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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q37143 | MKQPTTNKLRFTITLVILFLARVGIFIPISGIDHQTFNNTIQQNGIINFLNIFAGGGFSTIGIFALGIVPYIYASIIIQLLIKLIPYLENLQKEEGEIGRQKINQLTRYLTLLWALIQSLSIAIWINHMYLIHLFELCASLTTSSMIAMWFSEIISEYGVGNGPSLLIFQNIISSIPKNLQNYTFNIGTTNTVLNGSLILSFGIIILIINILIQEGERKIAILSAKQLGKINELNHKVIFLLKLNQGGVMPFVFASAVVHTFLFISNNTNSKITQFINLFLPNQFLYLPLYLIFIITFSYVYTSLILNPEDIAKNLKKMGASIPNIRPGSETIKYLNTRINRLTLIGACFLFTITLFPTITYYIFKINTLKGLGATSLLILVGVAIDTAKQIQTYLYHTYDNMME | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45629
Sequence Length: 405
Subcellular Location: Plastid
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O66491 | MSEYLKALFELKELRQKFIFTLLMFVIYRLGSHIPIPGINPEALRDFLKAFEGSVFALYDIFSGGNLGRLTVFALGVMPYISASIMMQLLTVAIPSLQRLAKEEGDYGRYKINEYTKYLTLFVATVQSLGIAFWIRGQVSPKGIPVVENPGISFILITVLTLVAGTMFLVWIADRITEKGIGNGASLIIFAGIVANFPNAVIQFYEKVKTGDIGPLTLLLIIALIIAIIVGIVYVQEAERRIPIQYPGRQVGRQLYAGRKTYLPIKINPAGVIPIIFAQALLLIPSTLLNFVQNPFIKVIADMFQPGAIFYNFLYVTFIVFFTYFYTAVLINPVELAENLHKAGAFIPGVRPGQDTVKYLERIINRLIFFGALFLSVIALIPILISVWFNIPFYFGGTTALIVVGVALDTFRQIETYLIQKKYKSYVRR | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48100
Sequence Length: 429
Subcellular Location: Cell inner membrane
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P16336 | MFKTISNFMRVSDIRNKIIFTLLMLIVFRIGAFIPVPYVNAEALQAQSQMGVFDLLNTFGGGALYQFSIFAMGITPYITASIIIQLLQMDVVPKFTEWSKQGEVGRRKLAQFTRYFTIVLGFIQALGMSYGFNNLANGMLIEKSGVSTYLIIALVLTGGTAFLMWLGEQITSHGVGNGISIIIFAGIVSSIPKTIGQIYETQFVGSNDQLFIHIVKVALLVIAILAVIVGVIFIQQAVRKIAIQYAKGTGRSPAGGGQSTHLPLKVNPAGVIPVIFAVAFLITPRTIASFFGTNDVTKWIQNNFDNTHPVGMAIYVALIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGVRPGKMTQDRITSILYRLTFVGSIFLAVISILPIFFIQFAGLPQSAQIGGTSLLIVVGVALETMKQLESQLVKRNYRGFMKN | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47243
Sequence Length: 431
Subcellular Location: Cell membrane
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O51451 | MKELFLSLFTVKDLRNKFLFTLFVLFLFRVGSYLPIPGIDSVALKSYFKSQSDFSIANYFDFFSGGAFSNFSIFMLSIGPYISASIIVQLLVYSFPSLKKMQEGDGGRQKTKKYTKYLTIVAAVVQGYATSLYAKGIPGAVTIPFYRYIFVAILTVTTGTFILLWFGEQINQRGVGNGTSLIIFSGIVVRLQAALFNLFQSMQDPSQNVNPVFVILIISIFILVVILIIYEYKAQMRIAIHYARANSNNTVSSYLPIKLNPSGVLPVIFASVLITLPLQILSGFAETSSIARQILSYLRPNGFYYTFLNVILIIGFTYFYSKIQLSPKDISNNIRKNGGTIPGIKSDEMEKYLDEIMNKTLFSGSIFLSIIAIIPFLVQNIFRFPHDVSRIMGGSSLLIMVGVALDTLIHIDAYLKTQGFSHGNKKNYAFLQKI | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48610
Sequence Length: 434
Subcellular Location: Cell inner membrane
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P28539 | MATLRQVFSISELRQKIFFTFSLLALCRIGVFIPVPGINGDRAVAYFNQLLGSSQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLLVVFMPTLQREMRESPDQGKRKLGRMTRLFTLVLACVQSLLFAKFALRMNLVVPGIVLPAMLSLKLFGVPWVFYLTTVVVMITGTLLLMWVGEQISDKGIGNGISLIITLGILASFPSVLGSIFNKLNLGSQDPSEFGIVSLLILCAVFVFVLMATVLIIEGMRKIPVQHARRIIGRREVVGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFLSSESSWLKRIATMLSPGSVAYSIFYVLLIIFFTYFWTATQFRPEQIASEMKKNGAFIPGIRQGKPTQTYLEYTMNRVTLLGAVFLAVVAILPSILGRILRVDANVSYFLGGTAMLIVVGVILDTMKQIDAFLLVRRYDGVLKKDRPKGRP | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50303
Sequence Length: 457
Subcellular Location: Cell inner membrane
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P46249 | MRPENNLRLRLFQTMKFIALERLGLFVPIPGIDQKLFSSDYSNNAISNLLNVFDNNQAPKLSVFALGIIPYINATITIQILSSAFPALKKLQSEEGEIGKKKLNKITKYLSFCFAFIESLAIVLRLQKYAFDWNLYFIVQTTLILISGAMLVMWLADNISYKGIGTGASVIIFVNIASAFAKFLLNQLFVHSIKFLDFASYFALIVFSIACIVFVQEAIRKVPIISAKQLDSTSFYSNDYFLPLRINQGGVMPIILASSLLALVDYVIRYGLSTLQAVYFINDILPFKILFLLLYSAFIIFFNYLYCSLVLNCFELSNNLKKASVVIPSIRPGKMTEKFFKDTLDNLTLFGSGFLAFIVLAPNFLEFVFHIRVFKGLAVSSLLIVVGVAIDLIKQSKTYVIAKNYENMVH | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46243
Sequence Length: 410
Subcellular Location: Plastid
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Q85FU6 | MQDNWPTRLAITCLLVAIERLGMYIPVGLISNPQANWLNGGGWFVLGIIPTINASIVMQILISIVPALTRLQKEEGEMGQKQIQKYTRYLTFFLAGIQAFTLSQQWCTWLLIVSGAMLVMWLAEQMTHKGIGNGTSIFVCSNIAANFLHHPIEAPWSLAMVVLIFTMLGMIALQEAVRAIPILSAKQLIQSIAQVYLLPMRLNQGGVMPIIFASSTLALLHTWSIWWLYVACIIFFSHFYNLVIANPKELSENLNKMAVVIPSIRPGAETQQYLNRTLNRMSWIGGIALSLIALLPWLFSSLKIFSGFGATSLLIVIGVSIDTMRQIRTYFIANAYEKMI | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38022
Sequence Length: 340
Subcellular Location: Plastid
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P25014 | MLSRLIISIFIIFETIYLQIFKPVNKTFKQGEAKLKRTLQTLQSRELSEIRKRAISTLCLIFLIRIGTFLPIPGTALNFDLESFQQNNSRNELANILNLLSGGAFLEIGFFTLGILPYMNASFFLQVLTKILPSLERFQKEQEEIAQREFKKWTRYLTVIWAFIQSIVISWIWIRPYALNWDFFLGLKVVVALTLGAVIVMIIAEQITEIGLTNGSSLLIFINIIARIPNSIEQLFNSNINWTFPMISSLILSLSLSFITMFVIIGLQESGRPVPVLIARQEAERQKFNEPITEAERRKTQAYIFFQLLPAGIMPVIFASTIFDLALPAFTNFLLQQGNWGYQLIKSFPFNSLFKDFCYLITIMLFSSNYALTIMINPKTLAENLNSMNALIPGVRPGSETKVYSEQLIHRLNFIGSFVLALVCILPSIVERSLGLPKLQILSPVSISIALGVAVDTTRRITSYLGSSSPFKRDSSKREPLKRDFSKRRSAN | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55927
Sequence Length: 492
Subcellular Location: Plastid
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P28540 | MKKAFVLEGPLVLRLFRTIMILIFARLGNYIPIPGITEVESFYESSFRNTSIYNLSALSGGSNVISILTLGLGPFFSASLAVQFLVKLYPAFEKLQNEEGEEGRKTIVRYTRILTVLFCIIESFFLSNSLRSFVFNWNSISYFVVAAAVTTGSLVLVWLSEVITERGIGNGSSLLILIGNLSRFRFLINKDDFDSLNVSSQSNLYIIYIIITLVSMLIFSTLSQEGARKIPVVSAKQLIDGVEDDMRRSYIPIRFGQAGVVPIIFSSSILLFLTTSIKQLPNANIATRVILDSVNLQQIFYFFTFLVLIIFFSFFYTLIILSPSDIAKNLKKMSSVIQDTKPGVATKVYIRKFILQASFVGSILLSALILIPSILAAALGVHPLSISGITSLILSFSIINDTVRQVLAYRDTRKFLLSS | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46618
Sequence Length: 419
Subcellular Location: Plastid
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Q7MY02 | MTHKPCLLYSQLPAIDRLLREPQITPLVEQYGQTLVTATLRRMQEQARINIKQYQALPDWCDNWASALGQQLEQKQALALKPVFNLSGTVIHTNLGRALMAESAIEAVTQVMRSPVTLEYSLNNAERGHRDHALADLLCELTGAEDACIVNNNAAAVLLLLATVASGKQVVVSRGELVEIGGAFRIPDVMVQAGCRLVEVGTTNRTHLKDYRQAINEETALLMKVHTSNYNIDGFTAEVSGRELATLGIASQIPTAIDLGSGSMINMVQYGLPAEPMPQDYLNQGIDLVTFSGDKLLGGPQAGIILGKKHWIEAIQRHPLKRALRADKMTLAALEATLRLYQRPEQLCQQLPTLRLLTRSQQQMHDMAQRLLPQLQAHYGDQFIVRDEPCYSQIGSGSLPVDRLPSWALTFAAVEGQGSSLERLARCWRGLAKPVLGRISGGRLWLDLRCLEDEKALLQALLL | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 51114
Sequence Length: 463
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
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Q73JP8 | MSCSLINEDFDLLKAAKNPGUGAKLSAGALDKLLKNFSVRNDDNLLVGFNTSDDAAVYKINDKTALISTIDFFPPVSGDPYIFGQVAAANSLSDIYAMGGEPKLALNLFCITKDMPEDMIKEILRGGFDKVYEAGAIVCGGHTIYDDSPKYGLAVNGFVHPKKILENSTAKEGDVLILTKPIGTGILLTASKADMSPPEELDRCYKIMAFLNAKARNIMVKYKINACTDITGFGLLGHLYEMGKGSGMSIEVDYKSVPIYKSVIESAEMGMMPAGVYSNRNFVGDNIVFENVPLAYQDLMFDPQTSGGLLISVDKEDAAALYEELSQALENTPCGKPAIIGLVTKRDEKILRVS | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 38311
Sequence Length: 354
EC: 2.7.9.3
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B3E7F7 | MTNKKIKLTQTVKAAGUAAKLGPEGLADALAGLNRPADPRLIVGPETSDDGGVYCLTPEIALIESCDVITPPADAPRAFGRIAAANALSDIYAMGGRPLTAMNLAFFPACSLQPEVLGEVLAGGQDALNEAGCCLVGGHTVEDDELKYGLSVTGTVHPEQVLRNSTARPGDCLLLTKPLGSGILSTAVKGEMATVEQEAEAVAWMSLLNRAAAELMLRYTPSACTDITGFGLIGHSCEMALGSGVTIRLYLDAVPLMQGVTDQVADGMVPAGCYRNRSYYLSRIDAGDCDPERLLPLFDPQTSGGLLIALQPGAAALFQAEAAENSIFCVLIGDVLPRAELPVIVV | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 36061
Sequence Length: 346
EC: 2.7.9.3
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Q8ZEK1 | MASPAIRLTQYSHGAGCGCKISPKVLDKILHTEQQKFFDPRLLVGNETRDDAAVYDIGNGVGIISTTDFFMPIVDDPFDFGRIAATNAISDVYAMGGKPIMAIAILGWPIDKLAPEIAQQVIEGGRYVCQQAGISLAGGHSIDAPEPILGLAVTGIVSTEQVKKNSAAKPGCKLFLTKPLGIGILTTAEKKSKLRPEHRGLATETMCQLNKPGADFAHIPGVTAMTDVTGFGLLGHLSEICQGSGVQAILHYSAIPRLPAVEDYIAEGCVPGGTGRNFDSYGHLIGNMSDLQKQLLCDPQTSGGLLLAVLPDAEADVQAIAAQHGMTLSPIGELTSADSRRALIEIVV | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 36623
Sequence Length: 348
EC: 2.7.9.3
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Q7Z2C4 | MVYIDHNGRVWEKRPWDWRRIVELFVGIWFAIKQLFLTFLAPFTGNNNQANPRRGNGWGGGGGWGGGGGGGGGGGGGRPGSGSGGLRPNRRIGRIQPTMSCNMPAGGGUG | Function: Plays a role in the life span. May be involved in regulating the redox state of the cell and possesses anticarcinogenic properties.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 11574
Sequence Length: 110
Subcellular Location: Golgi apparatus membrane
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Q32PE3 | MVYISNGQVLDSRSQSPWRLSFITDFFWGIAEFVVLFFRTLLQQDVKKRRGYGSSSDSRYDDGRGPPGNPPRRRMGRINHLQGPNPPPMAGGUGR | Function: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (By similarity). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins (By similarity). Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (By similarity). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Plays a role in protection of cells from ER stress-induced apoptosis. Protects cells from oxidative stress when overexpressed in cardiomyocytes (By similarity).
