ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9Y3A3 | MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA | Function: May play a role in membrane trafficking, specifically in membrane budding reactions.
PTM: Phosphorylated on serine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26032
Sequence Length: 225
Subcellular Location: Cytoplasm
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P28581 | MKKNIIAGCLFSLFSLSALAAIPAGNDATTKPDLYYLKNEQAIDSLKLLPPPPEVGSIQFLNDQAMYEKGRMLRNTERGKQAQADADLAAGGVATAFSGAFGYPITEKDSPELYKLLTNMIEDAGDLATRSAKEHYMRIRPFAFYGTETCNTKDQKKLSTNGSYPSGHTSIGWATALVLAEVNPANQDAILERGYQLGQSRVICGYHWQSDVDAARIVGSAAVATLHSDPAFQAQLAKAKQEFAQKSQK | Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 26999
Sequence Length: 249
Subcellular Location: Periplasm
EC: 3.1.3.2
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Q01605 | MKKSTLALVVMGITASASVQAAEVYNKNGNKLDLYGKVKAMHYMTDYDSKDGDQSYIRLGFKGETQINDELTGYGRWEAEFAGNKAESDSNQQKTRLAFAGSKLKNLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGVVDGLDLTLQYQGKNQDRDVKKQNGDGFGTSVTYDFGGSDFAVSGAYTNSDRTNQQNLQTRGTGDKAEAWATGLKYDANDIYIATFYSETRNMTPISGGFANKTQNFEAVVQYQFDFGLRPSLGYVLSKGKDIEGVGNEDLVNYIDVGATYYFNKNMSA... | Function: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38807
Sequence Length: 351
Subcellular Location: Cell outer membrane
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P02932 | MKKSTLALVVMGIVASASVQAAEIYNKDGNKLDVYGKVKAMHYMSDNASKDGDQSYIRFGFKGETQINDQLTGYGRWEAEFAGNKAESDTAQQKTRLAFAGLKYKDLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGVIDGLNLTLQYQGKNENRDVKKQNGDGFGTSLTYDFGGSDFAISGAYTNSDRTNEQNLQSRGTGKRAEAWATGLKYDANNIYLATFYSETRKMTPITGGFANKTQNFEAVAQYQFDFGLRPSLGYVLSKGKDIEGIGDEDLVNYIDVGATYYFNKNMSA... | Function: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38922
Sequence Length: 351
Subcellular Location: Cell outer membrane
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A0A8J9WH54 | MGADMQPDYARLPEVDQQSCDGFVSSEFLPTRRDRRKGILYLVWFVFGVASGALLLKMLQDLPLLMTLDSSEAKLQSLLWMPTEIVVFQPNDLFASIPSPTSDRAWDELLGPSRGFVNFENPEEELGLPPGRPVPDDPKSAVYGISMFHQLHCLIMIREIYYGILLGEYNTTMFHVEMDNADGGADKDNHEHEHDRSGKAFKIKHTKHCFDYLQQSIRCAGLMQVEMPQGPDRNIFDGYGSPHVCKRWDITVFMEEHRVIEE | Function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock . Within the pathway, phomYa catalyzes the hydroxylation of C-beta of Tyr . The pathway starts with the processing o... |
A0A142I729 | MDGYSSKKPRSASPSRSSLTEVEEEERDTLLKTVSLEEEDKSGENGPRKLRRSRFLYAIGILMLSNIAFIAAFLTVFVQKRALEPARLPPWAPPERYESRVFKYMDVYGGEPGPKSEEAWTNLIPKGKGWIKVHNETAIPDMPGLDQSLPEQSALVSVFHQLHCLYMTRAGYFAARSGNLDEVNVVHVSHCWDYLRQAIMCHSDTTLEWLHAPPDNFGSTGWGYEHQCRDYEAIFAFATEHRAGERQVIHG | Function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock . Within the pathway, phomYb is probably involved in the construction of the macrocyclic structure of the phomopsins... |
A0A142I739 | MGHRQSVDYTSIPPSELDAHERLPRRKSRFDLFYGWKGIAFLSTLTNVLFISGFFYFGTHLFSPSSSFGHEECHLGSERLWERPVPWKKVVLENHQEFVDGDPWDSKFAGDGTSSNGGAPSPWDSVWLPNWVALENDPAAQGYGFGTPLTGPGSEGNEHDPTPWTPGSQAFGLAVMHQLHCVASIKKAINDYRYTGGHRGSNSSANIGHVDHCVEVLRQATMCHGDMSLIRPNVKGHSYTGYDGWGNEHLCRDWEAIEDIVREHGISFVKGAGMQGWTHLKKGVS | Function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock . Within the pathway, phomYe catalyzes the desaturation of the Pro moiety into 3,4-dehydroproline (dPro) . The pathw... |
A0A142I728 | MSSFLVQTAVVRLFLLGVVFWFPFALSSSCAEIASKFGTWKSEGDAPPSYLSPTVDLLDGLDRIRKKIINGTISSQYDFDNLLHRLISQANDGHLQIGLCSREIFRFQHGTPLTSVSRDGLDLPQLYVHSDAVIMHSGQVEAISPVVEINGLEADYYLQSRIAVTLGYQDPDARYNALFPSPSAGFTGTYSAGAWASNSGEWPGSAVLTIRFANGTRLEVKPTATWPATNGPMNYTDGQALFEAACLPGTSSKYIFGSFPGMYLGLPAYELPRSGPSVFPAPTIKDSNGLVRLYSLEDAALQDVAVLQITSFRMGGEDSR... | Function: Peptidase S41 family protein; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock . Within the pathway, phomP1 and phomP1' are probably involved in the processing of the phomA and phomA' pre... |
Q32PA4 | MAAAGLAQIPDVDIDSDGVFKYVLIRVYAAPPSGDPAVETKEIVRGYKWAEYHADIYDKVSGEIQKKGYDCECLGGGRISHQSQDRKIHVYGYSMGYGRAQHSVSTEKIKAKYPDYEVTWADDGY | Function: Exhibits phosphohistidine phosphatase activity.
Catalytic Activity: H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate
Sequence Mass (Da): 13931
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 3.9.1.3
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Q9NRX4 | MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKVSGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTWANDGY | Function: Exhibits phosphohistidine phosphatase activity.
Catalytic Activity: H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate
Sequence Mass (Da): 13833
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 3.9.1.3
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P59083 | MAAAADLAQIPDVDIDSDGVFKYVLIRVHAVSPPGTPAGESKEIVRGYKWAEYHADIYDKVSGEMQKKGIDCECLGGGRISHQSQDKKIHVYGYSMGYGRAQHSISTEKIKARYPDYSVTWADDGY | Function: Exhibits phosphohistidine phosphatase activity.
Catalytic Activity: H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate
Sequence Mass (Da): 13932
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 3.9.1.3
|
A0A142I735 | MEADPKVPFTDEMNIQDEHNWESGSWSSSRRSNDSNVTLLSRRSSVEQHEDERQKDSDTLFEHGDAALDAQGIADPRLKDYPIPLVAQTVHLRNDDSEPILTFRVWLLSTFWVLAGCSISTVYYFKPFSVRLSGYVVQLCTWKMGQLLASALPTRPFTVLGRRWTLNPGRWSAKEHALVVIAYWGSSYTAYGLGPLSAMELFYGKRLSSPWAITFLVTTQLTGYGLVGLYRHILVRPPSMYYPGILPTVSLFNAMHGDPRQTASSLRVFMAIASAAFVYQWLPSFVFPLLSSLPLLCWVGRGSWEAFVLGSGSLGFGLMD... | Function: Oligopeptide transporter; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92468
Sequence Length: 842
Subcellular Locat... |
Q91901 | MAGKVHRLSGEEREQLLPNLRAVGWHELDGRDAICKEFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYDKVHITLSTHDCGGLSERDINLASFIEQIAASLS | Function: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also a... |
Q8VYM2 | MAEQQLGVLKALDVAKTQLYHFTAIVIAGMGFFTDAYDLFCVSLVTKLLGRIYYFNPESAKPGSLPPHVAAAVNGVALCGTLSGQLFFGWLGDKLGRKKVYGLTLVMMILCSVASGLSFGHEAKGVMTTLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGVGILAGGFVALAVSSIFDKKFPAPTYAVNRALSTPPQVDYIWRIIVMFGALPAALTYYWRMKMPETARYTALVAKNIKQATADMSKVLQTDIELEERVEDDVKDPKQNYGLFSKEFLRRHGLHLLGTTSTWFLLDIAFYSQNLFQKD... | Function: High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.
