ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q93324 | MRTSLVVCLFWLLFQLHTTHGYNTLVNLAGNWEFSSSNKTVNGTGTVPGDIYSDLYASGIIDNPLFGENHLNLKWIAEDDWTYSRKFRLIDLDDTVGAFLEIESVDTIATVYVNGQKVLHSRNQFLPYHVNVTDIIALGENDITIKFKSSVKYAEKRADEYKKIFGHSLPPDCNPDIYHGECHQNFIRKAQYSFAWDWGPSFPTVGIPSTITINIYRGQYFHDFNWKTRFAHGKWKVAFEFDTFHYGARTIEYSVQIPELGIKESDYYRLSATKSLQTRSKNIMSLSIPMEHEPERWWPNGMGEQKLYDVVVSMGGQVKEKKIGFKTVELVQDLIDPKKPEKGRNFYFKINDEPVFLKGTNWIPVSMFRSDRENIAKTEFLLDSVAEVGMNAIRVWGGGFYESNHFYYYASKKGILVWQDLMFACALYPTTEEFIQNAEEEVSYNVDRISQHTSVIVFSGNNENEAAIRGHWWKASNYTESQQVKDYVLLYQRLAKIAKKVAPTIPFIMSSPSNGVETEEEGGVSKNPYDVRYGDIHYYNEFVNLWRDDTYLTPRCASEYGVQSYPMKETMLNWINESDWEYTSKAMFHRQHHPGGIATNLLMIFQHLPIPAECGSKSVSDVPSCKYISSASYMSRLAYFSQVHQSIALKTQTLHYRRFRNTTTNEGLGNTMCAMYWQLNDVWAAPTWSTIDFEQNWKMAHYEARRFFSNVAVYSFADETDFNLKVFLLNDNPYLLHNITVNVQMLSWGNGLDPILTNEFHIDSVPAGSSEVLKTGITFSKITELSEYLYVSTLYDSSGVKIHEDVLVPDFLFEVDFNTFGDVQISDVQRIDEKTYDLTITTDRVSPFTWITCKKPFTGWFSDNGFHMIQRLRKIRLIAKFEVDLEKSDFTVCNLKNCYV | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Mass (Da): 103978
Sequence Length: 900
Subcellular Location: Lysosome
EC: 3.2.1.25
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C6D9S0 | MKIVSAEVFVTCPGRNFVTLKITTDSGLTGLGDATLNGRELPVASYLNDHVCPQLIGRDAHQIEDIWQYFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASRTGVMVYCHTTGHSIDEVLDDYAKHRDQGFKAIRVQCGVPGMETTYGMAKGKGLAYEPATKGSLPEEQLWSTEKYLDFTPKLFEAVRDKFGFNEHLLHDMHHRLTPIEAARFGKSVEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSDLSPICMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWTFDNGYMHPGEKPGLGIEFDEKLAAKYPYDPAYLPVARLEDGTLWNW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 45595
Sequence Length: 404
EC: 4.2.1.-
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D9UNB2 | MASSAHSDSASADASAEIPAEILAPAPWSTPADDSEHLRITAVRTFLTAPQGCPYVIVRVETNQPGLYGLGCASDPQRTLAIRSVVDDYYAPMLLGRDPSDIEDLHRLLFNSGYWRGGSIGQNALAGVDVALWDIKGKVAGLPLHQLLGGRAREAADAYTHVDGDNAGEIAEKVLAAHERGYRHVRVQVSVPGTDTYGTAPRDAAEARRRELRAGSWDSLAYLRHVPPVLREIRERVGTGVELLHDAHERLTPSQARELVHEVEDARLFFLEDALAPEDAAHFDQLRAAGSVPLAVGELYHDVMMYLPLLQRQVIDFARIRIPTLGGLTPTRKLVAAVELFGARTAPHGPGDVSPVGMAANLGLDLSSPAFGVQEAATFREATREVFPGTPVPERGRFHGTGLPGLGVDFDEAAARKYPVPEPLRHDRWALLRNGDGSVQRP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 47830
Sequence Length: 442
EC: 4.2.1.-
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Q5SRI9 | MAKFRRRTCIILALFILFIFSLMMGLKMLRPNTATFGAPFGLDLLPELHQRTIHLGKNFDFQKSDRINSETNTKNLKSVEITMKPSKASELNLDELPPLNNYLHVFYYSWYGNPQFDGKYIHWNHPVLEHWDPRIAKNYPQGRHNPPDDIGSSFYPELGSYSSRDPSVIETHMRQMRSASIGVLALSWYPPDVNDENGEPTDNLVPTILDKAHKYNLKVTFHIEPYSNRDDQNMYKNVKYIIDKYGNHPAFYRYKTKTGNALPMFYVYDSYITKPEKWANLLTTSGSRSIRNSPYDGLFIALLVEEKHKYDILQSGFDGIYTYFATNGFTYGSSHQNWASLKLFCDKYNLIFIPSVGPGYIDTSIRPWNTQNTRNRINGKYYEIGLSAALQTRPSLISITSFNEWHEGTQIEKAVPKRTSNTVYLDYRPHKPGLYLELTRKWSEKYSKERATYALDRQLPVS | PTM: Undergoes proteolytic cleavage in the C-terminal region.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: H2O + N-{alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->6)]-alpha-Man-(1->6)]-beta-Man-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc}-L-asparaginyl-[protein] = alpha-D-glucosyl-(1->3)-D-mannopyranose + N(4)-{alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlaNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,2)
Sequence Mass (Da): 53671
Sequence Length: 462
Subcellular Location: Golgi apparatus membrane
EC: 3.2.1.130
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Q5RD93 | MAKFRRGTCIILALFILFIFSLMMGLKMLRPNTATFGAPFGLDLLPELHQRTVHLGKSFDFQKSDRINSETNTKNLKSVEITMKPSKASELNLDELPPLNNYLHVFYYSWYGNPQFDGKYIHWNHPVLEHWDPRIAKNYPQGRHNPPDDIGSSFYPELGSYSSRDPSVIETHMRQMRSASIGVLALSWYPPDVNDENGEPTDNLVPTILDKAHKYNLKVTFHIEPYSNRDDQNMYKNVKYIIDKYGNHPAFYRYKTKTGNALPMFYVYDSYITKPEKWANLLTTSGSWSIRNSPYDGLFIALLVEEKHKYDILQSGFDGIYTYFATNGFTYGSSHQNWASLKLFCDKYNLIFIPSVGPGYIDTSIRPWNTQNTRNRINGKYYEIALSAALQTHPSLISITSFNEWHEGTQIEKAVPKRTSNTVYLDYRPHKPGLYLELTRKWSEKYSKERATYALDHQLPVS | PTM: Undergoes proteolytic cleavage in the C-terminal region.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: H2O + N-{alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->6)]-alpha-Man-(1->6)]-beta-Man-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc}-L-asparaginyl-[protein] = alpha-D-glucosyl-(1->3)-D-mannopyranose + N(4)-{alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlaNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,2)
Sequence Mass (Da): 53537
Sequence Length: 462
Subcellular Location: Golgi apparatus membrane
EC: 3.2.1.130
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Q5AWB7 | MKFSQLILPFSAALSLVGSGVATPTTKPVNPRASRPARNLLAHLVRSAGNGTTLSGQQELKDADWVTDNVGFSPVILGVDLMDYSPSRVEFGAVSTSIEDAITYATQGGIITICWHWGELSHDWMTDERLTTLLTLGSPSGTYNTTEQPWWSNFYTEATSFNLSAAMNPASRDYKLILRDIDAIAEQLARLKDIPVLFRPLHEAEGGWFWWGATGAEPCKALYRLLFDRLTKKHGLNNLLWVWNSKDPLWYPGNEYVDVVSVDVYADNGDHSSQLEAYQALQGLTGNFSKLIALGEVGNIPDPELMREDGAQWAYWVTWNGDFIRGETKNPMEFKKAVYASELVYTLDEIQGWNL | Function: Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 39620
Sequence Length: 355
Subcellular Location: Secreted
EC: 3.2.1.78
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Q4WBS1 | MHPLPSVALLSAIGAVAAQVGPWGQCGGRSYTGETSCVSGWSCVLFNEWYSQCQPATTTSTSSVSATAAPSSTSSSKESVPSATTSKKPVPTGSSSFVKADGLKFNIDGETKYFAGTNAYWLPFLTNDADVDSVMDNLQKAGLKILRTWGFNDVNSKPSSGTVYFQLHDPSTGTTTINTGADGLQRLDYVVSAAEKRGIKLLIPLVNNWDDYGGMNAYVKAYGGSKTEWYTNSKIQSVYQAYIKAVVSRYRDSPAIMAWELSNEARCQGCSTDVIYNWTAKTSAYIKSLDPNHMVATGDEGMGVTVDSDGSYPYSTYEGSDFAKNLAAPDIDFGVFHLYTEDWGIKDNSWGNGWVTSHAKVCKAAGKPCLFEEYGLKDDHCSASLTWQKTSVSSGMAADLFWQYGQTLSTGPSPNDHFTIYYGTSDWQCGVADHLSTL | Function: Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 47327
Sequence Length: 438
Domain: Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Subcellular Location: Secreted
EC: 3.2.1.78
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Q9LYG3 | MGSTPTDLPGEDVADNRSGVGGGISDVYGEDSATLDQLVTPWVTSVASGYTLMRDPRYNKGLAFTDKERDAHYLTGLLPPVILSQDVQERKVMHNLRQYTVPLQRYMALMDLQERNERLFYKLLIDNVEELLPVVYTPTVGEACQKYGSIFRKPQGLYISLNEKGKILEVLKNWPQRGIQVIVVTDGERILGLGDLGCQGMGIPVGKLSLYTALGGIRPSACLPITIDVGTNNEKLLNDEFYIGLKQRRATGQEYAEFLHEFMCAVKQNYGEKVLVQFEDFANHNAFDLLSKYSDSHLVFNDDIQGTASVVLAGLIAAQKVLGKKLADHTFLFLGAGEAGTGIAELIALKISKETGAPITETRKKIWLVDSKGLIVSSRKESLQHFKQPWAHEHKPVKDLIGAVNAIKPTVLIGTSGVGQTFTKEVVEAMATNNEKPLILALSNPTSQAECTAEQAYTWTKGRAIFGSGSPFDPVVYDGKTYLPGQANNCYIFPGLGLGLIMSGAIRVRDDMLLAASEALAAQVTEEHYANGLIYPPFSNIREISANIAACVAAKTYDLGLASNLPRAKDLVKFAESSMYSPVYRNYR | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 64413
Sequence Length: 588
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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Q9XGZ0 | MGTNQTQISDEYVTGNSSGVGGGISDVYGEDSATLDQLVTPWVTSVASGYTLMRDPRYNKGLAFTDKERDAHYITGLLPPVVLSQDVQERKVMHNLRQYTVPLQRYMALMDLQERNERLFYKLLIDNVEELLPVVYTPTVGEACQKYGSIYRRPQGLYISLKEKGKILEVLKNWPQRGIQVIVVTDGERILGLGDLGCQGMGIPVGKLSLYTALGGIRPSACLPITIDVGTNNEKLLNNEFYIGLKQKRANGEEYAEFLQEFMCAVKQNYGEKVLVQFEDFANHHAFELLSKYCSSHLVFNDDIQGTASVVLAGLIAAQKVLGKSLADHTFLFLGAGEAGTGIAELIALKISKETGKPIDETRKKIWLVDSKGLIVSERKESLQHFKQPWAHDHKPVKELLAAVNAIKPTVLIGTSGVGKTFTKEVVEAMATLNEKPLILALSNPTSQAECTAEEAYTWTKGRAIFASGSPFDPVQYDGKKFTPGQANNCYIFPGLGLGLIMSGAIRVRDDMLLAASEALASQVTEENFANGLIYPPFANIRKISANIAASVGAKTYELGLASNLPRPKDLVKMAESCMYSPVYRNFR | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 64610
Sequence Length: 588
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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Q92060 | MKRGYEVVRDPHLNK | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP (+) and divalent metal ions, and decarboxylation of oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 1842
Sequence Length: 15
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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P40927 | MKKGYEVLRDPHLNKGMAFTLEERQQLNIHGLLPPCFLGQDAQVYSILKNFERLTSDLDRYILLMSLQDRNEKLFYKVLTSDIERFMPIVYTPTVGLACQHYGLAFRRPRGLFITIHDRGHIATMLQSWPESVIKAIVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVKPHQCLPVMLDVGTDNETLLKDPLYIGLRHKRIRGQAYDDLLDEFMEAVTSRYGMNCLIQFEDFANANAFRLLHKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNRLSDHTVLFQGAGEAALGIANLIVMAMQKEGVSKEEAIKRIWMVDSKGLIVKGRASLTPEKEHFAHEHCEMKNLEDIVKDIKPTVLIGVAAIGGAFTQQILQDMAAFNKRPIIFALSNPTSKAECTAEQLYKYTEGRGIFASGSPFDPVTLPSGQTLYPGQGNNSYVFPGVALGVISCGLKHIGDDVFLTTAEVIAQEVSEENLQEGRLYPPLVTIQQVSLKIAVRIAKEAYRNNTASTYPQPEDLEAFIRSQVYSTDYNCFVADSYTWPEEAMKVKL | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
PTM: The N-terminus is blocked.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 62054
Sequence Length: 557