PTM: Cleaved by CAPN2/m-calpain in resting macrophages but not in activated macrophages. Macrophage activation up-regulates expression of the calpain inhibitor CAST/calpastatin, resulting in inhibition of CAPN2 activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10805
Sequence Length: 95
Subcellular Location: Endoplasmic reticulum membrane
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Q9Y6D0 | MVYISNGQVLDSRSQSPWRLSLITDFFWGIAEFVVLFFKTLLQQDVKKRRSYGNSSDSRYDDGRGPPGNPPRRMGRINHLRGPSPPPMAGGUGR | Function: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (By similarity). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins . Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (By similarity). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function . Plays a role in protection of cells from ER stress-induced apoptosis . Protects cells from oxidative stress when overexpressed in cardiomyocytes .
PTM: Cleaved by CAPN2/m-calpain in resting macrophages but not in activated macrophages. Macrophage activation up-regulates expression of the calpain inhibitor CAST/calpastatin, resulting in inhibition of CAPN2 activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10645
Sequence Length: 94
Subcellular Location: Endoplasmic reticulum membrane
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Q5LQK9 | MTIAIPFDNSYARLPGGFYTAQAPQPVRAPRLVAFNADLARLLGIAPGEVEEMAQVFAGNAVPQGAEPLAQLYSGHQFGNYNPQLGDGRAILLGEVLGSDGIRRDIQLKGAGRTPYSRGGDGRAWLGPVLREYVVSEAMAALGIPTTRALAAVETGETVRRESALPGAVLTRVAQSHLRVGTFQVFAARGEIAHLKRLTDYAIARHYPDAQGPMGLLAAVRDAQARLIARWMGVGFIHGVMNTDNSSIAGETIDYGPCAFMDTYHPDTVYSSIDRYGRYAYSNQPDIAVWNLAQLATALIQQAEDKEAVVEEATEIVHAMPELLERAWLEVFAAKIGIARPGEGDKALVSELLTRMAREQADFTNTFRALGAPRARDQFTDPTAYDSWAEDWRQRLTQEATPEAVIRAANPAFIPRNHRIEQMITAAVEGDYTLFERLNTVLARPYADQPDHIDLTRPPSASEIVPATFCGT | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 51487
Sequence Length: 472
EC: 2.7.7.108
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Q21HQ5 | MLEHLKFDNSFDKLGSDFATRVNPRPLVNPKLVCVDSKTCELLGISKDSVSSENGVNMFSGNRVPPQFAPLAMVYAGHQFGGYSSQLGDGRGLLLGELNTHSGKYDLHLKGAGKTPYSRFGDGYAVLRSCIREYLAGIAMRGLGIPTSHALCVVRGDNAVTRETIEPAATLTRVARSHIRFGSFEYFYYTQQHTQLEQLADYAVEQYIPEYVDKDGRFNALLHYTTEQTAKLIAAWQAVGFCHGVMNTDNMSIIGETLDYGPYGFMEAYNPTHICNHSDTYGRYAYDQQPSIGLWNLNALAAALSPLIDRDQARASLESYEGILTKEYNSRMTKKLGFLSAKQGDAKLINTMFIQLEQLQLDYTLFFRLLALAKADDLQSSFIQPLLGCDNIAKGEQLAAWAAEYLTRRQLEDVPQATITADMNHHNPIYCLRNYFAQQAIDEAYQQGTYSTLEKLAAVLAAPFTSHPNASEFETPPPSELANIAVSCSS | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54357
Sequence Length: 490
EC: 2.7.7.108
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Q8ZPS5 | MTLSFTARWRDELPATYTALLPTPLKNARLIWYNDELAQQLAIPASLFDATNGAGVWGGETLLPGMSPVAQVYSGHQFGVWAGQLGDGRGILLGEQLLADGSTLDWHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMHYLGIPTTRALSIVTSDTPVQRETQETGAMLMRLAQSHMRFGHFEHFYYRREPEKVQQLADFAIRHYWPQWQDVPEKYALWFEEVAARTGRLIAEWQTVGFAHGVMNTDNMSILGLTIDYGPFGFLDDYDPGFIGNHSDHQGRYRFDNQPSVALWNLQRLAQTLTPFIEIDALNRALDRYQDALLTHYGQRMRQKLGFFTEQKDDNVLLNELFSLMAREGSDYTRTFRMLSHTEQQSASSPLRDTFIDRAAFDAWFDRYRARLRTEAVDDALRQQQMQRVNPAIVLRNWLAQRAIDAAEQGDMAELHRLHEVLRQPFTDRDDDYARRPPEWGKRLEVSCSS | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54941
Sequence Length: 480
EC: 2.7.7.108
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O13890 | MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFLRYSYRNQPDIIIWNLSKLASALVELIGACDKVDDLQYMEQLHNSTDLLKKAFAYTSEVFEKIVEEYKNIVQNDFYDLMFKRVGLPSDSSNKILITDLLQILEDYELDMPNCFSFLSRNSPSSMENEEYAAKLMQACICLNPNNERVRNESVKAFTNWVGRYSEATKTQEDSSRLASMKKVNPHFTLRNWVLEEVIKEAYIGKFELFKKVCKMAACPFEDTWGFSKEEEDYLCYNTTPSKSQIQCSCSS | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Tyr residues of target mitochondrial proteins (AMPylation). Involved in redox homeostasis by regulating the cellular response to oxidative stress. Regulates protein S-glutathionylation levels possibly by AMPylation of deglutathionylation enzymes such as glutaredoxins.
PTM: Forms probably one or more intrachain disulfide bridges.
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 63951
Sequence Length: 568
Subcellular Location: Mitochondrion
EC: 2.7.7.-
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Q8ZR88 | MQDRQKAQDYRALLLADTPLIDVRAPIEFEQGAMPGAINLPLMMDDERAAVGTCYKRQGADAALALGHRLVCGDIRQQRLEAWKAAYQRFPNGYLCCARGGQRSHIVQRWLQETGIDCPLIEGGYKALRQTAIQATWQLAQKPILLIGGCTGSGKTQLVRQQPNGVDLEGLARHRGSSFGRTLNPQLSQASFENKLAVELLKINARQTLKRWVLEDEGRTIGANHLPECLRERMAQAPIAVVEDPFALRLERLREEYFIRMHHDFTHAYGDEAGWQAYSEYLHHGLFAIRRRLGLQRFAELTDTLDRALAEQLSSGSTDGHMAWLVPLLNEYYDPMYRYQLEKKAANIVFRGTWQDVANWLKAQ | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln) . Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA) . Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain (Probable).
Catalytic Activity: (2E)-geranyl diphosphate + 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + H2O + selenophosphate = (2E)-thiogeraniol + 5-methylaminomethyl-2-selenouridine(34) in tRNA + diphosphate + phosphate
Sequence Mass (Da): 41328
Sequence Length: 364
Domain: Composed of a rhodanese domain and a P-loop domain, which probably binds geranyl diphosphate. The two activities are mechanistically different, but the rhodanese domain is important for both.
EC: 2.9.1.3
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A0QR01 | MSLLTLIAGVAVGVTVVPRIVARRQRRAAYAAGMTVSQMLQHITSLSPMGVAVVDTFNDVVYSNDRAVELNVVRDRILDDRAWQAAQRVFETGQDVEVDLSPLKVANPGRSGISVRGKVRLLTDDDRRFAVVYIDDQSEHARMEATRRDFVANVSHELKTPVGAMSVLAEALLASADDPDTVRRFAEKMVAESHRLADMIGELIELSRLQGAERLPDLDAVDVDSIVSEAVSRHKVAADNSQISITTDAPTGYRVLGDEGLLVTAIANLVSNAIAYSPNGTDVSISRRKRGGNIEIAVTDRGIGIAKDDQERVFERFFRVDKARSRATGGTGLGLAIVKHVAANHNGSIRLWSQPGTGSTFTLSIPEYPDPESHSDEREDQRER | Function: Member of the two-component regulatory system SenX3/RegX3 involved in stress response . The system is involved in phosphate starvation response . Probably exhibits a dual role as a phosphatase or a phosphodonor for the response regulator RegX3, depending upon phosphate availability (Probable). When environmental phosphate is abundant, SenX3 is required to maintain RegX3 in an unphosphorylated state, where it is unable to bind target DNA (Probable). Under conditions of phosphate limitation, SenX3 autophosphorylates and then transfers the phosphate group to RegX3 (Probable). Probably does not itself sense phosphate concentrations, which may be relayed to SenX3 by the PstSCAB phosphate transporter system .
PTM: Autophosphorylated.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 41862
Sequence Length: 384
Subcellular Location: Cell membrane
EC: 2.7.13.3
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P39709 | MYSIVKEIIVDPYKRLKWGFIPVKRQVEDLPDDLNSTEIVTISNSIQSHETAENFITTTSEKDQLHFETSSYSEHKDNVNVTRSYEYRDEADRPWWRFFDEQEYRINEKERSHNKWYSWFKQGTSFKEKKLLIKLDVLLAFYSCIAYWVKYLDTVNINNAYVSGMKEDLGFQGNDLVHTQVMYTVGNIIFQLPFLIYLNKLPLNYVLPSLDLCWSLLTVGAAYVNSVPHLKAIRFFIGAFEAPSYLAYQYLFGSFYKHDEMVRRSAFYYLGQYIGILSAGGIQSAVYSSLNGVNGLEGWRWNFIIDAIVSVVVGLIGFYSLPGDPYNCYSIFLTDDEIRLARKRLKENQTGKSDFETKVFDIKLWKTIFSDWKIYILTLWNIFCWNDSNVSSGAYLLWLKSLKRYSIPKLNQLSMITPGLGMVYLMLTGIIADKLHSRWFAIIFTQVFNIIGNSILAAWDVAEGAKWFAFMLQCFGWAMAPVLYSWQNDICRRDAQTRAITLVTMNIMAQSSTAWISVLVWKTEEAPRYLKGFTFTACSAFCLSIWTFVVLYFYKRDERNNAKKNGIVLYNSKHGVEKPTSKDVETLSVSDEK | Function: Not known; suppressor of sulfoxide ethionine resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68842
Sequence Length: 593
Subcellular Location: Membrane
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Q2KJB1 | MASEVARHLLFQSHITTKTAHTSSQVSDHEQKQKDSPRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDHESSHFYPHVRLKAQTYELQESNVRLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFNYHDSRVHVCLYFISPTGHSLKTLDLLTMKSLDSKVNIIPVIAKADAISKTELQKFKIKLMSELVSNGVQIYQFPTDDETIAKINASMNGHLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLRDQTHTRHYELYRRRKLEEMGFMDVGPENQPLSLQETYEAKRHEFYGERQRKEEEMKQLFVQRVKEKEAILKEAERELQAKFEHLKRVHQEEKLRLEEKRRLLEEEIMAFSKKKATSEIYQNQTFMTPGSNLRKDKDRKNSNFM | Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
PTM: Proteolytically cleaved in vitro in a calmodulin-dependent manner.
