wanglab/gogpt-training-data huggingface dataset:
Protein: diguanylate cyclase (EC 2.7.7.65) (A0A0H2X560)
Organism: Xanthomonas campestris pv. campestris (strain 8004)
Interaction partners:
Sequence:
MLLDDPTAALQATDRQLRQARASGQADATFWAALAQARVLISLEDSARRNQALTQARDVLGQLHGSGAQARLWLHTVQALSDVRENPNRSMVARLEELRRQARALGRRDLLCEVDAVDMWSMLASGSSDEAWNAAQASYQCAVREGSLSLELDALTQLGSLASRVGGRTAKENEAEAYLLRALARLGDLPARFQRSLIEYEYGASLALQQPDAALVHFRRALALSRALGDQAGVAAALTSASEALIETGDAAAALVTANEALPLMQAQGNIGRVAACHAVLLKAMTALTDARLGEEIAAARRADGPQLASSRRVDLADAIAAALASMGQHAQAYAELQRANALRERSQEGQRDTVMLRLQARYEDARRSAETAELRRRSETAQLALQAREAGQRTLWIALCAACLLLIAALVVVAVGWRHRRQLSTLAMRDELTGLPNRRAIRTEAQQQIEHALRTRTSCMLALIDLDHFKQINDVHGHATGDAVLKALAAASRRALRERDQLGRLGGEEFLLVLPGCTADEIGNVFARLRSAVAAIAIAGLPADAPVRFCLGAVRVTPATGLDVLLSQADLALYAAKTAGRDQWAVYGA
Protein: AMP deaminase (EC 3.5.4.6) (D0IQK3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNFNRMDTAHRLRVDVRLYGGSMGNQLNDKGTASSTPTISSDDLSDLADSPVDEKAEADVEVTNEISAPYEVPQFPIEQIEKKLQIQRHLNEKQATGPRPVATAAVLATNRESSSSTEGRESAVTMERNDADINFQRVSISGEDTSGVPLEDLERASTLLIEALRLRSHYMAMSDQSFPSTTARFLKTVKLKDRINNLPVKEVSESADVHLRHSPMKITNPWNVEFPNDEDFKIKPLNGVFHIYENDDESSEIKYEYPDMSQFVNDMQVMCNMIADGPLKSFCYRRLCYLSSKYQMHVLLNELRELAAQKAVPHRDFYNTRKVDTHIHAASCMNQKHLLRFIKKTLKNNANEVVTVTNGQQMTLAQVFQSMNLTTYDLTVDMLDVHADRNTFHRFDKFNSKYNPIGESRLREVFLKTDNYLNGKYFAQIIKEVAFDLEESKYQNAELRLSIYGKSPDEWYKLAKWAIDNDVYSSNIRWLIQIPRLFDIFKSNKMMKSFQEILNNIFLPLFEATARPSKHPELHRFLQYVIGFDSVDDESKPENPLFDNDVPRPEEWTYEENPPYAYYIYYMYANMTVLNKFRQSRNMNTFVLRPHCGEAGPVQHLVCGFLMAENISHGLLLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLNYHRNPLPEYLARGLIISLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSSCDMCELARNSVMMSGFPHAIKQQWLGPIYYEDGIMGNDITRTNVPEIRVAYRYETLLDELSNIFKVNQTCSIADMNAT
Protein: Klf5 protein (Q66HP1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEKYLTPQLPPVPIISEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTQIKTEPVTIFSHQSESTAPPPPAPTQALPEFTSIFSSHQTTAPEVNNIFIKQELPIPDLHLSVPSQQGHLYQLLNTPDLDMPSSTNQTAVMDTLNVSMAGLNSHPSAVPQTSMKQFQGMPPCTYTMPSQFLPQQATYFPPSPPSSEPGSPDRQAEMLQNLTPPPSYAATIASKLAIHNPNLPATLPVNSPNIQPVRYNRRSNPDLEKRRIHFCDYDGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFQCVVCNRSFSRSDHLALHMKRHQN
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJY0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Small ribosomal subunit protein eS25
- RP28
- Ribosomal protein
- Candida glabrata strain CBS138 chromosome M complete sequence
