wanglab/gogpt-training-data huggingface dataset:
Protein: Proline-rich family protein (Q8GYK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Histone-binding protein MSI1
- Integral membrane hemolysin-III-like protein
- Hydroxyproline-rich glycoprotein family protein
- Protein ALWAYS EARLY 3
- Transcription factor E2FB
- Transcription factor E2FC
- Transcription factor-like protein DPB
- Protein ALWAYS EARLY 1
- At2g40630/T2P4.2
- Protein ALWAYS EARLY 2
Sequence:
MSTPDPNPNPNPNPSVSVAVSTPIVTASESPVTQPNTVITPSSQPQPQTPASSYRAIAPLHRHHPHQNIYTNPLPIRRSNSVTNSPHQPPHPDPSSLIYPFGSSGRGFPTRPVRQNSNSVADPVGSPSPGGYTPRGPVYGYHHGQFVSNLDPMNQFMRAAHPQNQQSPQLGSGHMKGVPHFLQPRATPSPTSILDNSGHKKARSRDDALVLVRKRKVRITEGASLYSLCRSWLRNGAHEGIKPQRIDMMTCLPKPLPVDKTETSLPKDLVEEAICEEDKEDEESVKHLSESDLLKRHIDRAKKVRARLREERLKRIARYKARLALLLPPFGEQCRNE
Protein: Beta-defensin 106 (Beta-defensin 6) (BD-6) (DEFB-6) (Defensin, beta 106) (Q8N104)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity. Acts as a ligand for C-C chemokine receptor CCR2.
Subcellular location: Secreted {ECO:0000305}. Membrane {ECO:0000269|PubMed:23938203}. Note=Associates with tumor cell membrane-derived microvesicles (PubMed:23938203). {ECO:0000269|PubMed:23938203}.
Interaction partners:
- Beta-defensin 105
- Beta-defensin 104
- Beta-defensin 107
- Beta-defensin 103
- Beta-defensin 108B
- Beta-defensin 1
- Sperm associated antigen 11B
- Defensin beta 4A
- Beta-defensin 126
- Beta-defensin 110
Sequence:
MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGTCKNNCGKNEELIALCQKSLKCCRTIQPCGSIID
Protein: Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein) (P0AFX7)
Organism: Escherichia coli (strain K12)
Function: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E. Overexpression of RseA blocks sigma-E from acting, results in cell lysis in stationary phase and temperature-sensitivity above 37 degrees Celsius.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}; Single-pass type II membrane protein {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Following cleavage by DegS the large fragment of the protein is still in the inner membrane and retains its anti-sigma-E activity.
Interaction partners:
- Sigma-E factor regulatory protein RseB
- ECF RNA polymerase sigma-E factor
- Serine endoprotease DegS
- Protein RseC
- Stringent starvation protein B
- Regulator of sigma-E protease RseP
- RNA polymerase sigma factor RpoD
- Negative regulator of flagellin synthesis
- Periplasmic serine endoprotease DegP
- RNA polymerase sigma factor RpoS
Sequence:
MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ
Protein: NAC domain-containing protein 90 (ANAC090) (Q9FMR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
Sequence:
MADEVTIGFRFYPTEEELVSFYLRNQLEGRSDDSMHRVIPVLDVFEVEPSHLPNVAGVRCRGDAEQWFFFVPRQEREARGGRPSRTTGSGYWKATGSPGPVFSKDNKMIGAKKTMVFYTGKAPTGRKTKWKMNEYHAVDETVNASTIPKLRREFSLCRVYITTGSSRAFDRRPEGVLQTERMLTSDVAVAETSFRVESSLETSISGGEHIDVSMNTEFVDGLSEPMWDWEQLTWP
Protein: Methylcytosine dioxygenase TET (EC 1.14.11.80) (D4AC33)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- Histone deacetylase 2
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Homeobox protein NANOG
- DNA
- DNA
- ASXL transcriptional regulator 1
- DNA
- Transcription factor PU.1
- Methylcytosine dioxygenase TET
- CXXC-type zinc finger protein 5
Sequence:
MEQDRTTHAEGTRQSPFLIASPSPVSHTEPLAVKLQNGSPLAERPHPEVNGDTKWQSFQSYYGIPHMKGSQSSHESPDFIHEGRGYSGCLQNGGIKRTVSEPSLSGLHLNTKLTLDQKAKGESNNFGESQEGNPGKSSSHPNVSGLSDDREPGTSTAQESTDIDAFPTRNYNGVENTEIPEEQEGGNDRNALLLKNKAVLMPNGATVSAPSVEDTHGEFLEKTQCYPDCVSMAVQNNTTPHVNALSGQAAIELPREITQPSLTSAQINFSQTSSAQLPPEPAAMVTKACDLDSASKPAGVLGTCAFQKAEHQQKSVLGIGPSSCAENINIQGNTKPFAEEYYAGSDSDLQTSLGSSEQCIKQKETNGAYFRQSSVFPEDSISATTMTPPSPSPLAPRPVLQLPSEGKGTLNDVALEEHHRYPNQSDLTLSREGKTEHQPKKTTSSQSLNTSVHTPNPPLMLPEQHQNDCVPPCSEKTRKVSDYRMYYLPNHGHGGDLQENSQYLMGHGEHEILKDANKGQTQGSVLAAPGWIELKASHFHKALHQTECKATSLHSGLRYQTSPTNQIGSIQSTGSVNMTGEFQRPPYIQKTAQPEHKSQMYQVEMNQGPSPGMGDQHLQFQKTSYQECISRTDLPPEAHGPQYHFHQRVDPSTDKQQATEAELFSSFLQHTPHKQAAQTQASQNSNFPQVCQQQHQLQRKNKEQMPQTFSHLHGTNHEQSQGQCFGTIKAEESFCGENQYSKPSNFQTHSAQGGLEQVQNVNRSFPYAKIETPNSSKVQTLCSNYTHPASESREQNLHLDLFIGNRTPNQQNTQCFPNNVTPSQDVAHRCFQEQEQKPHQASSLQGLKGRSRDEFSVPPAEATQARYLVHIQAKALPVPKQGGSHTQISPQKDTQKHAALRRLLLQKQEQQQIQQSQSESGHHQMPRPIKIEPGSKLSSCKHPTSGPQENMPKRIKQESPLLSCDGGRTESIIETMERHLKQFQLKALCDYKILTLNSQRQGDVETATNARSAGSENHTPAAEPQASLSEKTPTKRTADSVLTDVSESPSDSDTPVEDISCEACKNAEKDEGPYYTHLGAGPNVAAIRTIMEERFGEKGKAIRIERVIYTGKEGKSSQGCPIAKWVYRRSSTEEKLLCLVRVRAKHTCDTAVIVIVILLWDGIPKPLASELYSELTEILSNRGICTNRRCAQNENRNCCCQGENPETCGASFSYGCSWSMYYNGCKFARSKNPRKFRLHGDEPKEEEKLGSHLQNLATVIAPIYKKLAPDAYRNQVEFEHRAIECRLGLKEGRPFSGVTACLDFSAHAHRDQQNMANGSTVVVTLTREDNREVGGQPEDEQLHVLPLYTIATEDEFGSTEGQEEKILQGSIQVLHSFRRRRVRRLVDPPKNCRQKKLEAKKARKLSSLENCSNKNEKEKSSSRTRPMENASPMIQMTAQLRLSGSVIQQPQSLQRHLQQVQRPPQPQPPQPQHILPSNSQPVGSHSSGSTNVYMRQPAPLSPYPSSSHAADMYGDANHVNFHPTSSHAAGLYLSPSNSMNPYPGLFNQNNQYAASQCNGSMSADSGPPFLGPYSPQSQSRGLHRYPNQDHLSNLNLPPIHTLYPQRSDSPFKYLNYGNQNNVQRDRDAFTNCPLKPNVHHLPTFSSYATPKMDGHFMGAASRLPYSHPNMEYKSSDHHLPPHMIHGYPTAASGSVSSSSHAFHNKENDNMVSHTANGLSRVLPGFNHDRTASAQGPLYSLPDYSQEKQPGVSGQDGASVEDIEVWSDSEHNFQDPSIGGVAIAPTHGSILIECAKCEVHATTKVNKPNRKKPARISLVFYQHKNLNEPKHSLAVWEAKMAGKARKEEEECEKYGSDHVSQKNHGKRVKREPTGPQETPKPSYLRFIHSLAENTVSMTTDSTVTTRPYAFTQVTGPYNTYV
Protein: Protein lev-9 (Q22328)
Organism: Caenorhabditis elegans
Function: Scaffolding protein that is necessary to cluster acetylcholine receptors at neuromuscular junctions.