Sequence Mass (Da): 52809
Sequence Length: 453
Subcellular Location: Cytoplasm
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Q9P0V9 | MASSEVARHLLFQSHMATKTTCMSSQGSDDEQIKRENIRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDYESSHFCPNVKLKAQTYELQESNVQLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFTYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMGFTDVGPENKPVSVQETYEAKRHEFHGERQRKEEEMKQMFVQRVKEKEAILKEAERELQAKFEHLKRLHQEERMKLEEKRRLLEEEIIAFSKKKATSEIFHSQSFLATGSNLRKDKDRKNSNFL | Function: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential).
PTM: Proteolytically cleaved in vitro in a calmodulin-dependent manner.
Sequence Mass (Da): 52593
Sequence Length: 454
Subcellular Location: Cytoplasm
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Q8C650 | MASCDEIKEHPRSLSMCGHVGFESLPDQLVDRSIEQGFCFNILCVGETGIGKSTLINTLFNTNFEELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEDSYQPIVDYIDDQFEAYLQEEVKIKRALFNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSELQKFKMKLMNELVINGVQIYQFPTDDDTTSKINGAMNGHLPFAVVGSMDEIKVGNKMVKGRQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMGFVDMGPENKPLSLQETYEAKRHEFYGERQRKEEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRMLEEESVAFAKKKATCELFPNQSFLASGSSIRKDKDRKKADGASAFCDCLTAQESVRLCISSPRKDMD | Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
PTM: Proteolytically cleaved in vitro in a calmodulin-dependent manner.
Sequence Mass (Da): 52422
Sequence Length: 452
Subcellular Location: Cytoplasm
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A0A3Q0KDV9 | MTADVLKALPPDVRTLKLSGHVGFDSLPDQLVNKAISQGFVFNILCVGETGIGKSTLLETLFNQKFDFSPSNHDLTDPKLKAVTYDLKEANVKLKLTVVETCGYGDQINKENNIKPVVDYIDNQFENYLQEELKMKRSMQAFHDTRVHVCLYFIAPTGHSLKSIDLVAMKKLENKVNVIPVIAKSDTITKSELQKFKARILSEIQSNEIGIYQFPTDDEAVSETNSVMNQHIPFAVVGSSEEVKINGKTVRVRQYPWGSVQVENENHCDFVRLREMLLRVNMEDLRERTHGVHYETYRRQRLIEMGFRDDEKMSLQETYEKRRELQRKELQQKEEEMRQMFVQRVKEKEQVLKEAERELQTKFESLKKTHAEEKKKLEEKKRFLEEEIAAFERRKQLAEQARQGNLTMKKRK | Cofactor: Mg(2+) is essential for the GTP-binding, but GDP-binding does not require a metal cofactor.
Function: Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability . Able to bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which serve as a model of biological membranes. Self-assembles into ordered cage-like structures on the vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS)-containing vesicles suggesting the requirement for negatively charged membranes. Is also able to promote deformation of the GUVs .
Sequence Mass (Da): 48090
Sequence Length: 412
Domain: C-terminus (307-412) is necessary for binding to liposomal membranes as assessed by phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), models of biological membranes.
Subcellular Location: Cytoplasm
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O29445 | MKVLVAEPISEEAIDYMRKNGLEVEVKTGMSREELIREVPKYEAIVVRSQTKVDAEVIQAAKNLKIIGRAGVGVDNIDINAATQRGIVVVNAPGGNTISTAEHAIALMLAAARKIPQADRSVKEGKWERKKFMGIELRGKTAGVIGLGRVGFEVAKRCKALEMNVLAYDPFVSKERAEQIGVKLVDFDTLLASSDVITVHVPRTKETIGLIGKGQFEKMKDGVIVVNAARGGIVDEAALYEAIKAGKVAAAALDVYEKEPPSPDNPLLKLDNVVTTPHIAASTREAQLNVGMIIAEDIVNMAKGLPVRNAVNLPSIEPSDFEFMMPFLTLAEKMGKIASVRLGGAIRKVKVTCSGKLATKNTEFVTRALLKGLFEPILSNEINLVSAKPVAVERGITIEESKVESVEHYESLLEVWVESNGKEMYLAGTCFGNEYRILKIDVYNVNFVPKGHYIISLHEDKPGVIGRVGTLFGRNNINIAGMIVGRSGDKPGGIQLMLLLVDDPPTPEVLEEMTKLDGIIDATYVEL | Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 57204
Sequence Length: 527
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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P35136 | MFRVLVSDKMSNDGLQPLIESDFIEIVQKNVADAEDELHTFDALLVRSATKVTEDLFNKMTSLKIVGRAGVGVDNIDIDEATKHGVIVINAPNGNTISTAEHTFAMISSLMRHIPQANISVKSREWNRTAYVGSELYGKTLGIVGLGRIGSEIAQRARAFGMTVHVFDPFLTEERAKKIGVNSRTFEEVLESADIITVHTPLTKETKGLLNKETIAKTKKGVRLINCARGGIIDEAALLEALENGHVAGAALDVFEVEPPVDNKLVDHPLVIATPHLGASTKEAQLNVAAQVSEEVLQFAKGLPVMSAINLPAMTKDEFAKIKPYHQIAGKIGSLVSQCMKEPVQDVAIQYEGTIAKLETSFITKALLSGFLKPRVDSTVNEVNAGGVAKERGISFSEKISSSESGYDNCISVKVTGDRSTFTVTATYIPHFGERIVEINGFNIDFYPTGHLVYIQHQDTTGVIGRVGRILGDNDINIATMQVGRKEKGGEAIMMLSFDRHLEDKIVKELTNVPDIVSVKLIDLP | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 57129
Sequence Length: 525
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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Q5EAD2 | MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTSDIINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQAAASMKDGKWERKKFMGTELNGKVLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEQIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVCVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVNHENVISCPHLGASTKEAQSRCGEEIALQFVDMVKGKALAGVVNAQALASIFCPHTKPWVSLAKALGALMQAWAGSPKGAIQVVTQGSSLKNSGSCLAPAVIIGLLKDASQQSNVNLVNAMLLVKEAGLDVTTSHNPATPREQDFGECLLTVALAGAPYQAVGLVQGTKPVLQALNGAVFRPEVPLHPGQPLLMFRAQASNPAMLPTMIGLLAEAGVQLLSYQSSVVSDGETWHVMSISSLLPSLAPWKPHVTEAFQFCF | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 56452
Sequence Length: 533
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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Q54UH8 | MDPTTSFPKDKIKILLLENIHIAAIKQFEEQGFQVESISSSLPEDKIIEKIKDVHVLGLRSKTKVTEKILSEAKRLLAIGCFCIGTDQVDLIEAEKRGVPVFNSPFCNSRSVAELIICEIITLSRKLGDRSTEMHNKIWRKESANCHEIRGKTLGIIGYGHIGSQLSVLAEAMGMSVLYYDIARRLPLGNSKMCPDMKTLLENSNFVTLHVPDTKETVGLIGEEEINTMKKGSYLLNASRGKVVQIPHLANALRSGHLAGAAVDVYPEEPSANCKDWECELQKCPNTILTPHIGGSTEEAQEAIGLEVSDLIVQFINSGASAGSVNFPEIALPVSPSTHRILNIHNNKPGVLRDINNILSEFNVSAQVLSTRKQIGYIIADVDSEASKEIKKKISSLPNSIKTRVLY | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 44749
Sequence Length: 407
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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P0A9T2 | MAKVSLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSAVNFPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 44176
Sequence Length: 410
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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P21138 | MFAFLLFIAFTSATNIILDLDQEVKDTNIYGVFLKNEASPEKLEEAEEKEKSSSAKPESSSNEDNEDDEDEKASSSDNSESSSSDKPDNKPEASSSDKPEASSSDKPDNKPEASSSDKPDNKPEASSSDKPDNKPEASSSDKPDNKPEASSSDKPDNKPEASSTNKPEASSTNKPEASSTNKPEASSTNKPEASSTSNSNDKSGSSSDNDNNNLDAASSPFIVFCAIIIAIIF | Function: Plays a role in the adhesion to host cells . Involved in the adhesion to host apoptotic cells thereby facilitating their phagocytosis .
PTM: Phosphorylated on serine residue(s).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24719
Sequence Length: 233
Subcellular Location: Cell membrane
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O43175 | MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 56651
Sequence Length: 533
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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Q58424 | MVKILVTDPLHEDAIKILEEVGEVEVATGLTKEELLEKIKDADVLVVRSGTKVTRDVIEKAEKLKVIGRAGVGVDNIDVEAATEKGIIVVNAPDASSISVAELTMGLMLAAARNIPQATASLKRGEWDRKRFKGIELYGKTLGVIGLGRIGQQVVKRAKAFGMNIIGYDPYIPKEVAESMGVELVDDINELCKRADFITLHVPLTPKTRHIIGREQIALMKKNAIIVNCARGGLIDEKALYEALKEGKIRAAALDVFEEEPPKDNPLLTLDNVIGTPHQGASTEEAQKAAGTIVAEQIKKVLRGELAENVVNMPNIPQEKLGKLKPYMLLAEMLGNIVMQVLDGSVNRVELIYSGELAKEKTDLIKRAFLKGLLSPILLAGINLVNAPIIAKNRNINVVESSTSEEKYGNAIKITAESDKKKFSIVGAIINNKPVILEVDGYEVSFIPEGVLAIIKHIDRPGTIGRVCITLGDYGINIASMQVGRKEPGGESVMLLNLDHTVPEEVIEKIKEIPNIKDVAVINL | Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 56924
Sequence Length: 524
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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P0A545 | MSLPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIAAFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAALADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVNEEVAPWLDLVRKLGVLAGVLSDELPVSLSVQVRGELAAEEVEVLRLSALRGLFSAVIEDAVTFVNAPALAAERGVTAEICKASESPNHRSVVDVRAVGADGSVVTVSGTLYGPQLSQKIVQINGRHFDLRAQGINLIIHYVDRPGALGKIGTLLGTAGVNIQAAQLSEDAEGPGATILLRLDQDVPDDVRTAIAAAVDAYKLEVVDLS | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 54554
Sequence Length: 528
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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O33116 | MDLPVVLIADKLAQSTVAALGDQVEVRWVDGPDRTKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIAEADASLRAHIWKRSSFSGTEIFGKTVGVVGLGRIGQLVAARIAAFGAHVIAYDPYVAPARAAQLGIELMSFDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEVALADAVRSGHVRAAGLDVFATEPCTDSPLFELSQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVDGGVVNEEVAPWLDLVCKLGVLVAALSDELPASLSVHVRGELASEDVEILRLSALRGLFSTVIEDAVTFVNAPALAAERGVSAEITTGSESPNHRSVVDVRAVASDGSVVNIAGTLSGPQLVQKIVQVNGRNFDLRAQGMNLVIRYVDQPGALGKIGTLLGAAGVNIQAAQLSEDTEGPGATILLRLDQDVPGDVRSAIVAAVSANKLEVVNLS | Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Mass (Da): 54469
Sequence Length: 528
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
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C4L432 | MSTYTYSAGPGMLPTEVMQEIQQHLLTFEYEGVSIIETSHRSASFQRVVDSLEWRLRRLMHIPENYAVLWLQGGATLQFSMIPMNLRKQNRFAYVDTGIWSKKAMEDAKHFGEVDVIHPLVDATGGMSFESSLVQEVDYLHVTLNNTIEGTRFTHIPEIDVPLIADASSNILAEQIDVERFGVIYAGAQKNIGPAGLTVVIIRRDLIQSLQLPSYLQYASHVDTLFNTPSTFSMYAAERVLKWVEDCGGVEAMERLNRQKSDRIYSYLEESTCFSPIVTGERRSLTNIPFSTGNQELDQRFERYALERGLLELGGHRSVGGLRASLYNAMPLEGAERLVDVMRAFEEETHVSHQNI | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence Mass (Da): 40289
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
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A6GXC2 | MKKHNYSAGPCILPQEVFEKSAQAILDFNHSGLSLLEISHRSKDFVAVMEEARALVLELLGLKGKGYQALFLAGGASLEFLMVPYNLMKENGKAAYLDTGTWASGAIKEAKHFGETVVIASSKEENYNHIPKNYSIPSDANYFHCTSNNTIFGTQMKSFPEVNIPVVCDMSSDIFSRVLDFSKFDLIYAGAQKNMGPAGTTLVIVKEEILGKTGRYIPSMLDYEKHIKAESMYNTPPVFPIYASLLTLQWLKNLGGISAIEKINNAKANLLYSEIDRNTLFKGTANAEDRSNMNATFLLNNKNHTELFDKMWAAAGISGLSGHRSVGGYRASMYNALPLESVQVLVNVMKELENKI | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence Mass (Da): 39361
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
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Q5L296 | MKRAYNFNAGPSALPLPVLERAQKELLNFQNTGMSVMELSHRSKEYEAVHHAAKERLKRLLNVPDGYDILFLQGGASLQFSMVPMNLLTEGKIGCYVLTGAWSEKALKEAQKIGLTTVVASSKEANYTYIPPLDDVQWPKNAAYVHITSNNTIFGTQWKEFPNTPVDLVADMSSDILSRPFDVSQFALIYAGAQKNLGPSGVTVVILRNDLLERIPDGLPTMLDYRTHQKSNSLYNTPPTFAIYMLSLVLEWVEEQGGVAAMEERNQQKAAVLYEAIDESGGFYKPHAEKGSRSLMNVTFTLPNEELTKTFLAEAKERGFVGLGGHRSVGGCRASIYNAVPLEACEALASFMNEFRRRFA | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence Mass (Da): 39983
Sequence Length: 360
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
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Q2SCF2 | MADRKFNFCAGPSALPTEVLLQAQAELLDWRGKGLSIMEMSHRSDDFVAVAVEAERDFRELMSVPDNYKVLFVQGGAATQFASVPLNLLKLGAEADYIDTGIWSKKAIAEAGRYLKVNVAASAKDNGYACIPARSEWRLSESAGYVHYTPNETIGGVEFLDIPDVGDKPLVADMSSTILSRPVDISRFGVIYAGAQKNIGPAGLTLVIVREDLLGYASDSLPTMLNYKVASENDSMVNTPPTFSWYLAGLVFKWLKGKGGVQAMEAINCRKADKLYSYIDDSEFYANPIDLSCRSWMNVPFTLKDDRLDQKFLQEAEGAGLLNLQGHRSVGGMRASLYNALPEEAVDALIGFMQDFAGRNA | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence Mass (Da): 39513
Sequence Length: 361
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
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Q9Y617 | MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLVRELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGTINIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSNFLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLYNTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSKMNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAFMKKFLEMHQL | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence Mass (Da): 40423
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
EC: 2.6.1.52
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Q553P6 | MSQSRTLRQKSQKYQENIEKRGVASPKKKEDGLNINPYVLGFIIFVVVGSTLLQILKGQ | Function: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 6678
Sequence Length: 59
Subcellular Location: Membrane
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C1IBY0 | MLKYSALFLYLIYVGGSESAHSRIVGGVPVAEEKVPYVVSIRMKEIHVCGGSILSESIVLTAAHCFDKSKGYSNYAVFAGSNRLSGGLKVEIQNITIHPKYIGPSDWWKNDLAVVKLKKPLNFSKSVRTVKIFPSYVPENETVYAYGWGKTIVPFFTLPNVLQKLETKALNLTACQKSWKEHVVESQLCLWTGHGTGVGLCKADSGGPVVYKGKLVGVISWVQVHCNTKKPDVAVRLSPYFENGLRKR | Function: Serine protease that inhibits blood coagulation in a dose-dependent manner. May act by destroying coagulant factors to inhibit blood coagulation.