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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Q6TU48 | MQNKPSFILRNPSANKGTGFNNEEREKLGLKGLLPPKVESLQEQSDRALSQFTSFNTNLERYIFLNCLRDRNETLFYYLLSNNLELMMPIIYTPTVGEACQKFGNEFRFAQGMYFASQDKGNIRAMMDNWPAEGVDIIVVSDGSRILGLGDLGTNGMGIPVGKLQLYVAGAGFCPTRTLPVIIDSGTNTKKYLEDKYYLGERHPRIPDSEYYPLVDEFLAAAFNKWPKVIVQFEDISNDHCFNLLDEYRNKYLCFNDDIQGTGSVILSGFINAVRSVQKPIKEHRMVFLGAGSAGIGVADCIMSLFDEAGVSKEEARKSFWFVDSKGLITTTRGDELTSQKKQYAREDYTYQLKSLLEVVRDVKPTAIIGLSGIGGSFSQEVIEEMAKHVEKPIVFALSNPTTNAECTAEQAYQWTDGRCIFASGSPFKPVEYKGKTFVPGQGNNMYIFPGLGLAASVCEAKHVTDAMIITAAKTLASFVEDSEVLTGKIYPGLQHIREISTRIAVKVIEKAYEEGMAQLPRPDNIEALVKSRQYVPSYDKSKN | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 60652
Sequence Length: 544
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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P16468 | MALPGGAAMNITIRLQFEKDIVSFSDIAAAIGKAGGDIVGIDVISSSKVHTVRDITVSALDTKQCDLIIEALKKIRGVKIVNVSDRTFLMHIGGKIETNSKIPVKTRDDLSRVYTPGVARVCTAIAEDPRKAYSLTIKRNTVAVVSDGTAVLGLGDIGPYAAMPVMEGKAMLFKEFAGVDAFPICLDTKDTEEIIQIVKAIAPAFGGINLEDISAPRCFEIEKRLKEELDIPVFHDDQHGTAVVLLAGLLNALKIVDKKLEDIKVVLTGIGAAGIACTKILLAAGVRNIIGVDRHGAIHRDETYENPYWQEYAQLTNPDNLKGSLSDVIAGADVFIGVSAPGILKVEDVKKMARDPIVFAMANPIPEIDPELAEPYVRVMATGRSDYPNQINNVLCFPGIFRGALDCRAREINEEMKLAAAKAIASVVTEDELNETYIIPSVFNSKVVERVRQAVVEAAYRTGVARKDNIPVGGYTGQ | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Function: In addition to the NAD-dependent oxidative decarboxylation of L-malate, the enzyme catalyzes the decarboxylation of oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = CO2 + NADH + pyruvate
Sequence Mass (Da): 51537
Sequence Length: 478
EC: 1.1.1.38
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P48163 | MEPEAPRRRHTHQRGYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQVLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDIEKFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIASVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQRRVRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFRLLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLVDSKGLIVKGRASLTQEKEKFAHEHEEMKNLEAIVQEIKPTALIGVAAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQCYKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFPGVALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRLYPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAFVRSQMYSTDYDQILPDCYSWPEEVQKIQTKVDQ | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 64150
Sequence Length: 572
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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P9WK24 | MSDARVPRIPAALSAPSLNRGVGFTHAQRRRLGLTGRLPSAVLTLDQQAERVWHQLQSLATELGRNLLLEQLHYRHEVLYFKVLADHLPELMPVVYTPTVGEAIQRFSDEYRGQRGLFLSIDEPDEIEEAFNTLGLGPEDVDLIVCTDAEAILGIGDWGVGGIQIAVGKLALYTAGGGVDPRRCLAVSLDVGTDNEQLLADPFYLGNRHARRRGREYDEFVSRYIETAQRLFPRAILHFEDFGPANARKILDTYGTDYCVFNDDMQGTGAVVLAAVYSGLKVTGIPLRDQTIVVFGAGTAGMGIADQIRDAMVADGATLEQAVSQIWPIDRPGLLFDDMDDLRDFQVPYAKNRHQLGVAVGDRVGLSDAIKIASPTILLGCSTVYGAFTKEVVEAMTASCKHPMIFPLSNPTSRMEAIPADVLAWSNGRALLATGSPVAPVEFDETTYVIGQANNVLAFPGIGLGVIVAGARLITRRMLHAAAKAIAHQANPTNPGDSLLPDVQNLRAISTTVAEAVYRAAVQDGVASRTHDDVRQAIVDTMWLPAYD | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NAD(+) = CO2 + NADH + pyruvate
Sequence Mass (Da): 59423
Sequence Length: 548
EC: 1.1.1.38
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P12628 | MSSISLKENGGEVSVKKDYSNGGGVRDLYGEDSATEDHLITPWTFSVASGCSLLRDPRYNKGLAFTEGERDAHYLRGLLPPSVFNQELQEKRLMHNLRQYEVPLHRYMALMDLQERNERLFYKLLIDNVAELLPVVYTPTVGEACQKYGSIFRRPQGLYISLKEKGKILEVLKNWPEKSIQVIVVTDGERILGLGDLGCQGMGIPVGKLSLYTALGGVRPSSCLPVTIDVGTNNEKLLNDEFYIGLRQRRATGQEYATFLDEFMRAVKQNYGEKVLVQFEDFANHNAFDLLEKYSSSHLVFNDDIQGTASVVLAGLLASLKLVGGTLADHTFLFLGAGEAGTGIAELIAVEVSKQTKAPVEETRKKIWLVDSKGLIVSSRLESLQQFKKPWAHEHEPVKGLLEAVKAIKPTVLIGSSGAGKTFTKEVVETMASLNEKPLILALSNPTSQSECTAEEAYTWSKGRAIFASGSPFDPVEYEGKLFVPGQANNAYIFPGFGLGLIMSGAIRVRDEMLLAASEALAAQVSEENYDKGLIYPPFTNIRKISANIAAKVAAKAYDLGLASHLKRPKDLVKYAESCMYSPGYRSYR | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 64932
Sequence Length: 589
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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Q29558 | GYGLTRIPHLNKDLAFTLEERQQLNIHGLLPPCFISQDIQVLRVIKNFERLNSDFDRYLLLMDLQDRNEKLFYKVLMSDIEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDRGHVASVLNAWPEDVIKAVVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQECLPVILDVGTENEELLKDPLYIGLRQRRVRGPEYDDFLDEFMEAVSSKYGMNCLIQFEDFANINAFRLLKKYQNQYCTFNDDIQGTASVAVAGILAALRITKNKLSDQTILFQGAGEAALGIAHLIVMAMEKEGVPKEKAIKKIWLVDSKGLIVKGRAALTNEKEEFAHEHEEMKNLEAIVQDIKPTALIGVAAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECTAERGYTLTQGRAIFASGSPFDPVTLPSGQTLYPGQGNNSYVFPGVALAVVACGLRHITDKIFLTTAEVIAQQVSDKHLEEGRLYPPLNTIRDVSLKIAEKIVRDAYQEKTATIYPEPSNKEAFVRSQMYSTDYDQILPDGYSWPEEAQKIQTKLD | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 62006
Sequence Length: 557
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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P13697 | MDPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLKIHGLLPPCIVNQEIQVLRVIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSNVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANLNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLIVMAMEKEGLSKEKARQKIWLVDSKGLIVKGRASLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSNPTSKAECSAEECYKVTKGRAIFASGSPFDPVTLPDGRTLFPGQGNNSYVFPGVALGVVACGLRHINDSVFLTTAEVISQQVSDKHLEEGRLYPPLNTIRDVSLKIAVKIVQDAYKEKMATVYPEPQNKEEFVSSQMYSTNYDQILPDCYSWPEEVQKIQTKVNQ | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = CO2 + NADPH + pyruvate
Sequence Mass (Da): 64003
Sequence Length: 572
Subcellular Location: Cytoplasm
EC: 1.1.1.40
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P40375 | MPAGTKEQIECPLKGVTLLNSPRYNKDTAFTPEERQKFEISSRLPPIVETLQQQVDRCYDQYKAIGDEPLQKNLYLSQLSVTNQTLFYALISQHLIEMIPIIYTPTEGDAIKQFSDIYRYPEGCYLDIDHNDLSYIKQQLSEFGKSDSVEYIIITDSEGILGIGDQGVGGVLISVAKGHLMTLCAGLDPNRFLPIVLDVGTNNETHRKNHQYMGLRKDRVRGEQYDSFLDNVIKAIREVFPEAFIHFEDFGLANAKRILDHYRPDIACFNDDIQGTGAVALAAIIGALHVTKSPLTEQRIMIFGAGTAGVGIANQIVAGMVTDGLSLDKARGNLFMIDRCGLLLERHAKIATDGQKPFLKKDSDFKEVPSGDINLESAIALVKPTILLGCSGQPGKFTEKAIREMSKHVERPIIFPISNPTTLMEAKPDQIDKWSDGKALIATGSPLPPLNRNGKKYVISQCNNALLYPALGVACVLSRCKLLSDGMLKAASDALATVPRSLFAADEALLPDLNNAREISRHIVFAVLKQAVSEGMSTVDLPKDDAKLKEWIIEREWNPEYKPFV | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NAD(+) = CO2 + NADH + pyruvate
Sequence Mass (Da): 62535
Sequence Length: 565
EC: 1.1.1.38
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Q6CA79 | MAEAIEKVADKVADLVVDDKPAAVPESTSDHEDGDDNDDAVNEGEAVDGEKKKKKKKNKKKKKKGPAVQTEPPTVPIDRFFTSGIFPEGEICEHPHKTFKPKGTAVDPFADSEDEREAAEERAKDDAKHGSDDPLDFNRLRTTNEEKRYLDREQAAVHNEWRKGAEIHRVVRKYARDNIKAGMTMTSIAEMIEDSVRALSNEEDSLKGGQGFPTGVSLNHCAAHYTPNAGDKIVLKEDDVLKVDFGVHVNGKIIDSAFTHVQNDKWQGLLDAVKAATETGIREAGIDVRLGDIGEAIQETMESHEVEVDGKVYQVKSIRNLNGHNIAPYEIHGGKSVPIVKSADMTKMEEGETFAIETFGSTGRGYVVTDGECSHYAKNVGVGHVPLRVNKAKQLLATIDKNFGTLPFCRRYLDRLGEEKYLLALKNLVQSGVVQDYPPLVDQKGCQTAQYEHTIYLRPTCKEILSRGDDY | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 52156
Sequence Length: 471
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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P31397 | MLPIGIFYQFYAYFALVLSIPILYMQLRARNIPCLLLLFWLTLTTLIYVVESAIWSNPYAETIRWMGYGLCDITSRIVTCSSIGIPASAFTLVLYLDTVIRRDHPLKRYENWIWHVCLSILLPLIIMAMMVPLESNRYVVICMNGCYSSFYQTWYTLLFFYIPPCLLSFGGLFFVSRIVVLYWRRQRELQQFFQRDSQLTSKRFLRLLCLAAVFFLGYFPLTIFMVVANGKLQQFLPFNHELVEAWHQESITYYPTTKVGLNDWVPPTVLYLMSLFFSTSGGWTEKVALILWSLLVWLPFTKNTALGRHAQFKLDCCKSIESTMAGKTLDSTDFKEKCLVLERQWSKSSIPSDNSSELQDAAKYV | Function: Receptor for the peptide pheromone M-factor, a mating factor of S.pombe. Pheromone signaling is essential for initiation of meiosis in S.pombe; M-factor signaling alone may be sufficient.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42498
Sequence Length: 365
Subcellular Location: Membrane
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P27874 | MPLPRAYLGTAQPPASVKEFYFVRHGATDLNEKEMHLQGEKHWGVQGAGTNIGLNGTGKRQAVLAGNVLRKLPIGSVVCSPLLRAIQTALIANIGFLCFDIDEDLKERDFGKHEGGYGPLKMFEDNYPDCEDTEMFSLRVAKALTHAKNENTLFVSHGGVLRVIAALLGVDLTKEHTNNGRVLHFRRGFSHWTVEIHQSPVILVSGSNRGVGKAIAEDLIAHGYRLSLGARKVKDLEVAFGPQDEWLHYARFDAEDHGTMAAWVTAAVEKFGRIDGLVNNAGYGEPVNLDKHVDYQRFHLQWYINCVAPLRMTELCLPHLYETGSGRIVNINSMSGQRVLNPLVGYNMTKHALGGLTKTTQHVGWDRRCAAIDICLGFVATDMSAWTDLIASKDMIQPEDIAKLVREAIERPNRAYVPRSEVMCIKEATR | Function: Reduces deoxy-fructosyl-glutamine to mannopine.
Sequence Mass (Da): 47722
Sequence Length: 430
Pathway: Opine metabolism; mannopine biosynthesis.
EC: 1.-.-.-
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Q8SRK0 | MSKDPKGYYKVLELSPGASVAEVRKAYAKQQAKYHLDSPYMKNKLKNAASDEEREKIKKECGEMSARLNSAKSVLFDEKKKKEYDSGMGEFGAHFSGGGYSDIFDIFSQFTGGRGHQRTNKVSSTKYVITVSLRESFVGKVSKFNVRTEKVCTTCDGKGGKDVETCKKCNGNGVYTSRRSLGGFVTLAETRCDGCDGSGHKIKGKPCSTCNGAEYIQDKTMFEVNIKPGVRKGEKIVFEGMGDQRRGHVPGDVIFIIDVQEDSRFERCGNDLVGNIDIPLYTAIGGGVVYFTHIDGRQLEINVSPFRTFDTALKIRNEGFKGSRTGNLILKPNIIIGSESDRAKIMQVLSAPSKKPYGTFTKVNSEFGSMPEPERDHEDASEEGAQSARSFFNNFSFF | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Probably involved in mitosomal protein import.
