wanglab/gogpt-training-data huggingface dataset:
Protein: Aldehyde dehydrogenase 1A1 (EC 1.2.1.19) (EC 1.2.1.28) (EC 1.2.1.3) (EC 1.2.1.36) (3-deoxyglucosone dehydrogenase) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) (Retinal dehydrogenase 1) (RALDH 1) (RalDH1) (P00352)
Organism: Homo sapiens (Human)
Function: Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid. Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (By similarity). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins. Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12941160}. Cell projection, axon {ECO:0000250|UniProtKB:P24549}.
Interaction partners:
- Retinol dehydrogenase 12
- Retinol dehydrogenase 10
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Dehydrogenase/reductase SDR family member 4
- Alcohol dehydrogenase 1A
- Cytochrome P450 26C1
- Aldehyde oxidase
- Retinol dehydrogenase 11
- Short-chain dehydrogenase/reductase 3
Sequence:
MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS
Protein: V-type proton ATPase proteolipid subunit (Q6P041)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029431}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00029431}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004644}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004644}. Vacuole membrane {ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363060}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit H
- ATP synthase F
- V-type proton ATPase subunit a
- H
- ATPase H+-transporting V1 subunit E1b.
- ATP synthase subunit alpha
Sequence:
MSSGSPEYSPFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSISDKITLYKSFLHLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4J982)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/arginine-rich splicing factor RS31
- Aluminum induced protein with YGL and LRDR motifs
- Cell division cycle 5-like protein
- Peptidyl-prolyl cis-trans isomerase CYP63
- At5g46870 family protein)
- F-box protein At2g32560
Sequence:
MEAEKWNSDGGEYTSEDEGTEDYRRGGYHAVRIGDSFKTGRYVVQSKLGWGHFSTVWLSWDTQSSRYVALKVQKSAQHYTEAAMDEITILQQIAEGDTDDTKCVVKLLDHFKHSGPNGQHVCMVFEYLGDNLLTLIKYSDYRGLPIPMVKEICYHMLVGLDYLHKQLSIIHTDLKPENVLLPSTIDPSKDPRKSGAPLVLPTDKDNTVVDSNGDFVKNQKTGSHRKAKLSAQGHAENKGNTESDKVRGVGSPVNGKQCAAEKSVEEDCPSTSDAIELDGSEKGKQGGKKGSRSSRRHLVASADLKCKLVDFGNACWTYKQFTSDIQTRQYRCPEVILGSKYSTSADLWSFACICFELVTGDVLFDPHSGDNYDRDEDHLALMMELLGMMPRKIALGGRYSRDFFNRHGDLRHIRRLRFWPMNKVLTEKYEFSEQDANDLSDFLVSILDFVPEKRPTAAQCLLHPWINSGPRSIKPSLKDENSDKLDTEKNKRENEEQEAVEVKMGNVVISSLDSKPGMSQSSSTLKLAI
Protein: GH09541p (Q8SXC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRQQQQQQQQQSMDQIDRAGTLPRYGYSSLQQQAENQGRRMGSTFLQKSHQFVDDVSREIRSSASNGIRPGFKRAPSEGSSQQPQAFRDESRVSQYVPELPNTEPVNAHLSRDELAQRQPLFITPLKDIAVGVGGTARFECIVQAHPQPQVNWTHNGGLLESGSRHCIEYRNGVCRLTLPQAYPDDNGSYACTAINPLGAATTSGNLTVSSTNRGFRY