Sequence Mass (Da): 27408
Sequence Length: 248
Subcellular Location: Secreted
EC: 3.4.21.-
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A0A1J1EM40 | MTAEQAINEGAFSLAASFGFVPLEYRGYEAEVLASKETAYIGTALNGAMSPIYDVTGPDALEFLRSVCINSFRGFQVGQIRHAVLCNDKGQILTDGVVARIDEDTYRTYWLAPALEYRLINSGLDVKGEDQSSNEFFFQLAGPRSLEVLEAAAHEDLHDIAFGRHRMSTIAGIPVRILRLGMAGGLAYEVHGAAADTETAYRAIWEAGQPFGLVKQGLNAYLMQHTEAGFPNINLHYPLPWYEDPDMAAFFDTRPTQNFYNKYRFFYGSVGPDAEARFVTPYQIGLGKMVDFNHDFIGKEALQREAEADHWAAVTLVWNEDDVADVVASKYRGRDVEPYDKIDDRPFDIYHNLGQPGFAYHADWVLADGERIGTSTGRINSVYYRRMISLGFIDKRHAAEGTELTVLWGRPGTPQKEIRVTVGRYPYFDLEKNNAIDVASIPRPALDVSAGA | Function: Converts sesamin into sesamin mono- and di-catechol. Catalyzes a ring cleavage to transfer the methylene group to tetrahydrofolate (THF). Also active with (+)-episesamin, (-)-asarinin, sesaminol, (+)-sesamolin and piperine.
Catalytic Activity: (+)-sesamin + (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) = (+)-sesamin monocatechol + (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n)
Sequence Mass (Da): 50386
Sequence Length: 452
EC: 2.1.5.1
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Q9Y6P5 | MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDEELGIRIPRPLGQGPSRFIPEKEILQVGSEDAQMHALFADSFAALGRLDNITLVMVFHPQYLESFLKTQHYLLQMDGPLPLHYRHYIGIMAAARHQCSYLVNLHVNDFLHVGGDPKWLNGLENAPQKLQNLGELNKVLAHRPWLITKEHIEGLLKAEEHSWSLAELVHAVVLLTHYHSLASFTFGCGISPEIHCDGGHTFRPPSVSNYCICDITNGNHSVDEMPVNSAENVSVSDSFFEVEALMEKMRQLQECRDEEEASQEEMASRFEIEKRESMFVFSSDDEEVTPARAVSRHFEDTSYGYKDFSRHGMHVPTFRVQDYCWEDHGYSLVNRLYPDVGQLIDEKFHIAYNLTYNTMAMHKDVDTSMLRRAIWNYIHCMFGIRYDDYDYGEINQLLDRSFKVYIKTVVCTPEKVTKRMYDSFWRQFKHSEKVHVNLLLIEARMQAELLYALRAITRYMT | Function: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway . This stress-inducible metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1 . Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 . However, this could not be confirmed (By similarity).
Catalytic Activity: a hydroperoxide + L-cysteinyl-[protein] = an alcohol + S-hydroxy-L-cysteinyl-[protein]
Sequence Mass (Da): 56557
Sequence Length: 492
Domain: The N-terminal domain may have an alkylhydroperoxide reductase activity.
Subcellular Location: Nucleus
EC: 1.11.1.-
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Q9NVD3 | MQKGKGRTSRIRRRKLCGSSESRGVNESHKSEFIELRKWLKARKFQDSNLAPACFPGTGRGLMSQTSLQEGQMIISLPESCLLTTDTVIRSYLGAYITKWKPPPSPLLALCTFLVSEKHAGHRSLWKPYLEILPKAYTCPVCLEPEVVNLLPKSLKAKAEEQRAHVQEFFASSRDFFSSLQPLFAEAVDSIFSYSALLWAWCTVNTRAVYLRPRQRECLSAEPDTCALAPYLDLLNHSPHVQVKAAFNEETHSYEIRTTSRWRKHEEVFICYGPHDNQRLFLEYGFVSVHNPHACVYVSREILVKYLPSTDKQMDKKISILKDHGYIENLTFGWDGPSWRLLTALKLLCLEAEKFTCWKKVLLGEVISDTNEKTSLDIAQKICYYFIEETNAVLQKVSHMKDEKEALINQLTLVESLWTEELKILRASAETLHSLQTAFT | Function: Histone-lysine N-methyltransferase that acts as a regulator of cell proliferation, cell differentiation and inflammatory response . Regulates the inflammatory response by mediating mono- and dimethylation of 'Lys-4' of histone H3 (H3K4me1 and H3K4me2, respectively), leading to activate the transcription of pro-inflammatory cytokines IL6 and TNF-alpha (By similarity). Also involved in the regulation of stem cell quiescence by catalyzing the trimethylation of 'Lys-20' of histone H4 (H4K20me3), thereby promoting heterochromatin formation . Involved in proliferation, migration, paracrine and myogenic differentiation of bone marrow mesenchymal stem cells (BMSCs) (By similarity).
Catalytic Activity: L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50416
Sequence Length: 440
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q5ZK17 | MAAPAKRRRAAGPDPDPTAGFVAWCEAAGVELSPKVSISRRGTVSGYGLLAAADLEPGELLFSVPRSALLSQHTCAIRALLHDAQESLQSQSVWVPLLLALLHEYTTGTSRWRPYFSLWQDFSSLDHPMFWPEEERVRLLQGTGIPEAVDKDLANIQLEYSSIILPFMKSHPDIFDPELHTLELYKQLVAFVMAYSFQEPLEEEDEDEKGPNPPMMVPVADILNHVANHNASLEYAPTCLRMVTTQPISKGQEIFNTYGQMANWQLLHMYGFAEPYPGNTNDTADIQMVTVRKAALQRAKNEAQQQLVAEQWDFLCQLEMVGEEGAFVLGWDEVLTEEELSVTLKVLCMSEEEFKEYKEQDGWEDDSEEEENSTLSNAALSRLKAPCKALLYDSVLLTLESYRSDLRAEQDLLSKQVYEKLSRREQQALHVRYGQKRILHQLLELVQ | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 50649
Sequence Length: 447
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q803K4 | MATEAKRPKTGDEKSVLEPLNNFLLWCESVQLTLSDKVYLSKEGTAAEYGMLAKEDIEEGHVLFTIPREALLHQGTTKVKKVLEEGKKCLESASGWVPLLLSLMYEYTSSTSHWKPYLSLWPDFRTLDQPMFWSEEECDKLLKGTGIPESVITDLRKLQDEYNSVVLPFMKSHPDLWDPEKHNLELYKSLVAFVMAYSFQEPVEDDDEDEEDDEKKPNLPMMVPMADMLNHISKHNANLEYTPECLKMVSIRRIGKGEEVFNTYGQMANWQLLHMYGFAEPFPNNINETADIKMASVYKAAAQVARSEANQQLLEDKWKMLCEMEVVGEKGVFIFGQSGSLTYHELYTTLKVLCMSSQIFEDFRENEGWEEDDEDDDDKMEQDLSFEGLASLSVEWKRLLCVAATETLDSYNEDVETDRRLMEDQRALAELSSRERRALYVRLGQKNILQRIQQLTKPAS | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 53007
Sequence Length: 460
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8TBK2 | MATQAKRPRVAGPVDGGDLDPVACFLSWCRRVGLELSPKVSERAGGRRTRGGARAALTSPPAQVAVSRQGTVAGYGMVARESVQAGELLFVVPRAALLSQHTCSIGGLLERERVALQSQSGWVPLLLALLHELQAPASRWRPYFALWPELGRLEHPMFWPEEERRCLLQGTGVPEAVEKDLANIRSEYQSIVLPFMEAHPDLFSLRVRSLELYHQLVALVMAYSFQEPLEEEEDEKEPNSPVMVPAADILNHLANHNANLEYSANCLRMVATQPIPKGHEIFNTYGQMANWQLIHMYGFVEPYPDNTDDTADIQMVTVREAALQGTKTEAERHLVYERWDFLCKLEMVGEEGAFVIGREEVLTEEELTTTLKVLCMPAEEFRELKDQDGGGDDKREEGSLTITNIPKLKASWRQLLQNSVLLTLQTYATDLKTDQGLLSNKEVYAKLSWREQQALQVRYGQKMILHQLLELTS | Function: Protein-lysine N-methyltransferase. Monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulation of NF-kappa-B transcription factor activity . Monomethylates 'Lys-8' of H2AZ (H2AZK8me1) . Required for the maintenance of embryonic stem cell self-renewal (By similarity). Methylates PAK4.
PTM: Automethylated; Lys-39 and Lys-179 serve as the major automethylation sites.
Catalytic Activity: L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53189
Sequence Length: 473
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9CWY3 | MAAPAKRARVSGGSPLVAPCPSPRAARAPLPLPAGSSGGEPEGDAVAGFLRWCRRVGLELSPKVTVSRQGTVAGYGMVARESVRAGELLFAVPRSALLSPHTCSISGLLERERGALQSLSGWVPLLLALLHELQAPASPWSPYFALWPELGRLEHPMFWPEEERLRLLKGTGVPEAVEKDLVNIRSEYYSIVLPFMEAHSDLFSPSVRSLELYQQLVALVMAYSFQEPLEEDDDEKEPNSPLMVPAADILNHIANHNANLEYSADYLRMVATQPILEGHEIFNTYGQMANWQLIHMYGFAEPYPNNTDDTADIQMVTVRDAALQGTKDETEKLLVCERWDFLCKQEMVGEEGAFVIGCEEVLTEEELATTLKVLCMPAEEFRDYKERAGWGEEETEDDSLAITDIPKLQESWKRLLRNSVLLTLQTYTTDLKTDQDLLSNKEAYATLSWREQQALQVRYGQKMILHRVLELTN | Function: Protein-lysine N-methyltransferase. Monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulation of NF-kappa-B transcription factor activity. Monomethylates 'Lys-8' of H2AZ (H2AZK8me1) (By similarity). Required for the maintenance of embryonic stem cell self-renewal . Methylates PAK4.