Subcellular location: Synapse {ECO:0000269|PubMed:19794415}. Secreted {ECO:0000269|PubMed:19794415}. Note=Secreted by muscle cells and localizes at cholinergic neuromuscular junctions.
Interaction partners:
- CUB domain-containing protein
- Immunoglobulin domain-containing protein oig-4
- Lipoma HMGIC fusion partner-like 3 protein
- CUB domain-containing protein
- Acetylcholine receptor subunit beta-type lev-1
- UDP-glucuronosyltransferase
Sequence:
MRFLLLLAISITYASALSCPEVTLSQRPKHCKKECIADEDCKRNKRCMCDGECGLSCVNPIAMCHPLPNIENGFIRTAGDLRFGSNAEYGCNKGYILVGASQRRCQANKEWSSSQPVCRLQLKCGPPPEIPFAVHDGSSFSGEYDLDAEVAYNCIPGYHKFNAKGLSISKCLLNRKNVAQWFGPDLRCKARACPDPGDIENGLREGDTFEYPHHVKYSCNPGFLLVGSTSRQCSSNGEWTNEPANCKATECSRPSSPLHGKVVGSSLTYQSVVTYSCDHGYRLVGQVQRICLAEGIWGGNEPRCEEIRCSVLPTLPNGYIEGSETSFGAVAVFRCLETMTHEGASKAKCMEDGQWSAPIPRCLASCRVPHIQNGKIRDKSEGQLIASGSKVIVECNKQHEANIDERLICSNSTWSHVPVCSPLSCHNWPPRVPHARILFSKSSHGSIAKYECNNGYHPNRNNQIIKCLYGEWTKDGPPMKCLPSWCEHPSKTYGTLPGGQILLEGILGAYEFQSYIQKVEEGRAISFQCGKGNYLIGPPKATCVNGEWMPKVSPKCVSQTHPMIEGKILWDRKKRSLPGRAVREYVDDELSTHRQHSGKCGIVSGKLERMIMQHSDNGVSVC
Protein: Probable glucuronoxylan glucuronosyltransferase IRX7 (EC 2.4.1.-) (Protein FRAGILE FIBER 8) (Protein IRREGULAR XYLEM 7) (Q9ZUV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the synthesis of the glycosyl sequence at the glucuronoxylan reducing end.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:16272433}; Single-pass type II membrane protein {ECO:0000305|PubMed:16272433}.
