ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q37143 | MKQPTTNKLRFTITLVILFLARVGIFIPISGIDHQTFNNTIQQNGIINFLNIFAGGGFSTIGIFALGIVPYIYASIIIQLLIKLIPYLENLQKEEGEIGRQKINQLTRYLTLLWALIQSLSIAIWINHMYLIHLFELCASLTTSSMIAMWFSEIISEYGVGNGPSLLIFQNIISSIPKNLQNYTFNIGTTNTVLNGSLILSFGIIILIINILIQEGERKIAILSAKQLGKINELNHKVIFLLKLNQGGVMPFVFASAVVHTFLFISNNTNSKITQFINLFLPNQFLYLPLYLIFIITFSYVYTSLILNPEDIAKNLKKMG... | 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 compose... |
O66491 | MSEYLKALFELKELRQKFIFTLLMFVIYRLGSHIPIPGINPEALRDFLKAFEGSVFALYDIFSGGNLGRLTVFALGVMPYISASIMMQLLTVAIPSLQRLAKEEGDYGRYKINEYTKYLTLFVATVQSLGIAFWIRGQVSPKGIPVVENPGISFILITVLTLVAGTMFLVWIADRITEKGIGNGASLIIFAGIVANFPNAVIQFYEKVKTGDIGPLTLLLIIALIIAIIVGIVYVQEAERRIPIQYPGRQVGRQLYAGRKTYLPIKINPAGVIPIIFAQALLLIPSTLLNFVQNPFIKVIADMFQPGAIFYNFLYVTFIV... | 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 compos... |
P16336 | MFKTISNFMRVSDIRNKIIFTLLMLIVFRIGAFIPVPYVNAEALQAQSQMGVFDLLNTFGGGALYQFSIFAMGITPYITASIIIQLLQMDVVPKFTEWSKQGEVGRRKLAQFTRYFTIVLGFIQALGMSYGFNNLANGMLIEKSGVSTYLIIALVLTGGTAFLMWLGEQITSHGVGNGISIIIFAGIVSSIPKTIGQIYETQFVGSNDQLFIHIVKVALLVIAILAVIVGVIFIQQAVRKIAIQYAKGTGRSPAGGGQSTHLPLKVNPAGVIPVIFAVAFLITPRTIASFFGTNDVTKWIQNNFDNTHPVGMAIYVALII... | 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 compos... |
O51451 | MKELFLSLFTVKDLRNKFLFTLFVLFLFRVGSYLPIPGIDSVALKSYFKSQSDFSIANYFDFFSGGAFSNFSIFMLSIGPYISASIIVQLLVYSFPSLKKMQEGDGGRQKTKKYTKYLTIVAAVVQGYATSLYAKGIPGAVTIPFYRYIFVAILTVTTGTFILLWFGEQINQRGVGNGTSLIIFSGIVVRLQAALFNLFQSMQDPSQNVNPVFVILIISIFILVVILIIYEYKAQMRIAIHYARANSNNTVSSYLPIKLNPSGVLPVIFASVLITLPLQILSGFAETSSIARQILSYLRPNGFYYTFLNVILIIGFTYFY... | 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 compos... |
P28539 | MATLRQVFSISELRQKIFFTFSLLALCRIGVFIPVPGINGDRAVAYFNQLLGSSQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLLVVFMPTLQREMRESPDQGKRKLGRMTRLFTLVLACVQSLLFAKFALRMNLVVPGIVLPAMLSLKLFGVPWVFYLTTVVVMITGTLLLMWVGEQISDKGIGNGISLIITLGILASFPSVLGSIFNKLNLGSQDPSEFGIVSLLILCAVFVFVLMATVLIIEGMRKIPVQHARRIIGRREVVGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFLSSESSWLKRIATM... | 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 compos... |
P46249 | MRPENNLRLRLFQTMKFIALERLGLFVPIPGIDQKLFSSDYSNNAISNLLNVFDNNQAPKLSVFALGIIPYINATITIQILSSAFPALKKLQSEEGEIGKKKLNKITKYLSFCFAFIESLAIVLRLQKYAFDWNLYFIVQTTLILISGAMLVMWLADNISYKGIGTGASVIIFVNIASAFAKFLLNQLFVHSIKFLDFASYFALIVFSIACIVFVQEAIRKVPIISAKQLDSTSFYSNDYFLPLRINQGGVMPIILASSLLALVDYVIRYGLSTLQAVYFINDILPFKILFLLLYSAFIIFFNYLYCSLVLNCFELSNNL... | 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 compose... |
Q85FU6 | MQDNWPTRLAITCLLVAIERLGMYIPVGLISNPQANWLNGGGWFVLGIIPTINASIVMQILISIVPALTRLQKEEGEMGQKQIQKYTRYLTFFLAGIQAFTLSQQWCTWLLIVSGAMLVMWLAEQMTHKGIGNGTSIFVCSNIAANFLHHPIEAPWSLAMVVLIFTMLGMIALQEAVRAIPILSAKQLIQSIAQVYLLPMRLNQGGVMPIIFASSTLALLHTWSIWWLYVACIIFFSHFYNLVIANPKELSENLNKMAVVIPSIRPGAETQQYLNRTLNRMSWIGGIALSLIALLPWLFSSLKIFSGFGATSLLIVIGVS... | 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 resid... |
P25014 | MLSRLIISIFIIFETIYLQIFKPVNKTFKQGEAKLKRTLQTLQSRELSEIRKRAISTLCLIFLIRIGTFLPIPGTALNFDLESFQQNNSRNELANILNLLSGGAFLEIGFFTLGILPYMNASFFLQVLTKILPSLERFQKEQEEIAQREFKKWTRYLTVIWAFIQSIVISWIWIRPYALNWDFFLGLKVVVALTLGAVIVMIIAEQITEIGLTNGSSLLIFINIIARIPNSIEQLFNSNINWTFPMISSLILSLSLSFITMFVIIGLQESGRPVPVLIARQEAERQKFNEPITEAERRKTQAYIFFQLLPAGIMPVIFAS... | 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 compose... |
P28540 | MKKAFVLEGPLVLRLFRTIMILIFARLGNYIPIPGITEVESFYESSFRNTSIYNLSALSGGSNVISILTLGLGPFFSASLAVQFLVKLYPAFEKLQNEEGEEGRKTIVRYTRILTVLFCIIESFFLSNSLRSFVFNWNSISYFVVAAAVTTGSLVLVWLSEVITERGIGNGSSLLILIGNLSRFRFLINKDDFDSLNVSSQSNLYIIYIIITLVSMLIFSTLSQEGARKIPVVSAKQLIDGVEDDMRRSYIPIRFGQAGVVPIIFSSSILLFLTTSIKQLPNANIATRVILDSVNLQQIFYFFTFLVLIIFFSFFYTLII... | 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 compose... |