PTM: Automethylated.
Catalytic Activity: L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52960
Sequence Length: 473
Subcellular Location: Nucleus
EC: 2.1.1.-
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A4QNG5 | MGPDAKKQKLQSEDHLQNDLPVSCFLAWCKKVGLELNPKVYISTEGTVSQYGMLAREDLSDGELLFSIPRSAILSQNTTRIRDLIEKEQDSLQSCSGWVPLLISLLYEATDSSSHWAPYFGLWPELDPPDMPMFWSEEEQTKLLQGTGILEAVHKDLKNIEKEYNSIVLPFIRRNPEKFCPMKHTLDLYKRLVAFVMAYSFQEPQEEDEEEDIEKDILPPMMVPVADLLNHVAQHNAHLEFTPECLRMITTKSVCAGQELFNTYGQMANWQLLHMYGFAEPHPQNCNETADIQMVTVREAAFQVARTEEDRLEMQKRWDFLCHIEIVGEEGAFVFGLEEVMTEEELKACLKVLCMSTDEFAEYKENDGWEEDEDNDEQTLLTQEISRLPIPWRKLLHLSAELTLKAYKTELSMDEALVNDPTAYAKLSSREQHSLQVQYGQKKILHLLLELTKS | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 52331
Sequence Length: 454
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q7Z0G7 | MDSSDDEIACDEGDYKGAKDDNDLPHGLGKVKFSSGDEFIGAFEHGIKCGPGKFHFFDDSTLEGNYVDGELHGIGIYTNDDGSITKSTYCEGVMEGPSWEYDPEGNITFRGQYSEGVRCGLCFYYFPDGGSLIGNVNASGDLSADNIAYIYPDRTTALIGSFEEGDMITAKEANVTITGEKGEEISFPTVNSISPDPVYRLDVSTPHVISTRPLVPDPYESELVYAAPSKIPNAGEGLYAKCDVDQDTVMAFYNGVRLKQDEVENRDWSQNSNTISLTDDIAIDVPEEYVSTDNYCASLGHKVNHSFDPNCRYDIYQHPRFGFIKCVRTIRGVSEGDELTVHYTYEHNDGNKTREAEAPEWYKSQLKVFGVDRPAEILENMDEDYC | Function: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes. Has also methyltransferase activity toward non-histone proteins.
Catalytic Activity: L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42850
Sequence Length: 386
Domain: The SET domain is necessary but not sufficient for histone methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.364
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Q8WTS6 | MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK | Function: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3 . H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation . Plays a central role in the transcriptional activation of genes such as collagenase or insulin . Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription . Has also methyltransferase activity toward non-histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins . Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II . Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation . Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS (By similarity).
Catalytic Activity: L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40721
Sequence Length: 366
Domain: The SET domain is necessary but not sufficient for histone methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.364
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Q8VHL1 | MDSDDEVVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDSDGRLIFKGQYKDNNRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGRPHFEVTSGSSVYHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDLFVHPRFGPIKCIRTLRAVEAEEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK | Function: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). Plays a central role in the transcriptional activation of genes such as collagenase or insulin . Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription (By similarity). Has also methyltransferase activity toward non-histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins . Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II (By similarity). Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation (By similarity). Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS .
Catalytic Activity: L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40506
Sequence Length: 366
Domain: The SET domain is necessary but not sufficient for histone methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.364
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Q06168 | MSHQNQLIPQAYISNFHNRLTNEDDGIPIFTMAQQTRQHKRAKVVNYAEYDNDLFDEFNMNGSNFNNADTHYKDNAVSHENTPALTNGVTMDGSEYNVLENMNGADSIISNNKYDAGSNMVVESLSGLNSNNNASNGPSNKAQAQDIGNAVLPDLQDQHHNPFNILRYPKIRDTFINGKVVSPYRLNTDQETKANANSGEAIMIPITLDIEHMGHTIKDQFLWNYNDDSISPEEFASIYCKDLDMTSATLQTQIANIIKEQLKDLENIAATEIMSDLHVIINLTCNLQDRFFEDNFQWNLNDKSLTPERFATSIVQDLGLTREFIPLISQSLHETILKIKKDWVDGHLIQDHVPNDAAFGYLSGIRLDIDELGSNWCPRVEILTKEEIQKREIEKERNLRRLKRETDRLSRRGRRRLDDLETTMRM | Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and required for cell cycle progression.
PTM: Phosphorylated in the G1 phase.
Sequence Mass (Da): 48777
Sequence Length: 426
Subcellular Location: Nucleus
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Q93ZE9 | MTDTMSAHMDRHNKLDYDGSEDEKKTKLCSLKKKAINASNKFKHSFTKRTRRNSRVMSVSIVDDIDLEELQAVDAFRQALILDELLPSKHDDHHMMLRFLRARKFDLEKAKQMWTDMIHWRKEFGVDTIMEDFDFKEIDEVLKYYPQGYHGVDKDGRPVYIERLGQVDATKLMQVTTIDRYVKYHVREFEKTFNIKLPACSIAAKKHIDQSTTILDVQGVGLKSFSKAARDLLQRIQKIDSDNYPETLNRMFIINAGSGFRLLWSTVKSFLDPKTTAKIHVLGNKYQSKLLEIIDSNELPEFLGGNCTCADKGGCMRSDKGPWNDPDIFKMVQNGEGKCPRKTLSNIEEKTISVDENTTMKSDSFAKNKFDAENTKFIPMIDKTVNASTWPTNLHKSNYPEPEDLYSAVKPSQRRGGEGYLFGGVMSLVMGLMTVVRLTKNMPRKLTEAAIYGGEVDKAETTMVSNQEYMSMVKRMAELEEKCRSLDNQPAAFSPEKEQILTAALSRVDELELQLAQTKKTLEETMATQHVIMAYIDKKKKKKKFFGF | Function: Required for transport of secretory proteins from the Golgi complex (By similarity). Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62832
Sequence Length: 548
Subcellular Location: Golgi apparatus membrane
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F4HP88 | MSGPLDRFTSPCFSNNGEKREKKSDFEVSEDEKKTRIGGILKKKSSKSKFRHSLKRRGSRSIDRTLSLTFEDIHDAEELRYVSEFRQSLISDHLLPPNLDDYHIMLRFLFARKFDLGKAKLMWTNMIQWRRDFGTDTILEDFEFPELDEVLRYYPQGYHGVDKEGRPVYIERLGKVDASKLMQVTTLERYLRYHVKEFEKTITVKFPACCIAAKRHIDSSTTILDVQGLGLKNFTKTARDLIIQLQKIDSDNYPETLHRMFIINAGSGFKLLWGTVKSFLDPKTVSKIHVLGNKYQNKLLEMIDASQLPDFFGGTCTCADQGGCMRSDKGPWKDSEILKMGRSGGTFCRHAGAFLSSDSQISSSDKPTYSLKVSDTSTAKSGSELEEMASPKTNTNNHVPKLTPVSEYANGNISPTVLSEYEECVPMVDKVVDVAWQLQEMPNASEGPQYTSSLGKIGSVRHIWSWLTAFFISFFTLLASLALPQTKEHSQLHSSSVRAELCDERIARESRPPSPPRSTITERVIISSVLSRLGDLEKQIENLHSRKSEMPHEKEELLNAAVYRVDALEAELITTKKALHEALIRQEELLGYIDRQKEAKCRRKKFCW | Function: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69280
Sequence Length: 608
Subcellular Location: Golgi apparatus membrane
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A6QT51 | MSETEKPVQAAAAAAVAAAGTADVPAVEKDPETTQDKQQSATDNSTTKAPQDEKNKQTENPSTDAPPAAATAPTADPITSAQPPDVDAIEAQKDGQKKNGPGSENKPDETPVDTRPEYLSKNPALSEFFEKLASILKKADHNEMWGVTLKDSDDVPTVNVLIKFLRANEGNVKLAEEQLRKALEWRKKMNPLALAEKATYSSSKFQGLGYVANYKDQNQGKVVFTWNIYGSVKDANRTFGDVDEFIKWRVALMEMAVKDLKLSEATSVIDYSGEDPYQMIQVHDYQNVSFLRLNPTIKSATKQTIDVFSTAYPELLKEKFFVNVPALMGWVFTALKVFLSKNTIRKFHPITNGVNLAREFSFADELPKSYGGKADELAESARTVALRQDTPEPPPESAPPAQASPPTTETNGSAKEVAKTAAEDAKKAEAPVAADAPATISEPEKPAASSANETPSEVAK | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49863
Sequence Length: 460
Subcellular Location: Cytoplasm
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Q8GXC6 | MSGSLDRFARPCFEGVSSNDERRERRSDFEVSEDEKKTRIGNFNFKKKAAKASSKLRHSLKKKGSSRRRSSDRTFSLTIEDIHDVEELRAVDEFRNLLVSENLLPPTLDDYHIMLRFLKARKFDIGKTKLMWSNMIKWRKDFGTDTIFEDFEFEEFDEVLKYYPHGYHGVDKEGRPVYIERLGLVDPAKLMQVTTVERFIRYHVREFEKTVNIKLPACCIAAKRHIDSSTTILDVQGVGFKNFSKPARDLIIQLQKIDNDNYPETLHRMFIINGGSGFKLVWATVKQFLDPKTVTKIHVIGNKYQNKLLEIIDASQLPDFLGGTCTCADRGGCMRSDKGPWNDPEILKMLQSGGPLCRHNSALNSFSRVSSCDKPSFSGIKASDTSTAESGSEVEEMASPKVNRELRVPKLTPVCEDIRGTAISYPTDSSEYDSPMVDKVVDVAWMAHEKPKASKGSEDTPDSGKIRTVTYIWRWLMMFFVNLFTLLISLALPQREGHSQSESSVDGPNARESRPPSPAFATIAERNVFSSVVNRLGDLEKQVETLHSKRHEMPREKEELLNTAVYRVDALEAELIATKKALHEALMRQDDLLAYIDREEDEKYHKKKKVCW | Function: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69956
Sequence Length: 612
Subcellular Location: Golgi apparatus membrane
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Q75BM4 | MPSDMLQFPSENDRQTFERLVSELPDLIHKRCHDYDELYGHKLLEEGPAEVAKFYSKDHAHALLFKFLKANAFSYEGAVKQLVSTLNWRREFQPLKAAFAEEHDERLMAAGYISYDASAAPNTRTVTWNLYGKLGACKDLFADQDTFIRYRVGLMERGLQALNLLDPDNCSMTQVHDYKDVSVWNMNADVKKCSRRVIAIFQDHYPELLYAKYFVNVPTILRWVYDVVRAFVSEETSRKFVVLNDGTKLAAYFAGVPAAYGGTAPATLAELPKPASRPSPYALFLLQKHISEELD | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33663
Sequence Length: 295
Subcellular Location: Cytoplasm
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Q4WEP0 | MSVTMADQQPEKTTAPASDVADSQPAVVSNTDTRKETTETAEPQSEDKTATTTAQPAVETTATQSGTAETPAEADKAPAEVQQPPQAEEEKPVAQQPEQPAYLAKNPALSQFFERLPAIVSSSGHAEMWGVPLKDSNDAPTVNVLIKFLRANEGNVKLAEEQLTKALKWRKETNPSALAESTSYSATKFGGLGYLTTYKEANGAETVVTWNIYGGVKDINTTFGDMNEFVKWRVALMELAVKELKMAEATSVIDYDGEDPYQMIQVHDYQNVSFLRLNPAIKAATKKTIEVFTTAYPELLREKFFVNVPAIMGWMFAAMKVFLSKNTTRKFHPISNGANLAREFPSLKDQFPKVYGGSAPALQEGARTVSLIQDESAPAATEQSKEQANKEEAAQEESKPESAPEQPKADPDVIVQEAPAADAK | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46170
Sequence Length: 424
Subcellular Location: Cytoplasm
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Q2UA18 | MADQQEKTASSAVPETQPPSQTAETTTQTTATPAPEVQTEQTQPTESGPSAANTTTEQPTNPPAAEASKENAAPAPAPAAEDAPSEPAPAQEQQKEEKPADNKPEYLAKNPALSQLFDRLPTVLSNSGHDEMWGVPLRDSSDVPTVNVLIKFLRANEGNVKLAEDQLTKALQWRKQTRPTALVEGRYSAKKFGGLGYLSTYKDADGKETVITWNIYGGVKDLGTTFGNVDEFINWRVALMELAVKDLKMDQATSVIDYEGEDPYQMIQVHDYLNVSFLRMNPSVKAATKKTIDVFATAYPELLREKFFVNVPSIMGWMFAAIKVFLSKNTTRKFHPISNGANLAREFPPAVKEQFPKVYGGSAPDLHEGARTVALEEDNEPAPAPAAPAEPTEEAKPEQEAPKQEPAPEAPKEEAIKEALVEAPKEEPKQPAVEEPAKTDTAVTTQETVAPAEAK | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49460
Sequence Length: 455
Subcellular Location: Cytoplasm
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A6S3N2 | MGYKNSVRKILGNIFKPKILKAKRQGAEGQLNVVQRPRSVIFLKAGVRLSRTPDTCVQNIAKERCDKVIGDKIPYGPSNQASSFAGQLGLKREKEINEEVGGWTKVVYKVEADLVEKEEEKAGLAGWDGLGFESNTKMSAEPNNNQAKADVPEEVVEPKPTTVEEPKSTTVEEPKSTTVEESKSTTVEEPKSTTAEQPKSTIEQDPKPSTTESSPVQIDDSTPIPQITTEEPKPTVAEPSTTESVTAEPTTEQPQEAAVKLESVKEADAEAAAKLEATKDADVEKAASTSQHSVSFDKATKTHDGSPLSKFYSELPAILEAAEYNEMWGIVLDPSETHVQTSIVLEKFLRANAKDVPKAKAQLIEALKWRKTMQPQKLLESTEFDKVKFGNLGYVTSYNTTEGGKEVITWNIYGAVKDVKKTFSDVPEFLKWRAALMELSIKELDLASATEKIPENGPDPYRMIQVHDYLNVSFLRMDPSIRAASKETIQTFSMAYPELLKEKFFVNVPLVMGWVFTAMKIFLSADTIKKFHPLSYGSNLGSEIPNVAEQLPKEYGGKGGELKSGLTVKYSEGEASKTA | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63764
Sequence Length: 579
Subcellular Location: Cytoplasm
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Q5AP66 | MSSSIEEVKATIKSVKLTDSQAEKLSKLIDSLPKILSGLDNPEYDEIFGYRINTKDKPYVDESIRNEILLKFLAADDYNLELSEKRLIDSLNWRNEFQPLSAAFEETFDKELNELGVITNFPNSNLKITTWNLYGNLKNPKKIFEKFGANNKVSKLPGSQFLRWRVGLMEKSLQLIDFTSTTDNRIAQVHDYNNVSMFKIDPGMKKATKEIITIFGANYPELLSTKFFINVPLIMGWVFTFFKTIRVITEATLKKFQVLNHGNLSESFNPDELPKVYGGKVEKSLFDIDVSDDIKLSEYGEVILKKVGDEEINHINDDVE | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36660
Sequence Length: 320
Subcellular Location: Cytoplasm
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Q8IWL1 | MWLCPLALTLILMAASGAACEVKDVCVGSPGIPGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF | Function: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.
