ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8C428 | MSEGSAGDPGHGSSRQRAVHPENLSLGSSCFSPPVNFLQELPSYRSVARRRTNILSRDKQSGTLLKPTDSFSCQLDGGITENLNSQSIRKYALNISEKRRLRDIQETQMKYLSEWDQWKRYSSKSWKRFLEKAREMTTHLELWRKDIRSIEGKFGTGIQSYFSFLRFLVVLNLVIFLIIFMLVLLPILLTKYKITNSTFVLIPFKDMDIQCTLYPISSSGLIYFYSYIIDLLSGTGFLEETSLFYGHYTIDGVKFQSFTYDLPLAYLISTIAYLALSLLWIVKRSVEGFKINLIRSEEHFQSYCNKIFAGWDFCITNRSMAELKHSSLRYELRADLEEERIRQKIAERTSEETIRIYTLRLFLNCIVLAVLAACFYAIYLATAFSQEHMKKEIDKMVFGENLLILYLPSIVITLANFITPIIFAKIIHYEDYSPGFEIRLTILRCVFMRLATICVLVFTLGSKITSCGDSTCELCGYNQKLYPCWETQVGQEMYKLMIFDFIIILAVTLFVDFPRKLLVTYCASSKLIQCWGQQEFAIPDNVLGIVYGQTICWIGAFFSPLLPAIATLKFVIIFYVKELSLLYTCRPSPRQFRASNSNFFFLLVLLIGLCLAIIPLTISMARIPSSKACGPFTNFNTTWEVIPQTVSTFPSSLQTLIHAVTSEAFAVPFFMIICLVMFYFIALAGAHKQVVVQLREQLSLESRDKRYLIQKLTEAQREVRSQPASA | 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 | MLLPRSVSSERAPGVPEPEELWEAEMERLRGSGTPVRGLPYAMMDKRLIWQLREPAGVQTLRWQRWQRRRQTVERRLREAAQRLARGLGLWEGALYEIGGLFGTGIRSYFTFLRFLLLLNLLSLLLTASFVLLPLVWLRPPDPGPTLNLTLQCPGSRQSPPGVLRFHNQLWHVLTGRAFTNTYLFYGAYRVGPESSSVYSIRLAYLLSPLACLLLCFCGTLRRMVKGLPQKTLLGQGYQAPLSAKVFSSWDFCIRVQEAATIKKHEISNEFKVELEEGRRFQLMQQQTRAQTACRLLSYLRVNVLNGLLVVGAISAIFWATKYSQDNKEESLFLLLQYLPPGVIALVNFLGPLLFTFLVQLENYPPNTEVNLTLIWCVVLKLASLGMFSVSLGQTILCIGRDKSSCESYGYNVCDYQCWENSVGEELYKLSIFNFLLTVAFAFLVTLPRRLLVDRFSGRFWAWLEREEFLVPKNVLDIVAGQTVTWMGLFYCPLLPLLNSVFLFLTFYIKKYTLLKNSRASSRPFRASSSTFFFQLVLLLGLLLAAVPLGYVVSSIHSSWDCGLFTNYSAPWQVVPELVALGLPPIGQRALHYLGSHAFSFPLLIMLSLVLTVCVSQTQANARAIHRLRKQLVWQVQEKWHLVEDLSRLLPEPGPSDSPGPKYPASQASRPQSFCPGCPCPGSPGHQAPRPGPSVVDAAGLRSPCPGQHGAPASARRFRFPSGAEL | 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 | MFRQWSVQSGPAPRRPESQAASEELWEQEVERLCASRTPVRMLPYAMADKRFIRELREPEGVKTTFWQRWHRPRRVARQHLREAEQRLARGFGLWEGALYEIGGLFGTGIQSYFTFLRFLLLLNLLTMLLTACFVLLPLVWLRPPELGPALKLRLQCSSSPLPQSDIPRFHNPLWNILTGRAFNNTYLFYGAYRAGPESSSEYSIRLAYLLSPMVCLLLCFCGILQRMAEGLPQQTLLGQRYRTPLSAKVFSSWDFCIRVWEAATIKKHEISNELKMELEEGRRVELAQQQTRAQKACRLLTYLRTNILIVLLVVGAISAIFWATKYSQDNKEESLFLVLQYLPPGVISLVNFLGPQLFTVLIQLENYPPGTEVNLTLIWCVVLKLASLGMFSFSLGQTVLCIGRNKTSCESYGYNACDYQCWENSVGEELYKLIIFNFLLTVAFAFLVSLPRRLLVERFSGWFWTWLDREEFLVPKNVLDIVAAQTVTWMGLFYCPLLPLLNSVFLFLTFYIKKYTLLRNSRASPRRFRASSSTFFFHLVLLLGLLLAAVPLAYVISSTHSSWDCGLFTNYSAPWQVVPELVALQLPLPSQRALRYLSSHAFSFPLLILLSIVLTVCISQSRANARAIQGLRKQLVWQVQEKWHLVDDLSRLLPELSPEPGSPHSRASRPRSFCPGFPCPGSPGPRTPRLAPSNRLSSSSLGAPSASVPASRFHFPSRTEL | 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 | MKVLGLIVEYNPFHNGHLYHLEESKKISGADFVVCVMSGNFIQRGEPAIVNKWARTKMALSAGADLVIELPLSCAMASAEYFASGAVRILNDIGIVDYICFGSEHGDVKTLDYIAQILVEEPESYKSFLKEELDNGLSYPAARESALKKYTAHSINIPQIISSSNNILGIEYLKALRRIKSSIIPLTIKRINNDYNTENITGSISSASSIRKYISTSNSTSFDDVLAMTMPKTSVDILFEEFSAGRGPVFKEDFYPVVTSLIRKMTPEQIRNFAYVSEGLENRIKSAADTAGTYEELVESICTRRYTKTRVQRILMGILMGVTSKDLDMLSRFDSPQYARILGFNSKGKQLLSQIKKKSSIPLVLKLSDFIKSCDPVLKRKLELEILATDLYVMCYKNPAFRKAGQEFTQNIIIM | 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(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 46456
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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C4Z916 | MKVAGVITEYNPFHNGHKYQLEQIKRQTSADYIVVVMSGDFVQRGEPAIIDKYERTRMALLSGADLVLELPSVFATASAEFFAGGGVSVLKNTGVVDMLCYGVESVDHELTKLVAGVLKNPPSEYSASLARLIQGGMSFPAARSRALCEYFRDTYDSASEKLDAFIASPNNILAIEYEKALMDCDITGFPIQRVGEGYHSTDSTSEFSSATAVRGVISTLIDIDKHNTITNMQLDNSWISTKFSQLIPSACADILVNCILGGHIVFPDDISEMLYYRLLTGKDKGFAQYADCTKELSAKIVKNIYKYEGFTQFCNLLKSKNLTYTRISRVLTHILLGIENNDFNICMNNPYLRILGFKKSSGELMHLLKKRASVPIITKVADAPYELISKDIFAADLYGRLCHSQQNEFTHGVVII | 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(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 46138
Sequence Length: 416
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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Q5WFF2 | MRALGLVVEYNPFHNGHLHHLTQAKQQTGADVVVAVMSGTFLQRGEPALLSRWYRAEMALAAGADLVVELPYAYSVQTAERFAEGAVTILAALRCSVLNFGSEKGEIAPFYALAEFMNDHQVAFNHHVKQFLKDGVSYPKASAQAFSMLSGHEKLLPLDQPNNILGYHYVKAIQRLGISMEATTTLRIQAGYHDKEFAGPIASATAIRKALLSGENIETAVPAHTARLIQMYKRRYRLLHTWEHYFPFLQHKVLTTPLAELAKTAECSEGLEHRLRDSLFSASSFQGWLSATKSKRYTQTRLQRLFAHLLTGTTAEENAAIQQSGPAYIRLLGMSETGKTYIRENKKTFSLPIVTRQGELRRYGQAGEQELRISQCYWLPLPPQALKQEVTREFQQKPINWEKRS | 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(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 45617
Sequence Length: 405