Interaction partners:
- Beta-1,4-xylosyltransferase IRX9
- Beta-1,4-xylosyltransferase IRX14
- Probable galacturonosyltransferase 12
- Probable galacturonosyltransferase-like 1
- Probable beta-1,4-xylosyltransferase IRX14H
- Probable beta-1,4-xylosyltransferase IRX9H
- Cellulose synthase A catalytic subunit 4
- Cellulose synthase A catalytic subunit 7
- Cellulose synthase A catalytic subunit 8
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
Sequence:
MTTHKHRRTEKNLCFKQYYKWILCFILTLYFFASFFVDHDQDHRSSTSISKHLLTNHKPKLFASRAMFESKIHDHKLGFTSQQPNIKTDVFNNLKIYVYDLPSKFNKDWLANDRCTNHLFAAEVALHKAFLSLEGDVRTEDPYEADFFFVPVYVSCNFSTINGFPAIGHARSLINDAIKLVSTQYPFWNRTSGSDHVFTATHDFGSCFHTMEDRAIADGVPIFLRNSIILQTFGVTFNHPCQEVENVVIPPYISPESLHKTQKNIPVTKERDIWVFFRGKMELHPKNISGRFYSKRVRTNIWRSYGGDRRFYLQRQRFAGYQSEIARSVFCLCPLGWAPWSPRLVESVALGCVPVIIADGIRLPFPSTVRWPDISLTVAERDVGKLGDILEHVAATNLSVIQRNLEDPSVRRALMFNVPSREGDATWQVLEALSKKLNRSVRRSNSFL
Protein: beta-galactoside alpha-(2,6)-sialyltransferase (EC 2.4.3.1) (Q9GU23)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}.
Interaction partners:
- CMP-sialic acid synthase
- Beta1,4-N-acetylgalactosaminyltransferase A
- N-acetylneuraminate-9-phosphate synthase
- Nidogen
- Hemolectin, isoform A
Sequence:
MRQVTRASSGQSQALLSCLIIAVCAALIIQSGHIQGVKAQPGREPGEVNSRQPGNGAYENSTGTERRLRKVIWKCIPTGNGTTGHRVPRSVFHVRWNPNEKFIVESRENPAINSSKLAPHPRLKVSKNTKLTLSPKLYLCHDKHSELCHNKTQQFRQRIVRAFEKAMVESVNESQANHYNVDYKPVFGDSFEEQYYPSTCLVMEAGVRVLRRKDAPFNKLPFGRLFPRQKLFRNVKDIKTCAIVSSAGSLAGSKLGRFIDTHDIVMRFNHAPTQGHEVDVGSKTTIRVVNSQVVTKPEFDFTRAPIFRNVTIAAWDPGKYNGTLEDWLTSADYDLFSNYELYRRRYPKSRAFLIDPHSVWRLWQSLQMFAGNRPISKNPPSSGFIGLALLLPHCPQVDFVEYVPSTRLNGRCHYYSKEMNSACTFGSWHPLAAEKLMALDMNMAEDDDMSVFQFGILRIRRPDKLLCGFNFFGY
Protein: Beta-toxin Ct1a (Beta-toxin Clt1) (Neurotoxin 1) (Toxin II.20.3.4) (P18926)
Organism: Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Is lethal to mice but does not show toxicity to freshwater shrimp and crickets.
Subcellular location: Secreted {ECO:0000269|PubMed:2849217}.
Interaction partners:
Sequence:
MNSLLMITACLALIGTVWAKEGYLVNHSTGCKYECFKLGDNDYCLRECRQQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCNGK
Protein: 14-3-3-like protein GF14-6 (P49106)
Organism: Zea mays (Maize)
Function: Is associated with a DNA binding complex to bind to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Interaction partners:
- Uncharacterized protein
- Growth-regulating factor 1
Sequence:
MASAELSREENVYMAKLAEQAERYEEMVEFMEKVAKTVDSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEEGRGNEDRVTLIKDYRGKIETELTKICDGILKLLETHLVPSSTAPESKVFYLKMKGDYYRYLAEFKTGAERKDAAENTMVAYKAAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACSLAKQAFDEAISELDTLSEESYKDSTLIMQLLRDNLTLWTSDISEDPAEEIREAPKRDSSEGQ
Protein: Vascular endothelial growth factor C (VEGF-C) (Flt4 ligand) (Flt4-L) (Vascular endothelial growth factor-related protein) (VRP) (O35757)
Organism: Rattus norvegicus (Rat)
Function: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors.
Subcellular location: Secreted.