Q7MY02 | MTHKPCLLYSQLPAIDRLLREPQITPLVEQYGQTLVTATLRRMQEQARINIKQYQALPDWCDNWASALGQQLEQKQALALKPVFNLSGTVIHTNLGRALMAESAIEAVTQVMRSPVTLEYSLNNAERGHRDHALADLLCELTGAEDACIVNNNAAAVLLLLATVASGKQVVVSRGELVEIGGAFRIPDVMVQAGCRLVEVGTTNRTHLKDYRQAINEETALLMKVHTSNYNIDGFTAEVSGRELATLGIASQIPTAIDLGSGSMINMVQYGLPAEPMPQDYLNQGIDLVTFSGDKLLGGPQAGIILGKKHWIEAIQRHPL... | 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)... |
Q73JP8 | MSCSLINEDFDLLKAAKNPGUGAKLSAGALDKLLKNFSVRNDDNLLVGFNTSDDAAVYKINDKTALISTIDFFPPVSGDPYIFGQVAAANSLSDIYAMGGEPKLALNLFCITKDMPEDMIKEILRGGFDKVYEAGAIVCGGHTIYDDSPKYGLAVNGFVHPKKILENSTAKEGDVLILTKPIGTGILLTASKADMSPPEELDRCYKIMAFLNAKARNIMVKYKINACTDITGFGLLGHLYEMGKGSGMSIEVDYKSVPIYKSVIESAEMGMMPAGVYSNRNFVGDNIVFENVPLAYQDLMFDPQTSGGLLISVDKEDAAA... | 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 | MTNKKIKLTQTVKAAGUAAKLGPEGLADALAGLNRPADPRLIVGPETSDDGGVYCLTPEIALIESCDVITPPADAPRAFGRIAAANALSDIYAMGGRPLTAMNLAFFPACSLQPEVLGEVLAGGQDALNEAGCCLVGGHTVEDDELKYGLSVTGTVHPEQVLRNSTARPGDCLLLTKPLGSGILSTAVKGEMATVEQEAEAVAWMSLLNRAAAELMLRYTPSACTDITGFGLIGHSCEMALGSGVTIRLYLDAVPLMQGVTDQVADGMVPAGCYRNRSYYLSRIDAGDCDPERLLPLFDPQTSGGLLIALQPGAAALFQA... | 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 | MASPAIRLTQYSHGAGCGCKISPKVLDKILHTEQQKFFDPRLLVGNETRDDAAVYDIGNGVGIISTTDFFMPIVDDPFDFGRIAATNAISDVYAMGGKPIMAIAILGWPIDKLAPEIAQQVIEGGRYVCQQAGISLAGGHSIDAPEPILGLAVTGIVSTEQVKKNSAAKPGCKLFLTKPLGIGILTTAEKKSKLRPEHRGLATETMCQLNKPGADFAHIPGVTAMTDVTGFGLLGHLSEICQGSGVQAILHYSAIPRLPAVEDYIAEGCVPGGTGRNFDSYGHLIGNMSDLQKQLLCDPQTSGGLLLAVLPDAEADVQAI... | 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... |
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 invol... |
Q5LQK9 | MTIAIPFDNSYARLPGGFYTAQAPQPVRAPRLVAFNADLARLLGIAPGEVEEMAQVFAGNAVPQGAEPLAQLYSGHQFGNYNPQLGDGRAILLGEVLGSDGIRRDIQLKGAGRTPYSRGGDGRAWLGPVLREYVVSEAMAALGIPTTRALAAVETGETVRRESALPGAVLTRVAQSHLRVGTFQVFAARGEIAHLKRLTDYAIARHYPDAQGPMGLLAAVRDAQARLIARWMGVGFIHGVMNTDNSSIAGETIDYGPCAFMDTYHPDTVYSSIDRYGRYAYSNQPDIAVWNLAQLATALIQQAEDKEAVVEEATEIVHAM... | 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 | MLEHLKFDNSFDKLGSDFATRVNPRPLVNPKLVCVDSKTCELLGISKDSVSSENGVNMFSGNRVPPQFAPLAMVYAGHQFGGYSSQLGDGRGLLLGELNTHSGKYDLHLKGAGKTPYSRFGDGYAVLRSCIREYLAGIAMRGLGIPTSHALCVVRGDNAVTRETIEPAATLTRVARSHIRFGSFEYFYYTQQHTQLEQLADYAVEQYIPEYVDKDGRFNALLHYTTEQTAKLIAAWQAVGFCHGVMNTDNMSIIGETLDYGPYGFMEAYNPTHICNHSDTYGRYAYDQQPSIGLWNLNALAAALSPLIDRDQARASLESY... | 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 | MTLSFTARWRDELPATYTALLPTPLKNARLIWYNDELAQQLAIPASLFDATNGAGVWGGETLLPGMSPVAQVYSGHQFGVWAGQLGDGRGILLGEQLLADGSTLDWHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMHYLGIPTTRALSIVTSDTPVQRETQETGAMLMRLAQSHMRFGHFEHFYYRREPEKVQQLADFAIRHYWPQWQDVPEKYALWFEEVAARTGRLIAEWQTVGFAHGVMNTDNMSILGLTIDYGPFGFLDDYDPGFIGNHSDHQGRYRFDNQPSVALWNLQRLAQTLTPFIEIDALNRALDRYQ... | 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 | MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFL... | 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 su... |
Q8ZR88 | MQDRQKAQDYRALLLADTPLIDVRAPIEFEQGAMPGAINLPLMMDDERAAVGTCYKRQGADAALALGHRLVCGDIRQQRLEAWKAAYQRFPNGYLCCARGGQRSHIVQRWLQETGIDCPLIEGGYKALRQTAIQATWQLAQKPILLIGGCTGSGKTQLVRQQPNGVDLEGLARHRGSSFGRTLNPQLSQASFENKLAVELLKINARQTLKRWVLEDEGRTIGANHLPECLRERMAQAPIAVVEDPFALRLERLREEYFIRMHHDFTHAYGDEAGWQAYSEYLHHGLFAIRRRLGLQRFAELTDTLDRALAEQLSSGSTDG... | 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-thio... |
A0QR01 | MSLLTLIAGVAVGVTVVPRIVARRQRRAAYAAGMTVSQMLQHITSLSPMGVAVVDTFNDVVYSNDRAVELNVVRDRILDDRAWQAAQRVFETGQDVEVDLSPLKVANPGRSGISVRGKVRLLTDDDRRFAVVYIDDQSEHARMEATRRDFVANVSHELKTPVGAMSVLAEALLASADDPDTVRRFAEKMVAESHRLADMIGELIELSRLQGAERLPDLDAVDVDSIVSEAVSRHKVAADNSQISITTDAPTGYRVLGDEGLLVTAIANLVSNAIAYSPNGTDVSISRRKRGGNIEIAVTDRGIGIAKDDQERVFERFFRV... | 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 environmen... |