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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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. Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side. Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles. In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (By similarity). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) (By similarity). Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus. Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization. In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC. Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9. Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24828
Sequence Length: 219
Domain: The GOLD domain is required for proper p24 heterooligomeric complex formation and efficient transport of GPI-anchored proteins.
Subcellular Location: Endoplasmic reticulum membrane
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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
Sequence Mass (Da): 24001
Sequence Length: 208
Subcellular Location: Endoplasmic reticulum membrane
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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
Sequence Mass (Da): 24066
Sequence Length: 213
Subcellular Location: Endoplasmic reticulum membrane
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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
Sequence Length: 206
Subcellular Location: Membrane
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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: 206
Subcellular Location: Membrane
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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 . Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side . Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles . In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER . Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment . Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) . Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation . Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus . Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization . In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC . Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9 . Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24976
Sequence Length: 219
Domain: The GOLD domain is required for proper p24 heterooligomeric complex formation and efficient transport of GPI-anchored proteins.
Subcellular Location: Endoplasmic reticulum membrane
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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 differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19998
Sequence Length: 181
Subcellular Location: Membrane
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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 differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19995
Sequence Length: 181
Subcellular Location: Membrane
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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: 294
Subcellular Location: Nucleus outer membrane
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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
Subcellular Location: Nucleus outer membrane
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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 membrane
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Q5U405 | MDRGSHRNSSPARTPPQASPARTSPARAPPQASPARTPPQASPARTPPQASPARAPPPQASPARASPARAPPSRSSSGRSSSARSASTTSSPTRVYLVRATPVGAVPIRASPARSAPATRATRESPGLSFPKFSWQETQRQLPLIGCVILLISLVISLILLFYFWRGHTGIKYKEPLESCPIHAVRCDGVVDCKMKSDELGCVRFDWDKSLLKVYSGSSGEWLPVCSSSWNDTDSKRTCQQLGFDSAYRTTEVAHRDITSSFLLSEYNTTIQESLYRSQCSSRRYVSLQCSHCGLRAMTGRIVGGALTSESKWPWQVSLHFGTTHICGGTLIDAQWVLTAAHCFFVTREKLLEGWKVYAGTSNLHQLPEAASISQIIINGNYTDEQDDYDIALIRLSKPLTLSAHIHPACLPMHGQTFGLNETCWITGFGKTKETDEKTSPFLREVQVNLIDFKKCNDYLVYDSYLTPRMMCAGDLRGGRDSCQGDSGGPLVCEQNNRWYLAGVTSWGTGCGQKNKPGVYTKVTEVLPWIYRKMESEVRFRKS | 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 embryos .
PTM: The inactive zymogen is post-translationally modified and then trafficked to the cell surface, whereby it undergoes autocatalytic cleavage resulting in an activated form that is released extracellularly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59806
Sequence Length: 543
Subcellular Location: Cell membrane
EC: 3.4.21.-
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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 but is likely one of the non-methylated methanopterin biosynthetic intermediates.