- L17A
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein uS14
- 40S ribosomal protein S7
- L33
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MVFIQNLKTSAYHSRFQTPFRRRREGKTDYYQRKRLVAQHKAKYNSPKYRLVVRFTNKDIICQIVSSTITGDIVLAAAYSHELPRYGITHGLTNWAAAYATGLLIARRALQKLGLDETYKGVEEVEGEYELTEAVEDGPRPFKVYLDIGLQRTTTGARVFGALKGASDGGLYVPHSENRFPGWDFEAEELDAELLRSYIFGGHVSQYMEELADDDEERFSELFKGYLADDIDADSIEDIYASAHEAIRADPSFKPTEKKFTKEQYAAESKKYKAKKLTKEERDARVAAKIAALAGQQ
Protein: Protein limb expression 1 homolog (lowfat) (Q9VKY1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Fat (ft) signaling pathway that functions in normal development of various organs such as the wing and leg. In developing imaginal disks, involved in regulating both the protein levels and apical localization of ft and ds. Involved in establishing planar cell polarity (PCP) along the anterior-posterior axis of the wing (the early Fz signaling event), probably by acting upstream of ds and ft to regulate Fz activity.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:19710173}; Peripheral membrane protein {ECO:0000269|PubMed:19710173}. Cytoplasm {ECO:0000269|PubMed:19710173}. Note=In wing imaginal disks, strong cytoplasmic expression in the wing pouch but in regions of the wing hinge preferentially expressed in the sub-apical membrane. {ECO:0000269|PubMed:19710173}.
Interaction partners:
- Cadherin-related tumor suppressor
- Discs overgrown protein kinase
- Zyx102 protein
- Protein crumbs
- Atypical protein kinase C
- Moesin/ezrin/radixin homolog 1
- Patj homolog
- Protein PALS1
- Protein lin-7 homolog
- Cadherin-86C
Sequence:
MVYPEEPFWVLPTVTGFYEDRDYRVNVVEALQEFWQMKQSRGAELKNGALVIYESIPSNSQPYICFVTLPGGSCFGSFQNCPTKAEARRSSAKIALMNSVFNEHPSRRISDEFIQKAVQDARTSFKGTSQINEGTESGIGAFRFMLEANKGRTMLEFQELMTVFQLLHWNGSLKAMRERHCSRQEVVAHYSNRSLDDEMRSQMALDWIAREHDNPGVIRRELVLAERELETFRMAGRELRFPKEKKDILMIAHNQLGGSALNSATIDD
Protein: Presenilin-2 (PS-2) (EC 3.4.23.-) (AD3LP) (AD5) (E5-1) (STM-2) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit] (P49810)
Organism: Homo sapiens (Human)
Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis. Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8574969}; Multi-pass membrane protein {ECO:0000269|PubMed:8574969}. Golgi apparatus membrane {ECO:0000269|PubMed:8574969}; Multi-pass membrane protein {ECO:0000269|PubMed:8574969}.