P39709 | MYSIVKEIIVDPYKRLKWGFIPVKRQVEDLPDDLNSTEIVTISNSIQSHETAENFITTTSEKDQLHFETSSYSEHKDNVNVTRSYEYRDEADRPWWRFFDEQEYRINEKERSHNKWYSWFKQGTSFKEKKLLIKLDVLLAFYSCIAYWVKYLDTVNINNAYVSGMKEDLGFQGNDLVHTQVMYTVGNIIFQLPFLIYLNKLPLNYVLPSLDLCWSLLTVGAAYVNSVPHLKAIRFFIGAFEAPSYLAYQYLFGSFYKHDEMVRRSAFYYLGQYIGILSAGGIQSAVYSSLNGVNGLEGWRWNFIIDAIVSVVVGLIGFYS... | 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 | MASEVARHLLFQSHITTKTAHTSSQVSDHEQKQKDSPRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDHESSHFYPHVRLKAQTYELQESNVRLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFNYHDSRVHVCLYFISPTGHSLKTLDLLTMKSLDSKVNIIPVIAKADAISKTELQKFKIKLMSELVSNGVQIYQFPTDDETIAKINASMNGHLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLRDQTHTRHYEL... | 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 | MASSEVARHLLFQSHMATKTTCMSSQGSDDEQIKRENIRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDYESSHFCPNVKLKAQTYELQESNVQLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFTYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYE... | 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 | MASCDEIKEHPRSLSMCGHVGFESLPDQLVDRSIEQGFCFNILCVGETGIGKSTLINTLFNTNFEELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEDSYQPIVDYIDDQFEAYLQEEVKIKRALFNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSELQKFKMKLMNELVINGVQIYQFPTDDDTTSKINGAMNGHLPFAVVGSMDEIKVGNKMVKGRQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMGFVDMGPENKPLSLQET... | 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 | MTADVLKALPPDVRTLKLSGHVGFDSLPDQLVNKAISQGFVFNILCVGETGIGKSTLLETLFNQKFDFSPSNHDLTDPKLKAVTYDLKEANVKLKLTVVETCGYGDQINKENNIKPVVDYIDNQFENYLQEELKMKRSMQAFHDTRVHVCLYFIAPTGHSLKSIDLVAMKKLENKVNVIPVIAKSDTITKSELQKFKARILSEIQSNEIGIYQFPTDDEAVSETNSVMNQHIPFAVVGSSEEVKINGKTVRVRQYPWGSVQVENENHCDFVRLREMLLRVNMEDLRERTHGVHYETYRRQRLIEMGFRDDEKMSLQETYE... | 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 remodeli... |
O29445 | MKVLVAEPISEEAIDYMRKNGLEVEVKTGMSREELIREVPKYEAIVVRSQTKVDAEVIQAAKNLKIIGRAGVGVDNIDINAATQRGIVVVNAPGGNTISTAEHAIALMLAAARKIPQADRSVKEGKWERKKFMGIELRGKTAGVIGLGRVGFEVAKRCKALEMNVLAYDPFVSKERAEQIGVKLVDFDTLLASSDVITVHVPRTKETIGLIGKGQFEKMKDGVIVVNAARGGIVDEAALYEAIKAGKVAAAALDVYEKEPPSPDNPLLKLDNVVTTPHIAASTREAQLNVGMIIAEDIVNMAKGLPVRNAVNLPSIEPSD... | 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 | MFRVLVSDKMSNDGLQPLIESDFIEIVQKNVADAEDELHTFDALLVRSATKVTEDLFNKMTSLKIVGRAGVGVDNIDIDEATKHGVIVINAPNGNTISTAEHTFAMISSLMRHIPQANISVKSREWNRTAYVGSELYGKTLGIVGLGRIGSEIAQRARAFGMTVHVFDPFLTEERAKKIGVNSRTFEEVLESADIITVHTPLTKETKGLLNKETIAKTKKGVRLINCARGGIIDEAALLEALENGHVAGAALDVFEVEPPVDNKLVDHPLVIATPHLGASTKEAQLNVAAQVSEEVLQFAKGLPVMSAINLPAMTKDEFA... | 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-phosphooxypyruvat... |
Q5EAD2 | MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTSDIINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQAAASMKDGKWERKKFMGTELNGKVLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEQIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVCVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVNHENVISCPHLGASTKEAQSRCGEEIALQFVDMVKGKALAGVVNAQA... | 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 Activ... |
Q54UH8 | MDPTTSFPKDKIKILLLENIHIAAIKQFEEQGFQVESISSSLPEDKIIEKIKDVHVLGLRSKTKVTEKILSEAKRLLAIGCFCIGTDQVDLIEAEKRGVPVFNSPFCNSRSVAELIICEIITLSRKLGDRSTEMHNKIWRKESANCHEIRGKTLGIIGYGHIGSQLSVLAEAMGMSVLYYDIARRLPLGNSKMCPDMKTLLENSNFVTLHVPDTKETVGLIGEEEINTMKKGSYLLNASRGKVVQIPHLANALRSGHLAGAAVDVYPEEPSANCKDWECELQKCPNTILTPHIGGSTEEAQEAIGLEVSDLIVQFINSGA... | 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-phosphooxypyruvat... |