PTM: N-acetylated.
Sequence Mass (Da): 26169
Sequence Length: 248
Subcellular Location: Secreted
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P23246 | MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF | Function: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA . The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator . Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity). Required for the assembly of nuclear speckles . Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 76149
Sequence Length: 707
Domain: The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation.
Subcellular Location: Nucleus speckle
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Q8VIJ6 | MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGGPKPPLPPPPPHQQQQQPPPQQPPPQQPPPHQQPPPHQPPHQQPPPPPQESKPVVPQGPGSAPGVSSAPPPAVSAPPANPPTTGAPPGPGPTPTPPPAVPSTAPGPPPPSTPSSGVSTTPPQTGGPPPPPAGGAGPGPKPGPGPGGPKGGKMPGGPKPGGGPGMGAPGGHPKPPHRGGGEPRGGRQHHAPYHQQHHQGPPPGGPGPRTEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHSQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGTMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF | Function: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (By similarity). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation . Required for the assembly of nuclear speckles (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity).
PTM: Phosphorylated on multiple serine and threonine residues during apoptosis (By similarity). Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest (By similarity). In resting T-cells is phosphorylated at Thr-679 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-679.
Sequence Mass (Da): 75442
Sequence Length: 699
Domain: The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation.
Subcellular Location: Nucleus speckle
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P39135 | MKIYGIYMDRPLSQEENERFMSFISPEKREKCRRFYHKEDAHRTLLGDVLVRSVISRQYQLDKSDIRFSTQEYGKPCIPDLPDAHFNISHSGRWVICAFDSQPIGIDIEKTKPISLEIAKRFFSKTEYSDLLAKDKDEQTDYFYHLWSMKESFIKQEGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVDPGYKMAVCAAHPDFPEDITMVSYEELL | Function: Activates the seven peptidyl carrier protein (PCP) domains of the first three subunits (SrfAA, SrfAB and SrfAC) of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis to become producers of the lipopeptide antibiotics surfactin and plipastatin B1.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 26168
Sequence Length: 224
EC: 2.7.8.7
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Q93Y07 | MELFALLIKVAGLLATVTVGANVVSYSRFRRQNLAKFRSPIDESKEVLADFNSIEHEEGKFFFGLATAPAHAEDDLDDAWLQFAKETPCSAEEAEAADKKARRKKVKLAVGAITKGLAKNTHGKEDKNAADKPPSKNVAAWHNAPHAEDRLKFWSDPDKEVKLAKDTGVTVFRMGVDWSRIMPVEPTKGIKEAVNYEAVEHYKWILKKVRSNGMKVMLTLFHHSLPPWAADYGGWKMEKTVDYFMDFTRIVVDSMYDLVDSWVTFNEPHIFTMLTYMCGSWPGNNPDFLEIATSTLPMGVFHRALHWMAVAHSKAYDYIHGKISLKKPLVGVAHHVSFMRPYGLFDIGAVTISNSLTIFPYIDSICEKLDFIGINYYGQEAVCGAGLKLVETDEYSESGRGVYPDGLYRVLLMFHERYKHLKVPFIVTENGVSDETDVIRRPYLIEHLLALYAAMLKGVPVLGYIFWTISDNWEWADGYGPKFGLVAVDRSHDLARTLRQSYHLFSKIVKSGKVTRKDRSLAWNELQKAAKAGKLRPFYRGVDNHNLMYADGLDKPQWRPFVDRDWRFGHYQMDGLQDPLSRVARTLLIWPLIMKKRIRKVKIKHTDDAGLVLHPALASPFD | Function: Glycosyl hydrolase family protein acting primarily as a highly specific galactosyltransferase . Synthesizes digalactosyldiacylglycerol from monogalactosyldiacylglycerol in the absence of UDP-galactose in vitro . Hydrolyzes o- and p-nitrophenyl beta-D-glucoside in vitro . Plays a role in freezing tolerance . May play a role in chloroplast protection .
Catalytic Activity: 2 a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70779
Sequence Length: 622
Subcellular Location: Plastid
EC: 2.4.1.184
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Q8L6H7 | MPLPAFVAAAARLAVLVAAAATAANAASYARYRRRHLRRIPSPIDESADPLADFRAFPSSDADDSEEDNFFFGLATAPAHVEDRLEDAWLQFATETSCDDNGNVRDQRPVDALMASAAGDGGSQQSWRSTGGENIGDREQRKPLRVAMEAMLRGFEILAESGESAGGDNCSHNVAAWHNVPCPQERLRFWSDPDAELKLAKETGISVFRMGVDWARLMPEEPTEELKSSVNFAALERYRWIIQRVREYGMKVMLTLFHHSLPPWAGKYGGWKMEKTVTYFMDFVRLVVDRVSNLVDYWVIFNEPHVFVMLTYCAGAWPGGDPNAIEVATSTLPTGVYNQALHWMAIAHSEAYDYIHSKSKNERKPIVGVAHHVSFTRPYGLFDVAAVALANSLTLFPYVDSICDKLDFIGINYYGQEVISGPGLKLVDNDEYSESGRGVYPDGLFRILIQFNERYKRLNIPFVITENGVSDETDLIRKPYILEHLLATYAAIIMGVRVLGYLFWTTSDNWEWADGYGPKFGLVAVDRANNLARKPRPSYFLFSRVVTTGKITRQDRMSAWRELQQAAVQKKTRPFFRAVDKHGRMYAGGLDRPIQRPFILRDWRFGHYKMEGLQDPLSCFIRCIFAPFSRQKKIHYIEDDVISYSIN | Function: Galactosyltransferase synthesizing digalactosyldiacylglycerol from monogalactosyldiacylglycerol in the absence of UDP-galactose (By similarity). Potentially involved in freezing tolerance .
Catalytic Activity: 2 a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
Sequence Mass (Da): 73271
Sequence Length: 647
Subcellular Location: Plastid
EC: 2.4.1.184
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D7AF63 | MVSLTIDGKDITVAKETTILDAAALLGITIPTLCWLKKVSPTGACRVCAVEIEGVDRPMTACNTPVKDGIKVTTQSEKLSRIRQKIMELMLVNHPLDCPVCDAGGECDLQNACYGLGAAKQEYGAVLERRKIRYDWPLIESDPNRCILCEKCVKVDHEIVGCNAIRVVNRGEATIIDTVDGNPLNCEFCGNCVAACPTGTLISKPFKFRGRPWAFTTTPSVCPFCATGCQIEYHSRNGRVERVTSDDSTYNSGNLCINGRFGYSYINSPDRLAEPMVKGQKADWNTAMGTAATALKQIVASHGADAVAGFGSPRVTNEDNYLFQKLMRSAIGTGNIDSEARLGFAATQKVLREMLGIAGASTTIDAIDRATAVLVVGCDLNAEATGMEYRVIKAATKNNAKLVLAAMRDIKLKKFANSHLKYRPGNETLLINALTKAVLEEGLENKEFCSANISNLSDLTAALAGVSIADAAAATGVTEADLRAAARLVGGKKGVAVIFGAELMRGGNTDAVKALINLALILGATAGDTGGLFPVYEKTNIRGLLDMGVAPDHFPGHQTDGTTFEKAWGKKLPAAAGKDLWQIIEGIEQGSVKALYLLGCDPVASFPEGERIRKALEKLELLIVQDPFPGEAAKMAHVVFPSSVAAEKNGTFTTIDGRVQPLAKAVAPSGDAREDWDILTELYNRLTGESRIHSPAAVLDEVAALVPAYASVGRTGGTITAQPRSGGLALAPVSARAVAGSPTTLLVGTILYHSGTTTTWSKNNLEIIPKGYIEIHPNDAAKLGIAEGGKVRLSAGSVKVEGTAKITPRVQPGLLFAPSHFRGMNVNALLSRDGGVVPVTVEKA | Function: The SfrAB enzymatic complex is probably involved in acetate metabolism and does not participate directly in the reduction of Fe(3+) chelates. May serve as a major route for NADP regeneration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89387
Sequence Length: 844
Subcellular Location: Cell inner membrane
EC: 1.-.-.-
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D7AF64 | MAQVVFSSWGRTIVDNRKGGEAQDVSFRLPTTLDGERQIAAFMGWDGIILYDLKVDVPAMAAEYMKRVQTQYCCGKCTPGKKGTKVLADVLAAIIEGRATEADLDTIDDLADLLTNCKCTLCQSSTIPVLDAVKHFREDFLAYITGIRKPANVHRFIDKYTAPCMDRCPAHIDIPAYIEAIKEYRFDESLDIIRDNMPLPSVCGRVCPHPCETHCRRKNVDDSVNIMVLKRSASDYEWMHNAAPPMQPKPQKNKKVAIVGAGPAGLACAYYLALEGYPCTIYEALPEGYGGGMIAVGIPPYRQPRHLLQRDIDIISSMGVDIIYDTRIGKDISLEELKQKFDAVFLAPGAHRSKPMGVEGEDKGYKGFLKGGIDFLREAYMGRPTGMGKKVVVVGGGNTAIDCVRVALREGAEESTLLYRRSRKEMPADVWEVDGADEEGVRFEFQVLPTRVLVDENEQVTGVECVRMALGEPDASGRRRPEPVPGSEFVVECDTVIPAIGQDPDLSFIPDNLGIDITKWNTVVTKYVPLKDAAGKDLKDGMGNPLARVLITDLEGVFAGGDAEIGPLTVVACIGNAHRAARVIQRWLEEGKAYLTEDELMEDILTNMPVYDKNEKVPWLDSRERAHQAEVHGQERASKGNYQEVELGFVDTQAVEEAERCLRCYRVAMAAI | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Probably involved in acetate metabolism and not in the reduction of Fe(3+) chelates. May serve as a major route for NADP regeneration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74273
Sequence Length: 672
Subcellular Location: Cell membrane
EC: 1.-.-.-
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P37678 | MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALSDIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWGGARA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L-gulonate.