Interaction partners:
- Gamma-secretase subunit APH-1A
- Presenilin-1
- Nicastrin
- Gamma-secretase subunit APH-1B
- Gamma-secretase subunit PEN-2
- Calsenilin
- Amyloid-beta precursor protein
- Apolipoprotein E
- Ryanodine receptor 3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLTGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI
Protein: Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (E9PU28)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P12268}. Nucleus {ECO:0000250|UniProtKB:P12268}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P12268}. Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine-nucleotide depletion. {ECO:0000250|UniProtKB:P12268}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 1
- AMP deaminase 3
- AMP deaminase 2
- AMP deaminase 1
- 5'-nucleotidase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNESDELVAIIARTDLKKNRDYPLASKDTKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHGLHSYEKRLF
Protein: Decapping protein 2, isoform A (Q9VUU4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEIAPLINNAVAVVTASASAAVSASASVGSSSKDDNVNNLALLASLTLQKVLNINNNNNQHSKNNNHSDNSNSKQHEQQKQQQQPQRRNLDIKSEYDVLNQLLKTGAVFTATPTAPIAIERRKQTQQQQRPYAQQAHQQQQQKQRLNSSISSTHSSTSTNSSYGSSSSEDAAGTSAPTGAGEVVTSAALTPRASTTKASSNKLPEKSKIPSDILDDLASRFIINVPDMELNNLIRMCFQIELAHWFYLDFFCAPESGEDGETPKCVQRKLPSVGIKQFAMQLFQHIPFLNKHFGTVDQILDEWKNYKLSVPTYGAILVSEDHNHCLLVQSYFARNSWGFPKGKINENEDPAHCATREVYEETGFDITDLIDANDYIEAFINYQYTRLYVVRNIPMDTQFAPRTRNEIKCCDWFRIDALPVNKNDAISKAKLGKTSNSFFMIMPFVKRLKKWVNDRKAGIEPRRRKFSGQQSPKAASPTNMNGNCKKDVTGVRNESQRQRHKSMGDLDGVKLNNLNGKGTVGTGAGSAASASATAAINSMNICNSNGKRNKQNAAAGSNQATPTTIATPMTSNGAVVGGTVSSKRQLFHSQSQNDAQQSASNEKIVSSFDLIRKEKQQQLKAAKAQKQQQQQQQRSRTKSQSDKQYNPQQPVKILGQQQPTTGMDLIAMLSAAAAAQKTPNNEQQTQEKQQQQQRPRPASVSLNLGAGSATGATTSAPDAQYMHRLQRMASGTNLRILKRAQSQQPQQHHQQQLQLEQQQQQQQQLGIDFTPNLNSWTNFSFTKNFIANVFC
Protein: L-carnitine CoA-transferase (EC 2.8.3.21) (Crotonobetainyl-CoA:carnitine CoA-transferase) (P31572)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01050}.
Interaction partners:
- Crotonobetainyl-CoA reductase
- Crotonobetaine/carnitine--CoA ligase
- Carnitinyl-CoA dehydratase
- L-carnitine/gamma-butyrobetaine antiporter
- Carnitine operon protein CaiE
- Protein FixB
- Protein FixA
- Probable acyl-CoA dehydrogenase YdiO
- Protein FixC
- Putative metabolite transport protein YaaU
Sequence:
MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED
Protein: Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein) (P28077)
Organism: Rattus norvegicus (Rat)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-10
- Proteasome subunit beta type-8
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-7
Sequence:
MLQAGAPTAGSFRTGEVHTGTTIMAVEFDGGVVVGSDSRVSAGAAVVNRVFDKLSPLHQRIYCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANIVKNISYKYREDLLAHLMVAGWDQHEGGQVYGTMGGMLIRQPFAIGGSGSTYIYGYVDAAYKPGMTPEECRRFTTDAITLAMNRDGSSGGVIYLVTITADGVDHRVILGDELPKFYDE
Protein: Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2) (Q92539)
Organism: Homo sapiens (Human)
Function: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Plays important roles in controlling the metabolism of fatty acids at different levels. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Translocates to endoplasmic reticulum membrane with increasing levels of oleate. {ECO:0000250}.
Interaction partners:
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Phosphatidate phosphatase LPIN3
- Phosphatidate phosphatase LPIN1
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
- Ethanolaminephosphotransferase 1
- Phosphatidate cytidylyltransferase 2
- Phospholipid phosphatase 5
- Phospholipid phosphatase 4
Sequence:
MNYVGQLAGQVIVTVKELYKGINQATLSGCIDVIVVQQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKLGDNGEAFFVEETEEEYEKLPAYLATSPIPTEDQFFKDIDTPLVKSGGDETPSQSSDISHVLETETIFTPSSVKKKKRRRKKYKQDSKKEEQAASAAAEDTCDVGVSSDDDKGAQAARGSSNASLKEEECKEPLLFHSGDHYPLSDGDWSPLETTYPQTACPKSDSELEVKPAESLLRSESHMEWTWGGFPESTKVSKRERSDHHPRTATITPSENTHFRVIPSEDNLISEVEKDASMEDTVCTIVKPKPRALGTQMSDPTSVAELLEPPLESTQISSMLDADHLPNAALAEAPSESKPAAKVDSPSKKKGVHKRSQHQGPDDIYLDDLKGLEPEVAALYFPKSESEPGSRQWPESDTLSGSQSPQSVGSAAADSGTECLSDSAMDLPDVTLSLCGGLSENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESWVKDKMPKKSGRWWFWRKRESMTKQLPESKEGKSEAPPASDLPSSSKEPAGARPAENDSSSDEGSQELEESITVDPIPTEPLSHGSTTSYKKSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKIIISDIDGTITKSDALGQILPQLGKDWTHQGIAKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFPLLSKEQNSAFPCPEFSSFCYWRDPIPEVDLDDLS
Protein: Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-I); Copeptin] (P35455)
Organism: Mus musculus (Mouse)
Function: Neurophysin 2 specifically binds vasopressin.