P0A9T2 | MAKVSLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGS... | 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-phosphooxypyruvat... |
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 | MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQA... | 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 Activ... |
Q58424 | MVKILVTDPLHEDAIKILEEVGEVEVATGLTKEELLEKIKDADVLVVRSGTKVTRDVIEKAEKLKVIGRAGVGVDNIDVEAATEKGIIVVNAPDASSISVAELTMGLMLAAARNIPQATASLKRGEWDRKRFKGIELYGKTLGVIGLGRIGQQVVKRAKAFGMNIIGYDPYIPKEVAESMGVELVDDINELCKRADFITLHVPLTPKTRHIIGREQIALMKKNAIIVNCARGGLIDEKALYEALKEGKIRAAALDVFEEEPPKDNPLLTLDNVIGTPHQGASTEEAQKAAGTIVAEQIKKVLRGELAENVVNMPNIPQEK... | 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 | MSLPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIAAFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAALADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVN... | 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-phosphooxypyruvat... |
O33116 | MDLPVVLIADKLAQSTVAALGDQVEVRWVDGPDRTKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIAEADASLRAHIWKRSSFSGTEIFGKTVGVVGLGRIGQLVAARIAAFGAHVIAYDPYVAPARAAQLGIELMSFDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEVALADAVRSGHVRAAGLDVFATEPCTDSPLFELSQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVDGGVVN... | 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-phosphooxypyruvat... |
C4L432 | MSTYTYSAGPGMLPTEVMQEIQQHLLTFEYEGVSIIETSHRSASFQRVVDSLEWRLRRLMHIPENYAVLWLQGGATLQFSMIPMNLRKQNRFAYVDTGIWSKKAMEDAKHFGEVDVIHPLVDATGGMSFESSLVQEVDYLHVTLNNTIEGTRFTHIPEIDVPLIADASSNILAEQIDVERFGVIYAGAQKNIGPAGLTVVIIRRDLIQSLQLPSYLQYASHVDTLFNTPSTFSMYAAERVLKWVEDCGGVEAMERLNRQKSDRIYSYLEESTCFSPIVTGERRSLTNIPFSTGNQELDQRFERYALERGLLELGGHRSVG... | 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 M... |
A6GXC2 | MKKHNYSAGPCILPQEVFEKSAQAILDFNHSGLSLLEISHRSKDFVAVMEEARALVLELLGLKGKGYQALFLAGGASLEFLMVPYNLMKENGKAAYLDTGTWASGAIKEAKHFGETVVIASSKEENYNHIPKNYSIPSDANYFHCTSNNTIFGTQMKSFPEVNIPVVCDMSSDIFSRVLDFSKFDLIYAGAQKNMGPAGTTLVIVKEEILGKTGRYIPSMLDYEKHIKAESMYNTPPVFPIYASLLTLQWLKNLGGISAIEKINNAKANLLYSEIDRNTLFKGTANAEDRSNMNATFLLNNKNHTELFDKMWAAAGISGL... | 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 M... |
Q5L296 | MKRAYNFNAGPSALPLPVLERAQKELLNFQNTGMSVMELSHRSKEYEAVHHAAKERLKRLLNVPDGYDILFLQGGASLQFSMVPMNLLTEGKIGCYVLTGAWSEKALKEAQKIGLTTVVASSKEANYTYIPPLDDVQWPKNAAYVHITSNNTIFGTQWKEFPNTPVDLVADMSSDILSRPFDVSQFALIYAGAQKNLGPSGVTVVILRNDLLERIPDGLPTMLDYRTHQKSNSLYNTPPTFAIYMLSLVLEWVEEQGGVAAMEERNQQKAAVLYEAIDESGGFYKPHAEKGSRSLMNVTFTLPNEELTKTFLAEAKERGF... | 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 M... |
Q2SCF2 | MADRKFNFCAGPSALPTEVLLQAQAELLDWRGKGLSIMEMSHRSDDFVAVAVEAERDFRELMSVPDNYKVLFVQGGAATQFASVPLNLLKLGAEADYIDTGIWSKKAIAEAGRYLKVNVAASAKDNGYACIPARSEWRLSESAGYVHYTPNETIGGVEFLDIPDVGDKPLVADMSSTILSRPVDISRFGVIYAGAQKNIGPAGLTLVIVREDLLGYASDSLPTMLNYKVASENDSMVNTPPTFSWYLAGLVFKWLKGKGGVQAMEAINCRKADKLYSYIDDSEFYANPIDLSCRSWMNVPFTLKDDRLDQKFLQEAEGAG... | 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 M... |
Q9Y617 | MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLVRELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGTINIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSNFLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLYNTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSKMNIPFRIGNAKGDDALEKRF... | 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 M... |
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: 5... |
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 | MTAEQAINEGAFSLAASFGFVPLEYRGYEAEVLASKETAYIGTALNGAMSPIYDVTGPDALEFLRSVCINSFRGFQVGQIRHAVLCNDKGQILTDGVVARIDEDTYRTYWLAPALEYRLINSGLDVKGEDQSSNEFFFQLAGPRSLEVLEAAAHEDLHDIAFGRHRMSTIAGIPVRILRLGMAGGLAYEVHGAAADTETAYRAIWEAGQPFGLVKQGLNAYLMQHTEAGFPNINLHYPLPWYEDPDMAAFFDTRPTQNFYNKYRFFYGSVGPDAEARFVTPYQIGLGKMVDFNHDFIGKEALQREAEADHWAAVTLVWNE... | 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) = (+)-... |