Sequence Mass (Da): 30434
Sequence Length: 260
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.-
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Q8XB34 | MENFKHLPEPFRIRVIEPVKRTTRAYREEAIIKSGMNPFLLDSEDVFIDLLTDSGTGAVTQSMQAAMMRGDEAYSGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQEKGLDRSKMVAFSNYFFDTTQGHSQINGCTVRNVYIKEAFDTGVRYDFKGNFDLEGLERGIEEVGPNNVPYIVATITSNSAGGQPVSLANLKAMYSIAKKYDIPVVMDSARFAENAYFIKQREAEYKDWTIEQITRETYKYADMLAMSAKKDAMVPMGGLLCMKDDSFFDVYTECRTLCVVQEGFPTYGGLEGGAMERLAVGLYDGMNLDWLAYRIAQVQYLVDGLEEIGVVCQQAGGHAAFVDAGKLLPHIPADQFPAQALACELYKVAGIRAVEIGSFLLGRDPKTGKQLPCPAELLRLTIPRATYTQTHMDFIIEAFKHVKENASNIKGLTFTYEPKVLRHFTAKLKEV | 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 | MSSLDRKKPQNRSKNNYYNICLKEKGSEELTCEEHARIIFDGLYEFVGLLDAHGNVLEVNQVALEGAGITLEEIRGKPFWKARWWQISKKTEATQKRLVETASSGEFVRCDVEILGKSGGREVIAVDFSLLPICNEEGSIVYLLAEGRNITDKKKAEAMLALKNQELEQSVERIRKLDNAKSDFFAKVSHELRTPLSLILGPLEAVMAAEAGRESPYWKQFEVIQRNAMTLLKQVNTLLDLAKMDARQMGLSYRRANLSQLTRTISSNFEGIAQQKSITFDTKLPVQMVAEVDCEKYERIILNLLSNAFKFTPDGGLIRCCLSLSRPNYALVTVSDSGPGIPPALRKEIFERFHQLSQEGQQATRGTGLGLSIVKEFVELHRGTISVSDAPGGGALFQVKLPLNAPEGAYVASNTAPRRDNPQVVDTDEYLLLAPNAENEAEVLPFQSDQPRVLIVEDNPDMRGFIKDCLSSDYQVYVAPDGAKALELMSNMPPDLLITDLMMPVMSGDMLVHQVRKKNELSHIPIMVLSAKSDAELRVKLLSESVQDFLLKPFSAHELRARVSNLVSMKVAGDALRKELSDQGDDIAILTHRLIKSRHRLQQSNIALSASEARWKAVYENSAAGIVLTDPENRILNANPAFQRITGYGEKDLEGLSMEQLTPSDESPQIKQRLANLLQGGGAEYSVERSYLCKNGSTIWANASVSLMPQRVGESPVILQIIDDITEKKQAQENLNQLQQQLVYVSRSATMGEFAAYIAHEINQPLSAIMTNANAGTRWLGNEPSNIPEAKEALARIIRDSDRAAEIIRMVRSFLKRQETVLKPIDLKALVTDTSLILKAPSQNNSVNLDVVADDELPEIWGDGVQIQQLIINLAMNAIEAISQADCETRQLTLSFSGNDTGDALVISVKDTGPGISERQMAQLFNAFYTTKKEGLGMGLAICLTITEVHNGKIWVECPPAGGACFLVSIPARQGSGT | 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 group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 108018
Sequence Length: 978
Domain: Toluene binds to the N-terminal PAS sensor domain but not to the C-terminal PAS domain. The two PAS sensor domains may sense two different signals.
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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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 Mass (Da): 25432
Sequence Length: 227
Subcellular Location: Cytoplasm
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H2KZH5 | MSSSRHFSIPYDEDVVHSVILENTPSPPPKPPRGILRKEAPMKPQRSALKIEPARDDDKENNSQPQARSQFKAKDTMEQMQSYFKRSISVLRKSEEHFTGAEAADILTAYIETHRNEFPRDNIGRSNAVKLLEIWLESNTIQSVESHQKKFVDSERTFYRLGGDSESLYIVNTPIASRNHDDSASVSRSESSRRSNSIKRLFSPFVRRNRSNSRGRDKDKDNLKDGSSTNLKSTWSLFSSSSEKNEKKLKKAEQQLIKEEEAEVYELSLFHLLSLIDVEFLEDVALPVQDSKNNASFLSSILGKVGLGASEERLDPHQEDHMDLLIETHPLIRDASQWFQMARCCAPLLYFEAKPVASNHKTSHNEQLYLWCRAALDAVKNRLEKMTQNGSSPLFPSEFAPLLTKIAQQLINDMDSGEKLSTAVMYIFLMVPHPIRKTIDQLVQWLQLTMRTDAVEDLRSPYYLGKKDPRRYKENVNVIIGELSSFIFPRGCMTNVQQDIFIETLVELRQKGKLGQRPAQLESSLRAKSVNGQIKWQRKERKHNSLEGDLTPVRYTVRRESIRSKTSKSKDGLNETDSALVTMINSVIDNKELSLTEKKKQLMNFKKFYPKLYNDFFPGMI | 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 function, perhaps regulating the apoptotic fate of the Q.pp neuroblast, but appears dispensable for subcellular localization.
Subcellular Location: Cytoplasm
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O88746 | MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELATDLIDMGPDPAATNNLSSQLAGMNLGSRSVRAGLQSLETSGHLEDDFDMFALTRGSSLADQRKGVKYEAPQTTDGLAGALDARQQSTGAIPATQARIMEDIEQWLSTDVGNSAEEPSGVTSEEFDKFLEERAKAADRLPNLASPSAEGPPRPSPGTAPRRKTQEKDDDMLFAL | 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 similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes by ZFYVE16 (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation . PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation . Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity).
PTM: Monoubiquitinated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54325
Sequence Length: 492
Domain: The GAT domain and the VHS domain are required for the interaction with polyubiquitinated proteins.
Subcellular Location: Cytoplasm
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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 preproteins into the translocation pore .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20426
Sequence Length: 188
Subcellular Location: Mitochondrion outer membrane
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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 the TOM40 translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases.
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16284
Sequence Length: 145
Subcellular Location: Mitochondrion outer membrane
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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 the translocation pore.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20229
Sequence Length: 181
Subcellular Location: Mitochondrion outer membrane
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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 the translocation pore (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22604
Sequence Length: 202
Subcellular Location: Mitochondrion outer membrane
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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 the translocation pore (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17529
Sequence Length: 152
Subcellular Location: Mitochondrion outer membrane
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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 the translocation pore.
PTM: The N-terminus is blocked.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22814
Sequence Length: 204
Subcellular Location: Mitochondrion outer membrane
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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 facilitates the movement of preproteins into the TOM40 translocation pore.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20317
Sequence Length: 183
Subcellular Location: Mitochondrion outer membrane
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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 movement of preproteins into the translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15292
Sequence Length: 140
Domain: The N-terminal domain (residues 1-60) is important for binding to the unfolded mature imported proteins. Residues (47-69) of the cytoplasmic domain interacts with TOMM20 while the C-terminal segment (residues 61-80) binds presequence of preproteins. Requires the transmembrane domain (TMD), a short segment (the import sequence) in the cytoplasmic domain localizing separately from the TMD and the C-tail signal in the C-terminal domain for efficient targeting and integration into the TOM complex (By similarity).