Protein: FAD-binding monooxygenase ausB (EC 1.14.13.-) (Austinoid biosynthesis clusters protein B) (Q5ATK1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methyltransferase ausD
- Terpene cyclase ausL
- Multifunctional dioxygenase ausE
- Polyprenyl transferase ausN
Sequence:
MAKLYYMPYIFNEGMPLASGPPTLPEDFTPEKSGFRVLVEVRRMKGHFPAQKWRKRNQEWQCINNETLLPDHVRNGHLAKNVPYRPYRPVYVPFAMTVSPTTDAMGTSEETRSKQTKGSNDDILSAKIAGRVARPVYHCTSARLHDLAYDPWPITTIDTHGLSSLKAPSTHTRILIIGAGFGGLLFAVRLLQAGFSRDDLLLVDSAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETGHMPSRKYVPGEELRTHAEGIAAKWELEQRALFRTTIRTLEWDEGGNQWIAHAEQLGVFTDAKQGGNGGGGPLTFTATFAIIASGTLSKPKVPNLHGVDDFQGHIFHTARWDYDYTGGSPANPAMHRLQGKRVGVIGTGSTAVQVIPQLARWSKELIVFQRTPAAVGLQKNQVTDPVWWKGNILKAGSGWQRKRSENFNAFISISNPPCMENLVNDGWTSSPSFSAAIGGALNMQPDFLDLVKAIDRPRLEAAQDHIRSTVRDDTTAEALINLNHGWCKRPCFHQGYFETYNLPHVRLIKTDAAGVTGLSPKGILVGDTLYEVDLVVLATGYDLGSLCPADRAQIQVLGSEGVAMKEKWAGGPTTLHGVMTRGFPNLFFPGTSQAGVTANQSYMFDRAAEHVAYIIQNSTLEAGGYIDKIRIEPTAEGEKHWTTQSVARISAFAATTACGTGDYTISNRYRSSDVDTMARHMPWGEGMASYVKILEAWRESGTMEGLDIRYHSSEGSR
Protein: DNA helicase (EC 3.6.4.12) (A0A1D8PF81)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATP-dependent DNA helicase II subunit 2
- DNA ligase 4
- Double-strand break repair protein
- DNA repair protein RAD50
- Serine/threonine-protein kinase TOR
- Pso2p
- Chromatin-binding protein
- DNA ligase
- Serine/threonine-protein kinase TEL1
- DNA repair and recombination protein RAD52
Sequence:
MSWHNQSNKNSNNDDEYGNKNFKQYEIKEGIAFLIEITPELLIPQSNLNSHSQLFEILSSINDLMQELIITSRSTGIGIYFYNCAKSNKLSSMKNTNCTGFERLFHLNVLNLQNMKKLNDLIQDDINNIKSIDEIFKYQPLKKIDLKVGKQSHSETQTQTQTQTQSSHTIQETQLTVVLNKMIDEFINKREFNKRRMVWITTNDKPYHEESEREALWRTIDDFYYYGFFIEPLFLSTNEQKPFDFELYKDIFMNTNYLKKSQENSESLRHTAHANYDNNDGNLGDDNNNDDDKNLIKPSGGFSKDSIIFKKSVVGDQIRKSIFRIKEVRRIQFTCDLILSDNGKIGGGFGCTVKGYMLYSHEKINRNELLLYTRSETLKRVFSSSKLMQNGKAIEIAKDTGKSYQDRKEEAGIRKGFEIGGGQDIIILNKQQLEFLTNYSFDHRLKDSDDEDNEDGNDSLETDISDDDDEEGGAGGTGGETKPVSFSKPPYLKLIGFRDISHFSPVYSCGAPIFVTPDVDNGMISSAVTGGFTNSFKTFASLYRSCVKLNQYAIVLGCTRSNSRPRLYALYPTHTTNSSKNPLPKNLDDEVDNDDNQDEFPQGFLLIKLPWLEDVRALPGEYIKNTQREEIHNDDTLIDNFKQLLPKFELSHYDPREFPNASLNYFYKVIKHEILQMELKPSQRPLMENDITMQKLAQLKNSINNDDTAIELLQKINSRMNEIDATVGAEVLKRKQMEDMQNNNSNNGGKRFKSGPVSDQEILDAWENNQLDRFSVDQLKAFRRKYPDVKSANKKADLIENISEFIRTHRK
Protein: GTP-binding protein GEM (GTP-binding mitogen-induced T-cell protein) (RAS-like protein KIR) (P55041)
Organism: Mus musculus (Mouse)
Function: Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- T-cell surface glycoprotein YE1/48
- Kelch-like ECH-associated protein 1
Sequence:
MTLNNVTMRQGTVGMQPQQRWSIPADARHLMVQKDPHPCNLRNRHSTAPEEHCRRSWSSDSTDSVISSESGNTYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMWENKGENEWLHDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL
Protein: Nickel-responsive regulator (P0A6Z6)
Organism: Escherichia coli (strain K12)
Function: Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel.
