wanglab/gogpt-training-data huggingface dataset:
Protein: Gallate 1-beta-glucosyltransferase 84A23 (EC 2.4.1.136) (UDP-glucose:gallate glucosyltransferase) (UDP-glycosyltransferase 84A23) (EC 2.4.1.120, EC 2.4.1.170, EC 2.4.1.177, EC 2.4.1.194, EC 2.4.1.81) (A0A193AUF6)
Organism: Punica granatum (Pomegranate)
Function: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27227328}.
Interaction partners:
- 4-coumarate--CoA ligase 2 isoform X2
- 4-coumarate--CoA ligase-like 1
- 4-coumarate--CoA ligase
- aldehyde dehydrogenase
- aldehyde dehydrogenase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
Sequence:
MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGYTVLTLPEGFLEKAGDRGKVVQWSPQEQVLAHPATACFVTHCGWNSSMEALTSGMPVVAFPQWGDQVTDAKYLVDEFKVGVRMCRGEAEDKLITRDVVEQCLREATQGPKAAEMKKNALKWKAAAEASFVEGGSSDRNLQAFVDEVKRRSIEITASKPAVKAAPNGVVAAAESVVETKANGKVELAA
Protein: Sucrose phosphorylase (EC 2.4.1.7) (Glucosyltransferase-A) (GTF-A) (Sucrose glucosyltransferase) (P10249)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Intracellular catabolism of sucrose. Being intracellular, probably not involved in synthesis of extracellular polysaccharides (Probable).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:2971020}.
Interaction partners:
- Multiple sugar-binding protein
- Multiple sugar-binding transport ATP-binding protein MsmK
- Glucan 1,6-alpha-glucosidase
- Multiple sugar-binding transport system permease protein MsmG
- Sucrose-6-phosphate hydrolase
- Multiple sugar-binding transport system permease protein MsmF
- Glucosyltransferase-I
- Alpha-galactosidase
- Levansucrase
- Glucosyltransferase-SI
Sequence:
MPIINKTMLITYADSLGKNLKELNENIENYFGDAVGGVHLLPFFPSTGDRGFAPIDYHEVDSAFGDWDDVKCLGEKYYLMFDFMINHISRQSKYYKDYQEKHEASAYKDLFLNWDKFWPKNRPTQEDVDLIYKRKDRAPKQEIQFADGSVEHLWNTFGEEQIDLDVTKEVTMDFIRSTIENLAANGCDLIRLDAFAYAVKKLDTNDFFVEPEIWTLLDKVRDIAAVSGAEILPEIHEHYTIQFKIADHDYYVYDFALPMVTLYSLYSSKVDRLAKWLKMSPMKQFTTLDTHDGIGVVDVKDILTDEEITYTSNELYKVGANVNRKYSTAEYNNLDIYQINSTYYSALGDDDQKYFLARLIQAFAPGIPQVYYVGFLAGKNDLELLESTKEGRNINRHYYSSEEIAKEVKRPVVKALLNLFTYRNQSAAFDLDGRIEVETPNEATIVIERQNKDGSHIAKAEINLQDMTYRVTENDQTISFE
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (Q4LDP7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MARIVESNFVPLAVGVVAVLAGALIVHYLLNKKSTKPRREPNRTARLRTLVDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFKDSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKLRKDPPKHVTAKRVNMIAGGTGITPMLQLAREVLKRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEGWQYSVGFINEEMIAAHLLPAKDDTIVLLCGPPPMINFACNPALDKLGYHPDTRFAY
Protein: Cryptochrome DASH (Protein CRY-DASH) (zCRY-DASH) (Q4KML2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May have a photoreceptor function (By similarity). Has weak cyclobutyl pyrimidine photolyase activity when expressed in E.coli and when tested in vitro.
Interaction partners:
- Period circadian protein homolog 2
- Aryl hydrocarbon receptor nuclear translocator-like 1a
- Period circadian clock 3.
- Protein timeless homolog
- Period homolog 1b
- Aryl hydrocarbon receptor nuclear translocator-like 2
- Deoxyribodipyrimidine photo-lyase
- Period circadian clock 1a.
- Aryl hydrocarbon receptor nuclear translocator-like 1b.