Subcellular Location: Mitochondrion outer membrane
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Q9WUL0 | MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKDKDKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSDKHKDKHKDRDKEKRKEEKIRAAGDAKIKKEKENGFSSPPRIKDEPEDDGYFAPPKEDIKPLKRPRDEDDADYKPKKIKTEDIKKEKKRKLEEEEDGKLKKPKNKDKDKKVAEPDNKKKKAKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPEGVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNDEKNTITNLSKCDFTQMSQYFKAQSEARKQMSKEEKLKIKEENEKLLKEYGFCVMDNHRERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFPGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENVPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQSKIDAKKDQLADARKDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMTDEDYEF | 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 the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter.
PTM: Sumoylated. Lys-119 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment.
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Mass (Da): 90760
Sequence Length: 767
Subcellular Location: Nucleus
EC: 5.6.2.1
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Q9ZDK2 | MKLVIVESPAKAKTINKYLGDEFKVIASFGHIRDLPSKKGSVLPDKNFLMEYDISDKAGKYVDAIVKEARKAEVVYLATDPDREGESISWHVAEVIKEKNKVESDDFFKRVAFNEITKKAIMNAVANPRKLDTNLVNAQQARRALDYLVGFTLSPLLWRKLPGCKSAGRVQSVALRLICDREDEIERFKSEEYWDISLKMQNSNNDLFTAKLTHVNDQKLKKFSIINEKEAKDLTQKLKLQKFYVEKIEKKQQKRQPQPPFITSSLQQEAARKLGFSAKKTMQIAQKLYEGVDIGKETIGLITYMRTDGVTLSNDAIADIRKLIDKNYGNQYLPIKPRIYQSKVKNAQEAHEAIRPTNITYTPDSLKQKLEKDYYKLYELIWHRTIACQMENVIMDLVIANLASENKEYLAKANGSIIAFDGFYKVYRESLDDEDEEDNKMLPPLKEQEHIKTKEVIPNKHFTEPPPRYSEASLVKKLEELGIGRPSTYASILSVLQDRKYVALEKKRFIPEELGRLVTVFLVGFFKKYVEYDFTAGLENELDEIAAGKLEWKTALNNFWRGFNHNIESVNEQKITEIINYLQKALDYHLFGEDKESKVCPSCKTGQLSLKLGKFGAFLACSNYPECTFKKSIVSGNDNNEDEGDPSTILNDNKILGTDQDGVEIYLKKGPYGPYIQLGEQCGKVKPKRTPVPANLKQSEITLEIALKLLNLPLKIGIHKDSGEEIIIGYSKFGPYIKYMCKFISVPKKYDFLNLSLNDAMKLIQNNKAKLEKKYG | 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 duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Mass (Da): 88722
Sequence Length: 776
EC: 5.6.2.1
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P07799 | MSSSDSDSVSLSIRRRQRRGSSKRISMKESDEESDSSENHPLSESLNKKSKSESDEDDIPIRKRRASSKKNMSNSSSKKRAKVMGNGGLKNGKKTAVVKEEEDFNEIAKPSPKHKRVSKANGSKNGAKSAVKKEESDTDDSVPLRAVSTVSLTPYKSELPSGASTTQNRSPNDEEDEDEDYKWWTSENIDDTQKWTTLEHNGVIFAPPYEPLPKNVKLIYDGNPVNLPPEAEEVAGFYAAMLETDHAKNPVFQDNFFRDFLKVCDECNFNHNIKEFSKCDFTQMFHHFEQKREEKKSMPKEQKKAIKQKKDEEEEKYKWCILDGRKEKVGNFRIEPPGLFRGRGSHPKTGSLKRRVYPEQITINIGEGVPVPEPLPGHQWAEVKHDNTVTWLATWHENINNNVKYVFLAAGSSLKGQSDLKKYEKSRKLKDYIDDIRKGYRKDLKSELTVERQRGTAMYLIDVFALRAGNEKGEDEADTVGCCSLRYEHVTLKPPRTVVFDFLGKDSIRYYNEVEVDPQVFKNLKIFKRPPKKEGDLIFDRLSTNSLNKYLTSLMDGLSAKVFRTYNASYTMAEELKKMPKNLTLADKILFYNRANRTVAILCNHQRSVTKNHDVQMERFAERIKALQYQRMRLRKMMLNLEPKLAKSKPELLAKEEGITDSWIVKHHETLYELEKEKIKKKFDRENEKLAAEDPKSVLPESELEVRLKAADELKKALDAELKSKKVDPGRSSMEQLEKRLNKLNERINVMRTQMIDKDENKTTALGTSKINYIDPRLTYSFSKREDVPIEKLFSKTIRDKFNWAADTPPDWKW | 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 the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. TThe free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Mass (Da): 93981
Sequence Length: 814
EC: 5.6.2.1
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Q2FHI8 | MADNLVIVESPAKAKTIEKYLGKKYKVIASMGHVRDLPRSQMGVDTEDNYEPKYITIRGKGPVVKELKKHAKKAKNVFLASDPDREGEAIAWHLSKILELEDSKENRVVFNEITKDAVKESFKNPREIEMNLVDAQQARRILDRLVGYNISPVLWKKVKKGLSAGRVQSVALRLVIDRENEIRNFKPEEYWTIEGEFRYKKSKFNAKFLHYKNKPFKLKTKKDVEKITAALDGDQFEITNVTKKEKTRNPANPFTTSTLQQEAARKLNFKARKTMMVAQQLYEGIDLKKQGTIGLITYMRTDSTRISDTAKVEAKQYITDKYGESYTSKRKASGKQGDQDAHEAIRPSSTMRTPDDMKSFLTKDQYRLYKLIWERFVASQMAPAILDTVSLDITQGDIKFRANGQTIKFKGFMTLYVETKDDSDSEKENKLPKLEQGDKVTATQIEPAQHYTQPPPRYTEARLVKTLEELKIGRPSTYAPTIDTIQKRNYVKLESKRFVPTELGEIVHEQVKEYFPEIIDVEFTVNMETLLDKIAEGDITWRKVIDGFFSSFKQDVERAEEEMEKIEIKDEPAGEDCEICGSPMVIKMGRYGKFMACSNFPDCRNTKAIVKSIGVKCPKCNDGDVVERKSKKNRVFYGCSKYPECDFISWDKPIGRDCPKCNQYLVENKKGKTTQVICSNCDYKEAAQK | 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 duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Mass (Da): 79113
