wanglab/gogpt-training-data huggingface dataset:
Protein: site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) (O25521)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Type I restriction enzyme endonuclease subunit
- Type I restriction enzyme S protein
- Anti-codon nuclease masking agent
- Restriction endonuclease subunit S
- Type I restriction enzyme S protein
- type I site-specific deoxyribonuclease
- Type I restriction enzyme endonuclease subunit
Sequence:
MENNPNNNQASLERNELHNTIWKVANELRGSVDGWDFKQYVLGILFYRYISENMTHYINKEERKRDPSFDYAKLSDEKAERGRKHLIEQKGFFIPPSALFCNALKNACHNEDLNVTLQNIFNEIEKSSLGTPSEENVKGLFADLDVNSNKLGSSHQNRVEKLTKILEAIGGMQLGDYLKSGIDVFGDAYEYLMAMYASNAGKSGGEFFTPQEVSELLAKITLHGQESVNKVYDPCCGSGSLLLQFSKVLGDKNVSKGYFGQEINLTTYNLCRINMFLHDINYSKFHIAHGDTLLDPKHEDDEPFDAIVSNPPYSTKWVGDSNPILINDERFSPAGVLAPKNAADLAFTMHMLSYLSNSGTAAIVEFPGVLYRGNAEAKIREYLVKENVIDCVIALPDNLFFGTSIATCILVLKKNKQDDTTLFIDASKEFVKEGKKNKLKERNREKILQTYIERKEIKHFCALANIEKIKENDYNLSVNRYVEQEDTKEAIDIKALNSEIAQIVEKQSALRNRLESIIKELEGGQNA
Protein: Uncharacterized protein YML053C (Q04978)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase 2
Sequence:
MLSYYEHNTAFQTNNCNSGSNAATTYNSDANNDTIMNKRKNDHFEFDTHTFYQRSKRTKRDSVSTKFSVGSGCANLNNNNNNIIINNNNNNNNNNNNHNHNNSNNTATYNNIHYKKNIEICPLKPVSMHHTMNSRLLNESEFYSETEEYMIHGYFGNTNRDITGTSPTGSASIIQHQYHLLPSQSIIASQAPGTAMAALTNNNIANDYMDID
Protein: Protoporphyrinogen oxidase 2 (Protox II) (EC 1.3.3.4) (SO-POX2) (Q94IG7)
Organism: Spinacia oleracea (Spinach)
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular location: [Isoform L]: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:11274159}; Peripheral membrane protein {ECO:0000305}; Stromal side {ECO:0000269|PubMed:11274159}.; SUBCELLULAR LOCATION: [Isoform S]: Mitochondrion inner membrane {ECO:0000269|PubMed:11274159}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVILPVSQLSTNLGLSLVSPTKNNPVMGNVSERNQVNQPISAKRVAVVGAGVSGLAAAYKLKSNGLNVTLFEADSRAGGKLKTVVKDGLIWDEGANTMTESDEEVTSLFDDLGIREKLQLPISQNKRYIARDGLPVLLPSNPVALLKSNILSAKSKLQIMLEPFLWKKHNGAKVSDENAQESVAEFFERHFGKEFVDYLIDPFVAGTSGGDPQSLSMRHAFPELWNIENRFGSVISGFIQSKLSSKKEKGGEKQSSNKKPRVRGSFSFQGGMQTLVDTICKEFGEDELKLQSEVLSLSYSHNGSLTSENWSVSSMSNSTIQDQPYDAVVVTAPINNVKELKIMKVENPFSLDFIPEVSCLPLSVIITTFKKTNVKRPLEGFGVLVPSNEQHNGLKTLGTLFSSMMFPDRAPSDVYLYTTFVGGSRNRELAKASTDELKQIVSSDLQQLLGTEGEPTFVNHFYWSKAFPLYGRNYDSVLRAIEKMERDLPGLFYAGNHKGGLSVGKSIASGYKAAELAISYLESNKMTEETI
Protein: Uncharacterized protein YPL245W (Q12179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- UPF0659 protein YMR090W
- Uncharacterized protein IRC4
Sequence:
MHGPTSKAISRNVRSVKRPRRAPRPVVSTQAMNKLSNVTLSAEQEKLRERVLSFMRSNLSQYKSDWKHPAMFVIQGDAGTGKSVILNSLFNEIQKLSQFSPSSEDILHGTHNYLVVNHPEMLKLYIRISDSFKYISKSSLERPTSLINNLQKRKVMADVVIVDEAHLLATSKDAFKRFYGENHLKDLMSLCKVLVLVYDDKQALRMGSYWDEGSNNGATLKDFYNEIPPKSRDWYTLKQQFRVAAPQNVLNWIDQISVAGKIPPIESVLSKGNADCADDKIKNFDFKIWDDCGAMYEAIKEKDRQYGQCRMLSTYDFPYRLDGKDYYVECGDNFKVRWDRYTPREVTPWSERCDTIDEVGSVYTIQGFDLNYAGVILGRSIGYDAANDCIKLRPELYDDRAGFTKKKNIHNAEDVKQKIIMNSINVLLTRGVRGLYVYAYDPELRERLLRPSKK
Protein: LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1) (P53667)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21682918}. Nucleus {ECO:0000269|PubMed:21682918}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10196227, ECO:0000269|PubMed:16230460}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P53668}. Note=Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:P53668}.