Interaction partners:
- Nickel-binding periplasmic protein
- Nickel import ATP-binding protein NikD
- Nickel transport system permease protein NikC
- Nickel import ATP-binding protein NikE
- Nickel transport system permease protein NikB
- Nickel/cobalt efflux system RcnA
- Transcriptional repressor RcnR
- Arsenical resistance operon repressor
- HTH-type transcriptional regulator ZntR
- HTH-type transcriptional regulator CueR
Sequence:
MQRVTITLDDDLLETLDSLSQRRGYNNRSEAIRDILRSALAQEATQQHGTQGFAVLSYVYEHEKRDLASRIVSTQHHHHDLSVATLHVHINHDDCLEIAVLKGDMGDVQHFADDVIAQRGVRHGHLQCLPKED
Protein: Integrin alpha 3 protein (Integrin alpha-3b precursor) (D7PS99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MAGKSLHLCVFVICAIQTNTGFNIDVQFPVIKEGKTKGSLFGFSVALHKQTEKAKKNLLLVGAPQEKAQPQLSKFKINETGAVYYCPITVNLDDCGSMDLISPPKSTDMLEGMWLGVTVASQRNGGRVLACGHRYVKKLLGAEEQQRMVGKCYVRGNDLSYDPSDYWQSETYELCDFNHDQDLEGMCNMGISGGMTEKDVYFGTPGSFTWQGTVHMKCRDTDSDYAGDANDRSFGKLGEDKFNIYIGYSVLEDIKLLDRSVFTVVMGAPRDEFKGSVILADKQDLILKQLMNITGEQIGSYFGSCLAVTDLNNDDWNDLIVGAPFYFDRYKEEGGAVYIFMNENGSFQKKASLVLKGKKGSGFGFAIAAVGDVNQDGFQDIAVGAPFQDSGKVYIWMGSKSGITKEPSQVIEGKSLGPSGFQTFGYSLSGGMDMDGNDYPDILVGSLDDRIALLRSRPVIHLSKNFTVEPKIVIPSQCGNSCIKVKVCFSYTLSNGNSNFRKEITVKFTIDADQNRRGARVRFIDNKQSTFTGLLSFSASSCQELELSVNNPVTDKLQPIVFSLNVSLNQQKAEAQQTLQSLDSFPVLSGQQILTDKAEINFHKECGDDNRCSSNLQLKARFADENYNPFPSQTLEFSSNVKKLVLMVEVSNTADENKPAEDAHQATLNISIPYSLKYSGVRPPAGFDMECSADEAVICDLGNPFKSNQKVSFIIIFETSGITLYTEQIQSQLQLSTISEQADLFPVLVTLNVKNTILTTFSLEKLIIDTSFSGNVIGESAMSSTSDVGSPLEFVFRVQVLGEPLGDLGTLVIDFDWPYAVANGKWLLYLTEIVIKGSSESHCVPPGNIVNYLNLTLSKEGTKRNKREVDSGFPHAEASVTVLATRKVAHFLDCSKKTALCQTFSCPLLNMSTQAEVRVRARVWNGTLLEDYAKALRVEVKGQATLRLLTDKPAIKMDNQTREFSVNIDPVLGEETPYEVPLWIIIVAAVAGILLLGIISLILWKCGFFRRASRREMYEAKSQKAEIKIQPSETERLTEEF
Protein: Ribonuclease VapC30 (RNase VapC30) (EC 3.1.-.-) (Toxin VapC30) (P9WF77)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB30.
