wanglab/gogpt-training-data huggingface dataset:
Protein: MutL homolog 1 (A0A087WX20)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC
Protein: Serine protease Hip1 (EC 3.4.21.-) (Hydrolase important for pathogenesis 1) (Serine hydrolase Hip1) (P9WHR3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Serine protease that promotes tuberculosis (TB) pathogenesis by promoting the processing and the extracellular release of the M.tuberculosis (Mtb) heat-shock protein GroEL2. Hip1-dependent cleavage of multimeric GroEL2 results in release of cleaved monomeric GroEL2 into the extracellular milieu. Conversion of multimeric GroEL2 into monomeric GroEL2 is likely to be a mechanism for regulating GroEL2 functions during Mtb pathogenesis. In vitro, exhibits proteolytic activity against synthetic peptides and the general protease substrate azocasein, and exhibits esterase activity against the ester substrate p-nitrophenylbutyrate.
Subcellular location: Cell envelope {ECO:0000269|PubMed:18172199}. Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:18172199}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Glutamine synthetase
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
Sequence:
MGMRLSRRDKIARMLLIWAALAAVALVLVGCIRVVGGRARMAEPKLGQPVEWTPCRSSNPQVKIPGGALCGKLAVPVDYDRPDGDVAALALIRFPATGDKIGSLVINPGGPGESGIEAALGVFQTLPKRVHERFDLVGFDPRGVASSRPAIWCNSDADNDRLRAEPQVDYSREGVAHIENETKQFVGRCVDKMGKNFLAHVGTVNVAKDLDAIRAALGDDKLTYLGYSYGTRIGSAYAEEFPQRVRAMILDGAVDPNADPIEAELRQAKGFQDAFNNYAADCAKNAGCPLGADPAKAVEVYHSLVDPLVDPDNPRISRPARTKDPRGLSYSDAIVGTIMALYSPNLWQHLTDGLSELVDNRGDTLLALADMYMRRDSHGRYNNSGDARVAINCVDQPPVTDRDKVIDEDRRAREIAPFMSYGKFTGDAPLGTCAFWPVPPTSQPHAVSAPGLVPTVVVSTTHDPATPYKAGVDLANQLRGSLLTFDGTQHTVVFQGDSCIDEYVTAYLIGGTTPPSGAKC
Protein: Cdc-42 Related Protein (O62422)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine/threonine-protein kinase pak-1
- Cell division control protein 42 homolog
- Rho GTPase-activating protein 68F
- Intersectin-1
- Mediator of RNA polymerase II transcription subunit 29
- C-type lectin domain-containing protein
- Cell-death-related nuclease 7
- Major sperm protein
- F-BAR domain-containing protein
- START domain-containing protein
Sequence:
MENKLKLVVVGDTYTGKTSLLVAYTKKQFLDNYTTTVFDNWAVSVHIDNKNYAVNLFDTAGQGNYEQIRCLSYPHANVFLVCFSMIDRKTLESCRSTWIPEIRKYAGDNVPIMLVGTKNDLVDDADSRNTVTEDYAKRVAHEIGCHKFYSCSALTHKGLKRVFDESFLAAVGVKLEEETPNPCCTIL
Protein: Arylamine N-acetyltransferase 1 (EC 2.3.1.5) (Arylamide acetylase 1) (N-acetyltransferase type 1) (AT-1) (NAT-1) (P50297)
Organism: Rattus norvegicus (Rat)
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Acetylates both arylamines and arylalkylamines.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Xanthine dehydrogenase/oxidase
- Arylamine N-acetyltransferase 2
- Carboxylesterase 1D
- Carboxylesterase 1C
- arylamine N-acetyltransferase
- Esco1 protein
Sequence:
MDIEAYFERIGYKNSVNKLDLATLTEVLQHQMRAVPFENLSMHCGEAMCLGLEATFDHIVRKKRGGWCLQVNHLLYWALTKMGFETTMLGGYVYITPVNKYSSEMVHLLVQVTISDRNYIVDSAYGSSYQMWEPLELTSGKDQPQVPAIFRLTEENGTWYLDQIRREQDVPNQEFVNSDLLEKSKYRKIYSFTLEPRTIEDFEYVNTYLQTSPASVFVSTSFCSLQTSEGVCCLIGSTLTSRRFSYKDNVDLVEFKSLTEEEIEDVLKTTFGISLEKKFVPKHGELVFTI
Protein: GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) (Q9V7W1)
