by a hydroxyl group to... |
Q54BE5 | MDYDIKFTWDKNQFLDQEIRIPKYTLPWDFKSSPFDKDFENQEMEYVKQFFQNYENAVNYVKKNEIGKIAALNFPLGEKDEYMVNSKLLDFLFILDDYIYESRNYEEDYVDNLMDRSSKSHDPFGREIWRLFDEYYRVGVKESVDLLIRDFEYWSRSAIKTNKYKSLNSSLSIEDYFNSRHGDFGMTITASSCTSTLYVENEIRESKNFKKFFKYFELCNLMINDCGSFKMEINEILLTNFVKVRAIQLGSIDLALKYCVGLLNKYIIKVDKYSTKLEQQYPNHSHLKKYIYTLKTFTAGHNKGYGHANRYN | Function: Terpene synthase; part of the gene cluster that mediates the biosynthesis of the trisnorsesquiterpene discodiene which has a function during later stages of multicellular development, during the transition from fingers to Mexican hats . The terpene synthase tps8 converts its substrate farnesyl diphosphate (FD... |
F0ZHE2 | MQEEILYKWNYDDFKDKKFKIPKLNMPWDYKFSPYFEEISLENREWIKGTKLISEESDFEKFVYLKTILMNSYLYPHCNKEVFRYINRLNEYIYIVDDFYLEDNVKGQEWVDELFDRNSKFVKENYIGSIMWEIFDDIISVGNDGATDYLIKKTHEWMDSVILFNSKKVNSKFTFEEYTNSRGVDVGMIFGLACTKVHIPPLCDEIENHPVYIDMLANYYNPIHLLINDIYSFNKETKSVRLGNYVKIAAYQLGSIQLAMDHLSKLFDEYIGKIQEKFAELEKIFPNNKDLETHLYIIKTIIACNFNCSTNPNYPRYYGE... | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several yet unidentified sesquiterpenes.
Sequence Mass (Da): 39480
Sequence Length: 331
Domain: Contains several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and th... |
U5PZT6 | MSLLLAPPSYFPFRGLRRSTAAKQPPCLRLVKCTADRQSPEAARRSAHYQPNMWSDDYIQSLTVESPLKVEEKEQTKKLMLLKERIAEVICEGKEVEEQLRLIDHLQQLGVAYHFKDDIKASLRNIHSSLEEISSTIIFKDGLHASALLFRLLRENGFSISEDIFEEFRDEKGQYFRSDGLKNQTDQAMLSLYEASYYEKDGEMVLQEAMECTTKHLENLLEEEGSDLKLKEQAAHALELPLNWRMERLHARWFIEACQREVMVIDNPLLLEFAKLDFNAVQSIYKKELSALSRWWTKLGVVEKLPFARDRLTENYLWTV... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene and monoterpene synthase involved in the biosynthesis of volatile compounds present in floral scent . Mediates the conversion of (2E)-geranyl diphosphate (GPP) into linalool, with trace levels of myrcene, limonene and (Z)-beta-ocimene . Acts a... |
Q7M711 | MVAVLQSTLPIIFSMEFIMGTLGNGFIFLIVCIDWVQRRKISLVDQIRTALAISRIALIWLIFLDWWVSVHYPALHETGKMLSTYLISWTVINHCNFWLTANLSILYFLKIANFSNIIFLYLKFRSKNVVLVTLLVSLFFLFLNTVIIKIFSDVCFDSVQRNVSQIFIMYNHEQICKFLSFTNPMFTFIPFVMSTVMFSLLIFSLWRHLKNMQHTAKGCRDISTTVHIRALQTIIVSVVLYTIFFLSFFVKVWSFVSPERYLIFLFVWALGNAVFSAHPFVMILVNRRLRLASLSLIFWLWYRFKNIEV | Function: Putative taste receptor which may play a role in the perception of bitterness.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36376
Sequence Length: 309
Subcellular Location: Membrane
|
Q7M713 | MNGVLQVTFIVILSVEFIIGIFGNGFIAVVNIKDLVKGRKISSVDQILTALAISRIALLWLILVSWWIFVLYPGQWMTDRRVSIMHSIWTTFNQSSLWFATSLSIFYFFKIANFSNPIFLYLKVRLKKVMIGTLIMSLILFCLNIIIMNAPENILITEYNVSMSYSLILNNTQLSMLFPFANTMFGFIPFAVSLVTFVLLVFSLWKHQRKMQHSAHGCRDASTKAHIRALQTLIASLLLYSIFFLSHVMKVWSALLLERTLLLLITQVARTAFPSVHSWVLILGNAKMRKASLYVFLWLRCRHKE | Function: Putative taste receptor which may play a role in the perception of bitterness.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35095
Sequence Length: 305
Subcellular Location: Membrane
|
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