Sequence Mass (Da): 43986
Sequence Length: 398
Subcellular Location: Cytoplasm
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Q1DB00 | MSPPQTTLPVTEAGLVPLLQPYGPYVLVRKLAEGGMAEIFLAKLLGADGFERNVVIKRMLPHLTNNPDFVEMFRDEARLAAKLAHPNIVQIQELGFAEGCYYICMEYLAGEDFSTTLRLAGRKRHYVPLPVVLRVLIDAARGLHFAHEFTNEAGQPLNVVHRDISPSNLYLTYQGQVKVLDFGIAKAESRLVNTRTGVVKGKYMYMAPEQARGKEVDRRADIFALGVSLYEALTHVRPFSRENDLAVLNALLQGELKPPRELRPDLPEELEAILLKAMAFKPEDRYPTAEAFADALETFLSEHLSGSGAMPLGAFLKGHFGEERFTERSRIPTLATLTATYGGAAAGAQGQAPGAEPHGTNLYGVLAREGDATSAQRPGMSMRPSSPGVPAHGAASRGSTSPESAPTAGGRRWRTLAVGLAGGLMLAAAGIVGYRQWMTTPASVSLVPATVPVVEAVAPEAAAAQVGAPMEAVAPVGAAAQAGSLTDAVANGAGGDVGETDSAQLSVDAAGVTETDEAGLAGAASDVEAEADEEGADAAPVRSKKASSQKRVTLGIDDVQRVVSRGRARITTCFERYKADLPSSQGEVQVQLTIVSSGKVRAGTRGPLASSGVGRCLEAQAERLRFPPHRDQEVTVVMPFSWRVTQ | Function: Essential for growth. Interacts with MglA to control social gliding motility.
PTM: Autophosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 68576
Sequence Length: 646
Subcellular Location: Cell inner membrane
EC: 2.7.10.2
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P48740 | MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN | Function: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development .
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Sequence Mass (Da): 79247
Sequence Length: 699
Subcellular Location: Secreted
EC: 3.4.21.-
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P98064 | MRFLSFWRLLLYHALCLALPEVSAHTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGVPKFSRKQISRIFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEQPSTEGTMVIVSGWGKQFLQRFPENLMEIEIPIVNSDTCQEAYTPLKKKVTKDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRITGVRN | Function: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Sequence Mass (Da): 79968
Sequence Length: 704
Subcellular Location: Secreted
EC: 3.4.21.-
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O00187 | MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF | Function: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Catalytic Activity: Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
Sequence Mass (Da): 75702
Sequence Length: 686
Subcellular Location: Secreted
EC: 3.4.21.104
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Q9JJS8 | MRLLIVLGLLWSLVATLLGSKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTSTAQPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKPVCGLSTHTSGGRIIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIINNF | Function: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
PTM: N-glycosylated.
Catalytic Activity: Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
Sequence Mass (Da): 75667
Sequence Length: 685
Subcellular Location: Secreted
EC: 3.4.21.104
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Q85212 | MKSIRQLLSLAKKEKKREKKSNHGSHSMEWESPPSYNEIKSPSAPIFGYDYEDMEYLPTLGVQTLKLQYKCVLQVRSESPFTSYLDAVDNVANWEKQYNGFSGKKPFYRAVMVRAVQAMKANPMSLQDGRSPEYTSEIEGRCLVFHSLGHIPPMMYMCEQFTRDWSGRRNQGIVNVKIWVGVTDTLDNLDQIFDPKKHFSEEEMLSAATILGLEVKKSSDNNYIISKSY | Function: Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibit interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity).
PTM: Phosphorylated by host.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26344
Sequence Length: 229
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. M contains two overlapping L domains: a PPXY motif which interacts with the WW domain 3 of NEDD4 and a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity).
Subcellular Location: Virion membrane
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P16629 | MPSISIPADPTNPRQSIKAFPIVINSDGGEKGRLVKQLRTTYLNDLDTHEPLVTFINTYGFIYEQDRGNTIVGEDQLGKKREAVTAAMVTLGCGPNLPSLGNVLGQLREFQVTVRKTSSKAEEMVFEIVKYPRIFRGHTLIQKGLVCVSAEKFVKSPGKIQSGMDYLFIPTFLSVTYCPAAIKFQVPGPMLKMRSRYTQSLQLELMIRILCKPDSPLMKVHTPDKEGRGCLVSVWLHVCNIFKSGNKNGSEWQEYWMRKCANMQLEVSIADMWGPTIIIHARGHIPKSAKLFFGKGGWSCHPLHEVVPSVTKTLWSVGCEITKAKAIIQESSISLLVETTDIISPKVKISSKHRRFVKSNWGLFKKTKSLPNLTELE | Function: The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane.
Sequence Mass (Da): 42250
Sequence Length: 377
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. The matrix protein contains one L domain: a FPIV motif.
Subcellular Location: Virion
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P31891 | MSAYATQGFNLDDRGRRIVVDPVTRIEGHMRCEVNVDANNVIRNAVSTGTMWRGLEVILKGRDPRDAWAFVERICGVCTGCHALASVRAVENALDIRIPKNAHLIREIMAKTLQVHDHAVHFYHLHALDWVDVMSALKADPKRTSELQQLVSPAHPLSSAGYFRDIQNRLKRFVESGQLGPFMNGYWGSKAYVLPPEANLMAVTHYLEALDLQKEWVKIHTIFGGKNPHPNYLVGGVPCAINLDGIGAASAPVNMERLSFVKARIDEIIEFNKNVYVPDVLAIGTLYKQAGWLYGGGLAATNVLDYGEYPNVAYNKSTDQLPGGAILNGNWDEVFPVDPRDSQQVQEFVSHSWYKYADESVGLHPWDGVTEPNYVLGANTKGTRTRIEQIDESAKYSWIKSPRWRGHAMEVGPLSRYILAYAHARSGNKYAERPKEQLEYSAQMINSAIPKALGLPETQYTLKQLLPSTIGRTLARALESQYCGEMMHSDWHDLVANIRAGDTATANVDKWDPATWPLQAKGVGTVAAPRGALGHWIRIKDGRIENYQCVVPTTWNGSPRDYKGQIGAFEASLMNTPMVNPEQPVEILRTLHSFDPCLACSTHVMSAEGQELTTVKVR | Cofactor: Binds 1 nickel ion per subunit.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68795
Sequence Length: 618
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P0ACD8 | MSTQYETQGYTINNAGRRLVVDPITRIEGHMRCEVNINDQNVITNAVSCGTMFRGLEIILQGRDPRDAWAFVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHLVHFYQLAGMDWIDVLDALKADPRKTSELAQSLSSWPKSSPGYFFDVQNRLKKFVEGGQLGIFRNGYWGHPQYKLPPEANLMGFAHYLEALDFQREIVKIHAVFGGKNPHPNWIVGGMPCAINIDESGAVGAVNMERLNLVQSIITRTADFINNVMIPDALAIGQFNKPWSEIGTGLSDKCVLSYGAFPDIANDFGEKSLLMPGGAVINGDFNNVLPVDLVDPQQVQEFVDHAWYRYPNDQVGRHPFDGITDPWYNPGDVKGSDTNIQQLNEQERYSWIKAPRWRGNAMEVGPLARTLIAYHKGDAATVESVDRMMSALNLPLSGIQSTLGRILCRAHEAQWAAGKLQYFFDKLMTNLKNGNLATASTEKWEPATWPTECRGVGFTEAPRGALGHWAAIRDGKIDLYQCVVPTTWNASPRDPKGQIGAYEAALMNTKMAIPEQPLEILRTLHSFDPCLACSTHVLGDDGSELISVQVR | Cofactor: Binds 1 nickel ion per subunit.
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66253
Sequence Length: 597
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P15284 | MTTQTPNGFTLDNAGKRIVVDPVTRIEGHMRCEVNVNDQGIITNAVSTGTMWRGLEVILKGRDPRDAWAFTERICGVCTGTHALTSVRAVESALGITIPDNANSIRNMMQLNLQIHDHIVHFYHLHALDWVNPVNALRADPKATSELQQMVSPSHPLSSPGYFRDVQNRLKKFVESGQLGLFKNGYWDNPAYKLPPEADLMATTHYLEALDLQKEVVKVHTIFGGKNPHPNWLVGGVPCPINVDGVGAVGAINMERLNLVSSIIDRCTEFTRNVYLPDLKAIGGFYKEWLYGGGLSGQSVLSYGDIPENPNDFSAGQLHLPRGAIINGNLNEVHDVDTTDPEQVQEFVDHSWYDYGEPGMGLHPWDGRTEPKFELGPNLKGTRTNIENIDEGAKYSWIKAPRWRGNAMEVGPLAATSSVTRKGHEDIKNQVEGLLRDMNLPVSALFSTLGRTAARALEAEYCCRLQKHFFDKLVTNIKNGDSSTANVEKWDPSTWPKEAKGVGMTEAPRGALGHWVKIKDGRIENYQCVVPTTWNGSPRDSKGNIGAFEASLLNTKMERPEEPVEILRTLHSFDPCLACSTHVMSAEGAPLTTVKVR | Cofactor: Binds 1 nickel ion per subunit.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66046
Sequence Length: 597
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P31883 | MTKRIVVDPITRIEGHLRIEVVVDENNVIQDAFSTATLWRGLETILKGRDPRDAGFFTQRICGVCTYSHYKAGISAVENALGIKPPLNAELIRSLMSISLILHDHTVHFYHLHGLDWCDITSALKADPVAASKLAFKYSPNPIATGADELTAVQKRVAEFAAKGNLGPFANAYWGHKTYRFSPEQNLIVLSHYLKALEVQRVAAQMMAIWGAKQPHPQSLTVGGVTSVMDALDPSRLGDWLTKYKYVADFVNRAYYADVVMAAEVFKSEPSVLGGCNVKNFYSYQEIPLNKTEWMYSTGIVMDGDITKVHEINEDLITEEATHAWYKENKALHPYDGQQDPNYTGFKDMETVGPDGTMVKTKVIDEKGKYTWIKAPRYGGKPLEVGPLATIVVGLAAKNPRIEKVATQFLKDTGLPLAALFTTLGRTAARMLECKLSADYGFEAFNSLIANLKVDQSTYTTYKIDKNKEYKGRYMGTVPRGVLSHWVRIKNGVIQNYQAVVPSTWNAGPRDANGTKGPYEASLVGMKLQDLSQPLEIIRVIHSFDPCIACAVHVMDTKGNELSQYRVDPITVGCNL | Cofactor: Binds 1 nickel ion per subunit.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: a menaquinone + H2 = a menaquinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63977
Sequence Length: 576
Subcellular Location: Cell membrane
EC: 1.12.5.1
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P0ACE1 | MSQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPRDAWMIVQRICGVCTTTHALSSVRAAESALNIDVPVNAQYIRNIILAAHTTHDHIVHFYQLSALDWVDITSALQADPTKASEMLKGVSTWHLNSPEEFTKVQNKIKDLVASGQLGIFANGYWGHPAMKLPPEVNLIAVAHYLQALECQRDANRVVALLGGKTPHIQNLAVGGVANPINLDGLGVLNLERLMYIKSFIDKLSDFVEQVYKVDTAVIAAFYPEWLTRGKGAVNYLSVPEFPTDSKNGSFLFPGGYIENADLSSYRPITSHSDEYLIKGIQESAKHSWYKDEAPQAPWEGTTIPAYDGWSDDGKYSWVKSPTFYGKTVEVGPLANMLVKLAAGRESTQNKLNEIVAIYQKLTGNTLEVAQLHSTLGRIIGRTVHCCELQDILQNQYSALITNIGKGDHTTFVKPNIPATGEFKGVGFLEAPRGMLSHWMVIKDGIISNYQAVVPSTWNSGPRNFNDDVGPYEQSLVGTPVADPNKPLEVVRTIHSFDPCMACAVHVVDADGNEVVSVKVL | Cofactor: Binds 1 nickel ion per subunit.
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake (By similarity).
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62491
Sequence Length: 567
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P31892 | MVETFYEVMRRQGISRRSFLKYCSLTATSLGLGPSFLPQIAHAMETKPRTPVLWLHGLECTCCSESFIRSAHPLAKDVVLSMISLDYDDTLMAAAGHQAEAILEEIMTKYKGNYILAVEGNPPLNQDGMSCIIGGRPFIEQLKYVAKDAKAIISWGSCASWGCVQAAKPNPTQATPVHKVITDKPIIKVPGCPPIAEVMTGVITYMLTFDRIPELDRQGRPKMFYSQRIHDKCYRRPHFDAGQFVEEWDDESARKGFCLYKMGCKGPTTYNACSTTRWNEGTSFPIQSGHGCIGCSEDGFWDKGSFYDRLTGISQFGVEANADKIGGTASVVVGAAVTAHAAASAIKRASKKNETSGSEH | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: A + H2 = AH2
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39472
Sequence Length: 360
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P69740 | MNNEETFYQAMRRQGVTRRSFLKYCSLAATSLGLGAGMAPKIAWALENKPRIPVVWIHGLECTCCTESFIRSAHPLAKDVILSLISLDYDDTLMAAAGTQAEEVFEDIITQYNGKYILAVEGNPPLGEQGMFCISSGRPFIEKLKRAAAGASAIIAWGTCASWGCVQAARPNPTQATPIDKVITDKPIIKVPGCPPIPDVMSAIITYMVTFDRLPDVDRMGRPLMFYGQRIHDKCYRRAHFDAGEFVQSWDDDAARKGYCLYKMGCKGPTTYNACSSTRWNDGVSFPIQSGHGCLGCAENGFWDRGSFYSRVVDIPQMGTHSTADTVGLTALGVVAAAVGVHAVASAVDQRRRHNQQPTETEHQPGNEDKQA | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
Catalytic Activity: A + H2 = AH2
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40681
Sequence Length: 372
Subcellular Location: Cell inner membrane
EC: 1.12.99.6
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Q91439 | MASATTSDHAKQAGGAHSRQRDSGLLDQLGKLFGQEGSRKVPEKGKEPATRSVLMAPTTHKAHQGARRQTDDSPVVHFFKNMMSPKKAPVQQKAKSGASRAITKFIWGTDGQRAHYGAAGSSKSKDGFRGRRDGSGTLSSFFKMGKKGEGSPARR | Function: This protein may function to maintain proper structure of myelin.