Catalytic Activity: 3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-phosphate
Sequence Mass (Da): 23445
Sequence Length: 220
EC: 4.1.1.85
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P44988 | MGKPLLQIALDAQYLETALVDVKQIEHNIDIIEVGTILACSEGMRAVRILRALYPNQILVCDLKTTDAGATLAKMAFEAGADWLTVSAAAHPATKAACQKVAEEFNKIQPNLGVPKEIQIELYGNWNFDEVKNWLQLGIKQAIYHRSRDAELSGLSWSNQDIENIEKLDSLGIELSITGGITPDDLHLFKNTKNLKAFIAGRALVGKSGREIAEQLKQKIGQFWI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P.
Catalytic Activity: 3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-phosphate
Sequence Mass (Da): 24867
Sequence Length: 225
EC: 4.1.1.85
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P37679 | MRNHQLGIYEKALAKDLSWPERLVLAKSCGFDFVEMSVDETDERLSRLDWSAAQRTSLVAAMIETGVGIPSMCLSAHRRFPFGSRDEAVRERAREIMSKAIRLARDLGIRTIQLAGYDVYYEDHDEGTRQRFAEGLAWAVEQAAASQVMLAVEIMDTAFMNSISKWKKWDEMLASPWFTVYPDVGNLSAWGNDVPAELKLGIDRIAAIHLKDTQPVTGQSPGQFRDVPFGEGCVDFVGIFKTLHKLNYRGSFLIEMWTEKAKEPVLEIIQARRWIEARMQEAGFIC | Function: Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate (Potential). May be involved in the utilization of 2,3-diketo-L-gulonate.
Catalytic Activity: L-ribulose 5-phosphate = L-xylulose 5-phosphate
Sequence Mass (Da): 32455
Sequence Length: 286
EC: 5.1.3.22
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P39363 | MINDIKWVQAQRKATDWRQAVEIATRPLVAYGAAQPCYVNGIIENTLNWGPYYLIAPGIALPHARPEQGANYNQVSITTLRTPVAFGNEECDPVWLLLCVSATDANAHILTIQRISQFIDSPQRLTAVGNASTDDALFALVSG | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
Sequence Mass (Da): 15638
Sequence Length: 143
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Subcellular Location: Cytoplasm
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Q16586 | MAETLFWTPLLVVLLAGLGDTEAQQTTLHPLVGRVFVHTLDHETFLSLPEHVAVPPAVHITYHAHLQGHPDLPRWLRYTQRSPHHPGFLYGSATPEDRGLQVIEVTAYNRDSFDTTRQRLVLEIGDPEGPLLPYQAEFLVRSHDAEEVLPSTPASRFLSALGGLWEPGELQLLNVTSALDRGGRVPLPIEGRKEGVYIKVGSASPFSTCLKMVASPDSHARCAQGQPPLLSCYDTLAPHFRVDWCNVTLVDKSVPEPADEVPTPGDGILEHDPFFCPPTEAPDRDFLVDALVTLLVPLLVALLLTLLLAYVMCCRREGRLKRDLATSDIQMVHHCTIHGNTEELRQMAASREVPRPLSTLPMFNVHTGERLPPRVDSAQVPLILDQH | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42875
Sequence Length: 387
Subcellular Location: Cell membrane
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P82350 | MAAAVTWIPLLAGLLAGLRDTKAQQTTLHLLVGRVFVHPLEHATFLRLPEHVAVPPTVRLTYHAHLQGHPDLPRWLHYTQRSPYNPGFLYGSPTPEDRGYQVIEVTAYNRDSFDTTRQRLLLLIGDPEGPRLPYQAEFLVRSHDVEEVLPTTPANRFLTALGGLWEPGELQLLNITSALDRGGRVPLPIEGRKEGVYIKVGSATPFSTCLKMVASPDSYARCAQGQPPLLSCYDTLAPHFRVDWCNVSLVDKSVPEPLDEVPTPGDGILEHDPFFCPPTEATDRDFLTDALVTLLVPLLVALLLTLLLAYIMCFRREGRLKRDMATSDIQMFHHCSIHGNTEELRQMAASREVPRPLSTLPMFNVRTGERLPPRVDSAQMPLILDQH | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43287
Sequence Length: 387
Subcellular Location: Cell membrane
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P58035 | MKKILVACGTGMSTSTMIAHKLQEFLTEQGISATTAQCCLNEIPLNCNGMDLIVTSMRTNSDYGIPTLNGAALLTGINDDALKQQIKALLTQ | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
Sequence Mass (Da): 9803
Sequence Length: 92
Domain: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Subcellular Location: Cytoplasm
EC: 2.7.1.-
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Q16585 | MAAAAAAAAEQQSSNGPVKKSMREKAVERRSVNKEHNSNFKAGYIPIDEDRLHKTGLRGRKGNLAICVIILLFILAVINLIITLVIWAVIRIGPNGCDSMEFHESGLLRFKQVSDMGVIHPLYKSTVGGRRNENLVITGNNQPIVFQQGTTKLSVENNKTSITSDIGMQFFDPRTQNILFSTDYETHEFHLPSGVKSLNVQKASTERITSNATSDLNIKVDGRAIVRGNEGVFIMGKTIEFHMGGNMELKAENSIILNGSVMVSTTRLPSSSSGDQLGSGDWVRYKLCMCADGTLFKVQVTSQNMGCQISDNPCGNTH | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: Disulfide bonds are present.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34777
Sequence Length: 318
Subcellular Location: Cell membrane
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Q60538 | MAAAAAAAAATEQQSSNGPVKKSMREKAVERRNVNKEHNSNFKAGYIPIDEDRLHKTGLRGRKGNLAICVIVLLFILAVINLLITLVIWAVIRIGPNGCDSMEFHESGLLRFKQVSDMGVIHPLYKSTVGGRRNENLVITGNNQPIVFQQGTTKLSVEKNKTSITSDIGMQFFDPRTQNILFSTDYETHEFHLPSGVKSLNVQKASTERITSNATSDLNIKVDGRAIVRGNEGVFIMGKTIEFHMGGNVELKAENSIILNGTVMVSPTRLPSSSSGDQSGGGDWVRYKLCMCADGTLFKVQVTGHNMGCQVADNPCGNTH | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: Disulfide bonds are present.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34847
Sequence Length: 320
Subcellular Location: Cell membrane
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P39365 | MFDYILSLGGTVFVPIIMIVIGLIFRIPWLQAIKAGVTVGIGFVGMGLVIVMAIDSLSPPIKVMIERFGLALHVFDVGAGPASGVGYATAIGAMIIPVIFLLNVAMLVTRLTKTMNVDIYNYWHYAITGTVVQLMTGSLIYGVLGAICHAALSLKMADWTAKRVQNIVGLEGISIPQGYGSSSVPLFVLLDAIYEKIPFMKGRNIDAQEIQKRYGMVGDPVIIGVVLGLIFGLAAGEGFKGCASLMITVAAIMVLFPRMIRLIVEGLLPISDGARKFFQKYFKGREVYIGLDTAVTLGHPTTIAVGLLLIPIMLILASILPGNKVLPLADLPVAPFFICMATVIHRGDLVRTLISGVIVMITVLLIATQFAPYFTEMALKGGFSFAGESAQISALSVGNMFGWSISELMSLGIIGVVVAVGIVASVVLFLRKRELSE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46684
Sequence Length: 437
Domain: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
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Q8GMG6 | MPHGAEREASPAEESAGTRPLTGEEYLESLRDAREVYLDGSRVKDVTAHPAFHNPARMTARLYDSLHDPAQKAVLTAPTDAGDGFTHRFFTAPRSVDDLVKDQAAIASWARKSYGWMGRSPDYKASFLGTLGANADFYEPFADNARRWYRESQEKVLYWNHAFLHPPVDRSLPADEVGDVFIHVERETDAGLVVSGAKVVATGSALTHAAFISHWGLPIKDRKFALVATVPMDADGLKVICRPSYSANAATTGSPFDNPLSSRLDENDAILVLDQVLIPWENVFVYGNLGKVHLLAGQSGMIERATFHGCTRLAVKLEFIAGLLAKALDITGAKDFRGVQTRLGEVLAWRNLFWSLSDAAARNPVPWKNGTLLPNPQAGMAYRWFMQIGYPRVLEIVQQDVASGLMYVNSSTEDFRNPETGPYLEKYLRGSDGAGAVERVKVMKLLWDAVGSDFGGRHELYERNYSGNHENTRIELLLSQTASGKLDSYMDFAQACMDEYDLDGWTAPDLESFHAMRSASRDLLGGL | Function: Oxygenase component of a two-component system involved in the biosynthesis of the enediyne antitumor antibiotic C-1027 . Uses FADH(2) supplied by SgcE6 to catalyze the C-5 hydroxylation of (S)-3-chloro-beta-tyrosyl-S-SgcC2 . Can also efficiently catalyze the regioselective hydroxylation of other 3-substituted beta-tyrosyl-S-SgcC2 analogs, including the bromo-, iodo-, fluoro-, and methyl-substituted analogs, but does not accept 3-hydroxy-beta-tyrosyl-S-SgcC2 as a substrate . Is only active with SgcC2 (peptidyl carrier protein)-tethered substrates .
Catalytic Activity: (3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[SgcC2 peptidyl-carrier protein] + FADH2 + O2 = (3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[SgcC2 peptidyl-carrier protein] + FAD + H(+) + H2O
Sequence Mass (Da): 58255
Sequence Length: 527
Pathway: Antibiotic biosynthesis.
EC: 1.14.14.15
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D4Q9Z4 | MEKKKGELKSIFLPFLSTSHIIPLVDMARLFALHDVDVTIITTAHNATVFQKSIDLDASRGRPIRTHVVNFPAAQVGLPVGIEAFNVDTPREMTPRIYMGLSLLQQVFEKLFHDLQPDFIVTDMFHPWSVDAAAKLGIPRIMFHGASYLARSAAHSVEQYAPHLEAKFDTDKFVLPGLPDNLEMTRLQLPDWLRSPNQYTELMRTIKQSEKKSYGSLFNSFYDLESAYYEHYKSIMGTKSWGIGPVSLWANQDAQDKAARGYAKEEEEKEGWLKWLNSKAESSVLYVSFGSINKFPYSQLVEIARALEDSGHDFIWVVRKNDGGEGDNFLEEFEKRMKESNKGYLIWGWAPQLLILENPAIGGLVTHCGWNTVVESVNAGLPMATWPLFAEHFFNEKLVVDVLKIGVPVGAKEWRNWNEFGSEVVKREEIGNAIASLMSEEEEDGGMRKRAKELSVAAKSAIKVGGSSHNNMKELIRELKEIKLSKEAQETAPNP | Function: Glycosyltransferase that transfers a galactosyl group from UDP-galactose to soyasapogenol B monoglucuronide in the biosynthetic pathway for soyasaponins.