Interaction partners:
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Neuropilin-2
- Extracellular link domain-containing 1
- Vascular endothelial growth factor D
- Angiopoietin-1 receptor
- Platelet-derived growth factor receptor beta
- Neuropilin-1
- Platelet-derived growth factor receptor alpha
Sequence:
MHLLCFLSLACSLLAAALIPGPREAPATVAAFESGLGFSEAEPDGGEVKGFEGKDLEEQLRSVSSVDELMSVLYPDYWKMYKCQLRKGGWQQPSLNMRTGDTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPANYVWNNYMCQCLAQQDFIFYSNVEDDSSNGFHDVCGPNKELDEDTCQCVCKGGLRPSSCGPHKELDRDSCQCVCKNKLFLNSCGANREFDENTCQCVCKRTCPRNQPLNPGKCACECTENTQKCFLKGKKFHHQTCSCYRRPCTNRLKHCDPGLSFSEEVCRCVPSYWKRPHLN
Protein: Isopimaradiene synthase (EC 4.2.3.-) (Kaurene synthase 6) (IrKSL6) (A0A1Z3GCD1)
Organism: Isodon rubescens (Rabdosia rubescens)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to isopimaradiene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MFSSSLKLKTNPLMDNKIHRSSSDRDFRGSTISSVKCSLNNSEDLIVKVRERVKGKVEISPSAYDTAWVAMVPERDYSGQKPRFPECLDWIVENQNADGSWGVQSSSMLKHSLSCTLACLLPLRKWNVASPQLLRNGVEFIRSSSSAATDKNQISPIGFDIVFPMMIQYANDLNLELLLNQDLVNILFQNREAQLTRNKNLEYVAEGLGSSIDWNKVLMHQRSNGSLFNSPATTAAALIHRHDKKCLEYLNSLLSIYKTWVPTIHPMDVYARLCLVDHLQGLGVDRFVHPEIEVVLQETFRLWQQKDDKIFTDATCRAMAFRLLRMQGYHVTPDELGGYVDEESFFATVSFESSGTDTVLELYKASQVRLPEDDDTLEKLHDWTSKFLKQKLQSKTILDQQLERKVEFNLKNYHGILDAVKHRRNFDLYDIDHRRILKTAYRCPTVYNEDILLLTAQDLMTRQVQNQKELQIMERWLEDCRLDKVSGRNAVLVSYFLNANNFPDPRLSEARLAYAKTVTLITFLDDFFDHHGSREDSLLIMELINKWTEPLTVSYPSDEVEILYSALHATITDTAEKVYAVQGRCIKSLIIELWMEVLTAMLGEMDSCNADTPPDFDEYMAFAPKSLGCSLSILPSLHLMGETISEEMVTSLECFELDKHVSIAIRLLNDQQTFERERKERTTNSVTLLMDADQISEEEAVSRIQKLIEHHTKELLKLVVQKEGSVLPRKCKDIFWNTIKVGYCLYRFSDEFTSPQQMKEDMKLLFHDPVLKTTP
Protein: Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (p94) (v-Raf murine sarcoma viral oncogene homolog B1) (P15056)
Organism: Homo sapiens (Human)
Function: Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway. May play a role in the postsynaptic responses of hippocampal neurons.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:19710016}. Cell membrane {ECO:0000269|PubMed:19710016}. Note=Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes. {ECO:0000250}.