PTM: Ubiquitinated by NLA. Ubiquitination of PHT1-1 leads to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Se... |
Q8GSD9 | MAGSQLNVLVKLDQAKTQWYHFMAIVIAGMGFFTDAYDLFCIALVTKLLGRLYYTDITKPNPGTLPPNVSSAVTGVALCGTLAGQLFFGWLGDKLGRKSVYGFTLILMVVCSIASGLSFGHTPKSVIATLCFFRFWLGFGIGGDYPLSATIMSEYASKKTRGAFIAAVFAMQGFGILFGAIVALVVSAGFRHAYPAPSYAQNPAASLAPQADYTWRLILMFGTIPAGLTYYWRMKMPETARYTALVARNAKQAAADMSKVLHAEIEERPEVVESQVVAGETWGLFSRQFMKRHGMHLLATTSTWFLLDIAFYSQNLFQKD... | Function: Low-affinity transporter for inorganic phosphate (Pi) . Involved in internal Pi transport from root to shoot . Responsible for most of the PHR2-mediated accumulation of excess shoot Pi under abundant Pi conditions, but not for PHO2-mediated accumulation of excess shoot Pi . Acts as a H(+):phosphate symporter ... |
B2CPI4 | TARYTALVAKDAKRAAADMGKVLHVEIDPEDAKVERMAKDESNQFGLFSWEFVRRHGLHLFGTCSTWFLLDIAFYSQNLFQKDVFTAIGWIPPAKTMNAVQEVYKIARAQTLIALCSTVPGYWFTVAFIDIIGRFAIQLMGFFFMTVFMFAIAIPYHHWTLQENRIGFVIMYSLTFFFANFGPNATTFV | Function: Low-affinity transporter for external inorganic phosphate (Pi).
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21656
Sequence Length: 189
Subcellular Location: Cell membrane
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B2CPI5 | MAKDQLQVLNALDVAKTQLYHFTAIVIAGMGFFTDAYDLFCISLVTKLLGRIYYFHEGAPKPGILPSGISAAVNGVAFIGTLSGQLFFGWLGDKLGRKKVYGMTLMLMVICSIACGLSFGKTANGVIATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGFGILAGGIVALIVSAGFKNAYPAPTYSAHGKDSTPPEADYVWRIIVMIGALPALLTYYWRMKMPETARYTALVAKNTVKAAADMSKVLNVEIEEDKATVEKIEENGNSFGLFSKEFLRRHGLHLLGTTSTWFLLDIAFYSQNLFQKD... | Function: Low-affinity transporter for external inorganic phosphate (Pi) probably involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi during AM symbiosis.
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58723
Sequence Len... |
Q96303 | MAREQLQVLNALDVAKTQWYHFTAIIIAGMGFFTDAYDLFCISLVTKLLGRIYYHVEGAQKPGTLPPNVAAAVNGVAFCGTLAGQLFFGWLGDKLGRKKVYGMTLMVMVLCSIASGLSFGHEPKAVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFVSAVFAMQGFGIMAGGIFAIIISSAFEAKFPSPAYADDALGSTIPQADLVWRIILMAGAIPAAMTYYSRSKMPETARYTALVAKDAKQAASDMSKVLQVEIEPEQQKLEEISKEKSKAFGLFSKEFMSRHGLHLLGTTSTWFLLDIAFYSQNLFQK... | Function: High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.
PTM: Ubiquitinated by NLA. Ubiquitination of PHT1-4 leads to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Se... |
P42347 | MTGNEFRFFLSCDISVPVTFRVERLEGNLPLPNPKSPDLETNAPTENRTKELFVECALYIDGAPFGLPTRTRLESSGPSYCWNELITLTTKYRDLTAQSQLTFTVWDLSHGEGLIGGATILLFNNKKQLKTGKQKLRLWAGKEADGTFPTSTPGKVPRHERGELERLEKLVNKYERGQIQRVDWLDRLTFKTMERIKERESLKNGSSHLYLVVDFCSFEHRVVFQESGANFLFPSPIASTNDIVVVWDPEVGKINPSEHKQLKLARSLTRGVIDRDLKPSSNERKSIQRILKYPPTRTLSGDERQLLWKFRFSLMSEKRA... | Function: Associated with membrane proliferation.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)
Sequence Mass (Da): 93282
Sequence Length: 814
EC: 2.7.1.137
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P42339 | MGANEFRFFLSCDINSPVTFRIEKLDGNLPVKKSSDSGVVSIAEEKKPELYIECALYIDGAPFGLPMRTRLKTTGPPYCWNELITLSSKYRDLTAHSQLAITVWDVSCGKTEGLIGGATVLLFNSKMQMKSGKQKLRLWQGKEADGSFPTSTPGKVPRHERGELERLEKLMNKYERGQIQSIDWLDRLMLKSLDTIKEQESTKHGSSHLFVVIDFCSFEHRVVFQESGANLFITAPIGSTNEFVTVWDTELGKTNPSENKQLKLARSLDRGIIDRDLKPSNIERKSIQRVLKYPPTRTLSGDERQLLWKFRFSLMSEKRA... | Function: Involved in the negative regulation of proline, hydrophobic and aromatic amino acids accumulation, especially in response to salt (NaCl), either through inhibition of their synthesis and/or promotion of their catabolism . Triggers defense responses (e.g. pathogenesis related (PR1 and PR5) gene expression and ... |
O02696 | MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLAPLALLFYSTVLCTPHFPPDSDLLLKAARTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLSTRSHRSSTVTVLLLNPVEVQAEFLDVADKLSTPGPSPHSAYITLLLHAFQATFGAHCDLSGLHRRLQSKTLAELEAIFTETAEAQELASGIGDAAEARQWLRTKLQAVGEKAGFPGVLDTAKPGKLRTIPIPVARCYTYSWNQDSFDILQEILLKEQELLQPEILDDE... | Function: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96994
Sequence Lengt... |
Q6INI0 | MQNTSCTEDRIQHALERCLHGLSGSTDISSNWTAGLCLNYWSLEELVNRDATNYIILAEKTLARTREAQKNGEYELLTPLALMFYFAVLRAPYIPETSDLLPKAFEVFHTFLTWPAPYCHVYQEMLSFISEEQKAPGITYQRLVRTEQGIPTRSSCSSTATVLLVNPAELPSEFLSVAEQLSNAEQPIQQTLVSLIQHLFQASLGTHAHTEELGASLKSRPIEKLQEIYSDLTEAMEHATMADIKPGKKRESLKAKLLEVAEKAGLMQGNTGSSLTSRIQPIFMPVAKCYTYSWDQDDFDILNQILLSESHLESLEDDVT... | Function: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9892... |
Q3U6Q4 | MESSDVELDFQRSVQAVLRELNTPNPALQSNQGMWRWSLHKKVERNPGKSSILVRILLRELEKAESEDGRRVIIPLLLTLMSVLTKATGIPEDLYHRAYTFCTRLLTLPAPYSTVALDCAIRLKTETAVPGTLYQRTVIAEQNLISELYPYQERVFLFVDPELVSASVCSALLLEIQAAQEQQTPEACMRHVVSHALQAALGEACHTGALNRKLQASSRRVLEYYFHAVVAAIEQVASEDSPSRLGHLEKMEEIYCSLLGPATTRRHCVGDLLQDRLPSIPLPSPYITFHLWTDQEQLWKELVLFLRPRSQLRLSADLDA... | Function: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G proteins than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requi... |
Q5F356 | MAAPGTVASVMASKTKTKKKHFVVQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVEIYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTFKDNDFINDGQKIHIDENNKRMFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEDEGESDGTHPIGTPPDSPGNTL... | Function: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities.
PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light ... |
P48426 | MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDGTHPVGTPPDSPGNT... | Function: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) . Has both ATP- and GTP-dependent kinase activities . May exert its function by regulating the levels of PtdIns5P, which f... |
Q10351 | MSPCKWLTMFLKGCWGKIANMNHLDSCFPLRYIIGRKKASKLLCTMDSGLKSDSHEVERSNFQLNKPEKSLKRYALLSFYVIILLAIPVWWKTTHYERSSLPFEDMENAPSTVQTHLRFSPTFRILDDKGNNLTKEVQKVLEAEPQIYSYNLKVLEDDPVDYRIVLRESTDLQWFWDENNFIIDTPSKGPSELAILIVNCLWEAFSPQVMEVWSKFTRFSSTVEPSRAETKRTVQFSPQYRVLLSLLVGEGNHEPINWDIENAIQKYFNPLIEQLASLAKLNIETQIQYFVEDAEAYIKDDKFCTKHADLPNLVNNFEKY... | Function: Component of the GPI transamidase complex. Involved in transfer of GPI to proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63962
Sequence Length: 554
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmi... |
Q969N2 | MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQREGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTVTDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREVVCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQTLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPPTTTYQDVILGTRKTYAIYDL... | Function: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates.
PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 657... |
Q8CHJ0 | MAAPLALVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSGAVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYAPDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSVFLSAIFLALATYQTLYPVTLFAPGLLYLLQRQYIPVKVKSKAFWIFSWEYAMMYIGSLVVIVCLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFYTVPLAIKLKEHPIFFMFIQI... | Function: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49980
Sequence Length: 435
Pathway: Glycolipid biosynthes... |
Q9H490 | MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSGAVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYAPDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAFLSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVIICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFYTIPLAIKLKEHPIFFMFIQI... | Function: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins . May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50052
Sequence Length: 435
Pathway: Glycolipid biosynthe... |
O13883 | MIPNEKLKLLGLLSISFFLQWYLANTWIAEFLYRRIEVSTPVSGFLRVREGLYLYENGLDPYSGGVFYQSPLLLILNYCCELLGGISVTRFVYTSISTMGGLFVYLIAKQARVLDPNQVLSTCSPLWISVIYLLNPLTFLPGIACSADMILNFTTLMTIYFASCGSYAIYACCMALTVFINPNALLLFFPSYLILRKCNSSIKFRQIFVVFLFYLAGLIITSGFFLNSLSFLKIPFRVYLDSHDLTPNLGLWWYFFTEMFNEFRTFFLFVFAILPLMFVLPVSIRLYYLPLPITIALIGLHSLFKAYPSICDLSIFLSLL... | Function: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46659
Sequence Length: 408
Pathway: Glycolipid biosynthesis; glycosylphosphatidylino... |
O02164 | MRRREPGRDVKRAAEEEFIELERRTDTYEDAVLNEDPQMKGFRFPSILSFPVPNKTIETGVTDENPFSARKSAFFTNRLIGREESDSSSSREDSPLGSTETGESCSTTDDEESKEKRIEYRDSQTQRCLGFCFRQLFFSRMWVFILQFIASYYAGDRFRTDGFNLVDKLIEPGQSVFGDVVVRRGLMGLRRWDAQQFLFIAEHHYIFEHSLAFFAGFPETVNYVRVGVNNGMESVFGWTFPPWVTITLAAVFVNLFCFLLCGMTLYQVVLIMTRSVKISLLAVSIFAFNPASIFFSSAYSESMFFTMTLTGFVFMLFGLR... | Function: Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis (By similarity). Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity). Required for maintenance of epithelial integrity during embryogenesis .
Location Topology:... |
Q9V7W1 | MTEKVTKLALASRLIVLLVQLVANGALPEHKPDVFRMPVSSDQNASWIDKVIKRCLGGLRHWDGEYFLHIAENLYSYENTLAFYPLYPVVVRHVGQAVEAIGISLSQESILLVVAVALNFWLFCESANLLFQLTQVLFNDLNKSWNAALIYCFNPATIFFTAAYSETFFAYSSLHLMLECSKPTGSFRYLRLGTALAACLLCRSNGLITLGYPLYFFGRQLLLKNKEPNTCMQLTQMTLTILGAIGILHTYYFYIYRLYCLPNTRPNHPQHIVDYAVERKYLLSGQGSEGSPWCQYTLPFPYTYVQSHYWDVGFLRYYKW... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly. Required for the GPI-mediated endoplasmic reticulum exit and proper targeting to the cell surface of chp. Required for GPI-mediated ... |
Q9NUD9 | MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYY... | Function: Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
PTM: Not N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55713
Sequence Length: 493
Pat... |
Q54MC0 | MDDQYKNDHQNFVSGNDGSTFFETCFILTLMPISVLFQRVVFATFFNNDKFPLPLALRFILEFFFIIVPFISAITFTELTPFLIVGMLITCLVVPMFAQKNVTIYFKNPKETLLNLNSMRKGFLEEYRAFVMAATCICILAVDFQVFPRRLGKTETYGISLMDIGVGSVVLSGALVSRQSRSSLIEKQQKKKREEEEDDNDKINKTSSSSSSSSSALKQQQQQVLSRSSLMWHQVKAQAPLMILGFVRMILTKSINYQEHVSEYGLHWNFFFTLGFVSISLAFLKFNANISAILGVVLICVYQFLLNSFGLTDYILNHPR... | Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56091
Sequence Length: 492
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellula... |
Q7Z7B1 | MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTDFVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNISLESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAMVCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFFTIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLNANREGIISTLGYVAIHMAGV... | Function: Required for the transport of GPI-anchored proteins to the plasma membrane . Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually rem... |
Q7TSN4 | MSQKQLKEAFVSNLSGTSVLEVTQGLCFPAFCILCRGLLIIFSQHLCSFLHTWTTQFFMDFVVLIVPLVITLTVLSSFILLENLTVILCGAWLLYQIYHRRTCYAKVPVQKVFASFLKISLESEYNPAITCYRVINSVFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFIFGAAMVCPEVRRKYTEGSRFNHLRKSLYSVWPLVFLGMGRLVIIKSIGYQEHSTEYGVHWNFFFTIIVVKLITSLLLIIFPLNKSWIVAISITVLYQLALDFTPLKGIILYGTDGRGTRVGLLNANREGIISTLGYVAIYMAGVQ... | Function: Required for the transport of GPI-anchored proteins to the plasma membrane (By similarity). Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and... |
A3MK86 | MSGERAKRFPLALEDLKREPRKPEGRVAERQAAGDAARQRLTAAAAVPAAASPIVPERRAPHGGVFAAKPARAKQHAPAAPGAAKRAPQGGAKQGDRSAAPNVALSGALALTSERVRERMVERLRANGVADPRVLAAMSAVPRHMFVDPGLAAQAYEDAALPIGHQQTISKPSVVARMIELAAAGRALERVLEIGTGCGYQAAVLSRVARDVYSIERVRPLYERAKLNLRPLRVPNIRLHYGDGRVGLPAAAPFDAIVIAAAGLDVPRALLEQLAIGGRLVAPVGEQAGEQVLTLVERVAPAQWRESRLDRVFFVPLKSG... | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q27873 | MAWRSSGSTNSELIDNLRNNRVFASQRAYDAMKSVDRGDFAPRAPYEDAPQRIGYNATVSAPHMHAAALDYLQNHLVAGAKALDVGSGSGYLTVCMAMMVGRNGTVVGIEHMPQLVELSEKNIRKHHSEQLERGNVIIIEGDGRQGFAEKAPYNAIHVGAASKGVPKALTDQLAEGGRMMIPVEQVDGNQVFMQIDKINGKIEQKIVEHVIYVPLTSREEQWNRN | Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-meth... |
Q9A6T6 | MSGGTTKAAENAKADLPRLMKALRDQGVTDPQVLKAIETTPRDLFTPDLFKDRSWEDSALPIACGQTISQPYIVGLMTQALTVEPRSRVLEIGTGSGYQTTILSKVSRLVYTIERYRTLMKEAEARFNTLGLTNVITKFGDGGEGWAEQAPFDRIMVTAAAEDDPKRLLSQLKPNGVLVAPVGKGPVQSLRRYAGDGKGGFRVEILCDVRFVPLLAGVAKDQ | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q2S176 | MTATPSDDRKYRHQRERLVETLRERGIHDERVLSAVGAVARHAFVDPALRDRAYADEALPIGLNQTISQPFTVAYQTALLGVQPDDRILEVGTGSGFQAAVLCEMGARVYSIERHDDLLRRARSVLDGLGYDVRTRHGDGTRGWPAFAPYDGIVVTAGAPEIPAPLLHQLREPSGEDDGPGGRLVIPIGGREGQTMTRVRRTGSGPHDYEQEEFHSFRFVPLVDEDEGGG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q9URZ1 | MFWSFNLSSNAALVQHLVESKFLTNQRAIKAMNATSRSFYCPLSPYMDSPQSIGYGVTISAPHMHATALQELEPVLQPGCSALDIGSGSGYLVAAMARMVAPNGTVKGIEHIPQLVETSKKNLLKDINHDEVLMEMYKEKRLQINVGDGRMGTSEDEKFDAIHVGASASELPQKLVDQLKSPGKILIPIGTYSQNIYLIEKNEQGKISKRTLFPVRYVPLTDSPDDSSDY | Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-meth... |