Sequence Length: 689
EC: 5.6.2.1
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Q5JH81 | MAEANQLFKEFKIQSVSEFFRRNAAMLGYTGKVRSLTTLVHEAVTNSLDACEEAGIPPYVRVEIEELGNEHYKVVVEDNGPGIPEKYITHVFGKMLAGTKAHRNIQSRGQQGIGISGAVMFAQITSGKATRVITSTGNDEIIEAWVKIDVDKNEGKIVKKEKHPNPKGWRGTRIELEVKNVKYMRSKQGVFWYLKLTAIANPHAHIELIEPDGKLIVFPRSSDYIPEPPVEMKPHPKGVLTDDVYRLAKKTRRNTVRRFLIGEFSRISDKKVDELIEYIAALRLIKTVEDKKLQEQYYQKLMEGHVKAVLRAFKGYTKVVKQVAKMMEKPPEKLTWHEAEEIVEAFKYMKFLAPPTHGLRPIGEENIEKGLKGILKPEFVTAVTRPPKVYSGGIPFQVEVGIAYGGEIPAGFDLYRYANRVPLLFDAGSCVTTQAARSIDWKRYKIDDLDRAPLVLMINVVSVHVPYTGTGKQSIASVDEIYNEIRLAIMDAARRLQTYLSGKHRKLAQVKRRKTFEKYVPEIARALSILTGEPEEKIREYFIRFIESKFASAEVEEVAAEEVAENA | 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
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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 disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q6DHU8 | MEASKESPSAFKTPCKPAKVKSPVNACGTPVTIPASPFMKKLGCGTGVNVYLMNRMGKQTHSPWAIKKINSKCAQGQVSVYQKRLCEEAKILKDLKHPNIVGFRAFTTAKDGSKCLAMEFGGEQSLNDLIEKRREEGLQAFPVDTIEKVALHVARGLLYLHNEKKLLHGDMKSCNVVIKGDFESIKICDVGVSLPLDENMQVSDPKAHYIGTEPWKPKEALEDGVITDKADIFAYGLTLWEMMTLSVPHLEMLDTEGDEDDDDESFEEDFDEDAYYERLGSRPALDAVTLGGSYQRMVELFCLCTEEDPQKRPSAAHIVQVLESNSQLSKQNTEVIVID | 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 | MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV | 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-cycle dependent manner at mitosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36085
Sequence Length: 322
EC: 2.7.12.2
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P09176 | MIKNEIKILSDIEHIKKRSGMYIGSSANETHERFMFGKWESVQYVPGLVKLIDEIIDNSVDEGIRTKFKFANKINVTIKNNQVTVEDNGRGIPQAMVKTPTGEEIPGPVAAWTIPKAGGNFGDDKERVTGGMNGVGSSLTNIFSVMFVGETGDGQNNIVVRCSNGMENKSWEDIPGKWKGTRVTFIPDFMSFETNELSQVYLDITLDRLQTLAVVYPDIQFTFNGKKVQGNFKKYARQYDEHAIVQEQENCSIAVGRSPDGFRQLTYVNNIHTKNGGHHIDCAMDDICEDLIPQIKRKFKIDVTKARVKECLTIVMFVRDMKNMRLIRQTKERLTSPFGEIRSHIQLDAKKISRDILNNEAILMPIIEAALARKLAAEKAAETKAAKKASKAKVHKHIKANLCGKDADTTLFLTEGDSAIGYLIDVRDKELHGGYPLRGKVLNSWGMSYADMLKNKELFDICAITGLVLGEKAFEEKEDGEWFTFELNGDTIIVNENDEVQINGKWITVGELRKNL | 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
Sequence Length: 516
EC: 5.6.2.2
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A0QPN1 | MTATLDVPEQNPDLVLDQSADDYWNHYQLTFALYSVSDRAIPSAYDGLKPGQRRLLYQMHDSKLLPGNKPQKSSKVCSAVTGNLHPHGGASMYGAAALMAADFQRVKVIDGQGAFPRIQGDIPAADRYTEMRLSAPGAALTAELNDHAVPMVPTFDGEWVEPTVLPAQWPVLLCNGAVGIAEGWATKVPAHNPREVMAACRALLKTPNMTDDRLCKLIPGPDWGSGASVVGTAGLREYITTGRGHFTVRGTISVEGKNCIITELPPGVASNTVQDRIRALVESGEMSGVADMSDLTDRRNGLRIVVTAKRGHNAEQIRDQLLALTPLESTFAASLVALDENRVPRWWSVRDLIMAFLQLRDSVVLHRSEYRLEKVTARRHLVAGLMKIHLDIDAAVAVIRGSETVDEARKGLQERFKIDAEQADYVLSLQLRRLTKLDVIELQAEAEKLDAEFAELNDLVTNPESRRKVIDKELVETAKLFKGPEYDRRTVLDFDATPVSRGDEDGSRERKVNTAWRLDDRGVFSDSHGELLTSGLGWAVWSDGRIKFTTGNGLPFKIRDIPVAPDITGLVRSGVLPEGYHLALVTRRGKILRVDPASVNPQGVAGNGVAGVKLAADGDEVIAALPVSCANGEAILSIAEKSWKVTEVADIPVKGRGGAGVAFHPFVKGEDALLAASISKTGYVRGKRAVRPENRAKASIKGSGADVTPAPAE | 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 supercoils in an ATP-dependent manner. Catenates and decatenates DNA. Generates dsDNA breaks in the presence of the quinolone antibiotic ciprofloxacin, showing it is a topoisomerase .