Interaction partners:
- Antitoxin VapB30
- Putative antitoxin VapB34
- Ribonuclease VapC15
- Antitoxin VapB2
- Antitoxin ParD1
- Ribonuclease VapC5
- Putative antitoxin HigA3
- Ribonuclease VapC2
- Ribonuclease VapC3
- Ribonuclease VapC4
Sequence:
MVIDTSALVAMLSDEPDAERFEAAVEADHIRLMSTASYLETALVIEARFGEPGGRELDLWLHRAAVDLVAVHADQADAARAAYRTYGKGRHRAGLNYGDCFSYGLAKISGQPLLFKGEDFQHTDIATVALP
Protein: V-set and transmembrane domain-containing protein 2-like protein (Q96N03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGAPLAVALGALHYLALFLQLGGATRPAGHAPWDNHVSGHALFTETPHDMTARTGEDVEMACSFRGSGSPSYSLEIQWWYVRSHRDWTDKQAWASNQLKASQQEDAGKEATKISVVKVVGSNISHKLRLSRVKPTDEGTYECRVIDFSDGKARHHKVKAYLRVQPGENSVLHLPEAPPAAPAPPPPKPGKELRKRSVDQEACSL
Protein: PRA1 family protein A1 (AtPRA1.A1) (Q9LZM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- PRA1 family protein C
- PRA1 family protein G1
- PRA1 family protein H
- PRA1 family protein B5
- PRA1 family protein E
- PRA1 family protein G2
- PRA1 family protein B1
- PRA1 family protein F3
- PRA1 family protein B4
- PRA1 family protein F4
Sequence:
MDWGNVTVDDLFDALREVDWSSPPRPPSEFFSRFTVPKSVPKWDSRLKCNLYYYRTNYFIMIVVILGLGVLTRPLAIFAALLTALSLAFLNDSFAGSFSEKATRTVRRFSPQLAAKMRPPLTPVTRGRPSSKRAIHVCGQPRWVFVLTCSLVSFALWYISSGLLRVSVALLIAHLATILHASLRTPNLKARFNTFREEFRAVWRNYSEI
Protein: Neuronal acetylcholine receptor subunit alpha-5 (P30532)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P32297}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P32297}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Proteasome subunit alpha type-4
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-4
- Cytochrome P450 2A6
- Hydroxylysine kinase
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-10
- Acetylcholine receptor subunit alpha
Sequence:
MAARGSGPRALRLLLLVQLVAGRCGLAGAAGGAQRGLSEPSSIAKHEDSLLKDLFQDYERWVRPVEHLNDKIKIKFGLAISQLVDVDEKNQLMTTNVWLKQEWIDVKLRWNPDDYGGIKVIRVPSDSVWTPDIVLFDNADGRFEGTSTKTVIRYNGTVTWTPPANYKSSCTIDVTFFPFDLQNCSMKFGSWTYDGSQVDIILEDQDVDKRDFFDNGEWEIVSATGSKGNRTDSCCWYPYVTYSFVIKRLPLFYTLFLIIPCIGLSFLTVLVFYLPSNEGEKICLCTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLVFTMIFVTLSIMVTVFAINIHHRSSSTHNAMAPLVRKIFLHTLPKLLCMRSHVDRYFTQKEETESGSGPKSSRNTLEAALDSIRYITRHIMKENDVREVVEDWKFIAQVLDRMFLWTFLFVSIVGSLGLFVPVIYKWANILIPVHIGNANK
Protein: Optomotor-blind-related gene-1 protein (O62535)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MTHLMGPTECAGAMMTTTSMQFLDTSLTDYNCYGNDYWTSPYMTGGLSPMKQIEACIQTAGKDRSSYKPLEQIDAKLADIETHSTGSTGTANSNSSTSSISNPSCPDQSSSSSSSSVSLPTDYAGVHSEASMAPTAGGTAVTTTSAGGVSASTASKKFKGQHKKDNNSAENGTVKPNSHNISKGESEPVHPSLAQAIVVLETKALWDQFHAQGTEMIITKTGRRMFPTFQVRIGGLDPHATYICMMDFVPMDDKRYRYAFHNSCWVVAGKADPISPPRIHVHPDSPAVGSNWMKQIVSFDKLKLTNNQLDENGHIILNSMHRYQPRFHLVYLPPKNASLDENEHSSHFRTFIFPETSFTAVTAYQNQRVTQLKISSNPFAKGFRDDGTNDVTTGGGSSMSSMSHESQARMKQQQQQQQQQQQQQQLQQQQQQQQQLKERTAATSNFGLSCSELAIEQQQQQQQQQGVLQLPATPSSSSTSGNSPDLLGYQMEQQLQQQHQQQQQQQHQSQQQHLHQQHQANQQQSLLQQSQNHTQYGSYHHAYQAQVQSHPLTPHSSSSASPPATAAPGASAATAAVAAAAAAAAAVAGGGAGAAGAGGATSATQVMSAANIYSSIGQPYAQEQSNFGAIYHHNAAAAAAAHYHHGHAHGHAHSHAHAHAHGPYASAYDKLKVSRHAAAAAYGMGATYPSFYGSAAHHQMMRPNSYIDLVPR