Organism: Drosophila melanogaster (Fruit fly)
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 membrane attachment of chp, qsm and Cont. Essential for microvillar stability in the rhabdomere.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI mannosyltransferase 1
- GPI mannosyltransferase 3
- GPI ethanolamine phosphate transferase 1
- GPI ethanolamine phosphate transferase 3
- Phosphatidylinositol-glycan biosynthesis class X protein
- Dolichol phosphate-mannose biosynthesis regulatory protein
- IP07787p
- GPI mannosyltransferase 4
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol glycan anchor biosynthesis class C, isoform C
Sequence:
MTEKVTKLALASRLIVLLVQLVANGALPEHKPDVFRMPVSSDQNASWIDKVIKRCLGGLRHWDGEYFLHIAENLYSYENTLAFYPLYPVVVRHVGQAVEAIGISLSQESILLVVAVALNFWLFCESANLLFQLTQVLFNDLNKSWNAALIYCFNPATIFFTAAYSETFFAYSSLHLMLECSKPTGSFRYLRLGTALAACLLCRSNGLITLGYPLYFFGRQLLLKNKEPNTCMQLTQMTLTILGAIGILHTYYFYIYRLYCLPNTRPNHPQHIVDYAVERKYLLSGQGSEGSPWCQYTLPFPYTYVQSHYWDVGFLRYYKWKQLPNFLLALPMLSFMHWHCYDYMQHLAKAVWAKLTPSGFKELIRDHTTFPFVLHAAILTLVCTVYVHIQVSTRLLASATPVFYWFAADHMPKTLAQLKLRSKAGALFVWCTTYSLVGTVLFSNNYPWT
Protein: Cathepsin B-like cysteine proteinase 6 (EC 3.4.22.-) (Cysteine protease-related 6) (P43510)
Organism: Caenorhabditis elegans
Interaction partners:
- Aspartic protease 3
- Aspartic protease 4
- legumain
- Neprilysin-2
- Cathepsin L-like
- Neprilysin-1
- Actin
- Peptidase A1 domain-containing protein
Sequence:
MKTLLFLSCIVVAAYCACNDNLESVLDKYRNREIDSEAAELDGDDLIDYVNENQNLWTAKKQRRFSSVYGENDKAKWGLMGVNHVRLSVKGKQHLSKTKDLDLDIPESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGELQVTLSADDLLSCCKSCGFGCNGGDPLAAWRYWVKDGIVTGSNYTANNGCKPYPFPPCEHHSKKTHFDPCPHDLYPTPKCEKKCVSDYTDKTYSEDKFFGASAYGVKDDVEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRGVDECGIESGVVGGIPKLNSLTSRLHRHHRRHVYDDNY
Protein: Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c reductase iron-sulfur subunit) (P49727)
Organism: Zea mays (Maize)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.
Interaction partners:
- Complex III subunit 9
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 7
- Cytochrome c1 1 heme protein mitochondrial
- Cytochrome b-c1 complex subunit 6
- Cytochrome b-c1 complex subunit 6
- NADH dehydrogenase iron-sulfur protein 3
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Complex III subunit 9
Sequence:
MLRVAGRRLSSSLSWRPAAAVARGPLAGAGVPDRDDDSARGRSQPRFSIDSPFFVASRGFSSTETVVPRNQDAGLADLPATVAAVKNPNPKVVYDEYNHERYPPGDPSKRAFAYFVLSGGRFIYASLLRLLVLKFVLSMSASKDVLALASLEVDLSSIEPGTTVTVKWRGKPVFIRRRTEDDIKLANSVDVASLRHPEQDAERVKNPEWLVVIGVCTHLGCIPLPNAGDFGGWFCPCHGSHYDISGRIRKGPAPFNLEVPTYSFLEENKLLVG
Protein: AAA+ ATPase domain-containing protein (Q5ZHL1)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MQAFLKGPSSISSKPPAAKERSAAGSSGEGNKLKPVPWVEKYRPKNVDEVAFQDEVVAVLKKSLEGADLPNLLFYGPPGTGKTSTILAAARELFGPELFRQRVLELNASDERGIQVIREKVKAFAQLTASGSRADGKVCPPFKIVILDEADSMTSAAQGALRRTMEKESKTTRFCLICNYISRIIEPLTSRCSKFRFKPLSDKIQQQRLLDVSEKENVKITSEAVSYLVKVSDGDLRKAITYLQSATRLMGGKEITEKTVTEIAGVIPRETIDGLLSACSSGSFEKLETVAKNLINEGYAVAQLVNQLHDIVVESEDFSDKQKSIIVEKLAEVDKCLADGADEYLQLISLCALVMQQLT
Protein: Splicing factor Cactin (F4I2J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Required for embryogenesis.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:23454656}.