P52960 | MYFTDESSPAMNRVGKKRNRLSFVCQACRKAKTKCDQEKPRCGRCTKQNLFCIYDVARQAAPRNPNKDATIARLKKEIRYWRNKTVDLTQEKKDFYTALKRPTEELAARRTCKSLQENSFPISLYKTHPRLIMTKVMKREINPLSEKYLIFQDTFLKTLIASVLLSCSRNSMIPALNADISRSRTQPCVKNNVVKMREVLLKNSKYESQRKSINEFTDRLLQRKNPEEQIAVNKVISLLYSNRESSYLEDTCPTENDYSDLLKGYINEIEKTLPPKAIIEQYLSHFFEHIFHLIPFASKEMLEESIHTTVQYNELGEVRL... | Function: The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (o... |
Q9GZU8 | MDGGDDGNLIIKKRFVSEAELDERRKRRQEEWEKVRKPEDPEECPEEVYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVSRQQELIEKQRREEELKELKEYRNNLKKVGISQENKKEVEKKLTVKPIETKNKFSQAKLLAGAVKHKSSESGNSVKRLKPDPEPDDKNQEPSSCKSLGNTSLSGPSIHCPSAAVCIGILPGLGAYSGSSDSESSSDSEGTINATGKIVSSIFRTNTFLEAP | Function: Promotes the association of the proteasome activator complex subunit PSME3 with the 20S proteasome and regulates its activity. Inhibits PSME3-mediated degradation of some proteasome substrates, probably by affecting their diffusion rate into the catalytic chamber of the proteasome. Also inhibits the interacti... |
Q91WE2 | MDGEDDSNLVIKKRFVSEAELDERRKRRQEEWEKVRKPEDPKECPEEAYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVSRQQELIEKQRREEELEELKEYRSNLNKVGISAENKEVEKKLAVKPIETKNKFSQAKLLAGAVKHKSSESGNSVKRLKPDPDPDDKAQEAPSCMSLGSSSLSGPPSIHCPSAAVCIGILPGLGAYSGSSDSESSSDSEGTINATGKIVSSIFRTNTFLEAP | Function: Promotes the association of the proteasome activator complex subunit PSME3 with the 20S proteasome and regulates its activity. Inhibits PSME3-mediated degradation of some proteasome substrates, probably by affecting their diffusion rate into the catalytic chamber of the proteasome. Also inhibits the interacti... |
Q8ZMM8 | MERSLDSLAGMAKSAFGAGTSAAMRQATSPKTILEYIINFFTCGGIRRRNETQYQELIETMAETLKSTMPDRGAPLPENIILDDMDGCRVEFNLPGENNEAGQVIVRVSKGDHSETREIPLASFEKICRALLFRCEFSLPQDSVILTAQGGMNLKGAVLTGANLTSENLCDADLSGANLEGAVLFMADCEGANFKGANLSGTSLGDSNFKNACLEDSIMCGATLDHANLTGANLQHASLLGCSMIECNCSGANMDHTNLSGATLIRADMSGATLQGATIMAAIMEGAVLTRANLRKASFISTNLDGADLAEANLNNTCFK... | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Involved in the reorganization of late endosome/lysosome (LE/Lys) compartments in mammalian cells. Necessary and sufficient to link kinesin-1 onto the Salmonella-containing vacuole (SCV) membrane. Required... |
A0A6B9HER0 | MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICG... | Function: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative,... |
Q86BJ3 | MSLNAERSYKMKLRDVENAFKYRRIPYPKRSVELIALLAISCTFFLFMHTNKLNSRLKEMEVKLQPSEFSALGLTGNHISGHDAGKHDDINTLHGTYQYLKSTGQKVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDKQLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDFVFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPKPHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPW... | Function: Sulfotransferase involved in dorsoventral axis patterning in early embryos. Required for the specific ventral activation of a series of proteases acting in the perivitelline space between the embryonic membrane and the eggshell. Probably acts by mediating the sulfation of some glycoprotein or glycosaminoglyca... |
Q2HJ54 | MVLLKEYRVILPVSVEEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTLENVHKLEPEAWKHVEVIYIDIADRSQVLSKDYKAEEDPAKYKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEDETKRQLDEMRQKDPVKGMTADD | Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes . Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions (By similarity). Preference order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and f... |
Q00169 | MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD | Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes . Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions . Preference order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and for PI is C16:1 ... |
P53810 | MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVLSKDYKAEEDPAKFKSVKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD | Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes . Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions (By similarity). Preference order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and f... |
Q9TR36 | MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANNPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKKGSVRGTSAADV | Function: Catalyzes the transfer of phosphatidylinositol, phosphatidylcholine and sphingomyelin between membranes . Required for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum; phosphatidylinositol and phosphatidylcholine transfer activity is essential for this function (By similarity).
... |
P48739 | MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKRGSVRGTSAADV | Function: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes . Also catalyzes the transfer of sphingomyelin (By similarity). Required for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum; phosphatidylinositol and phosphatidylcholine transfer activity i... |
Q8ITC9 | MSAGNMSHDLGPPRDPLAIVIPVTVVYSLIFITGVVGNISTCIVIKKNRSMHTATNYYLFSLAISDFLLLLSGVPQEVSYIWSKYPYVFGEYICIGRGLLAETSANATVLTITAFTVERYIAICHPFLGQAMSKLSRAIRIIVLVWIMAIVTAIPQAAQFGIEHYSGVEQCGIVRVIVKHSFQLSTFIFFLAPMSIILVLYLLIGVHLYRSTLVEGPASVARRQQLKSVPSDTILYRYGGSGTAMSFNGGGSGAGTAGLMGGSGAQLSSVRGRLNHYGTRRVLRMLVAVVVCFFLCWAPFHAQRLIAIYAPARGAKLRDQ... | Function: Receptor for the neuropeptide CAP-3/pyrokinin-1 (TGPSASSGLWFGPRL-amide) . Also activated weakly by other neuropeptides terminating in the sequence PRL-amide including pyrokinin-2, Hug-gamma, and ecdysis-triggering-hormone-1 . The activity of this receptor is mediated by G proteins which activate a phosphatidy... |
P34206 | MSRPEQQFKKVLKNPQAQYAVYPTIKVERISTTEHMYFIATKPMFEGGRRNNVFLGHQVGQPVVFKYVSKKEIPGNEVVVMKALQDTPGVIKLIEYTENAMYHILIIEYIPNSIDLLHYHYFKKLEENEAKKIIFQMILIIQNIYEKGFIHGDIKDENLIIDIDQKIIKVIDFGSAVRLNETHPQYNMFGTWEYVCPEFYYYGYYYQLPLTVWTIGMVAVNLFRFRAENFYLNDILKGENYIPDNISETGKQFITDCLTINENKRLSFKGLVSHPWFKGLKKEIQPISELGVDYKNVIT | Function: Essential for viral replication. It may mediate the virus progression through DNA replication.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35112
Sequence Length: 299
Subcellular Location: Virion
EC: 2.7.11.1
|
Q17850 | MKAFSSYDEKPPAPPIRFSSSATRENQVVGLKPLPKEPEATKKKKTMPNPFMKKNKDKKEASEKPVISRPSNFEHTIHVGYDPKTGEFTGMPEAWARLLTDSQISKQEQQQNPQAVLDALKYYTQGESSGQKWLQYDMMFIDDAPSRTPSYGLKPQPYSTSSLPYHGNKIQDPRKMNPMTTSTSSAGYNSKQGVPPTTFSVNENRSSMPPSYAPPPVPHGETPADIVPPAIPDRPARTLSIYTKPKEEEEKIPDLSKGQFGVQARGQKAKKKMTDAEVLTKLRTIVSIGNPDRKYRKVDKIGSGASGSVYTAIEISTEAE... | Cofactor: Divalent cations such as magnesium or manganese.