Protein: Transcription factor TCP8 (Q9C518)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Can specifically bind site II elements in the promoter region of PP438/PNM1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Small ribosomal subunit protein mL104
- Suppressor of RPS4-RLD 1
- Transcription factor TCP13
- Transcription factor TCP3
- Transcription factor TCP5
- Mediator of RNA polymerase II transcription subunit 14
- Transcription factor TCP4
- Transcription factor TCP15
- Mediator of RNA polymerase II transcription subunit 6
- WRKY transcription factor 28
Sequence:
MDLSDIRNNNNDTAAVATGGGARQLVDASLSIVPRSTPPEDSTLATTSSTATATTTKRSTKDRHTKVDGRGRRIRMPALCAARVFQLTRELGHKSDGETIEWLLQQAEPAIVAATGTGTIPANFSTLSVSLRSSGSTLSAPPSKSVPLYGALGLTHHQYDEQGGGGVFAAHTSPLLGFHHQLQHHQNQNQNQDPVETIPEGENFSRKRYRSVDLSKENDDRKQNENKSLKESETSGPTAAPMWAVAPPSRSGAGNTFWMLPVPTTAGNQMESSSNNNTAAGHRAPPMWPFVNSAGGGAGGGGGAATHFMAGTGFSFPMDQYRGSPLQLGSFLAQPQPTQNLGLSMPDSNLGMLAALNSAYSRGGNANANAEQANNAVEHQEKQQQSDHDDDSREENSNSSE
Protein: Glycosyl transferase (Serotype 016 putative O-antigen biosynthesis gene cluster, partial sequence) (Serotype 018 putative O-antigen biosynthesis gene cluster, partial sequence) (Serotype 02 putative O-antigen biosynthesis gene cluster, partial sequence) (Serotype 020 putative O-antigen biosynthesis gene cluster, partial sequence) (WbpL) (Q7B798)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MMIWMIACLVVLLFSFVATWGLRRYALATKLMDVPNARSSHSQPTPRGGGVAIVLVFLAALVWMLSAGSISGGWGGAMLGAGSGVALLGFLDDHGHIAARWRLLGHFSAAIWILLWTGGFPPLDVVGHAVDLGWLGHVLAVFYLVWVLNLYNFMDGIDGIASVEAIGVCVGGALIYWLTGHVAMVGIPLLLACAVAGFLIWNFPPARIFMGDAGSGFLGMVIGALAIQAAWTAPSLFWCWLILLGVFIVDATYTLIRRIARGEKFYEAHRSHAYQFASRRYASHLRVTLGVLAINTLWLLPLALMVALGWISGFIGILVAYAPLCLLAVGYKAGSLEKS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VRJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable tRNA N6-adenosine threonylcarbamoyltransferase
- L antigen family member 3
- Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- P53, isoform B
Sequence:
MSLEILKQGAEGRLYLGDFKGEACLIKERFVKKYRHPELNTQITRQRMKAEAKASGRCLAAGILAPKILHSDLNTHKLYMEYFDAAKTAKQFIQETVSTQTEDEAKKCLLEFCTRIGEIIGKMHSNHIIHGDLTTSNILINPKGGDYDVILIDFGLSHYNQATEDKGVDLYVLERALLSTHSEQPYIFEHVLAAYRTACGKDEQAVLTKFEEVRARGRKRTMIG
Protein: Phosphomevalonate kinase (EC 2.7.4.2) (Q9UT88)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg8 converts 5-phosphomevalonate to 5-diphosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mevalonate kinase
- Diphosphomevalonate decarboxylase
- Pre-mRNA-splicing factor dre4
- Uncharacterized protein C1782.03