PTM: Several charge isomers are produced as a result of optional post-translational modifications, such as phosphorylation, deamidation and citrullination. Dogfish MBP contains four major components designated as C1, C2, C3 and C8. C1 and C3, but not C2 are phosphorylated at either Ser-121 or Ser-122; C2 is phosphorylated at 2 or 3 sites among Ser-135, Ser-139 and Ser-140. Hydroxyproline and citrulline are present but were not identified in either C1, C2 or C3, which suggests their presence in C8.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16611
Sequence Length: 155
Subcellular Location: Myelin membrane
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P87346 | MASQKHSRGHGSKQMATASTYDHSRHGYGAHGRHRDSGLLDSLGRFFGGERSVPRKGSGKEVHMSRSGYLSSSPQRSPYHAHGRHVDDNPVVHFFRNIVSPRTPPPSQPKRGFSRFSWGAENHKPYYGGYGSRSLEHHKSSYKGYKDPHREGHGSLSRIFKLGGQRSRSSSPMARR | Function: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Plays a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity).
PTM: As in other animals, several charge isomers may be produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19720
Sequence Length: 176
Subcellular Location: Myelin membrane
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O49500 | MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTGSSSSGDGQPSMIHLPALTRNIHQFAWSASSSSRANSMPEEGLSPWDAPRINSEQPVFTTPANETRNPVQDQFCWSFTRGNPSTSGDSPFVPRAGSSSGIHGLQPNPTWVTPHNQSRISEVAPWSLFPSIESESATHGASLPLLPTGPSVSSNEAAAPSGSSSRSHRSRQRRSGLLLERQNDHLHLRHLGRSLAADNDGRNRLISEIRQVLSAMRRGENLRFEDYMVFDPLIYQGMAEMHDRHRDMRLDVDNMSYEELLALGERIGDVSTGLSEEVILKVMKQHKHTSSAAGSHQDMEPCCVCQEEYAEGDDLGTLGCGHEFHTACVKQWLMLKNLCPICKTVALST | Function: E3 ubiquitin-protein ligase that functions as regulator of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent way. Proteasome-dependent degradation of MED25 seems to activate its function as positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT and consequently to promote flowering. May function downstream of HAL3 and be required for HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 71539
Sequence Length: 666
Domain: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4ZIN3 | MSEHVEPAAPGPGPNGGGGGPAPARGPRTPNLNPNPLINVRDRLFHALFFKMAVTYSRLFPPAFRRLFEFFVLLKALFVLFVLAYIHIVFSRSPINCLEHVRDKWPREGILRVEVRHNSSRAPVFLQFCDSGGRGSFPGLAVEPGSNLDMEDEEEEELTMEMFGNSSIKFELDIEPKVFKPPSSTEALNDSQEFPFPETPTKVWPQDEYIVEYSLEYGFLRLSQATRQRLSIPVMVVTLDPTRDQCFGDRFSRLLLDEFLGYDDILMSSVKGLAENEENKGFLRNVVSGEHYRFVSMWMARTSYLAAFAIMVIFTLSVSMLLRYSHHQIFVFIVDLLQMLEMNMAIAFPAAPLLTVILALVGMEAIMSEFFNDTTTAFYIILIVWLADQYDAICCHTSTSKRHWLRFFYLYHFAFYAYHYRFNGQYSSLALVTSWLFIQHSMIYFFHHYELPAILQQVRIQEMLLQAPPLGPGTPTALPDDMNNNSGAPATAPDSAGQPPALGPVSPGASGSPGPVAAAPSSLVAAAASVAAAAGGDLGWMAETAAIITDASFLSGLSASLLERRPASPLGPAGGLPHAPQDSVPPSDSAASDTTPLGAAVGGPSPASMAPTEAPSEVGS | Function: May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67889
Sequence Length: 620
Subcellular Location: Endoplasmic reticulum membrane
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Q8CIV2 | MSEHAAAPGPGPNGGGGGGAAPVRGPRGPNLNPNPLINVRDRLFHALFFKMAVTYSRLFPPAFRRLFEFFVLLKALFVLFVLAYIHIVFSRSPINCLEHVRDRWPREGVLRVEVRHNSSRAPVILQFCDGGLGGLELEPGGLELEEEELTVEMFTNSSIKFELDIEPKVFKPQSGADALNDSQDFPFPETPAKVWPQDEYIVEYSLEYGFLRLSQATRQRLSIPVMVVTLDPTRDQCFGDRFSRLLLDEFLGYDDILMSSVKGLAENEENKGFLRNVVSGEHYRFVSMWMARTSYLAAFVIMVIFTLSVSMLLRYSHHQIFVFIVDLLQMLEMNMAIAFPAAPLLTVILALVGMEAIMSEFFNDTTTAFYIILTVWLADQYDAICCHTNTSKRHWLRFFYLYHFAFYAYHYRFNGQYSSLALVTSWLFIQHSMIYFFHHYELPAILQQIRIQEMLLQTPPLGPGTPTALPDDLNNNSGSPATPDPSPPLALGPSSSPAPTGGASGPGSLGAGASVSGSDLGWVAETAAIISDASFLSGLSASLLERRPTAPSTPDSSRPDPGVPLEDAPAPAGS | Function: May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63561
Sequence Length: 574
Subcellular Location: Endoplasmic reticulum membrane
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P84477 | IIGGYECKPHSQPWQAFLVDNK | Function: Serine protease that selectively cleaves Arg-|-Xaa bonds.
Sequence Mass (Da): 2531
Sequence Length: 22
Subcellular Location: Cytoplasm
EC: 3.4.21.-
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O74477 | MSYNSNPYNGGQYPPYNTYTRPNYSPNNGSQSNNTVHQYQPPRMPPPSTRPQTDGNSNQIPMENVGHISLSSANSHAYAPPSGPPPNTGANSYGNPNYSGPQLPNTQTQSYNLAGGGNFQYQYSTCQGKRKALLIGINYLNTQNELQGCINDVMSMSQLLIQRYGYKQEDMVIMTDTASNQRAIPTRQNMLDAMRWLVSDAQPNDALFFHYSGHGGQTKDLDGDEVDGYDETIYPLDHQYAGQIIDDEMHEIMVKPLPAGCRLTALFDSCHSGGALDLPFTYSTKGVLKEPNMLKESGMDVLHAGLSYASGDIMGAINNVKNIFTSATNGFNNNALQYSRQVKFSPADVISLSGCKDNQTSADTSVNGFATGALSYAFREVVTQNPQLSYLQLLRGIRQVLSNKYSQLPQLSCSHPLDMNLAMVL | Function: Involved in cell death (apoptosis).
Sequence Mass (Da): 46627
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A6ZP43 | MYPGSGRYTYNNAGGNNGYQRPMAPPPNQQYGQQYGQQYEQQYGQQYGQQNDQQFSQQYAPPPGPPPMAYNRPVYPPPQFQQEQAKAQLSNGYNNPNVNASNMYGPPQNMSLPPPQTQTIQGTDQPYQYSQCTGRRKALIIGINYIGSKNQLRGCINDAHNIFNFLTNGYGYSSDDIVILTDDQNDLVRVPTRANMIRAMQWLVKDAQPNDSLFLHYSGHGGQTEDLDGDEEDGMDDVIYPVDFETQGPIIDDEMHDIMVKPLQQGVRLTALFDSCHSGTVLDLPYTYSTKGIIKEPNIWKDVGQDGLQAAISYATGNRAALIGSLGSIFKTVKGGMGNNVDRERVRQIKFSAADVVMLSGSKDNQTSADAVEDGQNTGAMSHAFIKVMTLQPQQSYLSLLQNMRKELAGKYSQKPQLSSSHPIDVNLQFIM | Function: Mediates cell death (apoptosis) triggered by oxygen stress, salt stress or chronological aging. Regulated cell death can prevent a release of toxic cellular components, thus avoiding necrotic collapse of the colony, and can also provide nutrients for healthy cells. Therefore, regulated cell death in yeast colonies can be as important for their development as are apoptosis and related processes that occur within metazoa (By similarity).
Sequence Mass (Da): 47982
Sequence Length: 432
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q585F3 | MCSLITQLCDAGQLADYVGLGWLNAVSSQPYLVQALGLQPPPRRVDVDAAFRDAKGLHGHQPWVATPLPGQTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKGFKQVPQLSASKAIDLDQTFSLTEMFSVDRSIQ | Function: Cysteine protease that cleaves specifically after arginine or lysine residues.
PTM: Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates . After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds . In vivo, the unprocessed enzyme appears to be the predominant form (By similarity).
Sequence Mass (Da): 37779
Sequence Length: 347
Domain: There are 2 calcium binding sites with high and low affinity, respectively.
Subcellular Location: Recycling endosome
EC: 3.4.22.-
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B7G6D3 | MGFLRRQLREQFEKKKPEALQADIRMISGCQDVQTSADVSNVSSFQLPDPAGNAGGACTSTLLNVLYKDHQTPEDTMSFVELLNKMRENLEAKGFSQVPQLTASHPIDVNDDFDLVPPAATGTRRALLIGINYVGHEQGVLRGCHNDVKNMVEYIKAVHGFEDENITILMDDGEHTAPTHANMIAAYKKIVALSKADDALFCHFSGHGAKIRDDDRGEEDDGYDETLVPIDYHENGMIRDDDLYDILIKPLVQGVHLVCLMDCCHSGTVLDLPYVYKADGNFTEMEIDENFDFKKLLGKFGIDDFDKFGGEALGKINGDALGKVGKDALGKLNKFFG | Function: Cysteine protease that cleaves specifically after arginine residues.
PTM: Auto-proteolytic cleavage into a large and a small subunit which probably remain associated by non-covalent bonds.
Sequence Mass (Da): 37250
Sequence Length: 337
EC: 3.4.22.-
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Q9XVS1 | MSSSEVASHYNKVLQVGIEGRKESRIFFMRNMNNWVKSQLINDAKQRVNDNGVNNPRVLDLACGKGGDLKKWDIAGAKDVVMADVADVSIQQAEERYKQMFGYKKNNIFTVQFIVADCTKENLEDRIENKDPFDLVSCQFALHYSFVDEASARIFLKNAVGMLKPGGVFIGTLPDADRIVWSMRNGENGQFANEVCKITYENVEELAEGKVPLFGAKFHFSLDEQVNCPEFLAYFPLVKHLLEELDMELLFVHNFAEAINKWLEPGRRLLESMTGLETYPNEKLSGKSDDEYLEAKAKLDAFPEDERIKTMGTLSKSEWEAICMYLVFGFRKKKSEAEKTEEEPATTKPVAESESEQKEVTESEEKEDQEDCEHQEAQTN | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43312
Sequence Length: 380
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q5ADX5 | MSTDSYTPSQEPGSKRLKTGESVFARRGVSPSTGGVASAYGNESEKKPSWLQTNKSDIDGKYDKYGERRNAHTTTRDSRLDRLKRVRQKSAEREDVGHEGDEGDEDEGILPYIHLQAANPAIIHNEKQENYRTFQSRISNRENRDINSIVRAHYNQRTQQAKQQGSRVNSPIYKMRNFNNAIKYILLGNWAKHNPEELDLFSFLDLCCGKGGDLNKCQFIGIDQYIGIDIADLSVKEAFERYTKQKARFRHSNQNSNRYTFEACFATGDCFTQFVPDILEPNFPGIIERAFPVDIVSAQFSLHYSFESEEKVRTLLTNVTRSLRSGGTFIGTIPSSDFIKAKIVDKHLQRDEKGKAKFGNSLYSVTFEKDPPEDGVFRPAFGNKYNYWLKDAVDNVPEYVVPFETLRSLCEEYDLVLKYKKSFTDIFNQEIPKYFSKLNKNLIDGMKRSDGKYGAEGDEKEAVAFYIGFVFEKV | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54248
Sequence Length: 474
Subcellular Location: Nucleus
EC: 2.1.1.56
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P0CO64 | MVYDPIRDCDVPAPHISAPPLSRSRSPPPPHRTPSASGSLRGLLNDSPPPREPPRAASVHEDAESHRPKLSNILNDAEPPRQRSMLPPQQPIHAELEHGRRTSAGSHAAQLARSPSMSLSPRSQNQSLPYPSSRPGSAAGSAHPFGYDPRQGTLSPVLSARRTSEDQPRPTSSSSASGRRYTEPASQTPAPAPLGSSAYRPRHTSTPGNPSSAYAPRFTPQPTTTPSSPSTSQHTPYTPHHSAPPRILHYNPHRQSAPSSVLRPIYPDEVAHLRQLAHANNPLRQKPAARRYSYSGGRAPEPTPTPRTSLPGENDHSYFPPQWDDRPSMPPSEVSYGGPPSSTPGAPPSGYSQYPPNWEAQTPGGNWDGERPGRLGKRRARDEEDDEYERNKRVVSGPVAGQAYSKKVTVVAEHYNSRPEVGVERREFSPIIGLKKFNNWIKSVLIGKFAYRPRGKVLDVGCGKGGDLNKWKQARIALYVGLDVADQSVQQAADRYRRMPKPGFDAFFYAHDCFSNPLSDVLSPELQIKDLYDNVTMQFCMHYAFENAAKARMMIENVSRYLRRGGIFIGTIPNAELLLQLPDRDEELRFGNSCYSIQFTERRHKGVYGHDYRFYLTDAVEDVPEYLVDWENFVSLASESGLRLVYKKAFHEILQEEKDSRDFGPLLGKMGVLNEYGESAMDADQWEAANLYMGFAFEKM | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 77859
Sequence Length: 700
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q9VJQ4 | MSLNYEQNAADEQFARAHKAVSLSDDEESEGQAETTSAPNQEPHVSKSPREYYDEPGGKGNGSGADDQDEPETEAASGAANTHVVAHHYNELKEAGRKDRQKSKIFFMRNFNNWIKSQLINEYMSQIKQNKRMGDALRVLDMCCGKGGDLLKWEKAAISHLICTDIAEVSVEQCQRRYQDILQRSEKSKFANKFTAEFFACDSTLVRLRERYKDPSLQLNLVSCQFAFHYCFESMAQADCMMRNAAECLKPGGFFIATMPDAYEIIRRLRAAGPDARRFGNDVYSIEFDCETDPLPLFGAKYQFHLEGVVDCPEFLVHFPTLVKLGRKYGLQLLKRSTFADYYKENLHHGRHLLQRMSGLESVQPQRCENDEEFAHVSNFQGAQRSRSVGTLSKSEWEAATLYLVCAFKKCKNTWDTNGKPLFEFDD | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48679
Sequence Length: 427
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q8SR66 | MEGKKEEIREHYNSIRERGRESRQRSKTINIRNANNFIKACLIRLYTKRGDSVLDLGCGKGGDLLKYERAGIGEYYGVDIAEVSINDARVRARNMKRRFKVFFRAQDSYGRHMDLGKEFDVISSQFSFHYAFSTSESLDIAQRNIARHLRPGGYFIMTVPSRDVILERYKQGRMSNDFYKIELEKMEDVPMESVREYRFTLLDSVNNCIEYFVDFTRMVDGFKRLGLSLVERKGFIDFYEDEGRRNPELSKKMGLGCLTREESEVVGIYEVVVFRKLVPESDA | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33074
Sequence Length: 283
Subcellular Location: Nucleus
EC: 2.1.1.56
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O72908 | MNTDRITAFIKNGISARMPFYDTLPDMDLVFGKNHLPSLEYGANYFLQLSKINDINRLSTEMLSLYTHDLNKESDISKLFEPYNIKTIKSYGRSIQADAVVVDLRPSNSLYKNEHPYYKSNNYLKENNLYICDYTMITFEIYRPIFELSTEKTCIIKVPTLFGKTIVNAVRVYCSLFRYVKLYKLSADSWLKDSAIIVCQQPHAANINKFITYIRKVTKSQTWLDSNNVNFILIHDSVERVFIEKFLSFSYKIYESLYYVHSLLYSSMTSDLQSLDNEYQKKLIKLLRG | Function: Catalyzes the last reaction in the mRNA cap formation pathway.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33867
Sequence Length: 289
Subcellular Location: Virion
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O43148 | MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ | Function: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs . Binds RNA containing 5'-terminal GpppC .