Catalytic Activity: soyasapogenol B 3-O-beta-D-glucuronate + UDP-alpha-D-galactose = H(+) + soyasaponin III + UDP
Sequence Mass (Da): 55866
Sequence Length: 495
EC: 2.4.1.272
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D4Q9Z5 | MDSVALNGKSNDKPLHVAMLPWLAMGHIYPYFEVAKILAQKGHFVTFINSPKNIDRMPKTPKHLEPFIKLVKLPLPKIEHLPEGAESTMDIPSKKNCFLKKAYEGLQYAVSKLLKTSNPDWVLYDFAAAWVIPIAKSYNIPCAHYNITPAFNKVFFDPPKDKMKDYSLASICGPPTWLPFTTTIHIRPYEFLRAYEGTKDEETGERASFDLNKAYSSCDLFLLRTSRELEGDWLDYLAGNYKVPVVPVGLLPPSMQIRDVEEEDNNPDWVRIKDWLDTQESSSVVYIGFGSELKLSQEDLTELAHGIELSNLPFFWALKNLKEGVLELPEGFEERTKERGIVWKTWAPQLKILAHGAIGGCMSHCGSGSVIEKVHFGHVLVTLPYLLDQCLFSRVLEEKQVAVEVPRSEKDGSFTRVDVAKTLRFAIVDEEGSALRENAKEMGKVFSSEELHNKYIQDFIDALQKYRIPSAS | Function: Glycosyltransferase that transfers a rhamnosyl group from UDP-rhamnose to soyasaponin III in the biosynthetic pathway for soyasaponins.
Catalytic Activity: soyasaponin III + UDP-beta-L-rhamnose = H(+) + soyasaponin I + UDP
Sequence Mass (Da): 53518
Sequence Length: 472
EC: 2.4.1.273
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O43765 | MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE | Function: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails . Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module . Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins . It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states . Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex . Binds directly to HSC70 and HSP70 and regulates their ATPase activity .
Sequence Mass (Da): 34063
Sequence Length: 313
Domain: The second tetratricopeptide repeat (TPR 2) mediates the interaction with SARS-CoV accessory protein 7a.
Subcellular Location: Cytoplasm
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P44774 | MINKDTQLCMSLSGRPSNFGTTFHNYLYDKLGLNFIYKAFTTQDIEHAIKGVRALGIRGCAVSMPFKETCMPFLDEIHPSAQAIESVNTIVNDNGFLRAYNTDYIAIVKLIEKYHLNKNAKVIVHGSGGMAKAVVAAFKNSGFEKLKIYARNVKTGQYLAALYGYAYINSLENQQADILVNVTSIGMKGGKEEMDLAFPKAFIDNASVAFDVVAMPVETPFIRYAQARGKQTISGAAVIVLQAVEQFELYTHQRPSDELIAEAAAFARTKF | Function: In vitro, is able to catalyze the NADP(+)-dependent oxidation of shikimate to 3-dehydroshikimate. However, has much lower activity than classical shikimate dehydrogenases AroE, indicating that shikimate may not be the biological substrate. Cannot utilize NAD(+) instead of NADP(+). Is not able to catalyze the oxidation of quinate.
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29932
Sequence Length: 271
EC: 1.1.1.25
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A0A509AQU3 | MIFKKALYILLFLYIAIVKKGESKPGSKHPFLFKNLVIDKKKLDSSYYNKYDNIKWNGKIIAIGDIHGDIESLKLILRHSKLIGENDNWIGDNVLLVQNGDVFDRGIYGPIIYNFLFKLQKEAIKKNSRVILIMGNHEQLNLCGYFNYVNPKEIEMFFHNDANYRYHSFVNPYGEYHKRLIRLPPMVKVNNIIFTHGGLNLLISKLSINDINLKTRLQIENNCKPIKYDSFQNYLSRDGVLWSDAMSRNVPYYEKEKCSELFQILDKYDAKYLVVGHTRQPSHQIGSYCNNHYFLIDTGMSLFTNYGQPYPNYLKIDDHKIKAVRLIVEKKKKCPHTEIQLNTPNKIKYCVQESQTNLNPVL | Cofactor: Binds 2 manganese ions per subunit.
Function: Phosphatase which plays an essential role in the development and differentiation of the ookinete and in the formation of ookinete micronemes.
Sequence Mass (Da): 42358
Sequence Length: 362
EC: 3.1.-.-
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D6PVB5 | MDYNNNRYGGGGGAGSKFNLGHIVGDPFSLATIAIATAGWLIAFVSSIIANIDQEYPNYSWWALAYMFFVILGVTLAVAANAVYTYHVAMVGFLAAGLVFTTSSVNSLIYWSDKAKQAAAAGFILLSMVSIVWIFYFGSQPTASHRQTIDSFALHKDHAPSRASRHMTQSYRPETTHSAQHPQMYNSSQLAGFETSSPVTGYPGGAAGATTKRESASAFPQPGQGGNFPNNQQPITSHTQQQQQQSQDLTSPAATAHPPTEYPYRAKAIYSYEANPDDANEISFHKHEILEVSDVSGRWWQAKKENGETGIAPSNYLILL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34771
Sequence Length: 320
Subcellular Location: Cell membrane
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Q751J2 | MTLRATKARQQRVSPHIGHTFSFGNLVGDPFAISTLSISTIAWLITLGGGIATKKMPHFSWWGIAFQFVMMVCFVVIYLWDLVDYYRGFLAAGVGVAFVYSTNSCSQLIYQEEPQQAAGSAGFMMLSIVNMIWMFYFGADNAAPANRWIDSFSIRGIRASQVESSLALARSQKAVASPQPAATAFYGGLEGHSQKYVSSTALNGFENTDPHTSTAFALGPEGPTQRNLDTHGTSTYVTDTTNGNTETTMGDTLGLYSDMGDELVNFPYTAKALYAYEADASDAYEISFQQGEILRVGDIEGRWWKAKKANGETGIIPSNYVELVDDPAAL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35963
Sequence Length: 330
Subcellular Location: Cell membrane
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Q9CZN4 | MRRVLRLLLGCFLTELCARMCRAQERSGHGQLAQLGGVLLLTGGNRSGAASGEAGEGVGGSDAPPTRAPTPDSCRGYFDVMGQWDPPFNCSSGDFIFCCGTCGFRFCCTFKKRRLNQSTCTNYDTPLWLNTGKPPARKDDPLHDPTKDKTNLIVYIICGVVAVMVLVGIFTKLGLEKAHRPQREHMSRALADVMRPQGHCNTDHMERDLNIVVHVQHYENMDSRTPINNLHTTQMNNAVPTSPLLQQMGHPHSYPNLGQISNPYEQQPPGKELNKYASLKAVGNSDGDWAVATLKSPKADKVNDDFYAKRRHLAELAVKGNLPLHPVRVEDEPRAFSPEHGPAQQNGQKSRTNKMPPHPLAYNSTANFKTWDPSDQSLRRQAYGNKGKLGIAESGSCDPLGTRTQHFPPTQPYFITNSKTEVTV | Function: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46842
Sequence Length: 424
Domain: The extracellular domain contains a pattern of cysteine similar to the snail conotoxin Con-ikot-ikot (AC P0CB20), a toxin known to disrupt AMPA receptors (ionotropic glutamate receptor) desensitization.
Subcellular Location: Cell projection
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Q92340 | MISLKIYFVLIFLFLKGINSAYVSNEEGETVDFTFSGFYANLTYPNEISELNYVEGNYLSTRIVRFNGSFYCDTTILSETNNVTGSCYVANCANDTVLEICDSGKEVHFTDMSGTTWSADTFTENLYWFCGGDGNKPNMTTAAAMNSDIDSYYVYGNWTIDTADSTVADYTCNYTHFQEAGDIEKGDVYTASADSSDSSSASSTIFKPSYFISCLLSVGLYLVLNF | Function: High affinity heme transporter involved in the assimilation of exogenous heme during conditions of low cellular iron.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25022
Sequence Length: 226
Subcellular Location: Cell membrane
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Q8NDV1 | MACILKRKSVIAVSFIAAFLFLLVVRLVNEVNFPLLLNCFGQPGTKWIPFSYTYRRPLRTHYGYINVKTQEPLQLDCDLCAIVSNSGQMVGQKVGNEIDRSSCIWRMNNAPTKGYEEDVGRMTMIRVVSHTSVPLLLKNPDYFFKEANTTIYVIWGPFRNMRKDGNGIVYNMLKKTVGIYPNAQIYVTTEKRMSYCDGVFKKETGKDRVQSGSYLSTGWFTFLLAMDACYGIHVYGMINDTYCKTEGYRKVPYHYYEQGRDECDEYFLHEHAPYGGHRFITEKKVFAKWAKKHRIIFTHPNWTLS | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b . GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity .
Catalytic Activity: an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35395
Sequence Length: 305
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.7
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Q9WUV2 | MACILKRKPVLVVSFIALCILLLAMRLVNDATFPLLLNCFGQPKTKWIPLPYTFRQPLRTHYGYINVRTQEPLQLNCNHCAIVSNSGQMVGQKVGEEIDHASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASRTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQQMTHCDRVFKDETGKDRVQSGSYLSTGWFTFILAMDACYSIHVYGMINETYCKTEGYRKVPYHYYEQGKDECNEYLLHEHAPYGGHRFITEKKVFAKWAKKHRIVFTHPNWTLS | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b . GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (By similarity).
Catalytic Activity: an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35414
Sequence Length: 305
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.7
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Q9H4F1 | MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYSSVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRSTLRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCREKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRTE | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. Prefers O-glycans to glycoproteins or glycolipids.
Catalytic Activity: an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34201
Sequence Length: 302
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.7
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Q9R2B6 | MEHVVTCWRLKLLSWPVFLIWICLSLASVSLISWDQLPAFLIPSTGDSSLQTAKSRDSMKAPGRLLLLTLCILTFSAVCVFLCCWACLPLCLATCLDRHLPAAPRSTVPGPLHFSGYSSVPDGKPLIRELCHSCAVVSNSGQMLGSGLGAQIDGAECVLRMNQAPTVGFEEDVGQRTTLRVISHTSVPLLLRNYSHYFQHARDTLYVVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMIPALELCEEIVVYGMVSDSYCSEKSPRSVPYHYFEKGRLDECQMYRLHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRAK | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains . Prefers O-glycans to glycoproteins or glycolipids .
Catalytic Activity: an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40773
Sequence Length: 360
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.3.7
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Q9BVH7 | MKTLMRHGLAVCLALTTMCTSLLLVYSSLGGQKERPPQQQQQQQQQQQQASATGSSQPAAESSTQQRPGVPAGPRPLDGYLGVADHKPLKMHCRDCALVTSSGHLLHSRQGSQIDQTECVIRMNDAPTRGYGRDVGNRTSLRVIAHSSIQRILRNRHDLLNVSQGTVFIFWGPSSYMRRDGKGQVYNNLHLLSQVLPRLKAFMITRHKMLQFDELFKQETGKDRKISNTWLSTGWFTMTIALELCDRINVYGMVPPDFCRDPNHPSVPYHYYEPFGPDECTMYLSHERGRKGSHHRFITEKRVFKNWARTFNIHFFQPDWKPESLAINHPENKPVF | Function: Predominantly catalyzes the biosynthesis of ganglioside GD1alpha from GM1b in the brain, by transferring the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b . GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Also shows activity towards sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine) generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen .
Catalytic Activity: CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) = a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38443
Sequence Length: 336
Pathway: Glycolipid biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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Q9QYJ1 | MKTLMRHGLAVCLVLTTMCTSLLLVYSSLGSQKERPPQQQQQQQQQQQQAATATGSTQLVESSPQPRRTAPAGPRQLEGYLGVADHKPLKMHCKDCALVTSSGHLLRSQQGPHIDQTECVIRMNDAPTRGYGLDVGNRTSLRVIAHSSIQRILRNRHDLLNVSQGTVFIFWGPSSYMRRDGKGQAYNNLQLLSQVLPRLKAFMITRHRMLQFDELFKQETGKDRKISNTWLSTGWFTMTIALELCDRIDVYGMVPPDFCRDPKHPSVPYHYYEPSGPDECTMYLSHERGRKGSHHRFITEKRVFKNWARTFNIHFFQPDWKPESPAVNHAEGKPVF | Function: Predominantly catalyzes the biosynthesis of ganglioside GD1alpha from GM1b in the brain, by transferring the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b . GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis . Also shows activity towards sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine) generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (By similarity).
Catalytic Activity: CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) = a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38430
Sequence Length: 336
Pathway: Glycolipid biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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Q08E15 | MACPRPLSQCDHTPLPGPPAGHWPLPLSRRRREMKSNKEQRSAVFVILFALITILILYSSSSANEVFHYGSLRGRTRRPVNLRKWSITDGYIPILGNKTLPSRCGQCVIVTSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTFRVVAHSSVFHVLRRPQEFVNRTPETVFIFWGPPNKMQKPQGSLVRVIQRAGLVFPNMEAYAISLSRMRQFDDLFRSETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPDYCSLRPHLQRMPYHYYEPKGPDECVTYIQNENSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (By similarity). Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity).
Catalytic Activity: CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) = a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38034
Sequence Length: 332
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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