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 77225
Sequence Length: 713
EC: 5.6.2.2
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A0QPN2 | MSDPASTIPPAHHPTFWRERAVSYTAADITELDDVQHTRLRPAVNLGLDVLNTALREIVDNAIEEVADPGHGGSTVTITLHADGSVSVADDGRGLPVDTDPTTGKNGIVKTLGTARAGGKFSAHKDATSTGAGLNGIGAAAAVFISARTDVTVRRDGKTFLQSFGRGYPGVFEGKEFDPEAPFTRNDTQKLRGVSNRKPDLHGTEVRILFDPAIAPDSTLDIGEVLLRAHAAARMSPGVHLVVVDEGWPGEEVPPAVLEPFSGPWGTDTLLDLMCTAAGTPLPEVRAVVEGRGEYTTGRGPTPFRWSLTAGPAEPATVAAFCNTVRTPGGGSHLTAAIKGLSEALAERASRMRDLGLAKNEEGPEPQDFAAVTALAVDTRAPDVAWDSQAKTAVSSRSLNLAMAPDVARSVTIWAANPANADTVTLWSKLALESARARRSAEGAKARARAASKAKGLGTNLSLPPKLLPSRESGRGSGAELFLCEGDSALGTIKAARDATFQAAFPLKGKPPNVYGFPLNKARAKDEFDAIERILGCGVRDHCDPELCRYDRILFASDADPDGGNINSSLISMFLDFYRPLVEAGMVYVTMPPLFVVKAGDERIYCQDESERDAAVAQLKASSNRRVEVQRNKGLGEMDADDFWNTVLDPQRRTVIRVRPDESEKKLHHTLFGGPPEGRRTWMADVAARVDTSALDLT | 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 supercoils in an ATP-dependent manner. Catenates and decatenates DNA. Generates dsDNA breaks in the presence of the quinolone antibiotic ciprofloxacin, showing it is a topoisomerase.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 74445
Sequence Length: 698
EC: 5.6.2.2
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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-anchor
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 19727
Sequence Length: 173
Subcellular Location: Cell membrane
EC: 3.1.3.48
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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 with RABGGTB. Unfarnesylated forms are redirected to the nucleus and cytosol.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 19127
Sequence Length: 167
Subcellular Location: Cell membrane
EC: 3.1.3.48
|
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 response to angiotensin II.
PTM: Farnesylated. Farnesylation is required for membrane targeting (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 19535
Sequence Length: 173
Subcellular Location: Cell membrane
EC: 3.1.3.48
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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 response to angiotensin II.
PTM: Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 19652
Sequence Length: 173
Subcellular Location: Cell membrane
EC: 3.1.3.48
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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
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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
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Q8TEL6 | MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLKLHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQASIVFPPPGASEENGLPHTSARTQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE | 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 (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation . The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation . Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome (By similarity). Involved in JNK activation via its interaction with TRAF2 (By similarity). Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 (By similarity).
PTM: Phosphorylated by GSK3B; phosphorylation is required for ubiquitination.
Sequence Mass (Da): 90852
Sequence Length: 797
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q9JLV2 | MAAAPAAAGAGASRGRRLAATAAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKLSKWSGIPQLLLKLYATSHLHSDFVECQSILKEISPLLSMEAMAFVTEDRKFTQEATYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQAPTVFPSLGTSEEGGLPHTSARAQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE | 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 (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation (By similarity). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome . Involved in JNK activation via its interaction with TRAF2 . Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 .
PTM: Phosphorylated by GSK3B; phosphorylation is required for ubiquitination.
Sequence Mass (Da): 90727
Sequence Length: 797
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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
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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 (Da): 26730
Sequence Length: 248
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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
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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; gluconeogenesis.
EC: 5.3.1.1
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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
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
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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
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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
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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
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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
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F4KFG5 | MSASQNIVVSETTMSSIIPNNNNNNNNSSSQKLPPCLISISKKKLLKNIDIINGGGQRINAWVDSMRASSPTHLKSLPSSISTQQQLNSWIMQHPSALEKFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFCASVHFRCVDEKKWSELVLQVRSVLKKFPTLQLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDEDAFKMLRDRGEGFGILVSKFPKDTDASYSLQDPSEVMDFLRRLVEWKQMQPRM | 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
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
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Q5HZ05 | MVSQNVVVSDAKTGIITVSTVSNSSVFTPTAQKPPTAPGYISVSKKKLLKNLEINGADQSQRLNSWVDSMRASSPTHLKSLSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKLLRGRGQGFGILVSKFPKDTSASYSLQDPPEVMNFLGRLVEWKQMQQ | 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
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
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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 microtubule nucleation, an important step for elongation of the myelin sheath (By similarity). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network . Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
PTM: Phosphorylation may alter the tubulin polymerization activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 23473
Sequence Length: 218
Domain: Most of the protein is composed of disordered regions. Zinc-binding induces structural rearrangement by promoting molten globule state formation.
Subcellular Location: Golgi outpost
EC: 3.6.5.-
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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, an important step for elongation of the myelin sheath . Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes . Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear . In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network . Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 . Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility . Plays a role in cell proliferation by regulating the G1/S-phase transition . Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 .
PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity . Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis . Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase . Phosphorylation by CDK1 inhibits the microtubule polymerizing activity .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 23694
Sequence Length: 219
Domain: Most of the protein is composed of disordered regions . Zinc-binding induces structural rearrangement by promoting molten globule state formation .
Subcellular Location: Golgi outpost
EC: 3.6.5.-
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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, an important step for elongation of the myelin sheath . Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes . Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network . Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity. Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis. Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase. Phosphorylation by CDK1 inhibits the microtubule polymerizing activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 23575
Sequence Length: 218
Domain: Most of the protein is composed of disordered regions. Zinc-binding induces structural rearrangement by promoting molten globule state formation.