Subcellular location: Secreted.
Interaction partners:
- Vasopressin V1a receptor
- Vasopressin V2 receptor
- Vasopressin V1b receptor
- Oxytocin receptor
- Oxytocin-neurophysin 1
- Hypocretin neuropeptide precursor
- Pro-MCH
- Pro-thyrotropin-releasing hormone
- Aquaporin-2
- Type-1 angiotensin II receptor A
Sequence:
MLARMLNTTLSACFLSLLAFSSACYFQNCPRGGKRAISDMELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAVGICCSDESCVAEPECHDGFFRLTRAREPSNATQLDGPARALLLRLVQLAGTRESVDSAKPRVY
Protein: 5-beta-cholestane-3-alpha,7-alpha-diol 12-alpha-hydroxylase (EC 1.14.14.139) (CYPVIIIB1) (Cytochrome P450 8B1) (Sterol 12-alpha-hydroxylase) (Q7YRB2)
Organism: Sus scrofa (Pig)
Function: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis. Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase type 7
- 3-oxo-5-beta-steroid 4-dehydrogenase isoform 1
- Cholesterol 25-hydroxylase
- Terpene cyclase/mutase family member
Sequence:
MVLWGPVLGVLLVAIVGYLCLQGLLRQRRPEEPPLDKGSVPWLGHAMTFRKNMLEFLKHMWARHGDIFTVQLGGQYFTFVMDPLSFGPILKDAKRKLDFVEYAEKLVLKVFGYRSMQGDHRMIHSASTKHLMGDGLEELNKAMLDNLSLVMLGPKGPSPDASCWREDGLFHFCYDILFKAGYLSLFGRTEDKEQDLLQAEELFMQFRKFDRMFPRFVYSLLGPREWLEVGRLQCLFHKMLSVEHSLERHGISSWITDMLQVLREQGVAPAMQDKFNFMMLWASQGNTGPTTFWALLFLLKHPEAMRAVREEATRVLGEARLEDKQSFDVEVSALNHMPVLDSVMEETLRLGAAPTLLRVVNSDQILKMASGQEYRLRHGDILALFPYLSVHMDPDIHPEPTTFKYDRFLTPSGSRKVNFYKAGKKIHHYTMPWGSGISICPGRFFALTEMKLFVLLMVTHFDLELVDPDTPVPPVDPQRWGFGTMQPSYEVRFRYRLRPTE
Protein: Xylanolytic transcriptional activator xlnR (Xylanase regulator) (Q5AVS0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcriptional activator of the xylanolytic system. Involved in the regulation of extracellular cellulolytic and xylanolytic genes and in the regulation of the intracellular activities of D-xylose catabolic genes in the pentose catabolic pathway (PCP) in response to the presence of D-xylose. Binds to the DNA sequence 5'-GGNTAAA-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- Probable beta-glucosidase A
- DNA-binding protein creA
- Alpha-glucuronidase A
- Probable D-xylulose reductase A