Q9Y6P5 | MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDEELGIRIPRPLGQGPSRFIPEKEILQVGSEDAQMHALFADSFAALGRLDNITLVMVFHPQYLESFLKTQHYLLQMDGPLPLHYRHYIGIMAAARHQCSYLVNLHVNDFLHVGGDPKWLNGLENAPQKLQNLGELNKVLAHRPWLITKEHIEGLLKAEEHSWSLAELVHAVVLLTHYHSLASFTFGCGISPEIHCDGGHTFRPPSVSNYCICDITNGNHSVDEMPVNSAENVSVSDSFFEVEALMEKMRQLQECRDEEEASQEEMASRFEIEKRESMFVFSSDDEEVT... | 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 sig... |
Q9NVD3 | MQKGKGRTSRIRRRKLCGSSESRGVNESHKSEFIELRKWLKARKFQDSNLAPACFPGTGRGLMSQTSLQEGQMIISLPESCLLTTDTVIRSYLGAYITKWKPPPSPLLALCTFLVSEKHAGHRSLWKPYLEILPKAYTCPVCLEPEVVNLLPKSLKAKAEEQRAHVQEFFASSRDFFSSLQPLFAEAVDSIFSYSALLWAWCTVNTRAVYLRPRQRECLSAEPDTCALAPYLDLLNHSPHVQVKAAFNEETHSYEIRTTSRWRKHEEVFICYGPHDNQRLFLEYGFVSVHNPHACVYVSREILVKYLPSTDKQMDKKISI... | 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 pr... |
Q5ZK17 | MAAPAKRRRAAGPDPDPTAGFVAWCEAAGVELSPKVSISRRGTVSGYGLLAAADLEPGELLFSVPRSALLSQHTCAIRALLHDAQESLQSQSVWVPLLLALLHEYTTGTSRWRPYFSLWQDFSSLDHPMFWPEEERVRLLQGTGIPEAVDKDLANIQLEYSSIILPFMKSHPDIFDPELHTLELYKQLVAFVMAYSFQEPLEEEDEDEKGPNPPMMVPVADILNHVANHNASLEYAPTCLRMVTTQPISKGQEIFNTYGQMANWQLLHMYGFAEPYPGNTNDTADIQMVTVRKAALQRAKNEAQQQLVAEQWDFLCQLEM... | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 50649
Sequence Length: 447
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q803K4 | MATEAKRPKTGDEKSVLEPLNNFLLWCESVQLTLSDKVYLSKEGTAAEYGMLAKEDIEEGHVLFTIPREALLHQGTTKVKKVLEEGKKCLESASGWVPLLLSLMYEYTSSTSHWKPYLSLWPDFRTLDQPMFWSEEECDKLLKGTGIPESVITDLRKLQDEYNSVVLPFMKSHPDLWDPEKHNLELYKSLVAFVMAYSFQEPVEDDDEDEEDDEKKPNLPMMVPMADMLNHISKHNANLEYTPECLKMVSIRRIGKGEEVFNTYGQMANWQLLHMYGFAEPFPNNINETADIKMASVYKAAAQVARSEANQQLLEDKWKM... | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 53007
Sequence Length: 460
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8TBK2 | MATQAKRPRVAGPVDGGDLDPVACFLSWCRRVGLELSPKVSERAGGRRTRGGARAALTSPPAQVAVSRQGTVAGYGMVARESVQAGELLFVVPRAALLSQHTCSIGGLLERERVALQSQSGWVPLLLALLHELQAPASRWRPYFALWPELGRLEHPMFWPEEERRCLLQGTGVPEAVEKDLANIRSEYQSIVLPFMEAHPDLFSLRVRSLELYHQLVALVMAYSFQEPLEEEEDEKEPNSPVMVPAADILNHLANHNANLEYSANCLRMVATQPIPKGHEIFNTYGQMANWQLIHMYGFVEPYPDNTDDTADIQMVTVRE... | 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). Methyl... |
Q9CWY3 | MAAPAKRARVSGGSPLVAPCPSPRAARAPLPLPAGSSGGEPEGDAVAGFLRWCRRVGLELSPKVTVSRQGTVAGYGMVARESVRAGELLFAVPRSALLSPHTCSISGLLERERGALQSLSGWVPLLLALLHELQAPASPWSPYFALWPELGRLEHPMFWPEEERLRLLKGTGVPEAVEKDLVNIRSEYYSIVLPFMEAHSDLFSPSVRSLELYQQLVALVMAYSFQEPLEEDDDEKEPNSPLMVPAADILNHIANHNANLEYSADYLRMVATQPILEGHEIFNTYGQMANWQLIHMYGFAEPYPNNTDDTADIQMVTVRD... | 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 . Methyla... |
A4QNG5 | MGPDAKKQKLQSEDHLQNDLPVSCFLAWCKKVGLELNPKVYISTEGTVSQYGMLAREDLSDGELLFSIPRSAILSQNTTRIRDLIEKEQDSLQSCSGWVPLLISLLYEATDSSSHWAPYFGLWPELDPPDMPMFWSEEEQTKLLQGTGILEAVHKDLKNIEKEYNSIVLPFIRRNPEKFCPMKHTLDLYKRLVAFVMAYSFQEPQEEDEEEDIEKDILPPMMVPVADLLNHVAQHNAHLEFTPECLRMITTKSVCAGQELFNTYGQMANWQLLHMYGFAEPHPQNCNETADIQMVTVREAAFQVARTEEDRLEMQKRWDF... | Function: Protein-lysine N-methyltransferase.
Sequence Mass (Da): 52331
Sequence Length: 454
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q7Z0G7 | MDSSDDEIACDEGDYKGAKDDNDLPHGLGKVKFSSGDEFIGAFEHGIKCGPGKFHFFDDSTLEGNYVDGELHGIGIYTNDDGSITKSTYCEGVMEGPSWEYDPEGNITFRGQYSEGVRCGLCFYYFPDGGSLIGNVNASGDLSADNIAYIYPDRTTALIGSFEEGDMITAKEANVTITGEKGEEISFPTVNSISPDPVYRLDVSTPHVISTRPLVPDPYESELVYAAPSKIPNAGEGLYAKCDVDQDTVMAFYNGVRLKQDEVENRDWSQNSNTISLTDDIAIDVPEEYVSTDNYCASLGHKVNHSFDPNCRYDIYQHPR... | 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.