Interaction partners:
- 14-3-3 protein zeta/delta
- GTPase HRas
- RAF proto-oncogene serine/threonine-protein kinase
- GTPase KRas
- GTPase NRas
- Dual specificity mitogen-activated protein kinase kinase 1
- Heat shock protein HSP 90-beta
- Dual specificity mitogen-activated protein kinase kinase 2
- Serine/threonine-protein kinase A-Raf
- 14-3-3 protein theta
Sequence:
MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) (Cobalamin-independent methionine synthase) (Methionine synthase, vitamin-B12 independent isozyme) (P25665)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Interaction partners:
- Methionine synthase
- 5,10-methylenetetrahydrofolate reductase
- S-adenosylmethionine synthase
- Cystathionine gamma-synthase
- Cystathionine beta-lyase MetC
- HTH-type transcriptional regulator MetR
- Homocysteine S-methyltransferase
- S-ribosylhomocysteine lyase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Methionine--tRNA ligase
Sequence:
MTILNHTLGFPRVGLRRELKKAQESYWAGNSTREELLAVGRELRARHWDQQKQAGIDLLPVGDFAWYDHVLTTSLLLGNVPARHQNKDGSVDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLTWTQLLDEVDEALALGHKVKPVLLGPVTWLWLGKVKGEQFDRLSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQAWLDAYKPAYDALQGQVKLLLTTYFEGVTPNLDTITALPVQGLHVDLVHGKDDVAELHKRLPSDWLLSAGLINGRNVWRADLTEKYAQIKDIVGKRDLWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCHELALLRDALNSGDTAALAEWSAPIQARRHSTRVHNPAVEKRLAAITAQDSQRANVYEVRAEAQRARFKLPAWPTTTIGSFPQTTEIRTLRLDFKKGNLDANNYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPIVIGDISRPAPITVEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLRRSDWDAYLQWGVEAFRINAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEEFDYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAKRIPAERLWVNPDCGLKTRGWPETRAALANMVQAAQNLRRG
Protein: Aurora kinase A-A (EC 2.7.11.1) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Serine/threonine-protein kinase 6-A) (Serine/threonine-protein kinase Eg2-A) (pEg2) (Serine/threonine-protein kinase aurora-A) (p46Eg265) (Q91820)
Organism: Xenopus laevis (African clawed frog)
Function: Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Phosphorylates numerous target proteins. Important for microtubule formation and/or stabilization.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10329703, ECO:0000269|PubMed:9454730}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10329703, ECO:0000269|PubMed:9454730}. Note=Localizes to the spindle pole during mitosis especially from prophase through anaphase. Partially colocalized with gamma tubulin in the centrosome, from S to M phase. {ECO:0000269|PubMed:9454730}.
Interaction partners:
Sequence:
MERAVKENHKPSNVKIFHPMTEGAKRIPVNQPQSTQFRPPGTAVSAQRILGPSNVPQRVLAQAQKPILSSQKPTTQIPLRPATQGHQSSKPQGPNENRNPQQTSHSSTPNVEKKGSTDQGKTSAVPKEEGKKKQWCLEDFEIGRPLGKGKFGNVYLARERESKFILALKVLFKSQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDASRVYLILDYAPGGELFRELQKCTRFDDQRSAMYIKQLAEALLYCHSKKVIHRDIKPENLLLGSNGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDETVDLWSLGVLCYEFLVGKPPFETDTHQETYRRISKVEFQYPPYVSEEARDLVSKLLKHNPNHRLPLKGVLEHPWIIKNSQLKKKDEPLPGAQ
Protein: Thioredoxin (Q38FJ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- peptide-methionine
- Trypanothione reductase
- Tryparedoxin
- Tryparedoxin
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- Monothiol glutaredoxin, putative
- SUMO-conjugating enzyme UBC9