Interaction partners:
- Cofilin-1
- Cofilin-2
- Bone morphogenetic protein receptor type-2
- Serine/threonine-protein kinase PAK 4
- Serine/threonine-protein kinase PAK 1
- Protein phosphatase Slingshot homolog 1
- LIM domain kinase 2
- Serine/threonine-protein kinase PAK 2
- Serine/threonine-protein kinase PAK 6
- Rho-associated protein kinase 1
Sequence:
MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFRCCDCSASLSHQYYEKDGQLFCKKDYWARYGESCHGCSEQITKGLVMVAGELKYHPECFICLTCGTFIGDGDTYTLVEHSKLYCGHCYYQTVVTPVIEQILPDSPGSHLPHTVTLVSIPASSHGKRGLSVSIDPPHGPPGCGTEHSHTVRVQGVDPGCMSPDVKNSIHVGDRILEINGTPIRNVPLDEIDLLIQETSRLLQLTLEHDPHDTLGHGLGPETSPLSSPAYTPSGEAGSSARQKPVLRSCSIDRSPGAGSLGSPASQRKDLGRSESLRVVCRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKNVVVADFGLARLMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEHWLETLRMHLAGHLPLGPQLEQLDRGFWETYRRGESGLPAHPEVPD
Protein: DNA-directed RNA polymerases I and III subunit RPAC1 (E7EQB9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIFSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
Protein: Serpin 4 (Q8MPN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEAAAATGMFMSLTSLPMPKPDPIRFNVDHPFTFYILNKDSTALFAGSIKKL
Protein: Transcription factor Sox-21 (SRY (sex determining region Y)-box 21) (B0ZTE1)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a negative regulator of transcription (By similarity). May function as a switch in neuronal development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MSKPLDHVKRPMNAFMVWSRAQRRKMAQENPKMHNSEISKRLGAEWKLLTEAEKRPFIDEAKRLRAMHMKDHPDYKYRPRRKPKTLLKKDKFAFPMPYSLTGDHDGLKAVSLHGAGVLTDALLCHPEKAAAAAAAAAARVFFQPSAAAAAAAAAAASGSSTNPYSLFDLSSKMAEMTHSSSSIPYTSSIGYPQSSGGAFAGVTGGGHTHSHPSPGNPGYMIPCNCTGWPSPGLQPPLAYILFPGMGKPQLEPYPAAAYAAAL
Protein: Protein atonal (P48987)
Organism: Drosophila melanogaster (Fruit fly)
Function: Developmental protein involved in neurogenesis. Required for the formation of chordotonal organs and photoreceptors. Seems to bind to E boxes. Specifically required for the photoreceptor R8 selection.
Subcellular location: Nucleus.
Interaction partners:
- Achaete-scute complex protein T4
- Zinc finger protein sens
- Protein daughterless
- Achaete-scute complex protein T5
- Protein hedgehog
- Protein phosphatase eya
- Protein Optix
- Protein sine oculis
- Protein decapentaplegic
- Achaete-scute complex protein T8
Sequence:
MSSSEIYRYYYKTSEDLQGFKTAAAEPYFNPMAAYNPGVTHYQFNGNTLASSSNYLSANGFISFEQASSDGWISSSPASHRSESPEYVDLNTMYNGGCNNMAQNQQYGMIMEQSVVSTAPAIPVASPPAVEVMGSSNVGTCKTIPASAGPKPKRSYTKKNQPSTTATSTPTAAAESSASVNLYTEEFQNFDFDNSALFDDSVEDDEDLMLFSGGEDFDGNDGSFDLADGENQDAAAGGSGKKRRGKQITPVVKRKRRLAANARERRRMQNLNQAFDRLRQYLPCLGNDRQLSKHETLQMAQTYISALGDLLR
Protein: Glutaredoxin 2 (Grx2) (P0AC59)
Organism: Escherichia coli (strain K12)
Function: Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase.
Interaction partners:
- Glutaredoxin 3
- Glutaredoxin 1
- Glutathione reductase
- Thioredoxin reductase
Sequence:
MKLYIYDHCPYCLKARMIFGLKNIPVELHVLLNDDAETPTRMVGQKQVPILQKDDSRYMPESMDIVHYVDKLDGKPLLTGKRSPAIEEWLRKVNGYANKLLLPRFAKSAFDEFSTPAARKYFVDKKEASAGNFADLLAHSDGLIKNISDDLRALDKLIVKPNAVNGELSEDDIQLFPLLRNLTLVAGINWPSRVADYRDNMAKQTQINLLSSMAI
Protein: Epoxide hydrolase EphG (EH) (EC 3.3.2.10) (Cholesterol-5,6-oxide hydrolase) (EC 3.3.2.11) (O33283)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Epoxide hydrolase capable of hydrolyzing long or bulky lipophilic epoxides such as 9,10-epoxystearic acid and cholesterol 5,6-oxide in vitro. The physiological substrates have yet to be identified, but could be fatty acid or steroid derivatives.
Interaction partners:
- Possible monooxygenase
- Epoxide hydrolase A
- Epoxide hydrolase B
- Uncharacterised methyltransferase Rv1498c
- Probable epoxide hydrolase EphC
- Probable O-methyltransferase Rv1703c
- Possible epoxide hydrolase EphF
- Possible epoxide hydrolase EphE
- Possible alanine rich transferase
- DUF3046 domain-containing protein
Sequence:
MAELTETSPETPETTEAIRAVEAFLNALQNEDFDTVDAALGDDLVYENVGFSRIRGGRRTATLLRRMQGRVGFEVKIHRIGADGAAVLTERTDALIIGPLRVQFWVCGVFEVDDGRITLWRDYFDVYDMFKGLLRGLVALVVPSLKATL
Protein: Transport and golgi organization 5, isoform B (Q7KVQ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQETGSSATSLLAAGGKAKKNQKDKQRERERLERGQLVLWRRPLQTTKYCGLELFTLLRTWSTRLLQQRLLLATLIVLSIVFSVIYKIDGPHQLAIEFVRRNTWFFVYWLGLGVLSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSLRFPQPPYPDDIICPEEPYDKHVPNIWSIMSKVRLEAFLWGAGTALGELPPYFMAKAARLSGYDPEDAEELAEFEALNAKRHQKNLSMMDRGKLFMERVVERVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAVIKMHIQKIFVIIAFNETLIERAVDLLATLPVLGHKLQEPFKSFLKNQKQRLHRQQRGAAGATTGAGDSGNLLSRIFETFVIGMVCYFVVSIVNSLAQSYHKRLHKKPASPVAATTPTRQSTGASKKAGKQKALRD
Protein: Rab interacting lysosomal protein like 1 (A0A1B0GVV3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEERGSALAAESALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRLERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLSHKDVNFSEEEFQKHEGMSERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEENRIPQPPPIAHPRTSPQPESGIKRLIFTAIMPMVAAGLIIDDPTLQPVRRLVSLV
Protein: Uterine milk protein (UTMP) (P21814)
Organism: Ovis aries (Sheep)
Interaction partners:
Sequence:
MSHRRMQLALSLVFILCGLFNSIFCEKQQHSQQHANLVLLKKISAFSQKMEAHPKAFAQELFKALIAENPKKNIIFSPAAMTITLATLSLGIKSTMSTNHPEDLELELKLLDAHKCLHHLVHLGRELVKQKQLRHQDILFLNSKMMANQMLLHQIRKLQKMDIQMIDFSDTEKAKKAISHHVAEKTHTKIRDLITDLNPETILCLVNHIFFKGILKRAFQPNLTQKEDFFLNDKTKVQVDMMRKTEQMLYSRSEELFATMVKMPFKGNVSLILMLPDAGHFDNALKKLTAKRAKLQKISNFRLVHLTLPKFKITFDINFKHLLPKINLKHLLPKIDPKHTLTTTASSQHVTLKAPLPNLEALHQVEIELSEHALTTDTAIHTDNLLKVPANTKEVPVVVKFNRPFLLFVEDEITQTDLFVGQVLNPQVE
Protein: Formate hydrogenlyase maturation protein HycH (P0AEV7)
Organism: Escherichia coli (strain K12)
Function: Seems to be required for the conversion of a precursor form of the large subunit of hydrogenlyase (HycE) into a mature form.
Interaction partners:
- Formate hydrogenlyase subunit 7
- Formate hydrogenlyase subunit 5
- Hydrogenase 3 maturation protease
- Formate hydrogenlyase subunit 4
- Formate hydrogenlyase subunit 2
- Formate hydrogenlyase subunit 6
- Formate hydrogenlyase subunit 3
- Formate hydrogenlyase regulatory protein HycA
- Formate dehydrogenase H
- Electron transport protein HydN
Sequence:
MSEKVVFSQLSRKFIDENDATPAEAQQVVYYSLAIGHHLGVIDCLEAALTCPWDEYLAWIATLEAGSEARRKMEGVPKYGEIVIDINHVPMLANAFDKARAAQTSQQQEWSTMLLSMLHDIHQENAIYLMVRRLRD
Protein: BARP protein (Q38CV1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRADDIWNDCLASSNGPPLKHIEVLCNLAEQLRGLPDTVSSAVISVTEASIKASKAKVQAEEAVELAESKGLNVTKAKEAAVRATLAAEAAATAASNVEINAANIAELPWSQRRRDAGLQNIEHCKNLDKDVREAAVKCTKKAENVTADSLRAALEGLETLFSDVYILVTLRKEKVEMQEEMQSLEQNAATVLRVLQKAEDAAADANREALGNSVASPEGSVLLLMAGLFLGSVL
Protein: Ketimine reductase mu-crystallin (EC 1.5.1.25) (NADP-regulated thyroid-hormone-binding protein) (Q14894)
Organism: Homo sapiens (Human)
Function: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.
Subcellular location: Cytoplasm.
Interaction partners:
- Trans-3-hydroxy-L-proline dehydratase
- Arginase-2, mitochondrial
- Guanidino acid hydrolase, mitochondrial
- Arginase-1
Sequence:
MSRVPAFLSAAEVEEHLRSSSLLIPPLETALANFSSGPEGGVMQPVRTVVPVTKHRGYLGVMPAYSAAEDALTTKLVTFYEDRGITSVVPSHQATVLLFEPSNGTLLAVMDGNVITAKRTAAVSAIATKFLKPPSSEVLCILGAGVQAYSHYEIFTEQFSFKEVRIWNRTKENAEKFADTVQGEVRVCSSVQEAVAGADVIITVTLATEPILFGEWVKPGAHINAVGASRPDWRELDDELMKEAVLYVDSQEAALKESGDVLLSGAEIFAELGEVIKGVKPAHCEKTTVFKSLGMAVEDTVAAKLIYDSWSSGK
Protein: Glutaredoxin family protein (B3H604)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDSIMCVSSWKFYTMNDSWMYLDAFVYQWMILSYLIGNFSGICSKTYCPYCVRVKELLQQLGAKFKAVELDTESDGSQIQSGLAEWTGQRTVPNVFIGGNHIGGCDATSNLHKDGKLVPLLTEAGAIAGKTATTSA
Protein: NmrA like redox sensor 1 (I3L3Z0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
DGKSYLLSLPTGDVPMDGMSVSDLGPVVLSLLKMPEKYVGQNIGLSTCRHTAEEYAALLTKHTRKMTPEDYEKLGFPGARDLANMFRFYALRPDRDIELTLRLNPKALTLDQWLEQHKGDFNLL
Protein: Protein POF1B (Premature ovarian failure protein 1B) (Q8WVV4)
Organism: Homo sapiens (Human)
Function: Plays a key role in the organization of epithelial monolayers by regulating the actin cytoskeleton. May be involved in ovary development.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:21940798}.
Interaction partners:
- Protein diaphanous homolog 2
- Bone morphogenetic protein 15
- Homeobox protein NOBOX
- Factor in the germline alpha
- Forkhead box protein L2
- Fragile X messenger ribonucleoprotein 1
Sequence:
MSSSYWSETSSSSCGTQQLPEVLQCQPQHYHCYHQSSQAQQPPEKNVVYERVRTYSGPMNKVVQALDPFNSREVLSPLKTTSSYQNLVWSDHSQELHSPTLKISTCAPSTLHITQNTEQELHSPTVKLTTYPQTTIRKYVVQNPEQEPLSQFLRGSHFFPGNNVIYEKTIRKVEKLNTDQGCHPQAQCHHHIIQQPQVIHSAHWQQPDSSQQIQAITGNNPISTHIGNELCHSGSSQICEQVIIQDDGPEKLDPRYFGELLADLSRKNTDLYHCLLEHLQRIGGSKQDFESTDESEDIESLIPKGLSEFTKQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETCTGPMLQAKMDEIGNHYTEMVKNLRMEKDREICRLRSQLNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEIYSSHNQPSTGGRTTITTKKYRTQYPILGLLYDDYEYIPPGSETQTIVIEKTEDKYTCP
Protein: Probable L-ascorbate-6-phosphate lactonase UlaG (EC 3.1.1.-) (L-ascorbate utilization protein G) (P39300)
Organism: Escherichia coli (strain K12)
Function: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. Also shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ascorbate-specific PTS system EIIC component
- Ascorbate-specific PTS system EIIA component
- Ascorbate-specific PTS system EIIB component
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
- L-ribulose-5-phosphate 3-epimerase UlaE
- HTH-type transcriptional regulator UlaR
- L-ribulose-5-phosphate 4-epimerase UlaF
- L-xylulose/3-keto-L-gulonate kinase
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
Sequence:
MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAAGVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGGKFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL
Protein: RE13301p (Q86PC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKEPTNTLDEIVPSRLTSAELRAMALRQQQQIDSQHQLLATKEQRLRFLKSQEVRSAVASAEGERLRRLRERVEAQESKLRRLRALRGQVDLQKTYNVTLSNDLDSIRALFSEKEKELSLAVAKVEALTRQLEELRRDRRCPVNILTAAGNGVGGQSLPPQASRELEKLRRELMYRNQLSLQQDARLHMQREALQQRQAELRSTDQRIYELQTRLQRKKQANTHHQQQQQQQQQHQQQQHQQQHQQTTVQQQQQQQQQLHVQSAQLLAAAAAATAQQQQQHQQHQQQQQQQQQQSASNLGKHGGVAALKQQLLQKQVNQLAAAAAAAAAGRARGNVAAVEPFIHTPQKSTITSTASYLSGGMKHAAATANTNQQNQLIQDLTHVKLGQNSGFFAGSVPVPVASSSCESDESKLAKKLLAAPAKTEAELRKQAQTEAMDSTTHIYAEVGPKKRDREAAAAAAAAAAAAAAAAQAAAEAANQAATAAAASAISPPATANASKIPKSTTSSSSSASALISKLNQQATAKESQDQQQSQAKKNEISVTSETLSERNTQQQLTVHSMPLGAISKSVALAVSNASKPLQVQVSNVAVPPRKRISSVAPNSVSSGSSIPKMITYSPKVNRVAPNVVMTDPRPALPPKPSKMSPTEQPSPVEANTSGSAGGAGSGAASASTANKTQTATFGLQSLNINDNLPIKAKPLTIRKQPLFEQPRLKSSQSSSNGQQKPPLLQLQNQRKSEPSARQPTENLPDTSPQHSPSSESSADETDRMVAPSITTSQQETSTSATSTTTTVTTSNIKERTGNGKPKLGRRVSFDPLALLLDASLEGELELVKKTAMQVANPSAANDEGITALHNAICAGHIDIVKFLVEFGCDVNAQDSDGWTPLHCAASCNNLSMVKFLVESGACLFASTLSDHETPAEKCEEDEEGFDGCSEYLYSIQEKLGILHNGDVYAVFSYEAQNGDELSFHVNEPLIVLRKGDDAENEWWWARNAAGEEGYVPRNLLGLYPRVPPHSPHFSD
Protein: Nuclear factor NF-kappa-B p100 subunit (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100)) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, p49/p100) (Q0II00)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- V-rel avian reticuloendotheliosis viral oncogene homolog B.
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Proto-oncogene c-Rel
- NF-kappa-B inhibitor alpha
- Inhibitor of nuclear factor kappa B kinase subunit beta.
- Transcription factor p65
- NF-kappa-B inhibitor alpha
- N-lysine methyltransferase setd6
- Myeloid differentiation primary response protein MyD88
- NF-kappa-B inhibitor beta
Sequence:
MAGALRMDDTHYQIGFVVNEPMTFPSAYDDLPYMPEAFEVKHEPFVQETVDGPYIQIIEEPKQRGFRFRYECEGPSHGGLPGASSERNRRTYPTVKVLNFVGNARVEVQLVTHTDPPRVHAHSLVGRHCNESGVCSVDVGPSDFTAQFSNLGILHVTKRGVVEVLTKRLKEEKRKVKGPGYKFSDAEENALMQEAKELGKNMDLNIVRLKFTAYLQDSNGSYTRALKPVVSNPIYDSKSPNASNLKISRMDKTSGSVLGGEEVFLLCDKVQKDDIDIRFYEEEDEWEALGDFSPTDVHKQYAIVFKTPPYRCTNIDRPVTVFLQLKRKKGGDCSEPKQFTYVPHNQDKEEVQRKRMKALPDHYGGWRGGPQGGAGGFGGPGSGTGGGGGMGGGFPFNPMDNSSFFVGGCGGFGGGAQMSDSPPQTDGANTQSQSNSQIRQQLIQIALHNRANLAAKCNARALLQYSSTGDARPLLALQRHLCGVQDENGDTPLHLAIIHQKTVVAEQLIKALNSSPQQKFFNKLNKLSQAPLHLAVITKQPKLVEMLMKSGADPSLLDREGRTVLHLAAHTGDDVILRLVLSLLGEHHSHLINSADFTGQYPVHLAVKKDGERCLRLLVEAGAKINMPEQKSGCTALHLAVRDNLLKLACNLITELKADVNACTYGGNSPLHLAASQGSPHLCSMLIAAGADKRIENDEPLFLSSSSSDEDEESEKKLSEDMVQQVHCLSISSERGVFNPRKRPAAGHTPFDLAKSQKVRDLLDGRKGPKPNSLSPKRTKISTEEVNQDLDNEVLSKLCGILIHDDVPWRELAEKLGMLTLTHLYQDSASPCQKLLESYQLSGGPVDGLVEALQALGVREGVRLLRDSQPREDKQSSDSTEDSGFGSQSIGEEMANPAVGNH
Protein: Uncharacterized protein (Q38FS0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Actin A
Sequence:
MNRSCLEVNVSDYICLERIGGDYEWSNTLARVIGLPTSQHVRVELFDRVDAVPGGFEPYDEKLGELAVQQDRLDGLNELKALQQQYQQLVEDEDRSSERLYRAREVTQEKQAIAAAFTRQQMVELDQVRAAIEQVPARSWRELRSAGRPSEELFSLVRALMIALQEDHNGSWESMQIVMRQSDFVGRIMELDCTVAPLSKLQRKKIKNELALVPAESLKESKRKGASSQALQGAPLPVVIRRWLNVQMACSRAREAEERVVDGCFAQLQEQALLITEVNGLREMIAMLGVQISEKKQALIGEEPLNLLNDEEEPINVEGCYVQRTTNGRVVSDIVSLDSVLLVFGPKESKTLLGKEIPVYVQLQPEEVLKMQQTVRTVNDLHDIDELEALFAAEERDDQEKRELQLRMEELSKKELFTEDDEEEMRQLDAFLTDVDRRHERTVWRRRCLEKAGRDKLYLEKRRRIENTVYSDLHIFFTGDKWQEVLDNEEHREYLDAAFKEDASATLRLPKENFTNLTFEGYPLEASFTTEHDKSTPKEELQALLERCAFPTVCAFYHSLTGGTTKSMSKLRIDEWLVQLRRERMWELNFAGSGLVETLEDFGDEDYGYTDDEDYRKPCVEIAEVRCDYDPAVRYGYALLGYNEAADDFFDRGGRREQQTSSRQASAVRRDQVLAGTMKQLGGGDSPKSDGSNSDIPGPEGEAPTAAEHPADKLPSAELEELSFNDVAAGAAPGADEPSINDVEELGSEDASVQQAS
Protein: Cytochrome c oxidase subunit (Cytochrome c oxidase polypeptide VIa) (Q5ALV9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit Va
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 3
Sequence:
MFKAVQQLTFRRFNSHHLQPSKLLNELAYKPNKQVGEEFIKKYEEKVHHSEGITNLWKRLTYLVAIPAVLLVAIPVGKVELSHAEHRKHQAHLSDDEWPQQYDYQNIRSKPYFWGDGDKTLFWNSDVNRHVVKD
Protein: Uncharacterized protein (Q38AZ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNRGKGGGSPKKLRLPPVQQRGTSSQRLPQESRRKTTSKERTISTGSMSQQRGSMRGRQGSATSRSGPQGRTLSSDTSTRRSSVWGTGSRRPTSCFTADRLTYPTGSRGTTSKSGGNTSNSRLHRVAMEVSVSRLQRWFRVTLLRRLVDSPDALASRIEKRYTWEHRLWKLRTRIAKRIIVEACTAYALSLDLKGKEEGRVAEHNAVMVMTFLRALESLRLKWRKQQEVFKHAVSIIERAWIRCNTRTNPMQTSRERKLIRLLMDEESIERRELVRRRLLFVINCHQLCYNDPLVLETCLSAKTLHISENLFTNNTTDEKSWCGPATLQEEAPTDGTKERQVLSHSLSLWTRSSHCSSILKSMTNLTMAGYMDECGKGKEEKNYAWVNLADTENPSEGPYRRRANACFVTAILLEKGHLTFPESMGAGQSGLDPRPDLASGSAPVQCRARIQDTEKALEKVEVRFVREGPLSLREPLHSLSTFKEFRVLMNSRRKQNSREQTKAFILGPNVTLDNLHYLYPVYRKVKKGKDLKPLSHLSVTSDAMGEEWSKLLYVAWTEECLSRPPSHSFAWLSLARPESSRSYHRRPFHTGICEDSNHPLHDLLVGTGGKQRSLKTNLMSVSFYDDESDKQQQNADPYVDHEKIRYEVERLLIQEYRRRKCIEETHKAGIHTIEGMIARERGTAFSSVKKPSSAPVGRGMSTTFLRLLRESGRV
Protein: Uncharacterized protein (A4GXB8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
IGDAVRIDRAFLGIALMAVSAPAVADETAQSQLEALTARYVEYEQSRSADDEEGSRARLPDVTPKALAERAEFAAQLLASLDAIDKDSLSRTKRVDAIVLRTTLTEEIGDASFREWEMPFDSDNNFWSYLAARRGFRTVKEYEQYIARMRDIPRYFGEQTDNARAGLARGFSVPCVT
Protein: Membrane-bound O-acyltransferase GUP1 (Glycerol uptake protein 1) (Q5AKZ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell integrity and apoptosis (By similarity). Plays a role in virulence and antifungal resistance.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P53154}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53154}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P53154}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-aminoadipate reductase
- Acyl carrier protein
- Acyl carrier protein
- Lysophospholipid acyltransferase
Sequence:
MNYLSQLGKLFSLETLDTRLNPTTNPIKRQSIIKKANPTSRWSTLEFKIYLTILIIVVPLMIKAAMESSNETNPNYPRFQHLLSDGWILGRKVDNSDQQYRFFRNNFPLLCGLIFIHVTLRKLINTFIIIPNGRYNNNFKRTYFDLIFGIIFLIGAHGINVFKISFHLFINYLIGKYIKNYKLAIWCTWIYGIFSLFFNEWFGDSSFGLSIFVNGSGYYTGIIPRWDVFYNFTLLRMLSFNLDYIERERKLGNNDGQLNLNKQENINGADNPPTLLNLDDRQRLSAPLPLDDYNVSNYIAYISYTPLFIAGPIITFNDYVYQSNYQQSSTTQNYQRIFMYAIRFLFCLLVMEFLLHFMYVVAVSKTKAWDGDTPFQISMLGMFNLNLIWLKLLIPWRLFRLWALLDGIDPPENMIRCMDNNFSALAFWRAWHRSYNRWVIRYIYIPMGGSGTGKYRIINSLLVFSFVAIWHDIELKLLMWGWLVVIFLIPEISATLIFSKYNKNWWYRYLCGIGAVINIWMMMIANLVGFCLGTDGMWKLLHDLFQTFEGGRFFIISSICLFVGAQIMFELRESELRRAIDVRC