Cataly... |
Q8WTS6 | MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIR... | 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 insuli... |
Q8VHL1 | MDSDDEVVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDSDGRLIFKGQYKDNNRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGRPHFEVTSGSSVYHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDLFVHPRFGPIKCIR... | 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 . Recruit... |
Q06168 | MSHQNQLIPQAYISNFHNRLTNEDDGIPIFTMAQQTRQHKRAKVVNYAEYDNDLFDEFNMNGSNFNNADTHYKDNAVSHENTPALTNGVTMDGSEYNVLENMNGADSIISNNKYDAGSNMVVESLSGLNSNNNASNGPSNKAQAQDIGNAVLPDLQDQHHNPFNILRYPKIRDTFINGKVVSPYRLNTDQETKANANSGEAIMIPITLDIEHMGHTIKDQFLWNYNDDSISPEEFASIYCKDLDMTSATLQTQIANIIKEQLKDLENIAATEIMSDLHVIINLTCNLQDRFFEDNFQWNLNDKSLTPERFATSIVQDLGL... | 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 int... |
Q93ZE9 | MTDTMSAHMDRHNKLDYDGSEDEKKTKLCSLKKKAINASNKFKHSFTKRTRRNSRVMSVSIVDDIDLEELQAVDAFRQALILDELLPSKHDDHHMMLRFLRARKFDLEKAKQMWTDMIHWRKEFGVDTIMEDFDFKEIDEVLKYYPQGYHGVDKDGRPVYIERLGQVDATKLMQVTTIDRYVKYHVREFEKTFNIKLPACSIAAKKHIDQSTTILDVQGVGLKSFSKAARDLLQRIQKIDSDNYPETLNRMFIINAGSGFRLLWSTVKSFLDPKTTAKIHVLGNKYQSKLLEIIDSNELPEFLGGNCTCADKGGCMRSDK... | 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 appa... |
F4HP88 | MSGPLDRFTSPCFSNNGEKREKKSDFEVSEDEKKTRIGGILKKKSSKSKFRHSLKRRGSRSIDRTLSLTFEDIHDAEELRYVSEFRQSLISDHLLPPNLDDYHIMLRFLFARKFDLGKAKLMWTNMIQWRRDFGTDTILEDFEFPELDEVLRYYPQGYHGVDKEGRPVYIERLGKVDASKLMQVTTLERYLRYHVKEFEKTITVKFPACCIAAKRHIDSSTTILDVQGLGLKNFTKTARDLIIQLQKIDSDNYPETLHRMFIINAGSGFKLLWGTVKSFLDPKTVSKIHVLGNKYQNKLLEMIDASQLPDFFGGTCTCAD... | 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 appa... |
A6QT51 | MSETEKPVQAAAAAAVAAAGTADVPAVEKDPETTQDKQQSATDNSTTKAPQDEKNKQTENPSTDAPPAAATAPTADPITSAQPPDVDAIEAQKDGQKKNGPGSENKPDETPVDTRPEYLSKNPALSEFFEKLASILKKADHNEMWGVTLKDSDDVPTVNVLIKFLRANEGNVKLAEEQLRKALEWRKKMNPLALAEKATYSSSKFQGLGYVANYKDQNQGKVVFTWNIYGSVKDANRTFGDVDEFIKWRVALMEMAVKDLKLSEATSVIDYSGEDPYQMIQVHDYQNVSFLRLNPTIKSATKQTIDVFSTAYPELLKEKF... | 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 s... |
Q8GXC6 | MSGSLDRFARPCFEGVSSNDERRERRSDFEVSEDEKKTRIGNFNFKKKAAKASSKLRHSLKKKGSSRRRSSDRTFSLTIEDIHDVEELRAVDEFRNLLVSENLLPPTLDDYHIMLRFLKARKFDIGKTKLMWSNMIKWRKDFGTDTIFEDFEFEEFDEVLKYYPHGYHGVDKEGRPVYIERLGLVDPAKLMQVTTVERFIRYHVREFEKTVNIKLPACCIAAKRHIDSSTTILDVQGVGFKNFSKPARDLIIQLQKIDNDNYPETLHRMFIINGGSGFKLVWATVKQFLDPKTVTKIHVIGNKYQNKLLEIIDASQLPDF... | 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 appa... |
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 s... |
Q4WEP0 | MSVTMADQQPEKTTAPASDVADSQPAVVSNTDTRKETTETAEPQSEDKTATTTAQPAVETTATQSGTAETPAEADKAPAEVQQPPQAEEEKPVAQQPEQPAYLAKNPALSQFFERLPAIVSSSGHAEMWGVPLKDSNDAPTVNVLIKFLRANEGNVKLAEEQLTKALKWRKETNPSALAESTSYSATKFGGLGYLTTYKEANGAETVVTWNIYGGVKDINTTFGDMNEFVKWRVALMELAVKELKMAEATSVIDYDGEDPYQMIQVHDYQNVSFLRLNPAIKAATKKTIEVFTTAYPELLREKFFVNVPAIMGWMFAAMK... | 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 s... |
Q2UA18 | MADQQEKTASSAVPETQPPSQTAETTTQTTATPAPEVQTEQTQPTESGPSAANTTTEQPTNPPAAEASKENAAPAPAPAAEDAPSEPAPAQEQQKEEKPADNKPEYLAKNPALSQLFDRLPTVLSNSGHDEMWGVPLRDSSDVPTVNVLIKFLRANEGNVKLAEDQLTKALQWRKQTRPTALVEGRYSAKKFGGLGYLSTYKDADGKETVITWNIYGGVKDLGTTFGNVDEFINWRVALMELAVKDLKMDQATSVIDYEGEDPYQMIQVHDYLNVSFLRMNPSVKAATKKTIDVFATAYPELLREKFFVNVPSIMGWMFA... | 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 s... |
A6S3N2 | MGYKNSVRKILGNIFKPKILKAKRQGAEGQLNVVQRPRSVIFLKAGVRLSRTPDTCVQNIAKERCDKVIGDKIPYGPSNQASSFAGQLGLKREKEINEEVGGWTKVVYKVEADLVEKEEEKAGLAGWDGLGFESNTKMSAEPNNNQAKADVPEEVVEPKPTTVEEPKSTTVEEPKSTTVEESKSTTVEEPKSTTAEQPKSTIEQDPKPSTTESSPVQIDDSTPIPQITTEEPKPTVAEPSTTESVTAEPTTEQPQEAAVKLESVKEADAEAAAKLEATKDADVEKAASTSQHSVSFDKATKTHDGSPLSKFYSELPAILE... | 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 s... |
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 s... |
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: Secre... |
P23246 | MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKY... | 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 t... |