Interaction partners:
- At3g05070
- Riboflavin synthase
- CAAX amino terminal protease family protein
- Preprotein translocase subunit SECE1
- Pre-mRNA-processing factor 17
- AT4g02720/T10P11_1
- Ribosomal L18p/L5e family protein
- U1 small nuclear ribonucleoprotein 70 kDa
- U11/U12 small nuclear ribonucleoprotein 65 kDa protein
- Probable inactive leucine-rich repeat receptor-like protein kinase At3g03770
Sequence:
MGSHGKGKRDRSGRQKKRRDESESGSESESYTSDSDGSDDLSPPRSSRRKKGSSSRRTRRRSSSDDSSDSDGGRKSKKRSSSKDYSEEKVTEYMSKKAQKKALRAAKKLKTQSVSGYSNDSNPFGDSNLTETFVWRKKIEKDVHRGVPLEEFSVKAEKRRHRERMTEVEKVKKRREERAVEKARHEEEMALLARERARAEFHDWEKKEEEFHFDQSKVRSEIRLREGRLKPIDVLCKHLDGSDDLDIELSEPYMVFKKKKVRIGIWLNFQLSITNVYVEAEYKNDSACLLLRSRVDILLNKGLTVKDMEELRDDIKMYLDLDRATPTRVQYWEALIVVCDWELAEARKRDALDRARVRGEEPPAELLAQERGLHAGVEADVRKLLDGKTHAELVELQLDIESQLRSGSAKVVEYWEAVLKRLEIYKAKACLKEIHAEMLRRHLHRLEQLSEGEDDVEVNPGLTRVVEENEEEINDTNLSDAEEAFSPEPVAEEEEADEAAEAAGSFSPELMHGDDREEAIDPEEDKKLLQMKRMIVLEKQKKRLKEAMDSKPAPVEDNLELKAMKAMGAMEEGDAIFGSNAEVNLDSEVYWWHDKYRPRKPKYFNRVHTGYEWNKYNQTHYDHDNPPPKIVQGYKFNIFYPDLVDKIKAPIYTIEKDGTSAETCMIRFHAGPPYEDIAFRIVNKEWEYSHKKGFKCTFERGILHLYFNFKRHRYRR
Protein: Cytochrome P450 (P-450 monoxygenase) (Q7D2E2)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
Sequence:
MQLAPVDRVTTIDDLTLDPYPIYRRMRAQTPVVRVASVMRTFLTKASDTKMVKDQPRRFSSDDPNTPMKPAFQAHTLMRKDGAEHARERMAMAKAFAPKTTAEHWAAIYRDIVNEYLDRLSRGSTVDLFAEICGPVAARILAHILGISEASDAEMIRWSQRLIEGAGNFGWRPEPFERANEANAEMNRLFDNLVEKHRAEPNPSAFAIMVTASDPIPMSQIYANIKIAVGGGINEPRDALGTIIYGLLTNPEQFEEVKRQQCWGQVFEEGVRWVAPIQASSRLVLEDTEIRGFLVPKGDTVMTIQASANRDEDVFDDGERFNVFRQNNAHQSFGSGPHHCAGAQISRQTVGAIMLPTLFERFPNMTLTNPDAVQWRGFGFRGPISLPVTLI
Protein: Cellobionic acid phosphorylase (EC 2.4.1.321) (4-O-beta-D-glucopyranosyl-D-gluconate:phosphate alpha-D-glucosyltransferase) (Q7S0S2)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Catalyzes the reversible phosphorolysis of cellobionic acid (4-O-beta-D-glucopyranosyl-D-gluconate), a probable step in cellulose degradation. May be part of a metabolic pathway where cellobionic acid is converted into alpha-D-glucose 1-phosphate and D-gluconic acid to enter glycolysis and the pentose phosphate pathway, respectively. Produces 4-O-beta-D-glucopyranosyl-D-glucuronate from alpha-D-glucose 1-phosphate and D-glucuronate with low activity in the synthetic direction.
Interaction partners:
Sequence:
MTRKMPTLVRPTHNGERYEITNPTAMPKAAGFLWNQKMMIQITCRGFATAQFMQPEPAKYAYAPNIEAKTFMQPEPNYYAHHPGRFVYIKDEETGRLFSAPYEPVRAPHDRFVFSAGKTDVFWVIESMGIRVEMTMGLPTHHVAELWTIKVKNLSSRPRKLSVTPYFPIGYMSWMNQSAEWNHNLNGIVASCVTPYQKAADYFKNKYLKDKTYFLCDVPPDSWEASQQAFEGEGGLHNPSALQERNLSGSDARYETPTAAVQYKIALGTGEQQEYRFLFGPAHDEAEIGAMRSKYLSKEGFEQTAADYAAYMARGRGCLHVETPDKDLDNFINNWLPRQVYYHGDVNRLTTDPQTRNYLQDNMGMNYIKPEVSRRAFLTAIAQQEATGAMPDGILLVEGAELKYINQVPHTDHCVWLPVTLEAYLNETGDYSLLKEKVPSANGDKLTVFERFCRAMDWLLKSRDHRGLSYIAQGDWCDPMNMVGYKGKGVSGWLTLATAFSLNIWAKVCDHEGETDLAKRFREGADACNAAANEHLWDGEWFARGITDDNVVFGIKEDKEGRIWLNPQSWSILSGAASPEQIDKMLPQIDSHLNTPYGIQMFGPPYTKMREDVGRVTQKAIGSAENAAVYNHAGIFFIHSLYELGAQQDRAFTLLRQMLPGPTDTDYIQRGQLPIYIPNYYRGAWKECPRTAGRSSQLFNTGTVSWVYRCIIEGLCGLRGDGEGLLIRPQLPSSWNSMKVTREFRGATFNVDIRRGNVKEVTVRNGDKVLPAPHVKDIEPGQTYNLTVTIP
Protein: Bifunctional nitrilase/nitrile hydratase NIT4B (LaNIT4B) (EC 3.5.5.4) (EC 4.2.1.65) (3-cyanoalanine hydratase) (Cyanoalanine nitrilase B) (Q3LRV4)
Organism: Lupinus angustifolius (Narrow-leaved blue lupine)
Function: Involved in the cyanide detoxification pathway. Has nitrilase and nitrile-hydratase activity in the ratio 3.3:1, producing both asparagine and aspartic acid from beta-cyano-L-alanine (Ala(CN)). Can also use 3-phenylpropionitrile as substrate, but not indole-3-acetonitrile.
Interaction partners:
Sequence:
MALVTTTPTVNDEPLFAEVDMASYFTSTTVRATVVQASTIFYDTPATLDKAERLLVQAASYGAQIVVFPEAFIGGYPRGSNFGVSIGNRTAKGKEEFRKYHSAAIDVPGPEVDRLSAMAGKYKVYLVMGVIERDGYTLYCTVLFFDSQGRYLGKHRKVMPTALERIIWGFGDGSTIPVFQTPIGKIGAAICWENKMPLLRTAMYAKGVEIYCAPTADSRDLWQASTTHIALEGGCFVLSANQFCRRKDYPPPPEYVFSGTEEDLTPDSVVSAGGSVIISPSGAVLAGPNYEGEALISADLDLGEIARAKFDFDVVGHYSRSEVLSLIVKDHPTNPVTFTSTSTKIEDQTK
Protein: Translation initiation factor IF-1, chloroplastic (P0C378)
Organism: Oryza sativa (Rice)
Function: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_00075}.