Function: Required for hypodermal cell fusion, together with cdc-42 and ced-10, leading to embryonic body elongation, which involves dramatic cytoskeletal reorganization . Plays a redundant role with max-2 in dorsal axonal guidance in ventral cord commissural m... |
Q6MAN0 | MPHSFPDYSFTCPFCKNNCKLSFAQCPAFCPFCGKSQKNESTGLPIQSDFYQIIKSIGKGGMGEVFLAYDPCYERQIAIKKIRSDLLEHPQIKKRFLKEAHMTSQLTHPAIIPIYTIRSDADTAYYTMPFVEGDTLKQIIRKTKLQEKNGETLDYLGGSILALMRVFITICQAVAYAHSKGVLHRDLKPENIIIGKYGEVLILDWGLAKFIDQSPEEELLASFPESLTKQKDITKIGKVVGTVAYMAPERALGQPATIQTDIYSLGVILYQLLTLKSPFKRGTLDEFRKNMSREEWQDPVTAAPYREVPRMLASFTEKCL... | Function: Together with the serine/threonine kinase Pkn1, may play a role in the specific interactions with host proteins during intracellular growth.
PTM: Autophosphorylated on serine and threonine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 1133... |
A5U3A3 | MDGTAESREGTQFGPYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRLINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQLGNTVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGMAKNPEDRYVTCGDLSAAAHAALATADQDRATDILRRSQVAKLPVPSTHPVSPGTRWPQPTPWAGGAP... | Function: A serine/threonine-protein kinase, acts on HupB in vitro, modifying at least 2 Ser and 8 Thr residues . Important for bacterial survival in the host during infection (By similarity).
PTM: Autophosphorylated on serine and threonine residues . Dephosphorylated by PstP (By similarity).
Location Topology: Single-... |
A5U3A6 | MPLAEGSTFAGFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDFVDGTDTVSLLRDRYPNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANPDSPDRRIMLADFGIAGWVDDPSGLTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTPLDPVFAKALAKQPKDRYQRCVDFARALGHRLGGAGDPDDTRVSQPVAVAAPAKRSLLRTAVIVPAVLAMLLVM... | Function: A serine/threonine-protein kinase, acts on HupB in vitro.
PTM: Autophosphorylated . Dephosphorylated by PstP (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 50668
Sequence Length: 476
Su... |
P9WI71 | MSDAQDSRVGSMFGPYHLKRLLGRGGMGEVYEAEHTVKEWTVAVKLMTAEFSKDPVFRERMKREARIAGRLQEPHVVPIHDYGEVDGQMFLEMRLVEGTDLDSVLKRFGPLTPPRAVAIITQIASALDAAHADGVMHRDVKPQNILITRDDFAYLVDFGIASATTDEKLTQLGTAVGTWKYMAPERFSNDEVTYRADIYALACVLHECLTGAPPYRADSAGTLVSSHLMGPIPQPSAIRPGIPKAFDAVVARGMAKKPEDRYASAGDLALAAHEALSDPDQDHAADILRRSQESTLPAPPKPVPPPTMPATAMAPRQPPA... | Function: May regulate bacterial growth in response to external signals to facilitate adaptation to the host environment. In vitro, phosphorylates several substrates such as EmbR, DevR (DosR), DacB1 and Rv0681.
PTM: Autophosphorylated on threonine and serine residues. Dephosphorylated by PstP.
Location Topology: Single... |
P65731 | MALASGVTFAGYTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMNEQAGVAIADQSSGGVDASEVTAAAGEEAYVVDYPAYGWPEAVDCKEPSARAPAPAAPTPQRRGSMLQS... | Function: Plays an important role in slowing down the growth of mycobacteria within the infected host.
PTM: Autophosphorylated at serine and threonine residues.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 6180... |
Q53H76 | MPPGPWESCFWVGGLILWLSVGSSGDAPPTPQPKCADFQSANLFEGTDLKVQFLLFVPSNPSCGQLVEGSSDLQNSGFNATLGTKLIIHGFRVLGTKPSWIDTFIRTLLRATNANVIAVDWIYGSTGVYFSAVKNVIKLSLEISLFLNKLLVLGVSESSIHIIGVSLGAHVGGMVGQLFGGQLGQITGLDPAGPEYTRASVEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPTFFYAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGRCLDCFNPFLLSCPRIGLVEQGGVKIEPL... | Function: Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling . Cleaves phosphatidylserines exposed on the outer leaflet ... |
G5EEM9 | MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTEDESEVSTPTAVGLPIGTSTPDGDETPTQPDPNGKYTMAQTKDADLSRPSGLPSNGNPGSSTTVPPASKSGPVAPPRPSGTPVAPQRNRRRKVTELKCSEVRWFFQEPKGTLWNPFNGRDSIMLEIKYRKEKGIELDEAMQEIYDESLTHYKMEMKDEPEIENGNIGMEQEKPMVVVMNGQYKVNKDNSKIDPIYWKDDSKEIRRGSWFSPDYQPLEMPLSDQIEKNHLQCFRNQMIPEGTTVFSKSETSNKPVLAELHVDGYDIRWSSV... | Function: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids, being phosphatidylinositol (PI) its major substrate. PI is a versatile lipid that not only serves as a structural component of cellular membranes, but also plays important roles in signal transduction... |
Q8GT41 | MKLSFSLCIFFFNLLLLLQAVISADIVQGTCKKVAQRSPNVNYDFCVKSLGADPKSHTADLQGLGVISANLAIQHGSKIQTFIGRILKSKVDPALKKYLNDCVGLYADAKSSVQEAIADFKSKDYASANVKMSAALDDSVTCEDGFKEKKGIVSPVTKENKDYVQLTAISLAITKLLGA | Function: Invertase inhibitor (Probable).
PTM: Not glycosylated.