- GST N-terminal domain-containing protein
- Thioredoxin domain-containing protein
Sequence:
MSVVDVYSVEQFRNIMSEDILTVAWFTAVWCGPCKTIERPMEKIAYEFPTVKFAKVDADNNSEIVSKCRVLQLPTFIIARSGKMLGHVIGANPGMLRQKLRDIIKDN
Protein: tRNA pseudouridine(38/39) synthase (EC 5.4.99.45) (tRNA pseudouridine synthase 3) (tRNA pseudouridylate synthase 3) (tRNA-uridine isomerase 3) (Q9JI38)
Organism: Mus musculus (Mouse)
Function: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs. Also acts on position 38, but much less efficiently.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pseudouridylate synthase 7 homolog
- Pseudouridylate synthase PUS7L
- tRNA pseudouridine synthase Pus10
- tRNA
- Pseudouridylate synthase RPUSD4, mitochondrial
- RNA pseudouridylate synthase domain-containing protein 1
- Pseudouridylate synthase TRUB1
- tRNA
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Mitochondrial mRNA pseudouridine synthase Rpusd3
Sequence:
MAENTDRNQIEKLLNRVKELEQEVERLKKKKEQANNIKDSSIRENSLGSGKAKRAFDFSAHGRRHVALKIAYLGWGYQGFASQENTSNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPTSRDSEDSNLKHEADDLAKEIRYTHILNRVLPADIRVLAWAPVEPSFSARFSCLERTYRYFFPRADLDIATMNYAAQKYVGTHDFRNLCKMDVANGVINFQRTILCAQVQLVAQSPGEERRQEPFQLCQFEVIGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIQKNPQKPQYSMAVEFPLVLYDCKFENTKWIYDHEVQEFNVTHLQQLWANHAVKTHMLYSMLQGLDSVMVTCAAGTKMDEATEWRNIQPPVIKHTSAFVEGVKMRTYKPLMDRPKCQGLESRIRHFVSRGRIEHPHLLHKEEIKARRDCADKEENTVVENPSKRVCIIDAEINSIA
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (Q5A0M4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS6
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein RACK1
Sequence:
MVAFTIEQIRGLMDKVTNVRNMSVIAHVDHGKSTLSDSLVQKAGIISAAKAGDARFMDTRKDEQERGITIKSTAISLYASMTDEDVKDIKQKTDGNSFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQTTKEDLYQTFARTVESVNVIISTYCDPVLGDVQVYPQKGTVAFASGLHGWAFTVRQFANKYSKKFGVDKEKMMERLWGDSYFNPKTKKWTNKDKDADGKPLERAFNMFILDPIFRLFAAIMNFKKDEIPVLLEKLEIQLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAETLYEGPSDDPFCTAIRNCDPNADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYQVGKKEDLFLKSIQRTVLMMGRSVEQIDDCPAGNIIGLVGIDQFLLKSGTITTNEAAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLENDHAGVPLRISPPVVSYRETVEGESSMVALSKSPNKHNRIYVKAQPIDEEVSLDIENGVINPRDDFKARARILADKHGWDVVDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGENCRSVRVNILDVTLHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQLIFDHWQVMSGDVTDENSKPGAIVKEKRVRAGLKPEVPEYTEYYDKL
Protein: 6-phospho-beta-galactosidase (EC 3.2.1.85) (Beta-D-phosphogalactoside galactohydrolase) (PGALase) (P-beta-Gal) (PBG) (C7N8L9)
Organism: Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b)
Interaction partners:
- PTS system lactose-specific EIICB component
- PTS system lactose-specific EIIA component
- Galactose-6-phosphate isomerase, LacB subunit
- Galactose-6-phosphate isomerase, LacA subunit
- Tagatose-bisphosphate aldolase
- Phosphohexomutase
Sequence:
MSKKLPEDFIFGGATAAYQAEGAIKIDGKGPVAWDKFLEENYWYTAEPASDFYHQYPVDLKLCEEFGINGIRISIAWSRIFPNGYGEVNPKGVEFYHKLFAECKKRKVEPFVTLHHFDTPEVLHSNGDFLNRENIEHFVNYAKFCFEEFSEVNYWTTFNEIGPIGDGQYLVGKFPPGIKYDFEKLFQSHHNMVLAHAKAVNLFKKNGYHGEIGMVCALPTKYPYDPNNPKDVRAAELDDIIHNKFILDATFKGEYSKNTMEGVNHILQVNGGKLDLREEDFEELKAAKDLNDFLGINYYMSDWMAEYDGETEIIHNATGNKGSSKYQIKGVGQRKANESIPRTDWDWIIYPQGLYDQISRVKKDYPNYKKIYITENGLGYKDVFEDNTVYDDARIDYIRQHLEVISDAIKDGANVKGYFLWSLMDVFSWSNGYEKRYGLFYVDFETQKRYPKKSAYWYKKVSETKEV