Subcellular Location: Golgi outpost
EC: 3.6.5.-
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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 several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
EC: 4.2.3.-
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Q9LMI0 | MISRSYTNLLDLASGNFPVMGRERRRLPRVMTVPGNVSEFDEDQAYSVSSDNPSSVSSDRMIIVANRLPLKAEKRNGSWSFSWDQDSLYLQLKDGLPEDMEILYVGSLSVDVDSNEQDDVAQILLDKFKCVPTFFPPDLQSKFYDGFCKRQIWPLFHYMLPFSADHGGRFDRSLWEAYVATNKLFFQKVIEVINPDDDFVWIHDYHLMVLPTFLRRRFNRIRMGFFLHSPFPSSEIYRSLPVREEILKALLNSDLIGFHTFDYARHFLTCCSRMLGLEYQSKRGYIGLEYYGRTVGIKIMPVGINMGRIQSVMRYSEEEGKVMELRNRFEGKTVLLGIDDMDIFKGINLKLLAMEQMLRQHPNWRGRAVLVQIVNPARGKGIDVEEIRGEIEESCRRINGEFGKPGYQPIIYIDTPVSINEINAYYHIAECVVVTAVRDGMNLTPYEYIVCRQGLLGSESDFSGPKKSMLVASEFIGCSPSLSGAIRVNPWNVEATGEALNEALSMSDAEKQLRHEKHFRYVSTHDVAYWSRSFLQDLERICVDHFKKRCWGMGISFGFRVVALDPNFRKLSIPCIVSDYKRAKSRAILLDYDGTLMPQNSINKAPSQEVLNFLDALCEDKKNSIFIVSGRGRESLSKWFTPCKKIGIAAEHGYFLKWSGSEEWETCGQSSDFGWMQIVEPVMKQYTESTDGSSIEIKESALVWQYRDADPGFGSLQAKEMLEHLESVLANEPVAVKSGHYIVEVKPQGVSKGSVSEKIFSSMAGKGKPVDFVLCIGDDRSDEDMFEAIGNAMSKRLLCDNALVFACTVGQKPSKAKYYLDDTTEVTCMLESLAEASEASNFSMRELDEAL | 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
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W6HUT3 | MSVSLSFAASATFGFRGGLGGFSRPAAAIKQWRCLPRIQCHSAEQSQSPLRRSGNYQPSIWTHDRIQSLTLSHTADEDDHGERIKLLKCQTNKLMEEKKGEVGEQLQLIDHLQQLGVAYHFKDEIKDTLRGFYASFEDISLQFKDNLHASALLFRLLRENGFSVSEDIFKKFKDDQKGQFEDRLQSQAEGLLSLYEASYLEKDGEELLHEAREFTTKHLKNLLEEEGSLKPGLIREQVAYALELPLNRRFQRLHTKWFIGAWQRDPTMDPALLLLAKLDFNALQNMYKRELNEVSRWWTDLGLPQKLPFFRDRLTENYLWAVVFAFEPDSWAFREMDTKTNCFITMIDDVYDVYGTLDELELFTDIMERWDVNAIDKLPEYMKICFLAVFNTVNDAGYEVMRDKGVNIIPYLKRAWAELCKMYMREARWYHTGYTPTLDEYLDGAWISISGALILSTAYCMGKDLTKEDLDKFSTYPSIVQPSCMLLRLHDDFGTSTEELARGDVQKAVQCCMHERKVPEAVAREHIKQVMEAKWRVLNGNRVAASSFEEYFQNVAINLPRAAQFFYGKGDGYANADGETQKQVMSLLIEPVQ | 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-phellandrene, alpha-terpinene, beta-phellandrene, gamma-terpinene and terpinolene . Unable to use farnesyl diphosphate (FPP) as substrate .
Catalytic Activity: (2E)-geranyl diphosphate = diphosphate + sabinene
Sequence Mass (Da): 68541
Sequence Length: 593
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
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Q5GJ59 | MATTGTTSMPAPVFHPTVWGDYFIKFVPEPLQVSDETMAERIRHLREEVSGMFQACKNVVDKTNLVDVVQRLGIDHHFEEQIATALASIHSAGLFNSSSLHEAALRFRLLRQQGFWVPADELVKFIKNEDGSFIDGITNDPKGLLSLYNAAHLVTHDEGTTTLEDAIAFARQHLEAARRCSLKSPLAEQVGRALGIPLPRTLKREEAIAFIPEYSSQQDQQVYSPVILELAKLDFNLLQHLHQEELKEISQWWKDLSGEIGLGYVRDRIVECYFWSYTVHYERGQARARMILAKVFMLTSLLDDTYDVHATLEEARELNKAIQRWDESDVSLLPEYLKKFFVKVISNFREFEDELESHEKYRNVYNIKGFQTLSKHYLQEAEWFHHGCTPSFKDQVNVSVITGGAQVLSIGLLVGMGHEATREAFEWAIGDTDAIWACGEVSRFMDDMSAFKNGRNKMDVASSVECYIKEHNVPSEVALARINSLVEDAWKTINQAPFKYPALFPVVQRVTSLAKSMTLLFLDKRDAYTYSKDFQTTLETHFVRHIPL | 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-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.3.173
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J7LQ09 | MEARRSGNFKASIWDDDFLQSLTSPYTAKEYLKQADKLKWQVKVIIKETKQRLDQLDLIDNIQRLGISHHFRDEIQRVLQNIYEKMRVECPDRMLMEKDLYSTSLQFRLLRQHGYHVSQDVFCSFMDGAGNFQAVDDLKGILALYEASFLSREGENILGSARDFSTRHLKQKLEEITDPILAEKIRRALELPLHWRLQKLEAIWFINIYESRFDANLILLQLAKLEFNMVQAQYQEDLKWLSRWYKETGLPEKMNFARDRLAECFLWALGFIPEAHLGQARKILTKIAVLIVIMDDFYDIYGTLDEIKVFTEELQRWDINALDNLPEYMRICFLAIFNTANEIAYDILRDQGINIISNLRRLWAELGRVYYTEAKWYHSGYFPSTEEYLNVAWISITGPVLLFHAYFSIMNPIDMKELQYLEQYPGIIRWPSTVLRLADDLGTASDEIKRGDVPKSIQCYMHETGCSEEEAREYVKQLIDTTLKKMNKEILMEKPTNDFGATAMNLARISLFFYQYGDGFGVPHNQTKENLVSLIVKPICLT | 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-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.81
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B9RXW0 | MKVGQPVLQCQTNSEAFGMMQERRSGNYKPNIWKYDFLQSLSSKYDEEKYKTQAERLKEDAKHLFIEAVDLQGKLELVDCIIKVGLASHFKDEIKKALDTIASSIKNDKSDAIKNRYVTALCFRLLRQHGYEVSQAKKSDFLDENGTFLKAKSMDVKGVLELFEASYLALESENILDDAKAFSTTILKDINSATTESNLYKQVVHALELPFHWRVRWFDVKWHIKTFQKDKSINKTLLDLAKVNFNVVQATLQNDLKEISRWWRNLGLIENLKFSRDRLVESFLCTVGLVFEPQYSSFRRWLTKVVIMILVIDDVYDIYGSLEELQHFTNAINRWDTAELEQLPEYMKICFKTLHTITGETAHEMQREKRWDQEQTETHLKKVWADFCRALFVEAKWFNKGYTPSVQEYLKTACISSSGSLLSVHSFFLIMNEGTREMLHFLEKNQEMFYNISLIIRLCNDLGTSVAEQERGDAASSIVCHMREMEVLEEEARSYLKGIIGNYWKKVNEKCFTQSPEMQLFININVNMARVVHNLYQNRDGFGVQDHQNKKQILSLLVHPFKLD | 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 important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.46