Sequence Mass (Da): 19282
Sequence Length: 179
Subcellular Location: Secreted
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Q9SJI7 | MATTTTSWEELLGSKNWDTILDPLDQSLRELILRCGDFCQATYDAFVNDQNSKYCGASRYGKSSFFDKVMLENASDYEVVNFLYATARVSLPEGLLLQSQSRDSWDRESNWFGYIAVTSDERSKALGRREIYIALRGTSRNYEWVNVLGARPTSADPLLHGPEQDGSGGVVEGTTFDSDSEDEEGCKVMLGWLTIYTSNHPESKFTKLSLRSQLLAKIKELLLKYKDEKPSIVLTGHSLGATEAVLAAYDIAENGSSDDVPVTAIVFGCPQVGNKEFRDEVMSHKNLKILHVRNTIDLLTRYPGGLLGYVDIGINFVIDT... | Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine (PC) at the sn-1 position. High activity toward PC, medium activity toward monogalactosyldiacylglycerol (MGDG) and low activity toward triacylglycerol (TAG). Confers sensitivity to UV-B radiation probably by deesterifying membrane phospholipid... |
Q9XG80 | MPPRSPLLALVFLAAGVLSSATSPPPPPCSRSCAALNCDSVGIRYGKYCGVGWSGCDGEEPCDDLDACCRDHDHCVDKKGLMSVKCHEKFKNCMRKVKKAGKIGFSRKCPYEMAMATMTSGMDMAIMLSQLGTQKLEL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Catalytic Activity: a 1,2-diacy... |
Q9XG81 | MRFFLKLAPRCSVLLLLLLVTASRGLNIGDLLGSTPAKDQGCSRTCESQFCTIAPLLRYGKYCGILYSGCPGERPCDALDACCMVHDHCVDTHNDDYLNTMCNENLLSCIDRVSGATFPGNKCNVGQTASVIRGVIETAVFAGKILHKRDDGQ | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Catalytic Activity: a 1,2-diacy... |
Q10E50 | MARGGSFSRLRLRAGVVVAAAAAALLLFAVVAPPAAALNIGLQSAGDGASKAGLCSRTCESDHCTTPPLLRYGKYCGILYSGCPGEQPCDELDACCMHHDNCVQAKNDYLSTACNEELLECLARLREGSSTFQGNKCMIDEVIDVISLVIEAAVVAGRLLHKP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Catalytic Activity: a 1,2-diacy... |
Q8S8N6 | MAAPIILFSFLLFFSVSVSALNVGVQLIHPSISLTKECSRKCESEFCSVPPFLRYGKYCGLLYSGCPGERPCDGLDSCCMKHDACVQSKNNDYLSQECSQKFINCMNNFSQKKQPTFKGNKCDADEVIDVISIVMEAALIAGKVLKKP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Modulates the trafficking of PI... |
Q8GZB4 | MMFRTSLMRFAAAFFAIVFVVLVGVARSEECTRTCIAQNCDTLSIRYGKYCGIGHSGCPGEEPCDDLDACCKIHDHCVELNGMTNISCHKKFQRCVNRLSKAIKQSKNKKVGFSTKCPYSVVIPTVNQGMDIGILFSQLGNDMKTEL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Regulates the process of cell e... |
Q9M0D7 | MITGLALSRVAFGLTAFLLLAVVSSQEKCSNTCIAQNCNSLGIRYGKYCGIGYFGCPGEPPCDDLDACCMTHDNCVDLKGMTYVNCHKQFKRCVNKLSKSIKHSNGEKIGFSTQCPYSIVIPTVFNGMDYGIFFSGIGNIFNPPVLGSVPVVEVDLARSKVDTKDGLGTKLGLQTKEGSKVSASLNI | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Plays a role in pollen developm... |
Q0V8L6 | MAATPQSLFPSGDDLDSSQLQMEPDEVDTLKEGEDPADRMHPFLAIYHLQPLKLHPLVFAPGVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLLRHKVFMSLLPLARFAVASSPAPEGDSREIPSLPRAGPEGSSRRTASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGCKGLEGVIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVVKDSFLLYMCLETGAISFVQLFDPGFKVQVGKRSTEARYGVRVDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFIQL... | Function: Function as phospholipase selective for phosphatidylcholine. May have a role in signal-induced cytoskeletal regulation and/or endocytosis.
PTM: Phosphorylated by FGR.
Location Topology: Lipid-anchor
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + chol... |
P97813 | MTVTQKNLFPYGDYLNSSQLHMEPDEVDTLREGEDPADRMHPYLAIYDLQPLKAHPLVFAPGVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLQRHKVLMSLLPLARFAVTHSPAREAAAEDIPSLPRGGSEGSARHTASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGSKGLEGVIRKRSGGHRVPGFTFCGRDQVCYRWSKRWLVVKDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTETRYGVRIDTSHRSLILKCSSYRQARWWGQEITELAQGSGRDFLQL... | Function: Function as phospholipase selective for phosphatidylcholine . May have a role in signal-induced cytoskeletal regulation and/or endocytosis .
PTM: Phosphorylated by FGR (By similarity). Phosphorylated on Tyr-11; most likely by EGFR .
Location Topology: Lipid-anchor
Catalytic Activity: a 1,2-diacyl-sn-glycero-3... |
A5D6R3 | MLGRKKNPETVQTESKSVESKTHDPLRRLGVLDDEDVLLMLQGSKMMKVRSQRWRKDRRLKLLEDCVTVWCESSKTSRKSNRQQTFSVTEVECVREGCQSECLRRMTDLVPEKNCFTVVFRGGRKSLDLCCHTQEEAERWVRGIRTLKDRVSNMSQKEKLDHWIRGYLRRADQNQDGKMSYDEVKHLLQLINIDLNEQYARTLFKKCDRSCDGRLDHVEIEEFCREMMRRPELDAVFRHYSGNGCVLTTLELRDFLGDQGEDASLVHAKSLIQTFELNDWAQKNLFMTQNGFTMYMLSKENDVFNPDHTHVYQDMSKPLA... | Cofactor: Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound to the C2 domain.
Function: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC),... |
A0A6S6QPY4 | MLSVDLPSVANLDPRIAAAAAGSAVAVYKLLQLGSRESFLPPGPPTRPVLGNAHLMTKMWLPMQLTEWAREYGEVYSLKLMNRTVIVLNSPKAVRTILDKQGNITGDRPFSPMISRYTEGLNLTVESMDTSVWKTGRKGIHNYLTPSALSGYVPRQEEESVNLMHDLLMDAPNRPIHIRRAMMSLLLHIVYGQPRCESYYGTVIENAYEAATRIGQIAHNGAAVDAFPFLDYIPRGFPGAGWKTIVDEFKDFRNSVYNSLLDGAKKAMDSGIRTGCFAESVIDHPDGRSWLELSNLSGGFLDAGAKTTISYIESCILALI... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties . The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis . GGPP is then substrate of the premutili... |
A0A6S6QP77 | MNLSEIKAALLERNMFAPVAIPVACYLVYKLLRMGSREKTLPPGPPTKPVLGNLHQMPAMNDMHLQLSKWAQEYGGIYSLKIFFKNVVILTDSASVTGILDKLNAKTAERPTGFLPAPIKDDRFLPIALYKSDEFRINHKAFKLLISNDSIDRYAENIETETIVLMKELLAEPKEFFRHLVRTSMSSIVAIAYGERILTSSDPFIPYHEEYLHDFENMMGLRGVHFTALIPWLAKWLPDSLAGWRVMAQGIKDKQLGIFNDFLGRVEKRMEAGIFDGSHMQTILQKKEELGFKDRDLIAYHGGVMIDGGTDTLAMFTRVF... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties . The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis . GGPP is then substrate of the premutili... |
A0A6S6QNE4 | MEGKIVIVTGASHGIGLATVNLLLAAGASVFGVDLAPTPPSVTSEKFKFLQLNICDKDAPAKIVLGSKDAFGSDRIDALLNVAGISDYFQTALTFEDDVWDSVIDVNLAAQVRLMREVLKVMKVQKSGSIVNVVSKLALSGACGGVAYVASKHALLGVTKNTAWMFKDDGIRCNAVAPGSTDTNIRNTTDATKIDYDAFTRAMPVIGVHCNLQTGEGMMSPEPAAQAIFFLASDLSKGMNGVVIPVDNAWSVI | Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties (Ref.1). The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis (Ref.1). GGPP is then substrate of the... |
P37894 | MGRHGGPAAAGPTAPSAVRAKAVNAPSQVFVRIAILAALLLLAVYTAFGVHRLQREAMAQPGGAPLAAKADLIAGRVDANLAAQRAGLSAAADLLKRDPGATMDAAETTLRAAGGEAAAVAVVSEAGVVAVAGRDDGADWKAAALAAGASGRTNWVGSVGETGRLYVATTTSLDRARAFVIASGDASRLVADPEKGESGALALPDGKLIAARGRGVQGAGALREAFALSIEDLGDGPAAVRGQAADGALLDVAVRPVAQGALLAVAAAPTRSVANLDRQVMEGAFSLLVPLGVGIALALLLMIQSRKAEVAHREFIDSER... | Function: Member of the two-component regulatory system involved in the regulation of polar organelle development. PleC functions as a membrane-associated protein kinase that transfers phosphate to the response regulator PleD, leading to its activation.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-ph... |
Q9A5I5 | MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDP... | Function: Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition.
PTM: Phosphorylated by PleC and DivJ. Phosphorylation stimulates cyclase activity (By similarity).