Q8VIJ6 | MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGGPKPPLPPPPPHQQQQQPPPQQPPPQQPPPHQQPPPHQPPHQQPPPPPQESKPVVPQGPGSAPGVSSAPPPAVSAPPANPPTTGAPPGPGPTPTPPPAVPSTAPGPPPPSTPSSGVSTTPPQTGGPPPPPAGGAGPGPKPGPGPGGPKGGKMPGGPKPGGGPGMGAPGGHPKPPHRGGGEPRGGRQHHAPYHQQHHQGPPPGGPGPRTEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFI... | 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 t... |
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... |
Q93Y07 | MELFALLIKVAGLLATVTVGANVVSYSRFRRQNLAKFRSPIDESKEVLADFNSIEHEEGKFFFGLATAPAHAEDDLDDAWLQFAKETPCSAEEAEAADKKARRKKVKLAVGAITKGLAKNTHGKEDKNAADKPPSKNVAAWHNAPHAEDRLKFWSDPDKEVKLAKDTGVTVFRMGVDWSRIMPVEPTKGIKEAVNYEAVEHYKWILKKVRSNGMKVMLTLFHHSLPPWAADYGGWKMEKTVDYFMDFTRIVVDSMYDLVDSWVTFNEPHIFTMLTYMCGSWPGNNPDFLEIATSTLPMGVFHRALHWMAVAHSKAYDYIH... | 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 . M... |
Q8L6H7 | MPLPAFVAAAARLAVLVAAAATAANAASYARYRRRHLRRIPSPIDESADPLADFRAFPSSDADDSEEDNFFFGLATAPAHVEDRLEDAWLQFATETSCDDNGNVRDQRPVDALMASAAGDGGSQQSWRSTGGENIGDREQRKPLRVAMEAMLRGFEILAESGESAGGDNCSHNVAAWHNVPCPQERLRFWSDPDAELKLAKETGISVFRMGVDWARLMPEEPTEELKSSVNFAALERYRWIIQRVREYGMKVMLTLFHHSLPPWAGKYGGWKMEKTVTYFMDFVRLVVDRVSNLVDYWVIFNEPHVFVMLTYCAGAWPGG... | 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... |
D7AF63 | MVSLTIDGKDITVAKETTILDAAALLGITIPTLCWLKKVSPTGACRVCAVEIEGVDRPMTACNTPVKDGIKVTTQSEKLSRIRQKIMELMLVNHPLDCPVCDAGGECDLQNACYGLGAAKQEYGAVLERRKIRYDWPLIESDPNRCILCEKCVKVDHEIVGCNAIRVVNRGEATIIDTVDGNPLNCEFCGNCVAACPTGTLISKPFKFRGRPWAFTTTPSVCPFCATGCQIEYHSRNGRVERVTSDDSTYNSGNLCINGRFGYSYINSPDRLAEPMVKGQKADWNTAMGTAATALKQIVASHGADAVAGFGSPRVTNEDN... | 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: Ce... |
D7AF64 | MAQVVFSSWGRTIVDNRKGGEAQDVSFRLPTTLDGERQIAAFMGWDGIILYDLKVDVPAMAAEYMKRVQTQYCCGKCTPGKKGTKVLADVLAAIIEGRATEADLDTIDDLADLLTNCKCTLCQSSTIPVLDAVKHFREDFLAYITGIRKPANVHRFIDKYTAPCMDRCPAHIDIPAYIEAIKEYRFDESLDIIRDNMPLPSVCGRVCPHPCETHCRRKNVDDSVNIMVLKRSASDYEWMHNAAPPMQPKPQKNKKVAIVGAGPAGLACAYYLALEGYPCTIYEALPEGYGGGMIAVGIPPYRQPRHLLQRDIDIISSMGV... | 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.-.-... |
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 Lengt... |
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 E... |
Q16586 | MAETLFWTPLLVVLLAGLGDTEAQQTTLHPLVGRVFVHTLDHETFLSLPEHVAVPPAVHITYHAHLQGHPDLPRWLRYTQRSPHHPGFLYGSATPEDRGLQVIEVTAYNRDSFDTTRQRLVLEIGDPEGPLLPYQAEFLVRSHDAEEVLPSTPASRFLSALGGLWEPGELQLLNVTSALDRGGRVPLPIEGRKEGVYIKVGSASPFSTCLKMVASPDSHARCAQGQPPLLSCYDTLAPHFRVDWCNVTLVDKSVPEPADEVPTPGDGILEHDPFFCPPTEAPDRDFLVDALVTLLVPLLVALLLTLLLAYVMCCRREGRL... | 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 | MAAAVTWIPLLAGLLAGLRDTKAQQTTLHLLVGRVFVHPLEHATFLRLPEHVAVPPTVRLTYHAHLQGHPDLPRWLHYTQRSPYNPGFLYGSPTPEDRGYQVIEVTAYNRDSFDTTRQRLLLLIGDPEGPRLPYQAEFLVRSHDVEEVLPTTPANRFLTALGGLWEPGELQLLNITSALDRGGRVPLPIEGRKEGVYIKVGSATPFSTCLKMVASPDSYARCAQGQPPLLSCYDTLAPHFRVDWCNVSLVDKSVPEPLDEVPTPGDGILEHDPFFCPPTEATDRDFLTDALVTLLVPLLVALLLTLLLAYIMCFRREGRL... | 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 EII... |
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
S... |
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
S... |
P39365 | MFDYILSLGGTVFVPIIMIVIGLIFRIPWLQAIKAGVTVGIGFVGMGLVIVMAIDSLSPPIKVMIERFGLALHVFDVGAGPASGVGYATAIGAMIIPVIFLLNVAMLVTRLTKTMNVDIYNYWHYAITGTVVQLMTGSLIYGVLGAICHAALSLKMADWTAKRVQNIVGLEGISIPQGYGSSSVPLFVLLDAIYEKIPFMKGRNIDAQEIQKRYGMVGDPVIIGVVLGLIFGLAAGEGFKGCASLMITVAAIMVLFPRMIRLIVEGLLPISDGARKFFQKYFKGREVYIGLDTAVTLGHPTTIAVGLLLIPIMLILASIL... | 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): 4... |
Q8GMG6 | MPHGAEREASPAEESAGTRPLTGEEYLESLRDAREVYLDGSRVKDVTAHPAFHNPARMTARLYDSLHDPAQKAVLTAPTDAGDGFTHRFFTAPRSVDDLVKDQAAIASWARKSYGWMGRSPDYKASFLGTLGANADFYEPFADNARRWYRESQEKVLYWNHAFLHPPVDRSLPADEVGDVFIHVERETDAGLVVSGAKVVATGSALTHAAFISHWGLPIKDRKFALVATVPMDADGLKVICRPSYSANAATTGSPFDNPLSSRLDENDAILVLDQVLIPWENVFVYGNLGKVHLLAGQSGMIERATFHGCTRLAVKLEFI... | 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... |