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Exo-1,4-beta-xylosidase xlnD
- Endo-1,4-beta-xylanase C
- Endo-1,4-beta-xylanase B
- Alpha-L-arabinofuranosidase B
- Probable alpha-L-arabinofuranosidase A
Sequence:
MSTTSLQQFATATSFSPFSNSQSARMSQSQSQTIGLDTLAEGSQYVLEQLQLSREGGNSENNSTFKPSSVRDSLAEARSMIRKNSSSAPVRRRISRACDQCNQLRTKCDGQNPCAHCIEFGLTCEYARERKKRGKASKKDIAAAAAAAGHQGGMGNRSPTDRRLSQEPGGRYDSVLEASRVQSHLPANGLSSIHNTQAAHSQPPLGSALDALHLNHFTQLNESGRSQMPVSDLRSLQILHNNPRSPSALPHGLNAYNDNTFSLLNSQEPNTTSLNHFRLGNSTDNPSAQFLGLSPPAQSPGWLPLPSPSPANFPSFPMAPFSGTSLRYPVLQPVLPHIASIIPQSLACDLLDLYFTSSSSSHLSPQSPYVVGYIFRKQSFLHPTKPRVCSPGLLASMLWVGAQTSDAPFLTSPPSARGRVCQKLLELTIGLLRPLIHGPALGEASPNYAANMVINGVALGGFGVSMDQLGAQSTATGAVDDVATYVHLATVVSASEYKAASMRWWTAAWSLARELKLGRELPPNASQPGQDGERENEGDNPSKRNQSLHGGNSNVNVTEEEREERRRLWWLLYATDRHLALCYNRPLTLLDKECSQLLQPMNDDLWQAGDFPAATYRAVGPPIECTGHSMFGYFLPLMTILGGIIDLQQAREHPRYGLTFRSGPDLDQYIMAITQQLDAYGQSLKDFEARYINSLALAENEPPENPHIDHLSPSGRSSSTVGSRVNESIVHTKMVVAYGTHIMHVLYVLLAGKWDPINLLEDHDMWISSESFLAAMSHAVGAAEAAADILEYDPDLSFMPFFFGIYLLQGSFLLLLAADKLQGDANPSVVRACETIVRAHEACVVTLNTEYQRTFRKVMRSALAQVRGRVPDDFGEQQQRRREVLSLYRWTGDGTGLALS
Protein: Germacrene A synthase 2 (EC 4.2.3.23) (Terpene synthase 1B) (HaTPS1B) (B0FGA9)
Organism: Helianthus annuus (Common sunflower)
Function: Sesquiterpene synthase involved in germacrene A biosynthesis. Germacrene A is a precursor of several sesquiterpene lactones.
Interaction partners:
Sequence:
MAAVGASATLLTNTKSAEEPVRPVANFPPSVWGDLFLSFSLDNSMMEEYAEAMEEPKGQVRKLILDPTMDSNKKLSLIYTVHRLGLTYMFFKEIEGQLDRLFKEFNLEDYVEVDLYTISTNFQAFRHLGYKLSCDVFNKFKNYDSNTFKESITSDVRGMLGLYESAQLRLKGEKILDEASAFTETKLKSLVKTLEGSLAQQVKQSLKRPFHQGMPMVEARLYFSNYQEECSRHDSLLKLAKLHFNYLQLQQKEELRIVSQWWKDMRFQETTPYIRDRVPEIYLWILGLYFEPRYSLARIIATKITLFLVVLDDTYDAYATIEEVRLLTDAINRWDIGAMSQIPEYIRPFYKILLDEYAELEKQLAKEGRANSVIASKEAFQDIARGYLEEAEWTNSGYVASFPEYMKNGLITSAYNVISKSALVGMGEIVSEDALAWYESHPQILQASELISRLQDDVMTYQFERERGQSATGVDAYIKTYGVSEKEAIDELKKMIENAWKEINEGCLKPREVSMDLLAPILNLARMIDVVYRYDDGFTFPGKTLKEYITLLFVGSSPM
Protein: Solute carrier organic anion transporter family member (Q9W270)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}.