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54844
Sequence Length: 476
Subcellular Location: Nucleus
EC: 2.1.1.56
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A4R8D7 | MAGGADLDEPPRQSDSTTDRKRPADSTHEIGSADVPRDRAGNKTYDISKLEPARKRQRSKSPSGEAAPRKLKRPGARATISEADRKAARERALERERLAREAATADEERQQINDVVKAHYNAVPERGRDWRKTDSRIKGLRSFNNWIKSCIIQKFSPDEDHQPGRGGGPSILVLDMGCGKGGDLGKWQQAPQHVELYVGMDPADVSIDQARDRYRSMSSRGGRGGRGGRGGGRGPARLFEARFHVKDCFGEPISDIDIIRQVGFESGPHGGGRGFDVVSMMFCMHYAFETEQKARQMLKNVAGALRKGGRLIGAIPNSDVISTKVREHNERMVEMKKKQAEAGDGSKKDDGGDAEEGELDEPEVEKSAEWGNDIYRVRFPGKTPEDGIFRPPFGWKYNFFLHEAVEEVPEYVVPWEAFRALAEDYNLELQWHRSFKEIWDQEKDDRTLGPLSERMHVRDRNTGELLVSPEELEAANFYVGFCFYKV | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54649
Sequence Length: 486
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q9D0L8 | MEGSAKASVASDPESPPGGNEPAAASGQRLPENTPPCQQVDQPKMQKEFGEDLVEQNSSYVQDSPSKKRKLDVEIILEEKHSEDDGGSAKRSKLERGDVSEDEPSLGRLNQTKRKLQPQDDEVPQKLQKLEEGHSSAVAAHYNELQEVGLAKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRKTRDITVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRCRRDNEHIFSAEFITADCSKELLVEKFRDPEMYFDVCSCQFACHYSFESQVQADTMLRNACGRLNPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGNYPLFGCKYDFNLEGVVDVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKNNENKMLLKRMQALEQYPAHENSKLASEKVGDYTHAAEYLKKSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ | Function: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53291
Sequence Length: 465
Subcellular Location: Nucleus
EC: 2.1.1.56
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A5DDJ4 | MSGSKQGSEKASITSLIDSEEQGDEATSVSTQNQSPKTQITQTENVEVQNSDLKVTENKPKNTEMKPTDPNTNASTTENTPITTSNAQVSEKSEKTVPAWMREPEEAQNRYDRYVPRVDNRRRGEPRVAEVRQDPRYAKYLRQDQEERRIRRPDDEYEGDHKRRRPEMVTQFDDRRQGTRKNHPGQAGQSESEENGDEQQGDDEEETPGNEEPVEAQPYSRLATSVQSTQHYHTFQSHIANKENKDINSIVRSHYNQRTIQSKMQGSRTKSPIYKLRNFNNAVKYMLLGNHVRKNPNPGSPTVILDMCCGKGGDLNKAEFVGADQYVGIDISDASVKEAFHRYRRNKARFIPRDGGRAGQRDSRKYNFEACFATGDCFQQSIPEILEPNFPGIVNGLFPVDCVSIQFSMHYSFESEERVRTMLNNVSKSLRPGGTFVGTIPSSDFIRDKIVNKDFLPGTNNKFGNELYSVTFDRTPPSDGIFRPPFGNKYDYFLKDAVDNVPEYVVPFEVFRSMCEEVGLTLRYKKNFIEIFNQEIPKYFHKLNRNLVDGMKRADGKYGAEGAEKEAVSFYLGFAFEKLG | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 66197
Sequence Length: 580
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q07820 | MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR | Function: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis.
PTM: Cleaved by CASP3 during apoptosis. In intact cells cleavage occurs preferentially after Asp-127, yielding a pro-apoptotic 28 kDa C-terminal fragment.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37337
Sequence Length: 350
Subcellular Location: Membrane
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A9WC35 | MRKLAHNFYKPLAIGAPEPIRELPVRPERVVHFFPPHVEKIRARIPEVAKQVDVLCGNLEDAIPMDAKEAARNGFIEVVKATDFGDTALWVRVNALNSPWVLDDIAEIVAAVGNKLDVIMIPKVEGPWDIHFVDQYLALLEARHQIKKPILIHALLETAQGMVNLEEIAGASPRMHGFSLGPADLAASRGMKTTRVGGGHPFYGVLADPQEGQAERPFYQQDLWHYTIARMVDVAVAHGLRAFYGPFGDIKDEAACEAQFRNAFLLGCTGAWSLAPNQIPIAKRVFSPDVNEVLFAKRILEAMPDGSGVAMIDGKMQDDATWKQAKVIVDLARMIAKKDPDLAQAYGL | Cofactor: Divalent cations such as magnesium or manganese.
Function: Involved in the 3-hydroxypropionate cycle used for autotrophic carbon dioxide fixation, and in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. As a part of the 3-hydroxypropionate cycle, it catalyzes the cleavage of (S)-malyl-CoA to yield acetyl-CoA and glyoxylate. As part of the glyoxylate assimilation cycle, it catalyzes the condensation of glyoxylate with propionyl-CoA to yield (2R,3S)-beta-methylmalyl-CoA, and catalyzes the cleavage of (S)-citramalyl-CoA to yield acetyl-CoA and pyruvate (By similarity).
Catalytic Activity: (S)-malyl-CoA = acetyl-CoA + glyoxylate
Sequence Mass (Da): 38367
Sequence Length: 348
EC: 4.1.3.24
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Q9GZU1 | MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVTIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN | Function: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis . Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy . Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion (By similarity). Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events . By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels . Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy . Functions as a Fe(2+) permeable channel in late endosomes and lysosomes . Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (By similarity).
PTM: Palmitoylated; involved in association with membranes.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Ca(2+)(in) = Ca(2+)(out)
Sequence Mass (Da): 65022
Sequence Length: 580
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Late endosome membrane
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Q99J21 | MATPAGRRASETERLLTPNPGYGTQVGTSPAPTTPTEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLVVTFREENTIAFRHLFLLGYSDGSDDTFAAYTQEQLYQAIFYAVDQYLILPEISLGRYAYVRGGGGPWANGSALALCQRYYHRGHVDPANDTFDIDPRVVTDCIQVDPPDRPPDIPSEDLDFLDGSASYKNLTLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSILITFDNKAHSGRIPIRLETKTHIQECKHPSVSRHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVVFMWRRRGREISLWERLEFVNGWYILLVTSDVLTISGTVMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHKYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGHSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGTGTEKSELQAYIEQCQDSPTSGKFRRGSGSACSLFCCCGRDSPEDHSLLVN | Function: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis . Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy. Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion . Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events. By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels . Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy (By similarity). Functions as a Fe(2+) permeable channel in late endosomes and lysosomes. Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 (By similarity). In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells .
PTM: Palmitoylated; involved in association with membranes.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Ca(2+)(in) = Ca(2+)(out)
Sequence Mass (Da): 65506
Sequence Length: 580
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Late endosome membrane
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Q8K595 | MPGDEETLDLPAWNRVPDLTWGPHHRSAMASLDSEVREECLREDLKFYFMSPCEKYRARRQIPWKLGLQILKIVMVTTQLVRFGLSNQLVVAFKEDNTVAFKHLFLKGFSGVDEDDYSCSIYTQENTYESIFFAIKQYRHLKNISLATLGYGESEDNRTGLKVCKQHYKTGAMFSSNETLNIDSDIETDCIHLDLQVLTTEPEDWAQTSFFRLDFYRLVQVDISFALKGIDLQAVHSREIPDCYLFQNTITFDNTAHSGKIKIYLNSEANIEECKNMNISGSTQRSTHYLLVFDVFVIMICLASLILCTRSIVLALRLRKRFLNFFLEKYKQRVCGADQWEFVNGWYVLVTISDLMTIIGSILKMEIKAKKLTNYDVCSILLGTSTLFVWVGVIRYLGYFQTYNVLILTMQASLPKVLRFCACAGMIYLGYTFCGWIVLGPYHEKFENLNIVAECLFSLVNGDDMFATFAQIQQKSILVWLFSRLYLYSFISLFIYMVLSLFIALITDSYHTIKKYQQHGFPETDLQKFLKESGSKDGYQKQPSALLSCLCCLRRRRSNDHLILID | Function: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity . May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells . In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration . Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65450
Sequence Length: 566
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Cell membrane
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F6RG56 | MANPEIVISSCSSHEEENRCNFNQHTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTVAFKHLFLKGYIDRMDDTYAVYTQSDVYDQIIFAVNQYLQLYNVSVGNHAYENKGTDQSAMAICQHFYKRGNIYPGNDTFDIDPEIETDCFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHNMMIFDAFVILTCLVSLILCIRSVISGLQLQQEFVNFFLLHYKKDVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHNKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKHYQQDGFPETELRTFISECKDLPNSGKFRLEDDPPVSLFCCCKK | Function: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events . Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity (By similarity). Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth. Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64085
Sequence Length: 553
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Lysosome membrane
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Q8TDD5 | MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSDVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPEIETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSLILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLEDDPPVSLFCCCKK | Function: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity . Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway . Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth (By similarity). Involved in the regulation of autophagy . Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events . Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64248
Sequence Length: 553
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Cell membrane
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Q8R4F0 | MANPEVLVSSCRARQDESPCTFHPSSSPSEQLLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLVEPDEASHLGTPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKECKDWHVSGSIQKNTHYMMIFDAFVILTCLASLVLCARSVIRGLQLQQEFVNFFLLHYKKEVSASDQMEFINGWYIMIIISDILTIVGSVLKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVMRFCCCAAMIYLGYCFCGWIVLGPYHEKFRSLNRVSECLFSLINGDDMFSTFAKMQQKSYLVWLFSRVYLYSFISLFIYMILSLFIALITDTYETIKHYQQDGFPETELRKFIAECKDLPNSGKYRLEDDPPGSLLCCCKK | Function: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity . Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth . Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process . Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63748
Sequence Length: 553
Domain: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Subcellular Location: Early endosome membrane
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Q9VIE6 | MGPAQKSGTDISIDDEEEILALEKLLGAAENENTKSAESEKAKPTAPILVPKLREDNSFANAFTFEKIVKPEKQKNAAIIKEPELDSSDDEEVKNFLERKYNEYGSDINKRLKQQQENAYESKVAREVDQELKKSIHVVTSTPQPLKNPHNPIKRQSAVSTTFQRPPPVAAAVASTSQSSAPVSAVFTDPVFGLRMINPLVSSSLLQERMTGRKPVPFSGVAYHIERGDLAKDWVIAGALVSKNPVKNTKKGDPYSTWKLSDLRGEVKTISLFLFKEAHKSLWKTAEGLCLAVLNPTIFERRAGSSDVACLSIDSSQKVMILGQSKDLGTCRATKKNGDKCTSVVNLTDCDYCIFHVKQEYGKMSRRSELQSATAGRGINELRNKVLGKNEVFYGGQTFTAVPARKSAKLITKERDRLSMLAGYDVSPFAHTANHTSKPKTAEPTKIPYAERGGPVSRLAGGVEASRKQRVQDLERLRLLKEENERFEKKKQAEGHVLGSDNKKESEAGTPAVSMPTTPVPDKFKNRGFSFDASLTPKLSGSENFSFEINVGSRQAQNAKLKAAALLKKKPLEKINPNSTRGSESGKRRAIDELNEKFSSSAKRQKIDEDDRELMRKSRIEKIMAATSSHTNLVEMREREAQEEYFNKLERKEAMEEKMLTTYKMPCKAVICQVCKYTAFSASDRCKEQKHPLKVVDAEKRFFQCKDCGNRTTTVFKLPKQSCKNCKGSRWQRTAMIREKKILTGRETLSVRGDEETFMGCLAGSANLNLLVPDEE | Function: Proposed to be involved in DNA replication and to participate in the activation of the pre-replication complex (pre-RC). May be involved in chromosome condensation.