- Acetyl-CoA acetyltransferase
- Lanosterol synthase erg7
- Squalene synthase
- Squalene epoxidase erg1
- Ferrochelatase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase
Sequence:
MKVTCSAPGKVLIAGGYIVLDPQYSGLVIGLTAKGYASTTTLDDKCGTVRVKSPQFINAEWLYNIDWTVSPIRVHQIYENCELEKNPNPFVQLALFYVINYFFSTGRQPLCWQDLQVTLQVDNAYYHQPQLKPDQTSYPKFNFLNCTLGQVHKTGLGSSAAMITSLIGSLFLSLRRLTDDTGDKSLKIDDSTKVIVHNLAQIAHCSAQGKVGSGFDVGAATWGSCIYRRFDPKLIEQLLVPYDEQIKNINFSTELRKIVSKKWSDVVPFQLPATYCLLMGDVAGGSSTPGMVKKVQQWQKENPEESKNCFDDLYSRVLSIKNCFLSSESLDSELQSQFRSIRRILQRITVEAKVDIEPLKQTNILDNIEQLPGVIGVGVPGAGGFDAQFCLAINHTEIIENVIKTWKDDGVVPMDVSPAFDGLAVE
Protein: Arf GTPase activating protein (Q54DK9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Arf GTPase activating protein
- Coatomer subunit beta'
- Coatomer subunit gamma
- Coatomer subunit beta
- Coatomer subunit delta
- Coatomer subunit alpha
Sequence:
MEPILSAEETTQFFSKFINKTENKECFDCRARGPTWTSIPFGVFICFDCSSIHRNMGTHITFVRSIKLDRWKMSQLKYMELGGNQVAKQYFQEHGGDIRDTESKYQSQVGINYKQILDARVKKALKEISPFSSTSSTPLQAPTTPSPLSISTINSNPSTTTSSPMFSTNSSSSSGSGILQSKQQQQQQQQQSPTTSFSDKKVSSQQKSTTTTTTTTKNDSDDFDSFFSSSPPKSTSTKKVATKKIDQKSFDDDWDSLPDKKEEKFDNNNNNNNNNNYKNNKKKGGSSFKFNNEYIENDEDESDSNNRSDLSPELRSLYTSSKFSMDFSVDQTSNKQDSSSPLYSQKYNNSNNSNNNNNNNNNNNNNNNNNNNNSYNNNNNNNNKNYSNNSNNNSYNNNNRSPNNQSPRNNNENKNYQHQNETDYARKNFTNAKSISSSTYYGEDKEKVDSDKQQRISKFTNSKSISSAQYYDRDETPSFSERSASNIARDLAYNARSDLTSISNKISNIANNIINDLQDRYN
Protein: RNA polymerase sigma-like factor (Gene product 55) (gp55) (Promoter specificity factor) (P04524)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Plays a role in the transcription of the viral late genes by acting as a late promoter recognition subunit. Associates with host RNA polymerase (RNAP) core and thus replaces the host sigma-70/rpoD subunit in the complex. May also play a role in DNA packaging by interacting with the terminase subunit gp17.
Interaction partners:
Sequence:
MSETKPKYNYVNNKELLQAIIDWKTELANNKDPNKVVRQNDTIGLAIMLIAEGLSKRFNFSGYTQSWKQEMIADGIEASIKGLHNFDETKYKNPHAYITQACFNAFVQRIKKERKEVAKKYSYFVHNVYDSRDDDMVALVDETFIQDIYDKMTHYEESTYRTPGAEKKSVVDDSPSLDFLYEAND
Protein: Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30) (Q64374)
Organism: Mus musculus (Mouse)
Function: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- L-gulonolactone oxidase
- Probable gluconokinase
- Phenylalanine-4-hydroxylase
- Estradiol 17 beta-dehydrogenase 5
- Arylacetamide deacetylase
- Protein transport protein Sec16B
- GDH/6PGL endoplasmic bifunctional protein
- Calmodulin-like protein 4
Sequence:
MSSIKVECVLRENYRCGESPVWEEASQSLLFVDIPSKIICRWDTVSNQVQRVAVDAPVSSVALRQLGGYVATIGTKFCALNWENQSVFVLAMVDEDKKNNRFNDGKVDPAGRYFAGTMAEETAPAVLERHQGSLYSLFPDHSVKKYFDQVDISNGLDWSLDHKIFYYIDSLSYTVDAFDYDLQTGQISNRRIVYKMEKDEQIPDGMCIDAEGKLWVACYNGGRVIRLDPETGKRLQTVKLPVDKTTSCCFGGKDYSEMYVTCARDGLNAEGLLRQPDAGNIFKITGLGVKGIAPYSYAG