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Sequence Ma... |
Q9WV52 | MEDGVLKEGFLVKRGHIVHNWKARWFILRQNTLLYYKLEGGRRVTPPKGRIVLDGCTITCPCLEYENRPLLIKLKTRTSTEYFLEACSREERDSWAFEITGAIHAGQPGKIQQLHILKNSFKLPPHISLHRIVDKMHDTSTGIRPSPNMEQGSTYKKTFLGSSLVDWLISSNFAASRLEAVTLASMLMEENFLRPVGVRSMGAIRSGDLAEQFLDDSTALYTFAESYKKKVSSKEEISLSTMELSGTVVKQGYLSKQGHKRKNWKVRRFVLRKDPAFLHYYDPSKEENRPVGGFSLRGSLVSALEDNGVPTGVKGNVQGN... | Function: May help orchestrate cytoskeletal arrangement. Contribute to lamellipodia formation. Overexpression of pleckstrin 2 causes large lamellipodia and peripheral ruffle formation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40018
Sequence Length: 353
Subcellular Location: Cell projection
|
Q68WG0 | MKKLSVIFLSVSMLSSIAFCDQDKVVATYKGGEVKESQIMQEFKPQLNLQSGETIKNFDDFPLQDQEKLIKIYVNNLLLKEEVAKSSITSSKEFQEKLENAKNQLAQQELLANYIKSNITDKMFDDEYNKYVDNLKGKEQIKVAHILVKSQKEANTVKTKLSKGGNFNKLAEEFSLDKATASNGGVIGYIILNQSGQLVPEFENKAFALKVNEVSTPVKTDFGWHIIKVLEKKPVPIPTKKEAKVTIDNILAAEILKKYISDLEAKADLKIMLPKANSKTGS | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 31596
Sequence Length: 282
Subcellular Location: Cell outer membrane
EC: 5.2.1.8
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Q55500 | MVAQTPSSPPLWLTIIYLLRWHKPAGRLILMIPALWAVCLAAQGLPPLPLLGTIALGTLATSGLGCVVNDLWDRDIDPQVERTKQRPLAARALSVQVGIGVALVALLCAAGLAFYLTPLSFWLCVAAVPVIVAYPGAKRVFPVPQLVLSIAWGFAVLISWSAVTGDLTDATWVLWGATVFWTLGFDTVYAMADREDDRRIGVNSSALFFGQYVGEAVGIFFALTIGCLFYLGMILMLNPLYWLSLAIAIVGWVIQYIQLSAPTPEPKLYGQIFGQNVIIGFVLLAGMLLGWL | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of plastoquinone-9 (PQ-9) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 4-... |
Q56Y42 | MALTLSTTKTFTNINCSNNTSNITTFKPLKLPLFWPWQKVKMGPLSVSPMGFGTWAWGNQLLWGYQTSMDDQLQQAFELALENGINLFDTADSYGTGRLNGQSERLLGKFIKESQGLKGKQNEVVVATKFAAYPWRLTSGQFVNACRASLDRLQIDQLGIGQLHWSTASYAPLQELVLWDGLVQMYEKGLVRAVGVSNYGPQQLVKIHDYLKTRGVPLCSAQVQFSLLSMGKEQLEIKSICDELGIRLISYSPLGLGMLTGKYSSSKLPTGPRSLLFRQILPGLEPLLLALSEIAKKRGKTMPQVAINWCICKGTVPIPG... | Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+). Involved in the PLP salvage pathway.
Catalytic Activity: NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal
Sequence Mass (Da): 40576
Sequence Length: 365
Pathway: Cofactor degradation; B6 vitamer degradation; pyr... |
Q9U2B7 | MRLLLFILLNTTLLSTNYVHARPSVSHTTLASQFKFAEKADIFVTHTNINEDRTQDEKTIKLSGTFSPVGSNYETGGDIVQVSSFRACDARRKGLDNTVFEHVPVVFYDDVEKFLTGCVALDNQARFAEKSGAMALIVGPASRVERTTRPMMIGGSKIPVIVLDDEQTERLRSELRSASERGAVTKLRISFIDEKPTKVLKLQVFRPTVLNITLLGLLIILIVFVSLLVVVKIRCQPTMHRELWLRALARTALTKMEIRSFQKEKNVEAGQKKKTSSTFARLKQHRSSSSRHSSYLAVFGSLTSVAQSSSHSAQERCVIC... | Function: Probable E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled (By similarity). Acts on both canonical and non-canonical Wnt signaling pathway (By similarity... |
O14295 | MPIVSGFKVGPIGFGLMGLTWKPKQTPDEEAFEVMNYALSQGSNYWDAGEFYGVDPPTSNLDLLARYFEKYPENANKVFLSVKGGLDFKTLVPDGNPDFVSKSVENVIAHLRGTKKLDLFQCARVDPNVPIETTMKTLKGFVDSGKISCVGLSEVSAETIKRAHAVVPIAAVEVEYSLFSRDIETNGIMDICRKLSIPIIAYSPFCRGLLTGRIKTVEDLKEFAKSFPFLEYLDRFSPDVFAKNLPFLQAVEQLAKKFGMTMPEFSLLFIMASGNGLVIPIPGSTSVSRTKSNLNALNKSLSPEQFKEAKEVLSKYPIYG... | Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
PTM: The N-terminus is blocked.
Catalytic Activity: NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal
Sequence Mass (Da): 36815
Sequence Length: 333
Pathway: Cofactor degradation; B6 vitamer degradation; pyridoxa... |
Q06494 | MSVADLKNNIHKLDTGYGLMSLTWRAEPIPQSQAFEAMHRVVELSRERGHKAFFNVGEFYGPDFINLSYVHDFFAKYPDLRKDVVISCKGGADNATLTPRGSHDDVVQSVKNSVSAIGGYIDIFEVARIDTSLCTKGEVYPYESFEALAEMISEGVIGGISLSEVNEEQIRAIHKDWGKFLTCVEVELSLFSNDILHNGIAKTCAELGLSIICYSPLGRGLLTGQLKSNADIPEGDFRKSLKRFSDESLKKNLTLVRFLQEEIVDKRPQNNSITLAQLALGWVKHWNKVPEYSGAKFIPIPSGSSISKVNENFDEQKTKL... | Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Catalytic Activity: NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal
Sequence Mass (Da): 38601
Sequence Length: 345
Pathway: Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (dehydrogenase... |
Q9D3P8 | MGFIFSKSMNENMKNQQEFMVTHARLQLERHLTMQNEMRERQMAMQIAWSREFLKYFGTFFGIATISLATGALKRKKPAFLVPIVPLSFIFTYQYDLGYGTLLQRMKSEAEDILETEKTKLELPKGLITFESLEKARREQSKLFSDK | Function: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator-dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing.... |
P05402 | MAPAPSFRGHQWTYNPVRGSCLLLLLLMSNLLLCQGKSCPSCGPDVFVSLRKSFTDRFMNAASLSHDFYNLSTIMFNEFDEKYAQGKLYYINVTKSCHTNSFHAPEERDIVQQTNIEDLSKWTLVLLYSWNNPLHHLVTELQHMKELSNAFLSSATRFENMSEKLQAFIERQFSKIIVPVLNTMIQARSSWTGLPSLMSSDEDRRHSEFYNLFYCLRRDSRKVDMYIKILTCRTHKTC | Function: Placental prolactin-related proteins may play a specific role during gestation.