D4Q9Z4 | MEKKKGELKSIFLPFLSTSHIIPLVDMARLFALHDVDVTIITTAHNATVFQKSIDLDASRGRPIRTHVVNFPAAQVGLPVGIEAFNVDTPREMTPRIYMGLSLLQQVFEKLFHDLQPDFIVTDMFHPWSVDAAAKLGIPRIMFHGASYLARSAAHSVEQYAPHLEAKFDTDKFVLPGLPDNLEMTRLQLPDWLRSPNQYTELMRTIKQSEKKSYGSLFNSFYDLESAYYEHYKSIMGTKSWGIGPVSLWANQDAQDKAARGYAKEEEEKEGWLKWLNSKAESSVLYVSFGSINKFPYSQLVEIARALEDSGHDFIWVVRK... | 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:... |
D4Q9Z5 | MDSVALNGKSNDKPLHVAMLPWLAMGHIYPYFEVAKILAQKGHFVTFINSPKNIDRMPKTPKHLEPFIKLVKLPLPKIEHLPEGAESTMDIPSKKNCFLKKAYEGLQYAVSKLLKTSNPDWVLYDFAAAWVIPIAKSYNIPCAHYNITPAFNKVFFDPPKDKMKDYSLASICGPPTWLPFTTTIHIRPYEFLRAYEGTKDEETGERASFDLNKAYSSCDLFLLRTSRELEGDWLDYLAGNYKVPVVPVGLLPPSMQIRDVEEEDNNPDWVRIKDWLDTQESSSVVYIGFGSELKLSQEDLTELAHGIELSNLPFFWALKN... | 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 cons... |
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 ... |
A0A509AQU3 | MIFKKALYILLFLYIAIVKKGESKPGSKHPFLFKNLVIDKKKLDSSYYNKYDNIKWNGKIIAIGDIHGDIESLKLILRHSKLIGENDNWIGDNVLLVQNGDVFDRGIYGPIIYNFLFKLQKEAIKKNSRVILIMGNHEQLNLCGYFNYVNPKEIEMFFHNDANYRYHSFVNPYGEYHKRLIRLPPMVKVNNIIFTHGGLNLLISKLSINDINLKTRLQIENNCKPIKYDSFQNYLSRDGVLWSDAMSRNVPYYEKEKCSELFQILDKYDAKYLVVGHTRQPSHQIGSYCNNHYFLIDTGMSLFTNYGQPYPNYLKIDDHK... | 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 | MTLRATKARQQRVSPHIGHTFSFGNLVGDPFAISTLSISTIAWLITLGGGIATKKMPHFSWWGIAFQFVMMVCFVVIYLWDLVDYYRGFLAAGVGVAFVYSTNSCSQLIYQEEPQQAAGSAGFMMLSIVNMIWMFYFGADNAAPANRWIDSFSIRGIRASQVESSLALARSQKAVASPQPAATAFYGGLEGHSQKYVSSTALNGFENTDPHTSTAFALGPEGPTQRNLDTHGTSTYVTDTTNGNTETTMGDTLGLYSDMGDELVNFPYTAKALYAYEADASDAYEISFQQGEILRVGDIEGRWWKAKKANGETGIIPSNY... | 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 | MRRVLRLLLGCFLTELCARMCRAQERSGHGQLAQLGGVLLLTGGNRSGAASGEAGEGVGGSDAPPTRAPTPDSCRGYFDVMGQWDPPFNCSSGDFIFCCGTCGFRFCCTFKKRRLNQSTCTNYDTPLWLNTGKPPARKDDPLHDPTKDKTNLIVYIICGVVAVMVLVGIFTKLGLEKAHRPQREHMSRALADVMRPQGHCNTDHMERDLNIVVHVQHYENMDSRTPINNLHTTQMNNAVPTSPLLQQMGHPHSYPNLGQISNPYEQQPPGKELNKYASLKAVGNSDGDWAVATLKSPKADKVNDDFYAKRRHLAELAVKG... | 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
Sequ... |
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... |
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... |
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... |
Q9R2B6 | MEHVVTCWRLKLLSWPVFLIWICLSLASVSLISWDQLPAFLIPSTGDSSLQTAKSRDSMKAPGRLLLLTLCILTFSAVCVFLCCWACLPLCLATCLDRHLPAAPRSTVPGPLHFSGYSSVPDGKPLIRELCHSCAVVSNSGQMLGSGLGAQIDGAECVLRMNQAPTVGFEEDVGQRTTLRVISHTSVPLLLRNYSHYFQHARDTLYVVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMIPALELCEEIVVYGMVSDSYCSEKSPRSVPYHYFEKGRLDECQM... | 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... |
Q9BVH7 | MKTLMRHGLAVCLALTTMCTSLLLVYSSLGGQKERPPQQQQQQQQQQQQASATGSSQPAAESSTQQRPGVPAGPRPLDGYLGVADHKPLKMHCRDCALVTSSGHLLHSRQGSQIDQTECVIRMNDAPTRGYGRDVGNRTSLRVIAHSSIQRILRNRHDLLNVSQGTVFIFWGPSSYMRRDGKGQVYNNLHLLSQVLPRLKAFMITRHKMLQFDELFKQETGKDRKISNTWLSTGWFTMTIALELCDRINVYGMVPPDFCRDPNHPSVPYHYYEPFGPDECTMYLSHERGRKGSHHRFITEKRVFKNWARTFNIHFFQPDW... | 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... |
Q9QYJ1 | MKTLMRHGLAVCLVLTTMCTSLLLVYSSLGSQKERPPQQQQQQQQQQQQAATATGSTQLVESSPQPRRTAPAGPRQLEGYLGVADHKPLKMHCKDCALVTSSGHLLRSQQGPHIDQTECVIRMNDAPTRGYGLDVGNRTSLRVIAHSSIQRILRNRHDLLNVSQGTVFIFWGPSSYMRRDGKGQAYNNLQLLSQVLPRLKAFMITRHRMLQFDELFKQETGKDRKISNTWLSTGWFTMTIALELCDRIDVYGMVPPDFCRDPKHPSVPYHYYEPSGPDECTMYLSHERGRKGSHHRFITEKRVFKNWARTFNIHFFQPDW... | 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... |
Q08E15 | MACPRPLSQCDHTPLPGPPAGHWPLPLSRRRREMKSNKEQRSAVFVILFALITILILYSSSSANEVFHYGSLRGRTRRPVNLRKWSITDGYIPILGNKTLPSRCGQCVIVTSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTFRVVAHSSVFHVLRRPQEFVNRTPETVFIFWGPPNKMQKPQGSLVRVIQRAGLVFPNMEAYAISLSRMRQFDDLFRSETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPDYCSLRPHLQRMPYHYYEPKGPDECVTYIQNENSRKGNHHRFITEKRVFSSWAQ... | 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 ... |
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