Interaction partners:
Sequence:
MTEKKNRREKKNPREAKITFEGLVMEALPNGMFRVRLENDTIILGYISGKIRSSSIRILMGDRVKIEVSRYDSSKGRIIYRLPHKDSKRTEDSKDTEDLKDTKDSKG
Protein: Cyphokinin (Bradykinin-related peptide) [Cleaved into: Thr6-bradykinin (Thr6-BK)] (P83659)
Organism: Cyphononyx dorsalis (Spider wasp) (Cyphononyx fulvognathus)
Function: Inhibits angiotensin-converting enzyme (ACE) with a Ki of 2.2 uM and targets B2 bradykinin receptor (BDKRB2). Also provokes contraction of smooth muscle preparation (ileum). In vivo, induces hyperalgesic effects in living rats after intraplantar injection.
Subcellular location: Secreted {ECO:0000269|PubMed:11306139}.
Interaction partners:
Sequence:
DTRPPGFTPFR
Protein: Monoglyceride lipase (A0A0C4DFN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METGPEDPSSMPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP
Protein: Endospore coat-associated protein YheD (O07545)
Organism: Bacillus subtilis (strain 168)
Function: Involved in sporulation.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:15231775}; Peripheral membrane protein {ECO:0000269|PubMed:15231775}. Spore coat {ECO:0000269|PubMed:15231775}. Note=Forms two rings around the forespore that are offset from its midpoint, before it eventually redistributes to form a shell around the developing spore.
Interaction partners:
- Endospore coat-associated protein YheC
- Protein CotJA
- Spore coat protein E
- Endospore coat-associated protein YutH
- Protein CotJB
- Uncharacterized protein YsxE
- Protein CotJC
- Spore coat protein GerQ
Sequence:
MNPKRFLIGIDKTSENTLFLPSSLKQDGLLHAAFGTKVVRCHVAYRRHLEQTVLLSENLFHELLLPHRSRADILIHDHTVHIGPLVGIFTAGFTVSLERPFKDRSLFFSKLVTLHEQAGGYCFVFGAHQINWEEGTIEGLLYRENGWEKKIVPLPNVVYDRLPNRKIEDSLLLQHTKKRLIDEYQIPWFNKTFFNKWNVHQLLEKDPRTAPFLPRSELTPSVELIDELCGAYKKVYIKPANGALGTGIYQLTRTDGGLTVKHTNDAKTFTSIDYSDAASFLAEFQKHHNPSDFLIQQGVDLIEFQGKPADFRVHTNKNRKGKWTVTAIAVKISGKNSITTHLSNGGTVKTLAEVYDDPAERVEVIKKLSAAALTASHVLHDHIEGFIGEIGFDFGIDQNGKVWMFEANSRPGRSIFSHPNLHHVDSLTKRRSFEYASYLSEKAITSPEALWPS
Protein: Lethal (3) neo38, isoform A (RE72719p) (Q8SZN9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFSAANNMQYGQNISIPYSQPQGDLNFLNAAAAADHKGKIHPKIERDREEVLNQQILQNVNQSWQTLANTANTVDYSSHLLSATLPISIQHFLKYSETIKKESTGDVLKNGTNLASLALGGVALTPSNNGANGGHHNGLVGMDHGGHMTNMTDANGAALTNGASNGVNGNANGTVTNGGAGAVSSSGSVGTTNASGGTGTASGKKTKKKKPPKEKKPRPKPGEIRETKALDGSTLYCCPECQMAYPDRSLIEQHVISHAVERRFVCDICNAALKRKDHLTRHKLSHIPDRPHVCNICMKSFKRKEQLTLHIVIHSGEKKHVCIECGKGFYRKDHLRKHTRSHIARRVKSEVSAQNVNGSAGGGGGGGGGNSAQSNALHGS
Protein: Geranyltranstransferase (Q9A6M4)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Isoprenyl transferase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Octaprenyl diphosphate synthase