Sequence Mass (Da): 86524
Sequence Length: 776
Domain: The zinc finger-like domain binds a zinc ion and is involved in self-association.
Subcellular Location: Nucleus
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Q7L590 | MDEEEDNLSLLTALLEENESALDCNSEENNFLTRENGEPDAFDELFDADGDGESYTEEADDGETGETRDEKENLATLFGDMEDLTDEEEVPASQSTENRVLPAPAPRREKTNEELQEELRNLQEQMKALQEQLKVTTIKQTASPARLQKSPVEKSPRPPLKERRVQRIQESTCFSAELDVPALPRTKRVARTPKASPPDPKSSSSRMTSAPSQPLQTISRNKPSGITRGQIVGTPGSSGETTQPICVEAFSGLRLRRPRVSSTEMNKKMTGRKLIRLSQIKEKMAREKLEEIDWVTFGVILKKVTPQSVNSGKTFSIWKLNDLRDLTQCVSLFLFGEVHKALWKTEQGTVVGILNANPMKPKDGSEEVCLSIDHPQKVLIMGEALDLGTCKAKKKNGEPCTQTVNLRDCEYCQYHVQAQYKKLSAKRADLQSTFSGGRIPKKFARRGTSLKERLCQDGFYYGGVSSASYAASIAAAVAPKKKIQTTLSNLVVKGTNLIIQETRQKLGIPQKSLSCSEEFKELMDLPTCGARNLKQHLAKATASGIMGSPKPAIKSISASALLKQQKQRMLEMRRRKSEEIQKRFLQSSSEVESPAVPSSSRQPPAQPPRTGSEFPRLEGAPATMTPKLGRGVLEGDDVLFYDESPPPRPKLSALAEAKKLAAITKLRAKGQVLTKTNPNSIKKKQKDPQDILEVKERVEKNTMFSSQAEDELEPARKKRREQLAYLESEEFQKILKAKSKHTGILKEAEAEMQERYFEPLVKKEQMEEKMRNIREVKCRVVTCKTCAYTHFKLLETCVSEQHEYHWHDGVKRFFKCPCGNRSISLDRLPNKHCSNCGLYKWERDGMLKEKTGPKIGGETLLPRGEEHAKFLNSLK | Function: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 .
Sequence Mass (Da): 98183
Sequence Length: 875
Domain: Each zinc finger-like domain binds a zinc ion and is involved in both ssDNA and dsDNA binding, as is the OB-fold domain.
Subcellular Location: Nucleus
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O42709 | MHDPFIAEENDLDLEEKRLQRQLNEIQEKKRLRSAQKEASSENAEVIQVPRSPPQQVRVLTVSSPSKLKSPKRLILGIDKGKTGKDVSLGKGPRGPLPKPFHERLAEARNQERKRSDKLKTMKKNRKQSFQRKRNILEDGKSEEEKFPMKCDEIDPYSRQAIVIRYISDEVAKENIGGNQVYLIHQLLKLVRAPKFEAPEVDNYVVMGIVASNSGTRETVNGNKYCMLTLTDLKWQLECFLFGKAFERYWKIQSGTVIALLNPEVLKPKNPDIGRFSLKLDSEYDVLLEIGRSKHLGYCSSRRKSGELCKHWLDKRAGDVCEYHVDLAVQRSMSTRTEFASSMATMHEPRARREKRFRGQGFQGYFAGEKYSAIPNAVAGLYDAEDAVQTERERKERYKKQRAQAEREREILVRLSKRCCASSSSSSNSNNLSTGMSMRTLGHQYLNLQGSGVKNLHDKGNPTALSKDSEIDSSTKKPSVLASFNASIMNPKSSLPSFSNSAILGTNDAASGTPVPQDTTSTKVSPAVVFTSSPRIFSPQSLRKIGFDPTHSADASTTHSTATGLSRSGSLKNIKFRYEFTESDDEDDLEIVP | Function: Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the mcm2-7 complex prior to the recruitment of sna41. Probably is required to stimulate phosphorylation of the mcm2-7 complex by the dfp1-hsk1 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of sna41. May have primase activity. Binds to single-stranded DNA.
Sequence Mass (Da): 66633
Sequence Length: 593
Domain: The zinc finger-like domain binds a zinc ion and is involved in self-association.
Subcellular Location: Nucleus
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Q6HPT7 | MSLDKIMNEAISPWMKGDGPDSDIVLSSRIRLARNFKKYQFSTMQNEEEAKQIQELFKKEFINKTVEPFGEFELLKMNELTPLQRRVLVEKHLISPNLAGTEYGACLLSESEHISVMLNEEDHIRIQCLFSGLQLSEALQSANQIDNWIEKEVEYAFDESLGYITSCPTNVGTGLRASVMIHLPGLVLTKRISRIIQVIQKLGLVVRGIYGEGSEALGNIFQVSNQMTLGKSEEDIIADLKSVIQQIIQQEKMARELIVQNSSIELEDKVYRSYGILANSRLIQSAEAANCLSDLRLGIDLGYIQGISRNILTELMVLTQPGILQQYAGGPLGPEERDYRRATLIRERLRIEKN | Function: Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 40005
Sequence Length: 354
EC: 2.7.14.1
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P37570 | MSLKHFIQDALSSWMKQKGPESDIVLSSRIRLARNFEHIRFPTRYSNEEASSIIQQFEDQFSEQEIPGIGKFVLIRMNDAQPLEKRVLVEKHLISPNLTESPFGGCLLSENEEVSVMLNEEDHIRIQCLFPGFQLLEAMKAANQVDDWIEEKVDYAFNEQRGYLTSCPTNVGTGLRASVMMHLPALVLTRQINRIIPAINQLGLVVRGIYGEGSEAVGNIFQISNQITLGKSEQDIVEDLNSVAAQLIEQERSAREAIYQTSKIELEDRVYRSYGVLSNCRMIESKETAKCLSDVRLGIDLGIIKGLSSNILNELMILTQPGFLQQYSGGALRPNERDIRRAALIRERLHLEMNGKRQEDESI | Function: Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.
PTM: Autophosphorylated on Arg residues. Phosphorylation on Arg-40 and Arg-86 are up-regulated upon stress conditions.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 41124
Sequence Length: 363
Subcellular Location: Cytoplasm
EC: 2.7.14.1
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Q8R7S0 | MLQYDKDVVLSSRIRLARNVKDIPFPTVMTEEQGKKVIELARKAILGSNTILSTQFTEYEMKKLTPLDRQALVEKHLISPDLSQNIKTGYALIKDDNTVSIMVNEEDHLRIQCILPGLKLDESWDMADKIDDLIEETIDYAYDEKIGYLTSCPTNVGTGIRASVMVHLPALTITGQISNILNSVSKIGMAVRGIYGEGTQALGDIYQISNQVTLGQSEKEIIENIEGVAKQIISSERRAREELYKKQRVQIEDRVGRAFGILSHAKVMSTKEYMTLMSDVRLGIVLGILSVDLDKLDRLTTQIQPANLQKIYGMQLNPYERDVKRAEYVSTQLNKKE | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38009
Sequence Length: 337
EC: 2.7.14.1
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Q9Z7K4 | MTLPNDLLETLVKRKESPQANKVWPVTTFSLARNLSVSKFLPCLSKEQKLEILQFITSHFNHIEGFGEFIVLPLKDTPLWQKEFLLEHFLLPYDLVGNPEGEALVVSRSGDFLAAINFQDHLVLHGIDFQGNVEKTLDQLVQLDSYLHSKLSFAFSSEFGFLTTNPKNCGTGLKSQCFLHIPALLYSKEFTNLIDEEVEIITSSLLLGVTGFPGNIVVLSNRCSLGLTEELLLSSLRITASKLSVAEVAAKKRLSEENSGDLKNLILRSLGLLTHSCQLELKETLDALSWIQLGIDLGLIKVTENHPLWNPLFWQIRRAHLALQKQAEDSRDLQKDTISHLRASVLKELTKGLSPESF | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 40142
Sequence Length: 358
EC: 2.7.14.1
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B2TIE4 | MKNWINEECNKEDIVINSNISLSRNLKEKPFSNKLNEIEARENVGFIYQIVKSELKDESCIYQLWNEDKELINSYLDKQLISKELIKNKDKTAFVLNSEETLSIMINEDDHLKLRCITAGFDLETAFDNITKLDDKIEKRVHYAFDENLGYLTTSPTNLGTGMRASVNIHLPALNFNDEISNFSKGLTQIGMDMKGLYEEGNKAYGNMYKISNQVTLGLTEEEIIDNLKGAVLNVISEEKKFREVLLTKCKYDIEDKVFRAYGILTSAILLSEKECTELLSSVRFGVELSLLDISKNKLNKLLVYTRDSSLQNYLKRKLSNKELNYERAKFVRAILAQN | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38992
Sequence Length: 339
EC: 2.7.14.1
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B9DY81 | MNNWVTTYENHNYGLVISSRIRLARNLAKIPFSHKLNIEESKKVIKNVENAFYTFSNTEEKFKSNYLWDKNDNEKNIYLEKHLISKNLIDNSSKAAFILDDKETISIMINEEDHVRIQCITGGLNLEEVYDVSEKIDDLLEENLEYAFDEKLGYLTACPTNVGTGLRASVMLHLPSLSLNNQINGFLNALAQVGMTIRGLYGEGSKAIGNIYQISNQVTLGRSEEEILSNLKALVLQIINQEIISRENLMKKYKYELEDKIYRALGVLKSAVLLNSSECLKLLSDVRLGVEMGIIKDVNGITLNKLLVESQPATIQKIYGESLSNKDRDFNRAKFVREKLAVNTA | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39135
Sequence Length: 345
EC: 2.7.14.1
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Q9Y6D9 | MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA | Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate . Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling .
PTM: Phosphorylated; by BUB1 . Become hyperphosphorylated in late S through M phases or after mitotic spindle damage . Phosphorylated; by TTK .
Sequence Mass (Da): 83067
Sequence Length: 718
Subcellular Location: Nucleus
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Q9WTX8 | MEDLGENTTVLSSLRSLNNFISQRMEGTSGLDVSTSASGSLQKQYEYHMQLEERAEQIRSKSYLIQVEREKMQMELSHKRARVELERAASTNARNYEREVDRNQELLARIRQLQECEATAEEKMREQLERHRLCKQNLDAVSQQLREQEDSLASAREMISSLKGRVSELQLSAMDQKVQVKRLESEKQELKEQLELQQRKWQEANQKIQELQASQDERAEHEQKIKDLEQKLCLQEQDAAVVKSMKSELMRMPRMERELKRLHEENTHLREMKETNGLLTEELEGLQRKLSRQEKMQEALVDLELEKEKLLAKLQSWENLDQTMGLNLRTPEDLSRFVVELQQRELTLKEKNNSITSSARGLEKVQQQLQDEVRQANAQLLEERKKRETHEALARRLQKRNALLTKERDGMRAILGSYDSELTQTEYSTQLTQRLWEAEDMVQKVHAHSSEMEAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI | Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (By similarity). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (By similarity).
PTM: Phosphorylated; by BUB1. Become hyperphosphorylated in late S through M phases or after mitotic spindle damage.
Sequence Mass (Da): 83541
Sequence Length: 717
Subcellular Location: Nucleus
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Q556Y9 | MQAAVASKTNISLKGSTEIVTEFFSYSINTILFQRGLYPPESFTRVAKYGLPILVTNDQSLKDYLDNVLKQLSEWLLSGDVQKLVLVITDIVTKEVLERWVFDVTTDIPKEGEAPRQKPEKEIMNEIQAIIRQITASVTFLPLLPNACTFDLLVYTSKDLAVPQKWEESDPKFITNSQQVKLRSFTTTIHKVESMVAYKISND | Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex until all chromosomes are aligned at the metaphase plate (By similarity).
Sequence Mass (Da): 23050
Sequence Length: 203
Domain: The protein has two highly different native conformations, an inactive open conformation that cannot bind cdc20 and that predominates in cytosolic monomers, and an active closed conformation.
Subcellular Location: Nucleus
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Q13257 | MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND | Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate . In the closed conformation (C-MAD2) forms a heterotetrameric complex with MAD1L1 at unattached kinetochores during prometaphase, the complex recruits open conformation molecules of MAD2L1 (O-MAD2) and then promotes the conversion of O-MAD2 to C-MAD2 . Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate .
PTM: Phosphorylated on multiple serine residues. The level of phosphorylation varies during the cell cycle and is highest during mitosis. Phosphorylation abolishes interaction with MAD1L1 and reduces interaction with CDC20. Phosphorylated by NEK2.
Sequence Mass (Da): 23510
Sequence Length: 205
Domain: The protein has two highly different native conformations, an inactive open conformation that cannot bind CDC20 and that predominates in cytosolic monomers, and an active closed conformation. The protein in the closed conformation preferentially dimerizes with another molecule in the open conformation, but can also form a dimer with a molecule in the closed conformation. Formation of a heterotetrameric core complex containing two molecules of MAD1L1 and of MAD2L1 in the closed conformation promotes binding of another molecule of MAD2L1 in the open conformation and the conversion of the open to the closed form, and thereby promotes interaction with CDC20.
Subcellular Location: Nucleus
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Q8YJE7 | MARNKIALIGSGMIGGTLAHLAGLKELGDVVLFDIAEGTPQGKGLDIAESSPVDGFDAKFTGANDYAAIEGADVVIVTAGVPRKPGMSRDDLLGINLKVMEQVGAGIKKYAPEAFVICITNPLDAMVWALQKFSGLPAHKVVGMAGVLDSARFRYFLSEEFNVSVEDVTAFVLGGHGDSMVPLARYSTVAGIPLSDLVKMGWTSQDKLDKIIQRTRDGGAEIVGLLKTGSAFYAPAASAIQMAESYLKDKKRVLPVAAQLSGQYGVKDMYVGVPTVIGANGVERIIEIDLDKDEKAQFDKSVASVAGLCEACIGIAPSLK | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33666
Sequence Length: 320
EC: 1.1.1.37
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D9PVI7 | MKVSIIGSTGRVGRATALCLAEEEAVKTLHLISRRESLEQNIGEVLDMSDALAAKGVSVKLENSADIENVHGSRIVVITAGVPRTADMDRDDLAFQNGVIVAEYARQIARFAPDSIILVVTNPVDVMTYVALKYSGFHPSRVFGLGNHLDSLRLKNYMARHFNVHVSEVHTRVIGQHGPYMVPLISSTSIGGIPIEHYARRDYFSGYRRFDLKKTIEKVINAGSNIISRKGATEYGPAFAISNIVTTILNDERRILTVSTLMEGEIDGIRDVCLGVPVKLGKNGIEGVVPVLMDRDERETFREAASHVRNSTMKVMEFLDEELPL | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Can use NAD(+) and NADP(+) with similar specific activity.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 35860
Sequence Length: 325
EC: 1.1.1.299
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P61976 | MSASPLKVAVTGAAGQIGYSLLFRLASGSLLGPDRPIELRLLEIEPALKALEGVVMELDDCAFPLLSGVEIGADPNKIFDGANLALLVGARPRGPGMERSDLLEANGAIFTAQGKALNEVAADDIRVGVTGNPANTNALIAMSNAPDIPRERFSALTRLDHNRAISQLAKKTGAKVTDIKKMTIWGNHSATQYPDIFHAEVKGKNAAEVVGDQNWIENDFIPTVAKRGAAIIDARGASSAASAASATTDAARDWLLGTPAGDWVSMAVISDGSYGVPEGLISSFPVTTKDGDWTIVQGLEIDEFSRSRIDKTTAELADERNAVTQLGLI | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34631
Sequence Length: 329
EC: 1.1.1.37
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Q9L8F6 | AAGGIGQALALLLKNRLPAGSDLALYDIAPVTPGVAADLSHIPTPVTIKGYAGEDPTPALEGADVVLVSAGVARKPGMDRADLFNVNAGIVKALAETIAVVCPKACVGIITNPVNTTVPIAAEVLKKAGVYDKRKLFGVTTLDVIRSETFVAALKDKDPGQVRVPVIGGHSGVTILPLLSQVEGVTFTDEEVAALTKRIQNAGTEVVEAKAGGGSATFSMGQ | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 22601
Sequence Length: 222
EC: 1.1.1.37
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Q7M9A7 | MGIIGAGHVGSTVAFILATQGICQEIIIKDLNLDTARGIALDMGHAASATKTHTIVRVANEPSDLRGCDVVVFCAGSPRQPGMSRDDLLLANAKVIRTVLSEVKPYIQESVLVMVSNPLDAMVYTAIKESGLSPLQVLGMAGILDSARMASFIFEKLGYGSDQIVASVMGGHGDDMVPLPRYSNVAGVPITELLEPQEIEEIIHRTRNAGAEIVGYLKKGSAYFAPAKSTAIMVEAILKNSHQVFPCSVLLQGEYGYSDVVGGVPVKLGSRGVCEIIELELLHEERERFDQSIQSVKSLIDALYHHAFFVSSRP | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33735
Sequence Length: 314
EC: 1.1.1.37
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O42354 | MATESCLSSSQISKVDNEKLVRPKVQLKSLLEDAGADKDVFTMKEVMFYLGKYIMSKELYDKQQQHIVHCGEDPLGAVLGVKSFSVKEPRALFALINRNLVTVKNPESQSTFSEPRSQSEPDRGPGDTDSDSRSSTSQQQRRRRRSSDPESSSAEDESRERRKRHKSDSFSLTFDDSLSWCVIGGLHRERGNSESSDANSNSDVGISRSEGSEESEDSDSDSDNFSVEFEVESINSDAYSENDVDSVPGENEIYEVTIFAEDEDSFDEDTEITEADYWKCPKCDQFNPPLPRHCKSCWTVRADWLPETHSNWENLSRNTRTNPEDTSVTTTPNTTFEKKLSKPSSPLPETDDGVDVPTPPLLRRGSSQEETPELERFNSLEACLPATCLEPCVICQSRPKNGCIVHGRTGHLMACYTCAKKLKNRNKLCPVCREPIQSVVLTYMS | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 49950
Sequence Length: 445
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q00987 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome . Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation . Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis . Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis .
PTM: Phosphorylation on Ser-166 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 55233
Sequence Length: 491
Domain: Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P23804 | MCNTNMSVSTEGAASTSQIPASEQETLVRPKPLLLKLLKSVGAQNDTYTMKEIIFYIGQYIMTKRLYDEKQQHIVYCSNDLLGDVFGVPSFSVKEHRKIYAMIYRNLVAVSQQDSGTSLSESRRQPEGGSDLKDPLQAPPEEKPSSSDLISRLSTSSRRRSISETEENTDELPGERHRKRRRSLSFDPSLGLCELREMCSGGSSSSSSSSSESTETPSHQDLDDGVSEHSGDCLDQDSVSDQFSVEFEVESLDSEDYSLSDEGHELSDEDDEVYRVTVYQTGESDTDSFEGDPEISLADYWKCTSCNEMNPPLPSHCKRCWTLRENWLPDDKGKDKVEISEKAKLENSAQAEEGLDVPDGKKLTENDAKEPCAEEDSEEKAEQTPLSQESDDYSQPSTSSSIVYSSQESVKELKEETQDKDESVESSFSLNAIEPCVICQGRPKNGCIVHGKTGHLMSCFTCAKKLKKRNKPCPVCRQPIQMIVLTYFN | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome . Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain (By similarity). Also acts as a ubiquitin ligase E3 toward itself, ARRB1 and ARBB2 . Permits the nuclear export of p53/TP53 (By similarity). Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein (By similarity). Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation (By similarity). Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53 (By similarity). Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways (By similarity). Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus (By similarity). Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (By similarity). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells . Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis . Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis . Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis .
PTM: Phosphorylation on Ser-163 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54558
Sequence Length: 489
Domain: Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P56273 | MNLTSTTNCLENNHISTSDQEKLVQPTPLLLSLLKSAGAQKETFTMKEVIYHLGQYIMAKQLYDEKQQHIVHCSNDPLGELFGVQEFSVKEPRRLYAMISRNLVSANVKESSEDIFGNVCCFPDKQSSQKEKLQELPDKLIAPASDSKPCNLSQRKSSNETEEISSVDHPAEQQRKRHKSDSFSLTFDESLSWWVISGLRCDRNSSESTDSSSNSDPERHSTNDNSEHDSDQFSVEFEVESVCSDDYSPSGDEHGVSEEEEINDEVYQVTIYETEESETDSFDVDTEISEADYWKCPECGEVNPPLPSYCPRCWTVRKDWLPEQRRKEPPPSKRKLLEIEEDEGFDVPDCKKSKLTSSQDTNVDKKEAENIQNSESQETEDCSQPSTSGSIASCSQEVTKEDSSKESMESSLPLTSIDPCVICQTRPKNGCIVHGRTGHLMACYTCAKKLKKRNKPCPVCREPIQMIVLTYFS | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53464
Sequence Length: 473
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q05930 | MTKRRNLFMVGSSFTIDHLPPEIWLCISKLVGTSDLHNLCLINRRLYLTITSDEIWKRRCYDRWINRESLDILTGNDYDSIPVSQWYSYYLRRAKWENKIFCLLWGLTEETNPQHFREKYLHILQFRHYKLATFLHRIIKQGYIPDKRPLDLITYANYLLKNVRHKYVFPLFYPTNAAELKNLNNMASRDAEMIYLRLSAIDTSFDDLLDAREFILNGICSDLLQKYKKIEEFLKLRPVTRVSKLISISTDYLDCFTQPHDSVGQTNDRATGRELHREDFMLLRVYSREGRGYKTIILAIIQAITKRYNVDSYLARDHLVVSEPDFPDGRAFVTVNEDFQPYIFDKEDLLSVWSNNFHNAENFESTVLPALLEPISIQHLLTEFFRELLRCKPRPFEGYPNRAHGLRDMFPYGKVEVPRDVTMYFAFIYDLFDGMFESGMTSLRGQMLRDLLNYVNANNFGDLNIIIGQNALKEPNDCWSNKRDYVLLDDNNKIGYFYTDIETEDTLCALNQYEVDGKVFITTIDILGDIRVRLAEGLTPFQGDNDKLWESFSSVVPRTDWGLFFKGYDKERRRMQLNPYIEEKLSNLANDEQPLHNL | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). Recognizes FZO1 and regulates the amount of FZO1. Regulatory factor for the mitochondrial fusion machinery. Required for mitochondrial DNA maintenance.
Sequence Mass (Da): 70528
Sequence Length: 598
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q10070 | MLESRLAKNIARIVQARKPYLISYHVRASTQNALLKQTVLQSSSFKSFPTLPRLAARNISNSGILSRTTPVIIKQISMVRSYSSGDVENPEILNKNESNQSSGVKRAMPFRVLKKMKSFLFKQNKPLTVDNVTAFFSWWLVSHIVWIVVGTTTFFSLLLYTLNTVSAQELLGRWIGQLMTKNTGFQFVFESAIVPNWRKGLITFNKISVIRRPDTLNGIGAQNPNNKSDYEKEYMALRKRYDSNEEPDTEALSQGNYTQFELSIDKADVSFSFARFLNGKGIVKELQLKGVRGVVDRRFIEWDPSSDPRDYRRKHNWGDFEIEKFKLEDLRVTLLQPKGFRKFPVSVFFCELPRLRKQWLFYDLMNAKTLTGSFDNSMFTIHRLQLRPYSPYLKVGKQLDDMRHSRLRIDNVAIDHLNRGVSGAFGWINDGSVDFLVNISFPSEPSENSFQKAWISLMDKLKKKEKDEDVYKDVHFDVNVQLHNPKAVIPIFTNQVSYINNALIRPIIAYINSTRTFIPILCHVSKPLSDFDGSWTFYDSGVLQEISAQVYESFARDVLNQEIRRKRIQKVGYWSLRRFLHLVLVSLQELAPTTSSISNFE | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69429
Sequence Length: 601
Subcellular Location: Mitochondrion inner membrane
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P38880 | MSLFTRPFLRSPRQFSVARYVYWARSPALRSNLRIPSIAAASLRAYSNESKTGRDAPPDKKSKKLSNLKYITERDSLLVQTNNIFTKLKINIRWFLKKSTRPFNSDDISAFISWILVSNIFIFIFWTTTFVSLILYLINTVFAQEYLASKIGKFITKNESLSIVFESAIVPDWSSGKISFQKVFVSRRPKVSRGFTKGSQQDALQRAKLALSERILVNQQDFDNGNYTQFDLTIDQVDISLNFRKWINGKGILDEVTINGLRGVIDRTHVVWKKDDDPKNYLNVYQPGDFEISKFTMNDVLCTLYQPNGFRPFQVSIFNCDLPQLRKHWLFYDILNANNINGTYDNSMFTIHKKFRTDDQHQDPTLLWKQMTRFRVDNLDIDHLNAGIEGPFGWINEGRVNMIGDVLLPDDDAASDSLQLTEILTEIGDRLIKKAKRYTSSLPLVGPGFSPAVDEIDPNDYFIMDFSLRLYNVKAEVPLFTSGLTYINSALIRPIVGYINSHRTYIPIKCRIVKKKSDFEGSWTIYDSYLMRDLSAEAYDAFADYVADDEKRTLRLRRVGFWSLQLILQVILMSLGAIA | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66703
Sequence Length: 579
Subcellular Location: Mitochondrion inner membrane
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Q753C5 | MLPVLRSGLRRAVWRCGHGLLQRRIAAGAGWYARACASDDAASRSPLKQEMLNSTEYLHVQNILLQKNQQRMTKQKLLSEATGFYDRFKINTKWLLIRGNRPFSGEEISTLLSWLILSQVLWVILGTTTFVSLLLFLANTVLAKEMVGKFVGNSLNRYMDGVDVQFQDAMVPEWRKGQISFQKVRLRTTPGAQDAGLLTFDLMFSKLSLTLSVRKWLQGRGLINDVYVSGMKGDVSVGAAERKDAKLIDFFSNPNYELGEVEVCDSVIMCTDQEIGQKFRVSIYNMRMSQLRFRWSLLDLFNADVVSGALNHSLFSIHKRQHKLPLHEMEKDMAPWKRISRLRLNPISVKDLGLDKSNAFNWIEGGSVEMIADLMLPNIYPESAAAEDENKYVVMDLRITFKDLIASMNTVPPALSNGRELISFDELKPIIMFVNNRRGLFSSLRNLDNNKLWRPTVTIERQQSYPDTTVIPMRTFQWPEGEGSVQLNQEIIKYHENPSDNSNEIILRCRIAKHMNELQNTFLFKETDVYDKMALELYTDLMKMIEETEYKKKNDWVKLLGTTFASQLLIFGLGAMV | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66127
Sequence Length: 577
Subcellular Location: Mitochondrion inner membrane
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Q6FMB2 | MIRRRIVGFLRRPLGSEGGPLVSPIVGLVRPLVYPVNRAASPVTAVSPVVRPVGMRFISGPVEREAIRAGISNNTDFLHVQNILLQKDQERQRRELLLKDADNFFERFKVKTKWVLIRGNRPFSKDEIYTLFSWLLLSQIVWIVVGTTTFLSLVIMASNTMFAKEFVGETLGNILNNNKYINGIDFTFKDAMVPEWKKKMIRFHNVTMKSNDKDDTKGVSMNLKLNQVEVSLSVVKWLSGKGLVNDISIFGISGDISINDKKESNVESLINWVTESNPTYELNNFTINDSSTVIHDKANNKHLNMNIYSLVIPRLRFDHLLTDIFSADVLVGSVNDSLFNIHKRQNKLLPAFFSDKGRDNRSKTIDKNENDGRFTNLRLNAININELNLNRTGAFNWIDDGTIEISADIMIPNTDENNEGNGLKTLLGYPGGDPLVNKNTPENKYVVIDVKFKFKDLKTKFPNEEPKLSSGEKILSLNELKPVIAYVNSRSGFIHFLTSLEDSNQSRTNVESVDDNKNWGLSNISIRRKKSYPNTTVISSKPYWNSTSEDNERNLPLPLNQEIIKFHNISVQDDNELVLRCRIVQNVEQLENLSSLKISKMWDTITMEMYMDLLKVVEDWEYRNKNDWMKQWGATFASQLLLVGFGAMV | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74050
Sequence Length: 649
Subcellular Location: Mitochondrion inner membrane
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A7THL9 | MAGLLPRAYGGVLRRSYIYLGSQCSNSVSRLTVGSTFRLVRMKSWGTSKFHTNGSPVLNEIKKISKSNGITIINPLVNKVTTNNVSTSSNGKAAVAAATAATAVSLGSTGQDDALSRNTDFLHIQNILLQKNQDRMNKQKLLSEATNFYERFKINTKWLLIRGNRPFSADEIGTLFSWIILSQILWIILGTTTFVSILLIIFNTVFAKEMVGNVVGKLLNIFLDGIDVKFQDALVPEWRKGCIRFNNVQLRTHPLQASEPENINDYNELVNNMIEFDLKLHQIELSLSLKKWLLGNGLIQDLTIMGMRGNITVTPVSLENKIDDNQRVNLIDWFSNPYYHLGNVKVTDSSIILHDNQLSKDFKVSIYNLDMPQLRFQWIINDFLSSNVVDGSINHSLFNIHKRQHKLAYIKDLENDLSDWKRITRIRLDSIDVKKLGLNNSNAFNWMDDGQLDIIADVMLPNEQENEPDFDFTRNKKEHMSKSNNKYVVLDLKFRFKDLKAIFPDRAPRLSNGEEILSLDELKQIILFINRKYDLYHSYANSSYKNTLWDAPNIAINKAKSFPVTTVFQSKKDFSNEDSDEEDRKLKKQIIRFHDDISTPNNELVLSCKVVKNINELKNMVLFWETGIYDSLSMELYIDLMKMVEEWEYKKKTNWMTDWGSSVASQLIIVGFGAMV | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77502
Sequence Length: 676
Subcellular Location: Mitochondrion inner membrane
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Q12171 | MLITRLRVPTIKRPLLPITSHLVRHCIRTYVATNHGNVRPFITPYKSSLPVRCLIAQRHIRTFPSNDKFTTKASNIETILLRKNNEREFKQSLLADAKNFQERFKINLKWILIKNNRPFSLNEISIIASWLILSQILWLILSTTTFISFYLFVINSVFSQEYIHEKKIYERLLKWLLKDHKCSNQDLEITFSPEDKASMLVLSPDWESNSILIKRLNVRDEILDLDLKFHHINLNVSLKNWLLGRGLITNVSIYGIRGCLNLSNFINLVNSFQGDQKTENFLKTLNNVEITDSEILLKQSLSAQETPSLKFSIYNLSLPRLRLNHFISDILSAKTFSGSINNSLFNLFKRQQKLTAVIENNNKNRMASSKFDFTDNNQENYRTVTHQDDPNYVTTLRLNFININDLKFNGDGKFNWLKDGQVEILADIMLTNSTSHLSSESKYAVVDLKVTCRDLKTTFPQEPPVLSTGDSIVSLDELKPIITFINSYEGMANPILKDFSENERLTNSIIWNSPNVSINRQRKSYPLTTKVTSNSTKEIIKFHNQPNTNANEIVLRCKMVKNLSDLQLININQILDQITMELYVDLTKIVEDWEFKNKNDWMKQWGTTFASQLLLFGFGAMV | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72028
Sequence Length: 622
Subcellular Location: Mitochondrion inner membrane
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C5FRB0 | MAFNFNWSPLMADAGFYTRAQELLTAALNKSPKPPIIVGDITVTELNLGSIPPELEILEIGDLADDRFRGIFKMSYSGDAYLTLKTCVQANSLNTYMVTRPKFTSPCPLAADHGLTIPLQITLSDIKLSGFVVLVFSKQKGITLVFRNDPLESLKVSSTFDSIPFVRDYLQRTIEGQLRLLFMDELPAIIHRLSLRLWVPELRGQDTEVKADEEAGPGQDPLLSPPQDPVDASGNVLSVAQIASLSLDSGVEMHSLFSQRNLVRLATLTDSQRTLSLFTPTIHDVVFRALTGAMEQSESHGGLISPASPPLSRTHSHVASLHSLQESSMSKSSLGSPLSGCGLTMGAGRHPRTRPSRKHKRRVVDLRKPQKLDDTSSTCTDSEYTVSTDASTVFSSSARVGEKPDDPITPPVSPDATIKVKDRSRVPAMQGLGPSVTNKAGQSTPSAEAEKITLSNGEPSYIPHQNTPTIEAHEKGDDNTISLNGVPPSMLSFVAVSQDRSILEQAWMMKLANEISRRIQEGKGPGSVGSNYCGRRDPSPPPAYGQ | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59194
Sequence Length: 546
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q755S6 | MSFIFNRETFEDNSFNEVLREKLMRALNLHDRTVGSSSGAMTTGTGAVECSGAAAAGQRPPRSKGGFSKVDILKSGIIVKKVEFPTIPKLEILDLDVSIQSKSLIKGICKVSCRDAMVQITTEIESNLLLLHVNSSPKFTTPKLISNDSFTVPITMTFDKLHLEAITNIFVKNTGVGISFNDVNLDFRLQCSIKLLQSSIEKRLKASMEEVFKDVLPSVIFNMSQRWFTHGETVVPTVDKSMVSSDTPVQPRMILDESDLSDLSPANMLRLSTLVSSRQTLCLNPTAVDTISTIPGCLERQNLHRFNLRFPSLYNYYSNKEQQGAHNNEKNRVEHLKLWGRSSSNPIPTRASFKVENTLPKEVLDSNSYDVRVITAIQTKMYERASNDVVLRRRKIKMRSRKPSKANKDAVSPAQNDSGTSSCSNVASELPHASLQANPQSDEIDPAPEGGPNAEDAYKEELEDSGLRAPQDFPALENVTPVLAQLPNQQRSRLGSPLSAGRPTPLLSPLDDSHWLLQKRDPQDLRTTLYSPIRNGRFYVMPQPQLDTKEASAFLLENGKRFGFVGLLNNHNLKWGNDPPPPYREVSITQ | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65696
Sequence Length: 590
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q8XB24 | MSRFLICSFALVLLYPAGIDMYLVGLPRIAADLNASEAQLHIAFSVYLAGMAAAMLFAGKVADRSGRKPVAIPGAALFIITSVFCSLAETSTLFLAGRFLQGLGAGCCYVVAFAILRDTLDDRRRAKVLSLLNGITCIIPVLAPVLGHLIMLKFPWQSLFWTMAIMGIAVLMLSLFILKETRPAAPAASDKSRENSESLLNRFFLSRVVITTLSVSVILTFVNTSPVLLMEIMGFERGEYATIMALTAGVSMTVSFSTPFALGIFKPRTLMITSQVLFLAAGITLTVSPSHAVSLFGITLICAGFSVGFGVAMSQALGPFSLRAGVASSTLGIAQVCGSSLWIWLAAVVGISAWNMLIGILIACSIVSLLLIMFVAPGRPVTAHEEIHHHA | Function: Confers resistance to chloramphenicol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41612
Sequence Length: 391
Subcellular Location: Cell inner membrane
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P32259 | MMLGEHLMSWSKTGIIAYSDSQSSNANICLTFLESINGINWRFHTPQKYVLHPQLHEVQYQESSSTLSTHSTTTSVNGSTTAGVGSTPNFGGNSNKSPPQFFYNISSIHWNNWFSLPGDMLAVCDELGNMTMLITGQRPDRATTYEKLTMVFQDNVYKIYNHVMPLKPVDKLKPMNIERKQTRKEYNTSILEFRWLTSSKSVIVSQFCAFDSSSNTYRSRAQQVPPYGVYHPPFIKYACLAIRKNGQIDFWYQFSNSKDHKKITLQLLDTSNQRFKDLQWLEFARITPMNDDQCMLITTYSKLSKNISFYKLHVNWNLNATKPNVLNDPSLKIQFILSTTLDPTDDEGHVLKLENLHVVSKSSIEKDPSPEILVLYNVCDTSKSLVKRYRLAPTQLSAEYLVILKPDLNIDRNNSTNQIFQSRRYNLRRHSDIVLDKKVTLITSEMFDAFVSFYFEDGTIESYNQNDWKLETERLISQSQLGKFKNIIASPLSAGFNYGKLPLPPSVEWMKVSPSMCGVIVKQYNKKWPQFYAAVQKNYADPEKDSINATALAFGYVKSLHKQISAEDLTIAAKTHILRISFLDRKRAKEFITTLLKSLYSFFNISPDAPKEIMDKIITSRPLQKIMLLQLELGSCFSQENIEEMARVILYLKNVLFAFNGVARNFHFAIEQISNNSNQQQNPKLFQTIFSKQDLIHSLIPVAKWFVKFITYLTQEILILINDPTNKEYTLVHGIFGAKMSRTLILSILNEIKKVTQIVAKFPETSYPILNESSTFLKLVLSESPVDFEKFETFLVDVNNKFIALCEQQPSQEREFSLLVKAEIPPEYAKVGDFLLQYANNAVISHANAAAVYFADTSGLKISNSEFFNPEIFHLLQPLEEGLIIDTDKLPIKNRTSKSFSKLLYDDVTCDKLSVSEISDGKLKRCSRCGSVTRAGNIISSDKTIVPTSIQTKRWPTMYTRLCICSGMLFEMDG | Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
PTM: Phosphorylated by KIN28.
Sequence Mass (Da): 111297
Sequence Length: 974
Subcellular Location: Nucleus
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Q08014 | MSEAMVFSKIDEYTLFMSRSLQKSLKTFAEQVMALIYQYKDTLVEDRLALTNTLDEAVQILVDSGKEEADKLGFNIYSAVSRYISEIWASQSGQTTAAPPATDIDGLHRQLVALKNSLGQNAELYEQRCQLQAELRELQEFSENPAAAVEEIMQLKAQIDELKYGASNHNALVQEKRDLERHLADLRLSRQDTNSRLPQEIDRLRAEIEDEKRNLPHMDDLQRQRDELQRQLDTIRRRGNTSGVMAEIENIQRQIDDANSSASSEHELRMLRAEVETLRAQKSIVTRLEAENADLRRELQDIRGRAQEMSASQRYSANQAQELQEKAMQAEELLQQKIELRRQLHEALERADAGEAALRDKRRLEDEIKGLQLRLTENDFTKERSILRNEIQAKTTEIDTLISDRRALETKLLNKEAEVDQLLYEKQLLKTELNSYRGTNEDIDKLTFEKRQLVEELNDLREKTIKYDQLAREKAALETELKENSYNFDQLLEQKQQMRSDLNALREKAADYERVDRELRLKDKELEEKNAEIERLLEDRRVMRTELLHSKESATDVDSLIQEKRLRDRELAHLRDRMSEYERVVEERIQKEKENNLLKQRITELEQQQRTATVRETEMSALREKANELDGYNRERQAREHEINMLRDKALESDKLRQDNRVMAMELTELREKVQLLEKLQYEKRARDVEMLELRHKAMDVDTLVEEKQRLEMRLAELKIKVNNYDQLADDKARLQEQLKEMSDKLIEFEMIMDDNRRLKLQVKELDLKTANMEKLYEEYKKLEDQLKATKAMTSTGMGVSAASPAFYKTKSMRLTQQNNQMKNTTDNLLTRDIPKLIDKLIERPAGTTTMGRSGKF | Function: May have a role in immobilizing the microtubules between cell divisions.
Sequence Mass (Da): 100584
Sequence Length: 857
Domain: Shows an alpha-helical coiled coil structure (30 repeating heptads).
Subcellular Location: Cytoplasm
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O65312 | MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEADHVMDNDNSISNKIVVSDPNNTMWTPVEKDLYLKGIEIFGRNSCDVALNILRGLKTCLEIYNYMREQDQCTMSLDLNKTTQRHNQVTKKVSRKSSRSVRKKSRLRKYARYPPALKKTTSGEAKFYKHYTPCTCKSKCGQQCPCLTHENCCEKYCGCSKDCNNRFGGCNCAIGQCTNRQCPCFAANRECDPDLCRSCPLSCGDGTLGETPVQIQCKNMQFLLQTNKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLNDQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGPEHADWSRGREPRKTGASKRSKEARPAR | Function: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. Required to prevent the proliferation of the central cell of the female gametophyte by repressing target genes before fertilization. After fertilization, it probably also regulates the embryo and endosperm proliferation and anteroposterior organization during seed development. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Interacts with the promoter and repress the transcription of genes such as PHE1 and PHE2, that are paternally active and maternally silenced genes.
Catalytic Activity: L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 79310
Sequence Length: 689
Subcellular Location: Nucleus
EC: 2.1.1.356
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