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G1DGI7 | MIEEMRKLLATLDDGEISPSAYDTAWVARIPSQSNATCPEFPETLEWIAHNQLPDGSWGDRNHFQIYDRVLSTVSCLVALKTWNLGHDNINKGERFLKQNIYKLTKDKGDLLCGFELIFMTMLEEAKQKGLDIPIDIPALKILQGYRQKKLQKIPLEMVHSIPTTILYSLEGLQDHINWEKILQFIGTDGSFLSSPSATACVYMHTKDPRCLEYLKGVVKKVKNSVPCQYAIDLFERLWIVDTLERLGIDRYFQPEIKNILDYVYKYWSDKKGIGWGRESYLKDIDDTSMGFRLLRLHGYKVTPDVFLNFMSSEDKFFCFPGESYHGASDIFNLYRASQVAFANDNILTKAKNYAHKYLSQLDKAYLDKWSAKKNFFQEVEFELSNQWNSCLPRAYSKSYIHNYGPNDIWIAKTIYRLPFVNNELFINLAKEDFNACQSIHQSEIQTLLRWWAALKFGDLPFFGDKVVTAHFSIASCMFEPEFSELRLFYTKYALLSSTLDDLADYYGSPAQTRCILEAIRSWDPSLVSHLSEEVQICFSGLYRTINEMVKSASKVQTGSSINIREHMQEQLAKLISAQLVDAEWMERKHIPSFETYLSNATVSVGMQDLLLSSIFFCGESISKHLMQEIKNSRCLQLTCLIARLCNDIGTYQFEREKGEVASSITCYMRENRGITESQAIEHLQGIIDESWKELTEEFLTPSQIPRSIKRLMFETARIFQFIYPKKDNFKDPSKAMASLIQNVLYKPAE | 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 form (13E)-labda-7,13-dien-15-ol.
Catalytic Activity: geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol + diphosphate
Sequence Mass (Da): 86619
Sequence Length: 750
Domain: The Asp-Xaa-Asp-Asp (DXDD) and Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motifs are important for the catalytic activities, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 3.1.7.10
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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 (FDP) into the bicyclic sesquiterpene alcohol discoidol . The cytochrome P450 monooxygenase cyp521A1 then catalyzes the oxidative degradation of discoidol to form the trisnorsesquiterpene discodiene .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + discoidol
Sequence Mass (Da): 37305
Sequence Length: 312
Domain: Contains several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
Pathway: Sesquiterpene biosynthesis.
EC: 4.2.3.-
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F0ZHE2 | MQEEILYKWNYDDFKDKKFKIPKLNMPWDYKFSPYFEEISLENREWIKGTKLISEESDFEKFVYLKTILMNSYLYPHCNKEVFRYINRLNEYIYIVDDFYLEDNVKGQEWVDELFDRNSKFVKENYIGSIMWEIFDDIISVGNDGATDYLIKKTHEWMDSVILFNSKKVNSKFTFEEYTNSRGVDVGMIFGLACTKVHIPPLCDEIENHPVYIDMLANYYNPIHLLINDIYSFNKETKSVRLGNYVKIAAYQLGSIQLAMDHLSKLFDEYIGKIQEKFAELEKIFPNNKDLETHLYIIKTIIACNFNCSTNPNYPRYYGEVLEAELKIINE | 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 the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
EC: 4.2.3.-
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U5PZT6 | MSLLLAPPSYFPFRGLRRSTAAKQPPCLRLVKCTADRQSPEAARRSAHYQPNMWSDDYIQSLTVESPLKVEEKEQTKKLMLLKERIAEVICEGKEVEEQLRLIDHLQQLGVAYHFKDDIKASLRNIHSSLEEISSTIIFKDGLHASALLFRLLRENGFSISEDIFEEFRDEKGQYFRSDGLKNQTDQAMLSLYEASYYEKDGEMVLQEAMECTTKHLENLLEEEGSDLKLKEQAAHALELPLNWRMERLHARWFIEACQREVMVIDNPLLLEFAKLDFNAVQSIYKKELSALSRWWTKLGVVEKLPFARDRLTENYLWTVGWAFEPEHWSFRDAQTKGNCFVTMIDDVYDVYGTLDELELFTHVVDRWDINAIDQLPDYMKILFLALFNTVNDDGYKVMKEKGLDVIPYLKRSWADLCKAYLVEAKWYHRGYKPTINEYLDNTWISISGPAIFTNAYCMANNLTKQDLERFSEYPAIAKHSSMLGRLYNDLATSTAEIERGDVPKSIQCCMHERGVSEGVAREQVKELIRGNWRCMNGDRAAASSFEEMLKTVAVDIARASQFFYHNGDKYGKADGETMTQVMSLLINPII | 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 also as a sesquiterpene synthase by catalyzing the conversion of farnesyl diphosphate (FPP) to alpha-bergamotene and beta-bisabolene and to minor products including alpha-curcumene, cis-alpha-bisabolene, beta-farnesene and beta-sesquiphellandrene, as well as seven other unidentified sesquiterpenes .
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate
Sequence Mass (Da): 68357
Sequence Length: 591
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
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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
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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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