PTM: N-Glycosylated; the glycans terminate in either N-acetyl-galactosamine (GalNAc) or N-acetyllactosamine . Terminal GalNAc on Asn-linked glycans is greatly reduced prior to parturition while lactosamine-type N-glycans remain un... |
A3DDZ2 | MIILVDAMGGDNAPEAIVNGCLDAVSEADGFEILLIGDEGKIREILNKRSYDTSRIKIHHASEVITVEDTPTKAIKTKKDSSMVVGFKLLKEKKGDIFLSCGNSGALMTGALFILGRIKGVDRPAIGAIVPTKAGKGLIIDAGLNTVCKPVNYQQFGIMGSIYMKEMLGIENPKVGLLNIGAEVGKGNETLKQAYSLLSESNINFVGNVEGNDVALGKVDVVVCDGFTGNVLLKFYEGAGSYFYNLIKGIMLKNLKTKMAALMLKKDMKVLKKIMDADENGGAPILGVDGLVFKSHGSSNARTVKNVIIKASKFAETKAL... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36482
Sequence Length: 339... |
A9NES3 | MIKLAIDGMGGDNAPKEIVEGSILALKQFDDIELTIFGDVDKMKPYLIEHPRLKVVHTPKYFEMGVKDIGRHTLRDDKDTSMLMAINHVKEGLADGVVSSGPTQALIFASFFMIRPMKEMKRVAIAPMVPTVIGKPTILLDAGGNIDAKAEHLLDFAIFSTIALKEVYGVKSPKVGLINIGTEPGKGRDIDKETFELLSKHPLIDFYGNLEPKEILTSDAQILLSDGFTANIVMKTMEGTASALGKILKREIKASFWGKLAAVLFLKKPLKRFKQSMSADEVGGALIAGLDKVVVKAHGSSEAYAFMNAIRQAKTMVSHD... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36477
Sequence Length: 334... |
C1F8B4 | MLTDIALDAWGSDKAPEPEIKGAILACRHLPVRVHLVGQQDVLEPLLAQALRGARLPIEIVHASERIAMDEKAAQAVRTKRDSSMRVGLKLVREKKVAGFFTAGNTGAAMATAKMVLGALPGVDRPALALAVPTLTGPTILLDVGANTDCKAHNLEQFAVMGEMYARKVLKVDRPRVGILSVGEEEGKGNDLTREAFPLIKALPLNFIGNVEGRDIYNGHCDVIVCDGFVGNVALKTSEGILKLVREMLKISLKSTVTAQVGALLSRRAFDEFKRRLDPSEYGGTPLLGVRGVCIIGHGSSNDRAIMNGIRVAAEFATAG... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35956
Sequence Length: 337... |
B2UMF9 | MKIALDVMGGDNAPDINVDGAKRALQDFPLIEKIYLVGREETVRSSCDRWGLSGPRVEIVPAAEVVEMNESGLLAVRKKKNSSMSISVDLVKSGDADAVVSAGNTGAAVAAATVKLRLLDGVERAGIVTQLPNEFGVCNVTDTGANPDAKPRHLVGYAVMASILARSVYGKQMPKVGVMSNGSEDEKGTDFTKGTFCLLKHLEERGALPFKFVGNVEGHDLFEHEIDVALTDGFTGNVLLKTCEATAKAFSKWLKEELKANPFRMVGAACASGAFRAMKARLSADSVGGSPLLGVRGVTIIAHGSSTPVAIRNALRVSME... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37055
Sequence Length: 349... |
Q88WK2 | MIKIAIDAMGGDYAPNAVIEGVEQARDLFEDTVFLLYGQRDVINAQLKNRDRIQIINADEVITMEDEPVRAVRRKKHSSIVMAAQAVKDGQADAFFSAGNSGAVLAAGLFIVGRIKGIDRPGLVTVLPVVRNANQSNFVMMDIGANADSKPLNLQQYGVLGTYYAERMMQAKHPRVALLNNGTEDDKGNKVHKAAFELLSQTDGINFVGNVESRDLLNGVADVVVTDGFTGNAVLKSIEGTARSMLGLVKDAVYNTGISGKLGGLLLKNGFNEIRSQMDYSQYGGAVLLGLKAPVVKTHGSSKAPTIVNTIRQIRQMVST... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37409
Sequence Length: 348... |
C1DCE9 | MTLTVAVDAMGGDVGVGVTVPAAVDFLDRHPDVRLILVGQPDAIEDELTRLARPRSGRLTVHAASQVVAMDDSPQSALKNKKDSSMRVAINLVKEGQAQAAVSAGNTGALMATARFVLKTIPGIDRPAIAKLLPTMKGESCVLDLGANVDCTPEQLLQFGIMGATLIEGVTGRNNPTVGLLNIGSEEIKGNDTVKQAAELLRNSSLNFYGNVEGNDIYLGTVDVIVTDGFTGNVALKTSEGLAHMVGALLKQEFGRNLFTRLSALAALPVLKHFKKRLDSPALQWRQSGRPARHRGQEPRRHRQPRFWLCHRRGRRRSPR... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36617
Sequence Length: 340... |
B0SM41 | MWVAVDAMSGDYGPEGIVEGAVLAVREFGLSVSLVGDEQELLDILLKFDYDTEKIRVIHSTEIIGMNDSPSIAVRAMEDSSVVKAVRLVADKECIGVFSPGNTGATMAAALLHLGRLPGVLRPPIAAPIPREEGPPVILLDAGANVDCKPEYLAQFAIMGEIYSRELFGVKNPKVGILSNGEEDKKGNTVSVKTFDLLKKIPFNFVGNVEGRDLYGSGRDVDVVVCDGFIGNIVLKATEGLAKSIFNVLRNSIRQSSLAQTGALLLKSTFTAVKKRLDYAEYGGALLLGVEGICMIGHGSSNALAVKNAVRVISECAKHQ... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36476
Sequence Length: 340... |
Q67PG1 | MGFRIAVDAMGSDAAPAPEVSGTIQAAREWPDLRFVLLGDDSRIRAEAEKAGGLPGNVEVVHTTQVITPDEEPTKAVRSKKDAPLTVAARLVKEGQADALLSAGSTGALVVVGTLGIGRMKGIDRPALGTIMPTVKQPVFMLDVGATPDARPEWLVQFALMGDIYAREILGLSRPRVALLSNGTEAEKGNAVVKATYPLLQELPSIHFIGNIEARDVPFGGADVVVADGFPGNVLLKTYEGVAMALFQSLKEALTGSPLTAVGAALAKPGLKKMAKRFDYTEYGGALLLGLKAPVVKCHGSSNARAIYSGLRVMKLALEG... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36332
Sequence Length: 346... |
A0LI09 | MKIAVDAMGGDHAPEALIEGALLAGPQCSADILVIGNEARLSSLLAHSGDSTSLKVVHAPQVIGMGEAGPMALRRKREASLTIAMRLLAENEVDAVVSAGNSSAVVSAARHLVGLIPGLRRPAMAVPLPTPSGKLLLLDAGAHAEATAIHLAQSAVLAHCYLKIEEGLNRPRIGLLNIGHEPAKGNRAVQRAFALLRRCSLEFTGNVEPNDLFAGKVDAVICDGFVGNVLLKMYEGFSETVCRFLESLANHDGRDFSGGAGRILERFRRDYHYEFVGGAPLLGIRKTVVAAHGRSRATAIANAIRLACRLQEARVFERLA... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37771
Sequence Length: 353... |
Q2GI73 | MNIHAVVIVLSYLIGSIPFGLILSYIGGLGDIRKVGSGNIGATNVFRKSKKLAVMTLLLDAVKGLISVLLAKIYSTDQTFAFISAMFSIIGHMFPVWLLFKGGKGISTLLGSMVLIEYKFVICFLFIWITLFAIFKYSSLSSIVSTIFVALLVYMYYTMNDTAVFIAMSLLIITQHADNIARMLSGKENKLNIGL | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
B1GZE4 | MLIKILYIIITYLCGSIPSAYIVAKANGKVDIRTVGSGNSGATNVFREIGKCAGVITLIADILKGFIPVYFATFIDNSFSYSVAVAAAAMVGHVFTIFLKFKGGKGVATGLGVFFALMRWPSLIALAIFGLAFVFSRYVSLGSICAVISLPLTSYFLGYSTEVVIFTFAITLLIIYRHRTNIKRLIERSENKLRIFKKK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q834K7 | MKIVILLLVAYLLGSIPSGVWIGKLFFKKDIRQFGSGNTGTTNTFRVLGKPAGITVLLMDILKGTLATSLPYLFGLQGVNPLFFGVAAVLGHTFPIFANFKGGKAVATSAGMLLAYSPTFFIYSALIFVICLYLTSMVSLTSMISAVLITLSTIILPFTVPAILPTFNWLLTVIAIALTTFIFVRHRENIQRIKNGTESRLSFGLRAKKIKKKAVNK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q2NB90 | MDYNLDPSIAALIGYAFGSIPFGLLLTRMAGMGDVRSIGSGNIGATNVLRTGNKGLAALTLVLDLVKGFVPVWIAWRYFQNDIGWAALGAVVGHCFPIWLGFKGGKGVATNAGVCFGLGWGIGLAYAFVWLVMLAITRISSVAGMSAVVAAAGAAWYFGRPTFVPPLVIIAVIIIWLHRANIRRLLRGEEPRVGNKP | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
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