Sequence:
MSASRTVICLLRNDLRLHDNEVFHWAQRNAEHIIPLYCFDPRHYQGTYHYNFPKTGPFRLRFLLDSVKDLRALLKKHGSTLLVRQGKPEDVVCELIKQLGSVSTVAFHEEVASEEKSVEEKLKEICCQNKVRVQTFWGSTLYHRDDLPFSHIGGLPDVYTQFRKAVEAQGRVRPVLSTPEQVKSPPSGLEEGPIPTFDSLGQTEPLDDCRSAFPCRGGETEALARLKHYFWDTNAVATYKETRNGMIGVDFSTKFSPWLALGCISPRYIYEQIKKYEVERTANQSTYWVIFELLWRDYFKFVALKYGNRIFYMNGLQDKHVPWNTDMKMFDAWKEGRTGVPFVDANMRELALTGFMSNRGRQNVASFLTKDLGLDWRLGAEWFEYLLVDHDVCSNYGNWLYSAGIGNDPRENRKFNMIKQGLDYDNNGDYVRQWVPELRGIKGGDVHTPWTLSNSALSHAQVSLNQTYPCPIITAPEWSRHVNNKSSGPSSSKGRKGSSYTARQHKDRGIDFYFSKNKHF
Protein: RNA-binding Fox protein 1, isoform H (M9NFQ7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RNA-binding protein Pasilla
- Bruno 3, isoform A
- Protein held out wings
- Heterogeneous nuclear ribonucleoprotein A1
- GEO13361p1
Sequence:
MSASAVEVTGNVPPVEFHMREHMVQAGVAPFPGAPAGYAAAPNPGAAVVAAAAAAQQQQQQQQQQQQQQQQAQQQQQQQVAGGPPSAADSLSMAVAAAAAKQSADPVTQMKSGSEAAGSGNSNNNNTAGAGTGAPGAAGGLTTEYSSGGCGGGGASTANSVVVATSVSDVVNASLYMQQKTNLSTQTQTQYEYEYEYNGTSLAEPRVPGPIPHPLTNGHAVDQVQQPPVQQQHLQSSLPPQNVLSISTVLIANEAAESQQSSAMQNAGGGGNTGGGGGGGGGGTPSSPLSNSPSSATASQAGGCGLTLNGSATEGSMSGDTSPVASGEPLLQTPPAHQQQQQQQQPLLCSSPTSMQSSGTSVTGSSIASGTLAATSSSGVGLLPTTGLDSIANGGAPTGCAVVPASTSQVIAHLNAAAAAASGIVSPSANVATSLSSALVPAQSVAAVAAASLDAKSQPKRLHVSNIPFRFRDPDLRAMFGQFGTILDVEIIFNERGSKGFGFVTFANSNDAERARERLHGTVVEGRKIEVNNATARVQTKKVTAVPNVVLTKDGAIPAPALVCVQWPEAAVAAAMRGVAIQRGHVGVVGATPYHHPHHPHHHPALLAASAAAAQQQQQRQLAAAAVATAAVAQQQQQQQQAVVQQQQQQVAAAAQQQHQQQQQQQQQAVQQQQAVQQQQQHQQQQQQQQQQQHAAVAAAAAAASHPHMHAAHAHAHAHALGPQLAQLQAVAVPTAASNAAALQQSLAAAIQNPSGNPNAAAAAAAYAARLSAATGATQSPQTAAAAAAAASMAASANAANNAAALHGFAPVYYDPFLAAAASADPNLRFQAAKPVTEVPAAQPAAILNRRTVTTLNSNPHTINRIPVPQNVLATAPLLKTPLSQAQQQAYATAATTYTAVAARAAYGAAAAAAAQPALAGYATVAGYAREYADPYLGHGIGPVPGYGATMYRGGFNRFTPY
Protein: DNA-directed RNA polymerase subunit beta'' (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta'') (RNA polymerase subunit beta'') (P0C507)
Organism: Oryza sativa (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01324}.
Interaction partners:
Sequence:
MAERANLVFQNKEIDGTAMKRLISRLIDHFGMGYTSHILDQIKTLGFHQATTTSISLGIEDLLTIPSKGWLVQDAEQQSFLLEKHYYYGAVHAVEKLRQSVEIWYATSEYLKHEMNSNFRITDPSNPVYLMSFSGARGNASQVHQLVGMRGLMADPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVVQHIIVRRRDCGTIQAISVSPQNGMTEKLFVQTLIGRVLANDIYIGSRCIATRNQDIGIGLVNRFITTFRAQPFRAQPIYIRTPFTCRSTSWICQLCYGRSSTHGDLVELGEAVGVIAGQSIGEPGTQLTLRTFHTGGVFTGGTADLVRSPSNGKIQFNGDLVHPTRTRHGQPAFLCYIDLHITIQSQDILHSVTIPSKSLILVQNDQYVESEQVIAEIRAGTSALHFKEKVQKHIYSESDGEMHWSTDVYHAPEYQYGNLRRLPKTSHLWILSVSMCRSSIASFSLHKDQDQMNTYSFSVDGRYIFGLSMADDEVRHRLLDTFGKKDREILDYSTPDRIMSNGHWNFVYPSILQNNFDLLAKKRRNRFAIPLQYHQEQEKEPISCFGISIEIPFMGVLRRNTIVAYFDDPRYKKDKKGSGIVKFRYRTLEDEYRTREKDSENEYGSPENEYRTREEECKTLEDEYRTREEEYETLEDEYGIPENEYETLEDEYGILEDEYRTREEESEDEYGSPENKYRPREDKYGTLEEDSEDEHGTLEEDSEEDSEDEYGNPEEDSVLKKGVLIEHRGTKEFSLKYQKEVDRFFFILQELHILPRSSSLKVLDNSIIGVDTQLTKNTRSRLGGLVRVKRKKSHTELKIFSGDIHFPEEADKILGGSLIPLEREKKDSKESKKRENWVYVQWKKILKSKEKYFVLVRPAVAYEMNEGRNLATLFPQDLLQEEGNLQLRLVNFISHENSKLTQRIYHTNSQFVRTCLVLNWEQEEKEEARASLVEIRANGLIRDFLRIGLIKSTISYTRKRYDSRSAGLILHNRLDRTNTNSFYSKAKIQSLSQHQEAIGTLLNRNKEYQSLMVLSASNCSRIGFFKNSKNPNGVKESNPRIPIPKFWGLFRNFSGLLGTIAPSISNFSSSYYLLTYNQILLKKHLLLDNLKQNFKVLQGLKHSLINENQRTSNFDSNIMLDPFQLNWHFLPHDSWEETSAKIHLGQFICENVCLFKSHIKKSGQIFIVNIDSFVIRAAKPYLATTGATVHGHYGEILYKGDRLVTFIYEKARSSDITQGLPKVEQIFEARSIDSLSPNLERRIEDWNERIPRILGGPWGFLIGAELTIAQSRISLVNKIQKVYRSQGVQIHNRHIEIIIRQVTSKVRVSEDGMSNVFSPGELIGLLRAERAGRALDESIYYRAILLGITRVSLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGIIPVGTGFQKFVHRYPQNKNLYFEIQKKKLFASEMRDILFLHTELVSSDSDVTNNFYETSESPFTPFI
Protein: Sister-of-Sex-lethal, isoform C (X2JA35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSNADKMQDQEHDDEQSSDIEGSGDNVGRDDGTDDDDDSNGNMQQENGDGGNGGDGQEHSGDEEQHHSQDNEGNDNSAGQQQQMQQVDRTSATNLIINYLPQDMTDRELYNLFSGCGPINTCKIMRDFKLTLPSALYARQRNRPDIASATASWTTKRSRTRRTPSRS
Protein: T-type calcium channel alpha 1G subunit (Q27YN9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVVRGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP
Protein: Huntingtin interacting protein 1 (G3V8Y8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Huntingtin
- Clathrin heavy chain 1
- Clathrin light chain B
- Clathrin light chain A
- Caspase-3
- Intraflagellar transport protein 57 homolog
- Cyclin-G-associated kinase
- AP-2 complex subunit alpha
- AP-2 complex subunit beta
- AP-2 complex subunit sigma
Sequence:
MDRMASSMKQVPNPLPKVLSRRGVGAGMEAAERESFERTQTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTTAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFQRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEVSSPDSEPVLEKDDLMDMDASQQSLFDNKFDDIFGSSLSSDPFNFNNQNGVNKDEKDHLIERLYREISGLTGQLDNVKIESQRAMLQLKGRVSELEAELAEQQHLGRQATDDCEFLRTELDELKRQREDTEKAQRSLTEIEKKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSEQTQRKTQEQQDVLETLKHELATSRQELQVLHGNLETSAQSEAKWLTQIAELEKEQGSLATAAAQREEEFSALRDQLESTQLKLAGAQDSMCQQIKDQRRILLAGARKAAELEIQEALGQLEEPALLISCAGATDHLLSKVNSVSSCLEQLEKSRSQYLACPEEISELLHSITLLGHLTSDTIIQGTATSLRAPPESADSLTEACRQYGRETLAYLSSLEEEGAMEKADTTAIANCLGKIKTIGEELLPRGLDIKQEELGDLVDKEMAATSAAIEAATTRIEEILSKSRAGDTGVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSHEIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQIEETDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELAGVAEGWEEGTEASPSAVQEAVPDKE
Protein: ADP-ribosylation factor-like protein 5B (ADP-ribosylation factor-like protein 8) (Q96KC2)
Organism: Homo sapiens (Human)
Function: Binds and exchanges GTP and GDP.
Interaction partners:
- Pleckstrin homology domain-containing family M member 2
- Kinesin-like protein KIF1A
- Kinesin light chain 2
- Target of Myb1 membrane trafficking protein
- Kinesin light chain 1
Sequence:
MGLIFAKLWSLFCNQEHKVIIVGLDNAGKTTILYQFLMNEVVHTSPTIGSNVEEIVVKNTHFLMWDIGGQESLRSSWNTYYSNTEFIILVVDSIDRERLAITKEELYRMLAHEDLRKAAVLIFANKQDMKGCMTAAEISKYLTLSSIKDHPWHIQSCCALTGEGLCQGLEWMTSRIGVR
Protein: Mitogen-activated protein kinase p38a (MAP kinase p38a) (MAPK p38a) (EC 2.7.11.24) (MAP kinase 14A) (p38 MAPK) (O62618)
Organism: Drosophila melanogaster (Fruit fly)
Function: Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.
Subcellular location: Nucleus {ECO:0000269|PubMed:9417090}.
Interaction partners:
- mitogen-activated protein kinase kinase
- Activating transcription factor-2
- MAP kinase-activated protein kinase 2
- Mitogen-activated protein kinase p38b
- Forkhead box protein O
- Putative mitogen-activated protein kinase 14C
- Myocyte-specific enhancer factor 2
- protein-tyrosine-phosphatase
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- Transcription factor Jra
Sequence:
MSVSITKKFYKLDINRTEWEIPDIYQDLQPVGSGAYGQVSKAVVRGTNMHVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDIFHPHPANGSLENFQQVYLVTHLMDADLNNIIRMQHLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPTENEMTGYVATRWYRAPEIMLNWMHYDQTVDIWSVGCIMAELITRRTLFPGTDHIHQLNLIMEMLGTPPAEFLKKISSESARSYIQSLPPMKGRSFKNVFKNANPLAIDLLEKMLELDAEKRITAEEALSHPYLEKYAEPSVEQTSPPYDHSFEDMDLPVDKWKELIYKEVTNFKPPPSYAQVLKDVK
Protein: O-ureido-L-serine synthase (EC 2.6.99.3) (Cysteine synthase homolog DscD) (EC 2.5.1.47) (O-acetylserine sulfhydrylase) (D2Z027)
Organism: Streptomyces lavendulae
Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the addition of hydroxyurea on O-acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate.
Interaction partners:
Sequence:
MPLFNSILDTIGRTPIVRLQRMAPEHTSVYVKVESFNPGGSVKDRLALSVVLDAEAKGLLKPGDTIVECTSGNVGIALAMVAAARGYRFVAVMGDTYSVERRKLIRAYGGKLVLFPGHLGSKGGNLIADELAEKYGWFRARQFDNPANPSYHRETTASEILADFAGKRLDHFVTGFGTTGTLTGVGQMLRVARPEVRVVALEPSNAAMLARGEWSPHQIQGLAPNFVPGVLDRSVIDDLVTMDEVTARDTSRRLAAEEGIFAGISAGATVATALSIAEHAPEGTVLLAMLPDTGERYLSTFLFDGVDEGSDDAWLASLDTGSGL
Protein: Transmembrane 9 superfamily member 2 (Q04562)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With EMP70 and TMN3, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Subcellular location: Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein IRC10
- Protein HUA2
- Sorting nexin MVP1
Sequence:
MKRGVWLLIYCYATLTKGFSLPGLSPTTYHSGDEIPLLVNRLTPSIYFQHQDEEGNDVSGDKEHFLYSYDYYNKRFHFCRPEHVEKQPESLGSVIFGDRIYNSPFQLNMLEEKECVALCKSTIPGKDAKFINTLIKSGFFQNWLVDGLPAARKAYDSRTKTNYYGTGFELGFTDVKQTVDGKAVPSTMEELTSEASNEDVILDARLPKNVKPNLVKTVELPYFVNHFDIEVEFHDRGNDNYRVVGVIVNPVSIERSSPGACSTTGKPLILDEDKDNEVYFTYSVKFVASDTVWATRWDKYLHIYDPQIQWFSLINFSVIVILLSSVVMHSLLRALKSDLARYNELNLDNEFHEDSGWKLGHGDVFRTPSKSMLLSILVGSGMQLFLMVMCSIFFAAVGLVSPVSRGSLPTVMFVLYALFGFVGSYASMGVYKFFRGPYWKANMILTPILLPGAIFLLIVIMNFFLLFAHSSGVIPARSLFFIILLWFLVSVPLSFAGSIVAHKQCNWDEHPTKTNQIARQIPYQPWYLRTAQATLIAGIFSFGSIAVELYFIYSSLWFNKIFYMFGFLLFSFLLLTLTTSLVTILITYYSLCLENWLWQWRSFIIGGLGCSIYTFIHSILFTKFKLGGVITVVLYLGYSLIISALCCVVTGAIGFFSSMFFIRKIYSAIKVE
Protein: 40S ribosomal protein S21 (Q8IHS5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S3
- 60S ribosomal protein L31
- 60S ribosomal protein L36
- 60S ribosomal protein L18a
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L19
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS1
- 60S ribosomal protein L38
- Small ribosomal subunit protein uS5
Sequence:
MFNDQKVLVDIYIPRKCSATSRLIPAKEHGAVQINVGMVDANGVYNGKTETFAISGHVRQNGESDACLNRLMYEKKLLSFQN
Protein: Integrator complex subunit 11 (C9IYS7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPEIRVTPLGACPVLSWNLVLPPGRGSRAPSSTDTRTGFHVLPHGVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQRNMFEFKHIKAFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVLEVKMQVEYMSFSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTLPTSPSIPVGISLGLLKREMAQGLLPEAKKPRLLHGTLIMKDSNFRLVSSEQALKELGLAEHQLRFTCRVHLHDTRKEQETALRVYSHLKSVLKDHCVQHLPDGSVTVESVLLQAAAPSEDPGTKVLLVSWTYQDEELGSFLTSLLKKGLPQAPS
Protein: Alpha-crystallin B chain (Alpha(B)-crystallin) (P02510)
Organism: Bos taurus (Bovine)
Function: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
Interaction partners:
- Alpha-crystallin A chain
- Beta-crystallin B2
- Beta-crystallin A3
- Heat shock protein beta-1
- Gamma-crystallin S
- Gamma-crystallin D
- Beta-crystallin B1
- Beta-crystallin B3
- Heat shock protein beta-2
- Gamma-crystallin C
Sequence:
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPASTSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK
Protein: Toll-like receptor 5 (F8W4F1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 5b
- Interleukin family protein
Sequence:
MAATYTLFLMLLFIWTPTVKSTSVCSTDGYFAFCMDRGLQEVPKISTYITNVDLSKNRIAELNETSFSHLEALEVLILMHQTPGLVIRRNSFMRLSNLTSLQLDYNHHLRIDAGAFNGLSDLKNLTLTQCGLDDSLLSGNFLKPLMSLEMLDLSRNNIRRVQPASFFLNMRRFHVLDLTFNKVKSICEEDLLNFQGKHFTLLRLSSITLQDMNEYWLGWEKCGNPFKNTSITTLDLSGNGFNVDMAKRFFDAISSTKIQSLIISNTYRIGKSSGDNSKDPDKSTFSGLKSSGIKSFDLSNSSIFSLTYSVFSYLSDLEQITLAESQINKIENNAFLGMTNLLKLNLSKNFLGYIDFRTFQNLKGLEVLDLSYNHIWRLGSQSFQGLPNLLSLNLTGNSLGHVYTFATLPKLEKLYLGDNNIQYVYEIPNIAKHLKTLDLQFNQIASMSELYTILDEFPQIEEVVFRGNQLLYCPQDNHEVLSQNIQVLDLSFAGLQVIWSEGKCLNVFDDLHQLEVLHLSSNLLQSLPKDIFKDLTSLLILDLSFNSLKYLPTDVFPKTLQVLHLDYNSIYSVDPNLFSTLSYLSLMNNDFRCDCDLKDFQTWLNQTNITFVHSIEDVTCASPEDQYMVPVVSSSIQCEDEEEERRTEKLRLVLFISCTVLIILFSASTIVYISRRGVIFKIYKKLIGKFDNKPQEEPDANGFLYDVYLCFSSRDMKWVERALLKRLDSQFSEHNTLRCCFEERDFIPGEDHLTNMRNAIQHSRKTICVVSKHFLKDGWCLETFTLAQCRMLVELKDILVVLVVGNIPQYRLLKYEQLRSFIENRSYLVWPDDGQDLEWFYDQLLHKIIRNTKVKQTNIKEKDKVDENNPEAADVQADTAV
Protein: Holliday junction branch migration complex subunit RuvB (EC 3.6.4.-) (P0A812)
Organism: Escherichia coli (strain K12)
Function: The RuvABC complex is involved in recombinational repair of UV or chemically damaged DNA. The RuvAB complex also plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be separated. This subunit has a weak ATPase activity that is inhibited by its ADP product; binds ADP better than ATP. Promotes Holliday junction (HJ) branch migration in conjunction with RuvA. Binds to HJ cruciform DNA; in the presence of RuvA, ATP and Mg(2+) the junction is dissociated. Hydrolyzable (d)NTPs can replace ATP but other analogs cannot. The RuvB hexamer acts as a pump, pulling DNA into and through the RuvAB complex. Can bypass UV-induced lesions and physically cross-linked DNA strands, suggesting RuvB does not unwind large sections of DNA. RuvA gives specificity by binding to cruciform junctions, while the RuvB ATPase provides the motor force for branch migration; excess RuvB can promote branch migration in the absence of RuvA. In vitro the RuvA-RuvB complex has 5'-3' helicase activity that is ATP-dependent and works best on short dsDNA hybrids; 52 and 66-nucleotide (nt) pairs are easily displaced, hybrids greater than 140-nts are not. RuvA stimulates the weak ATPase activity of RuvB in the presence of DNA; HJ DNA stimulates ATPase about 10-fold.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
Interaction partners:
- Holliday junction branch migration complex subunit RuvA
- Crossover junction endodeoxyribonuclease RuvC
- UvrABC system protein A
- UvrABC system protein B
- UvrABC system protein C
- ATP-dependent DNA helicase RecG
- ATP-dependent DNA helicase RecQ
- Protein RecA
- DNA helicase II
- DNA repair protein RecN
Sequence:
MIEADRLISAGTTLPEDVADRAIRPKLLEEYVGQPQVRSQMEIFIKAAKLRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYQVPDLQYIVSRSARFMGLEMSDDGALEVARRARGTPRIANRLLRRVRDFAEVKHDGTISADIAAQALDMLNVDAEGFDYMDRKLLLAVIDKFFGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFLQRTPRGRMATTRAWNHFGITPPEMP
Protein: 1-aminocyclopropane-1-carboxylate oxidase 1 (ACC oxidase 1) (AtACO1) (EC 1.14.17.4) (Q9ZUN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme involved in the ethylene biosynthesis. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
Interaction partners:
- 1-aminocyclopropane-1-carboxylate synthase 4
- 1-aminocyclopropane-1-carboxylate synthase 2
- 1-aminocyclopropane-1-carboxylate synthase 8
- 1-aminocyclopropane-1-carboxylate synthase 7
- 1-aminocyclopropane-1-carboxylate synthase-like protein 1
- 1-aminocyclopropane-1-carboxylate synthase 9
- 1-aminocyclopropane-1-carboxylate synthase 5
- 1-aminocyclopropane-1-carboxylate synthase 11
- 1-aminocyclopropane-1-carboxylate synthase 6
- Aconitate hydratase 1
Sequence:
MVLIKEREMEIPVIDFAELDGEKRSKTMSLLDHACDKWGFFMVDNHGIDKELMEKVKKMINSHYEEHLKEKFYQSEMVKALSEGKTSDADWESSFFISHKPTSNICQIPNISEELSKTMDEYVCQLHKFAERLSKLMCENLGLDQEDIMNAFSGPKGPAFGTKVAKYPECPRPELMRGLREHTDAGGIILLLQDDQVPGLEFFKDGKWVPIPPSKNNTIFVNTGDQLEILSNGRYKSVVHRVMTVKHGSRLSIATFYNPAGDAIISPAPKLLYPSGYRFQDYLKLYSTTKFGDKGPRLETMKKMGNADSA