- Exodeoxyribonuclease 7 small subunit
Sequence:
MSDLAKRIVQAADIVTVALDELLPRADGPESRLTEAMRYAALGPGKRLRPFFALETGKMFDLPERPVLRAACALECIHAYSLVHDDLPAMDDDDVRRGRPTVHKQYDEATAILAGDALQTAAFEIMAHPDTHDDGHVRSELVRKLAIASGARGMCGGQMIDLLGVRDDLGAVARMQRLKTGALIAFAFEIPLIIARAKESERSALMAFAQDLGLAYQIVDDILDAEGDEETLGKAAGGKDAAKGKANYVTLLGLDAAKERVTLLAEQTRSHLEIFGERAEHLRASVDFVLDRRN
Protein: Integrin alpha-5 precursor (Integrin alpha5) (Integrin, alpha 5 (fibronectin receptor, alpha polypeptide)) (Q5I2A9)
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:
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
- Fibronectin
- Proto-oncogene tyrosine-protein kinase Src
- Integrin beta
- Integrin beta
Sequence:
MGCKRHRSKTSASTSCSPMGLSLLILLPLSVAFNLDVENPAVYNGPSGSYFGYSVDFYMTDSSVSIIVGAPKANTSQPKITEGGSVFYCPWSLSQSQCSSIEFDRLGDLNMSVNDTDHQGEFKSHQWFGATVRVHQDSVLACAPLYSWRTKEDTPHADTTGSCFMSVKNFTKFVEYAPCRTEFRGRKGQGYCQGGFSADFTQEGKVVLGGPGSYFWQGQVITAFKQEIVKAYYPGYFLTSVGGQIQTKQRKEIRFDDTYMGYSVAVGEFTGDDDEDFVTGVPRGVRLHGQVSILNSSLDVLKMFTGEQMGSYYGYSVAATDINNDGMMDLLVGAPMFMVRDSDGRLEELGRVYVYMQKGPLDLIPQLPHLTGTQMFARFGSSITPLGDLNQDGYNDVAISSPFGGEDKQGLVLIYNGNAGGLREKPSQVISGQWASAGLSAIPASFGYALRGGKDLDNNGYPDLIVGAFGADKAVLYRSRPIVNTSAILNVYPIMINPEEKVCAISRGNETLHVSCVNLSFCLSANGKHLPNHLEFNVEVQLDRLKQQQKGAVRRALFLETQLPALHRTLTVPNGARVCSDTKIYLRDEKDFRDKLSPIFVALNFSLNPQAAADRHGLQPILNYQTAELIEQKAQILLDCGEDNICVPDLKLSVHGDRKEVYMGDDNSLTLTFNAKNDGGGAYEAELYVVLPPEADYSGIARNNESLTQLTCSYETENQTRYLSCDLGNPMKSGTSLWAGLRFTVPRLKDTHNFVQFDLQIRSKNENNSQSEVVPYKLEVVVRSDVILQGVSRPDKVFFPPPNWKLTKNVMVEQNVGPSVQHTYELVNNGPSRISHTLLQLKCPMRLHSNRFIYPLEVTTEGPVNCTTHNIINPLNLKLQQSSTEQPPVRDSGHEHHIEKRDTHKGELSQLTNLSCSSVDCWTLMCNVGLLERGTSAILHVRSRIWAETFMENTYKNFILECHASYKVEKMPYAILPKVTPSGSKKMVTPVVWNKPDSSYAVPLWIIILAILAGLLLLALLIYVLYKLGFFKRTPYGTAMEKAQLKPQAASEA
Protein: Nuclear transport factor 2 family protein (P71819)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAGYPRDELEDVVHRWLQANRTAERRGDWTLLADFYTDDATYGWNVGPNEDVMCVGIDEIRDIALGQEMDGLQGWRYPYQRVVIDEKQGEVVGFWKQVATDANGAEQEVYGIGGSWFRYAGGGKWNWQRDFFDFGHVSALYLELIKAGKLSPGMQKRIERAVSGNKVPGYYPLGKTPVPLW
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3 (Q5U3Y2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- AT-rich interaction domain 1A
- Double PHD fingers 3
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- Protein polybromo-1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2
- AT-rich interactive domain-containing protein 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- PHD finger protein 10
Sequence:
MSPGVQHPPTVVQRPGMPSGARMPHQGAPMGPPGSPYMGSPAVRPGLAPAGMEPARKRAAPPPGQSQAQGQGQPVPTAPARSRSAKRRKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRVDIQEALKRPMKQKRKLRLYISNTFNPAKPDAEDSDGSIASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTPTTQETDGFQVKRPGDLSVRCTLLLMLDYQPPQFKLDPRLARLLGLHTQSRSAIVQALWQYVKTNRLQDSHDKEYINGDKYFQQIFDCPRLKFSEIPQRLTGLLLPPDPIVINHVISVDPSDQKKTACYDIDVEVEEPLKGQMSSFLLSTANQQEISALDSKIHETIESINQLKIQRDFMLSFSRDPKGYVQDLLRSQSRDLKVMTDVAGNPEEERRAEFYHQPWSQEAVSRYFYCKIQQRRQELEQSLVVRNT
Protein: 8-amino-7-oxononanoate synthase (AONS) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (Biotin synthase 4) (Biotin synthase F) (AtbioF) (Q8GW43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Required for the biosynthesis of D-biotin that prevents light-mediated cell death and modulates defense gene expression, probably by avoiding hydrogen peroxide H(2)O(2) accumulation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16299174}. Peroxisome {ECO:0000269|PubMed:21730067}. Note=The cytosolic localization observed in PubMed:16299174 is probably due to the lack of PTS1 domain at the C-terminus of the reporter gene construct. {ECO:0000303|PubMed:21730067}.
Interaction partners:
- Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial
- Biotin synthase, mitochondrial
- Downregulated in DIF1 18
- Organic cation/carnitine transporter 1
- 26S proteasome regulatory subunit 10B homolog A
- At2g03780
- Sorbitol dehydrogenase
- Syntaxin-71
- Syntaxin-72
- Syntaxin-73
Sequence:
MADHSWDKTVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDGYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDEPSNGEEIFSGDALAECRKGRFKKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATHIPSFLFPKL
Protein: Mast cell protease 4 (rMCP-4) (EC 3.4.21.-) (Mast cell protease IV) (rMCP-IV) (P97592)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted. Cytoplasmic granule. Note=Secretory granules.
Interaction partners:
- Mast cell carboxypeptidase A
Sequence:
MKALLFLMALLLPSGAGAEEIIGGVESIPHSRPYMALLKIVTEEGHVTFCGGFLISLQFVLTAAHCHGREITVTLGAHDMSKRESTQQKIKVVKQIFPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPNSNTLREVMLRIMEMKACKDYRHYDNRFQICVGIPQMLKLAYKGDSGGPLVCAGVAHGIVSHGPGRGIPPIIFTRISSYVSWINRVIRGN
Protein: Transthyretin-like family protein (Q9XV56)
Organism: Caenorhabditis elegans
Interaction partners:
- DUF305 domain-containing protein
- Trichohyalin-like
- Protein containing ALS2cr12
- Protein containing ALS2cr12
- Secreted protein
- Uncharacterized protein
- Neuropeptide-Like Protein
- Protein containing ALS2cr12
- Coiled-coil domain-containing protein 73
- Protein containing ALS2cr12
Sequence:
MEQNHDSRGTDRIRLSNVQQRDGSVSHFYQHQEGTDIQVQVRRGSAKLDGQRVPFHKLTITPDIPYRDLGLRLKVTGNNGQGIYLRNVETSRHSDQTRSSGRAHTDDQRYSFTIPSYYPYPTGVCLKIPYSAKAKNVQIKMRRSKSHNYREADIVGLNTPNQHIEARRLSFEESQRRLQDEARIAEQRRWENTRRQNDQSIRNVYGREYEADSRNSGGHHERNEQRRERECIMDREPRYTNGFDQIERTMRNNRAALEAQHAESDAQRRMREEEIKNTFIGRF