Interaction partners:
- AT06668p
Sequence:
MASEEIEASKFLKDKEAGINVADDEKRLNSSDTTCGFSIFRGPALQRFATAHMFVIVYGIASCFLAMAFTYFTGTITTMEKRFNIPTKISGLITVGNDISTVFSSAFLSYYASRGHRPRWVALGLIIIAIFCLLMLTPHIFYGPGEEALRLTEEYGMSESFGASLNITEKNDSLCHEKNSNCLERAGDYTPIVLFFIAQFIGGIGCSLFYAPGLSYMDDNSASSKTPAMLSWSSFLRMLGPAMGFSMVSLCLRLYIDPFKKPLITTNDPRWMGAWWIGWILLTFILTISAVFVGMFPKEMPRAKARRLKADGEEDIPLAGRSFQDMLDSLKRLASNKVYVYNMLASILYLFGYMPYWIFTPKYIEIQYRQSASTSTMATGTWALGFSAAGILISGYVISKYKPSARAMAAWNFVVDYLTVAGMLCYVLVGCDESDRANSLSIVPTGDSCSASCVCEYVYYAPVCSPENITFISACHAGCTDKAINELGKTIYTGCRCMGNVSSIISLSNVTSLASQSQIAMDGACPVDCNKQFLIFLAVMCFLKFVGATGRSSNLLLALRCVPSKDKTFSLGFGSMVYSVLAFIPSPIVFGWMLDSYCLVWGKTCSSKGNCWIYDTKSLRYTMNLVCASLIFLGSFWNIGVWYHAKDMKVFDEDEKTVQAKQSDDIELKEKPNDVVTKKK
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Q72D85)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative
- Xanthine-guanine phosphoribosyltransferase
- Carbamoyl phosphate synthase large chain
- 5'-nucleotidase SurE
- Hypoxanthine phosphoribosyltransferase
- dITP/XTP pyrophosphatase
- Adenylosuccinate lyase
- Riboflavin biosynthesis protein RibBA
Sequence:
MSKIVCKALTFDDVLLQPGYSEVTPDQVDVATWLTPSIRLNIPLLSAAMDTVTESGMAISMARNGGIGVIHKNVPIHRQRLEVEKVKKSESGMIIDPVTIAPGLTVRQALEVMAEYRVSGLPVVENDKLVGILTNRDVRFVKDLETTCVSEVMTSKNLVTVPVGTTLEEAKHHLHQHRIEKLLVVDGNNRLQGLITMKDIDKVVKYPNACKDENGRLRVGAAIGIGRDCEERASELIAAGVDVLVLDSAHGHSRNVLRAIEMVKTSFPQCQLIAGNVATYEGAKAILKAGADAVKVGIGPGSICTTRIVAGVGVPQVTAIMEAVKAANEMDRCLIADGGIKFSGDVVKALCVGAHTVMIGSLFAGTDESPGETILYQGRTYKIYRGMGSIDAMKDGSSDRYFQEKSKKLVPEGIVGRVPVKGPVADSLYQLIGGLRAGMGYVGAANMEELREKSRFVEISAAGLRESHVHDVIITKEAPNYRVEN
Protein: Vomeronasal type-1 receptor (A0A494BAP1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MNKANLLYTDTNMKTFLFSEVSVGISANSMLFIVHICILLGENRPKPINLYIAFLSLTQLMLLITMGLIVADMFMSQGIWDSITCQSLIYLHRLLRGLTLCATCLLNVLWTITLSPRSSCLTKFKHKSPHHISGAFLFFCALYMSFSSHLFLSIIATPNLTSEDFMYVTQSCSLLSMSYSRTSMFSTAIAIREAFLISLFALCSGYMVALLWRHKKQAWDLHSTNVSSKSSPKQRATRTIMLLMSFFVVLYVLENAVFHSRMKFKDGSMLYCVQIIVSHSYATVSPFVLICTEKRMIKFWGSMFGRIVNI
Protein: Olfactory receptor 6C1 (OST267) (Q96RD1)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MRNHTEITEFILLGLTDDPNFQVVIFVFLLITYMLSITGNLTLITITLLDSHLQTPMYFFLRNFSILEISFTTVSIPKFLGNIISGDKTISFNNCIVQLFFFILLGVTEFYLLAAMSYDRYVAICKPLHCLSIMNRRVCTLLVFTSWLVSFLIIFPALMLLLKLHYCRSNIIDHFTCDYFPLLQLACSDTKFLEVMGFSCAAFTLMFTLALIFLSYIYIIRTILRIPSTSQRTKAFSTCSSHMVVVSISYGSCIFMYIKPSAKDRVSLSKGVAILNTSVAPMMNPFIYSLRNQQVKQAFINMARKTVFFTST
Protein: Spn43Ac (Q6V6U2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
RFSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTXAXVLL