wanglab/gogpt-training-data huggingface dataset:
Protein: Phenolphthiocerol synthesis polyketide synthase type I Pks15/1 (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41) (B2HIL7)
Organism: Mycobacterium marinum (strain ATCC BAA-535 / M)
Function: Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).
Interaction partners:
- Fatty acid synthase Fas
- Fatty acyl-AMP ligase FadD28_1 and polyketide synthase
- Polyketide synthase and peptide synthetase
- Peptide synthetase Nrp
- Non-ribosomal peptide synthetase
- Polyketide synthase PKS
- Peptide synthetase Nrp
- Non-ribosomal peptide synthetase
- Phenyloxazoline synthase MbtB
- Non-ribosomal peptide synthetase
Sequence:
MTTSGESADQQNDKLFRYLKKVAVELDEARARLREYEQRATEPVAVVGIGCRFPGGADGPEGLWDLVSQGRDAVTEFPNDRGWDTEGLFDPDPDAEGKTYTRWGAFVENATNFDAGFFGIPPSEVLAMDPQQRLMLEVSWEALEHAGIDPMSLRGSSTGVFTGIFAPSYGGKDVGALQGYGLTGSPVSVASGRVAYVLGLEGPALSVDTACSSSLVAIHWAMASLRSGECDMALAGGVTVMGLPSIFVGFSRQRGLAADGRCKAFAAAADGTGWGEGAGVLVLERLSDAQRNGHNVLAVVRGSAINQDGASNGLTAPNGLAQQRVIQAALANCGLTSADVDVVEAHGTATTLGDPIEAEALLATYGQGRPTDQPLWVGSIKSNMGHTQAAAGVAGVIKMVQAMRHGLMPASLHVDEPSKRVDWESGAVSVLAEARDWPDAGRPRRAGVSSFGISGTNAHVILEEAPAPEAVPDSESNKGEPSLPVVPWVISARSAEALTAQAGRLLAHVQADPQSNPVDIGFSLAGRSAFEHRAVVVGADRQQLLTGLATLADGAPGAGVVTGQAGSVGKTAVVFPGQGSQRIGMARELHDQLPVFAEAFDAVADELDRHLRIPLREVMWGSDAALLDSTEFAQPALFAVEVALFAALQRWGLQPDFVMGHSVGELSAAYVAGVLTLADAAMLVVARGRLMQALPAGGAMVAVAAAEDEVLPSLTDGVGIAAINAPKSVVISGAEAAVTAISDQFAQQGRRVHRLAVSHAFHSPLMEPMLEEFARIAAQVEAREPQIALVSNVTGELASADGGFGSAQYWVEHVRRAVRFADSARQLHTLGVTHFVEVGPGSGLTGSIEQSLAPAEAVVVSMLGKDRPEVASVLTAFGQLFSTGMSVDWPAVFAGSGATRVDLPTYAFQRRRFWEVPGADGPADATGLGLGGAEHALLGAVVERPDSGGVVLTGRLALADQPWLADHVIGGVVLFPGAGFVELAIRAGDEVGCAVVEELVLAAPLVLHPGMGVQVQVIVGAADDSGNRALSVYSRGDQSEDWLLNAEGMLGVEAASSGADLSVWPPEGAESVDISDGYAQLADRGYAYGPGFQGLVGVWRRDSELFAEVVAPSGVAVDKMGMHPVVLDAVLHALGLTAEQNPDSDETKLPFCWRGVSLHAGGAGRVRARLTMSGPDSISVEIADAAGLPVLTVGALVTRAMSAAQLRAAVAAAGGGAPDQGPLDVIWSPIPLSGSGTNGSAQPAVVSWADFCAGGDGGAAGDAGVVVWEPNPAGEDVVGSVYAATHAALEVLQSWFDGDRAGTLVVLTHGAVAMPGENVSDLAGAAVWGIVRSAQAENPGRIVLVDADAAVEAAELVAVGEPQLVVRSGAAHAARLAPAAPLLAVPADESAWRLAAGGGGTLEDLVIEPCPEVQAPLAAGQVRVAVRAVGVNFRDVVAALGMYPGEAPPLGAEGAGVVLEVGPQVSGVAVGDSVMGFLGGAGPLSVVDQQLITRMPQGWSFAQAAAVPVVFLTALFGLQDLAKIQPGESVLIHAGTGGVGMAAVQLARHWGVEIFVTASRGKWDTLRAMGFDDDHIGDSRTLDFEEKFLAVTDGRGVDVVLDSLAGDFVDASLRLLVRGGRFLEMGKTDIRDADKIAANYPGVWYRAFDLSEAGPVRMQEMLAEVRELFDTAVLHRLPVTTWDVRCAPAAFRFMSQARHIGKVVLTMPSALADGLADATVLITGATGAVGAVLARHMLDAYGVRHLVLASRRGDRAEGAAELAAELSEAGANVQVVACDVADRDAVEAMLARLSGEYPPVRGVIHAAGVLDDAVISSLTPERIDTVLRAKVDAAWNLHEATLDLDLSMFVLCSSIAATVGSPGQGNYSAANSFLDGLAAHRQAAGLAGISVAWGLWEQSGGMAAHLSSRDLARMSRSGLAPMNPEQAVGLLDAVLAINHPLMVATLLDRPALEARAQAGGLPPLFAGVVRRPRRRQIEDTGDAAQSKSALAERLNGLSAGERQDALVGLVCLQAAAVLGRPSPEDIDPEAGFQDLGFDSLTAVELRNRLKSATGLTLPPTVIFDHPTPTAIAEYVGRQIPDSQATQAEEEKLPESDGEMVSVTA
Protein: KU80 protein (Q585N5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- KU70 protein
- Protein artemis
- Endo/exonuclease Mre11
- DNA ligase, putative
- DNA ligase, putative
- non-specific serine/threonine protein kinase
- DNA repair protein RAD51 homolog
- Telomerase reverse transcriptase
- DNA ligase
- DNA repair protein RAD50
Sequence:
MAFRTSTIFALDVNCSISSLAQAVEFCRLSVLKTMCPSSYDEVALVVAGGCRSYSGGTSTSVSTCGSAAQLSAPCLPAPPSVEFITILHRILRDREEQQGVGSSANFIETLTLCVEVFNLKKRRKQFREVLYLLTDAHAEVVRKSVFRDVLNALRARGVTLIVVGIDFSQVTGEGSLLPGASAPSLTSNRVKVDNETVLYTLCKALGNDSRVITLRDALVSAAQLVCRKVRSLAQKTVFTIGEVRLATNVLGKVRRMHVPANRTPAPTERVPGSRKAAHSQLFDEETLRLEGGEEDSQQTCLETPVNKPTASSSNRLSEATKIRGSRGIDAVACIPQNQVPVHVLVVDTSYMIAPLDDDPVGTRAFRSIVKALAAQDSALVVRYVRSTDGNPNMFLCVPLTTGDEDVLFMSRLPFMEEIRCLRFPTLQEMEMECDIPEADAQREQELVSSIVEEMTVGEEVLHPHRVLNPFVQQYYATQRAMVNRWCSRTAENPLSAHEDSDIKLALLPQLRGISAGFASPGCKVEQLVSRTREKLETCCRVFAYVPRTTSHSPERKVLWERTPAGQPPVSETVENTEVASPAAPSTLQCHLGSGSSVTCRPVCANPPHDAVSSFIQDKRTMFHPVAHPLGSGSS
Protein: Claudin-8 (Q9Z260)
Organism: Mus musculus (Mouse)
Function: Tight-junction protein required for paracellular chloride transport in the kidney. Mediates recruitment of CLDN4 to tight junction in the kidney. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tight junction protein 1
- Occludin
- Claudin-4
- Tight junction protein ZO-3
- Claudin-10
- Claudin-16
- Claudin-23
- Claudin-1
- Claudin-9
- Claudin-13
Sequence:
MATYALQMAALVLGGVGMVGTVAVTIMPQWRVSAFIESNIVVFENRWEGLWMNCMRHANIRMQCKVYDSLLALSPDLQASRGLMCAASVLAFLAFMTAILGMKCTRCTGDDENVKSRILLTAGIIFFITGLVVLIPVSWVANSIIRDFYNPLVDVALKRELGEALYIGWTTALVLIAGGALFCCVFCCTERSNSYRYSVPSHRTTQRSFHAEKRSPSIYSKSQYV
Protein: Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Q9C8D8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03009}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MDDWEDEKIAPLPAKVELKSNWDDEDVDENEIKDSWEDDDDEPAQPPVINPAPEKAPKKAAPKTVEKKGKAVEVPKEAPKEKPLDPIAEKLRQQRLVEEADYRATAELFGVKDDDKNLDMFIPKSESDFLEYAEMISHRIKPYEKSYHYIALLKTIMRLSLTNMKAADVKDVASSITTIANEKLKAEKEAAAGKKKGGKKKQLIVDKANDDLVAGPYDAMDDFDFM
Protein: DNA-directed RNA polymerase subunit (EC 2.7.7.6) (A0A1D8PUA6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerase II subunit
- DNA-directed RNA polymerase II core subunit
- DNA-directed RNA polymerase core subunit
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MSRQFPYSSAPLRSVKEVQFGLLSPEEVRAISVAKIEYPETMDQTTKRPREGGLNDPRLGSIDRNFRCQTCGEDMAECPGHFGHIELAKPVFHIGFIAKIKKACESVCMHCGKLLLDETNPAMAQAIKIRDPKKRFNAVWSLCKTKMVCETDNNEDEMTDQPSRGGCGHPQPTIRRDGLKLWGTWKQNKNYDDNDQPERRLLTPSEILNVFKHISPEDCYKMGFNEDYARPEWMLITVLPVPPPPVRPSIAFNETARGEDDLTFKLADIIKANINVQRLETDGSPQHVISEFEALLQFHVATYMDNDIAGQPQALQKTGRPIKSIRARLKGKEGRLRGNLMGKRVDFSARTVISGDPNLDLDQVGVPISIAKTLTYPEIVTPYNIHKLTELVRNGPNEHPGAKYVIRDTGDRIDLRYNKRAGDIALQYGWKVERHLMDDDPVLFNRQPSLHKMSMMAHRVRVMPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSPETRSELSQICAVPLQIVSPQSNKPVMGIVQDTLCGIRKMTLRDIFIEYDQVMNMCYWIPNWDGVIPPPAVVKPKQLWTGKQLLSLAIPKGIHLQRFDGGRDLLSPKDTGMLIVDGEIMFGVVDKKTVGATGGGLIHTVMREKGPKVCAELFSSIQKVVNYWLLHNGFSIGIGDTIADAQTMRDVNKTIQEAKQKVQEIIIDAQHNKLEPEPGMTLRESFEHNVSRVLNQARDTAGRSAEMSLKDLNNVKQMVTSGSKGSFINISQMSACVGQQIVEGKRIPFGFGDRSLPHFTKDDYSPESKGFVENSYLRGLTPQEFFFHAMAGREGLIDTAVKTAETGYIQRRLVKALEDIMVHYDGTTRNSLGDIIQFIYGEDGIDGTQVEKQSVDTIPGSDESFERRYKIDVLDTENVISESLLESGKEIRGDVQLQKILDEEYNQLLKDRKYLREVCFPNGDFSWPLPVNLRRIIQNAQQIFHNGRYRASDLRLEEIVLGVKELCMKLLVVRGDTPLVKEAQENATLLFQCLLRSRLAARRVIEEFKLNRASFEWVMGEIETQFQKSIVHPGEMVGVVAAQSIGEPATQMTLNTFHYAGVSSKNVTLGVPRLKEILNVAKNIKTPAMTVFLDPEVASDIEKAKIVQSAIEHTTLKNVTSSTEIYYDPDPRTTVIEDDYDTVEAYFAIPDQKVEESIDKQSPWLLRLELDRAKMLDKQLTMAQVAEKISQNFGEDLFVIWSDDTADKLIIRCRVVRDPKSLDEDADAEEDQILKRIEAHMLESISLRGIPGITRVFMMQHKVSHPDETGEFKQGKEWVLETDGVNLADVMAVPGVDSTRTYSNDFIEVLSVLGIEATRSSLYKEILNVIAFDGSYVNYRHMALLVDVMTSRGHLMAITRHGINRSDTGALMRCSFEETVEILLDAAAAAELDDCKGISENVMLGQMAPLGTGSFDLMVDDRMLQKAPSSMAMDDIADGGGATPYKDYENARDENIDIDAGAGFSPIHIAQMNEGNIGGLTSYGGQPTSPAATSPFSYGYNSITSPGYTSPGYGYSPTSPSYSPTSPSYAPTSPAYSPTSPSYAPTSPAYSPTSPSYAPTSPAYSPTSPAYSPTSPSYSPTSPQYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPSYSPTSPSYSPTSPQYSPTSPSYSPTSPQYSPTSPSYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPGSPGYEPEPPKKDEN
Protein: tRNA (guanine(37)-N(1))-methyltransferase 1 (EC 2.1.1.228) (M1G-methyltransferase 1) (tRNA [GM37] methyltransferase 1) (tRNA methyltransferase 5 homolog 1) (Q93YU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
Interaction partners:
- Putative tRNA
- tRNA
- tRNA
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- tRNA-specific adenosine deaminase TAD3
- WD repeat-containing protein 55
- BRISC and BRCA1-A complex member 1
- RNA-binding
- tRNA-specific adenosine deaminase TAD2
- Uncharacterized protein At1g27050
Sequence:
MFDESKFDVNLKLWALRIPRELCKSASRILNGYMLNMPRIKPITEDPTCEKTRLVILSESVKNADLSEIPEEKLNQLKKLSELEVVPHSVTLGYSYWSADHLLKQILPDGLDIPSSFETIGHIAHLNLHDELLPFKDVIAKVIYDKNYPRIKTIVNKVGTISNEFRVPKFEVLAGENGMETEVKQYGARFKLDYGLVYWNSRLEHEHMRLSSLFKPGETVCDMFAGIGPFAIPAAQKGCFVYANDLNPDSVRYLKINAKFNKVDDLICVHNMDARKFFSHLMAVSTCEDNLQSVADNDKTKEAAVSRGGETNSSGEEIRESNASINEPLGANKKPSGTTKTENGVGKDCKSIEGHANKRLRQTLLPIAKPWEHIDHVIMNLPASALQFLDSFSNVIQKKYWKGPLPLIHCYCFIRASETTEFIIAEAETALKFHIEDPVFHKVRDVAPNKAMFCLSFRLPEACLKQEE
Protein: NDUFC2-KCTD14 readthrough (A0A087WUM3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298}; Matrix side {ECO:0000256|ARBA:ARBA00004298}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 6
Sequence:
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEGGDIGLCCLSPGSLSDTPAVFAVGSSAATTH
Protein: Actin-binding LIM protein 1 (F1LWK7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEATCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQDRQSLGESPRTLSPTPSAEGFQDGRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPDQGINIYRKPPIYKQHAALAAQNKASEDIIKFSKFPAAQAPDPNEIPKIETDHWPGPPSLAAIGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKENRERASLLASRYDSPLHSASHAPSSKTSSLPGYGKSGLHRPVSTDFAQYNSYGDVSGGVRGKASIRRLTDTVSLLVTQARERLNQPTAAYELC
Protein: Bifunctional purine biosynthesis protein ATIC (AICAR transformylase/inosine monophosphate cyclohydrolase) (ATIC) [Cleaved into: Bifunctional purine biosynthesis protein ATIC, N-terminally processed] [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (IMP synthase) (Inosinicase)] (P31939)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Is able to convert thio-AICAR to 6-mercaptopurine ribonucleotide, an inhibitor of purine biosynthesis used in the treatment of human leukemias. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}.
Interaction partners:
- Adenylosuccinate lyase
- Trifunctional purine biosynthetic protein adenosine-3
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Adenylosuccinate synthetase isozyme 2
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Adenylosuccinate synthetase isozyme 1
- Amidophosphoribosyltransferase
- Serine hydroxymethyltransferase, mitochondrial
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Sequence:
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Protein: Golgi membrane protein 1 (Zgc:56525) (F1QI79)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MMGALGNGRRGGRSPSLLMAALISCILLLAFNYWVSNSRNVELQSKILELEDRIRLLSADREREEQSKLKAEDEMHRQNEQLELMEKTHHRQQENAINSWRQEKENLQLNISSSAKAVQNMKNRMKSLLEDVNKMQSELKSCHSSMDTLTKKANSDKTRCNKEIEATKEECSVKIAAAKQEKLKTAEKVDPQDADGPEQKVLKAKSDVLASNDLNKNPAEPPNGKPDVDSPSNLDAQVETNELVVEKDAKDAVILQDTPIAASKLTNKSETLKKPAYEAVAEAVEDIKEPAPKDAEAVLDEADILEPKENEAGIGDANEEDDVGIGDANQEEDDEDLKLKAGDLKEEDAAVGKEDAIMYDNEGEIEKQLSQIKDENQGAGQDLEDDVANYNGDDENQPESEDEKQAELAGM
Protein: Xylanolytic transcriptional activator xlnR (Xylanase regulator) (Q2UD93)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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:
- DNA-binding protein creA
- Probable beta-glucosidase A
- Probable alpha-glucuronidase A
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Alpha-L-arabinofuranosidase B
- Probable catabolite repression protein creC
- Exo-1,4-beta-xylosidase xlnD
- Endo-1,4-beta-xylanase A
- Probable endo-1,4-beta-xylanase B
- D-xylulose reductase A
Sequence:
MSTTSIQHFTSSFSPFSSGTQPVGMAQSQTVGLDTLAEGSQYALEQLQLSREANGASAVDGGVPNPLRSSISKPQGQQLYSDESSAQHTQNATTGFRNLPQRDQLAEARSTIRKSSNSGPVRRRISRACDQCNQLRTKCDGQNPCAHCIEFGLTCEYARERKKRGKASKKDLAAAAAAVANNGTAPTSNGNTSNDSVSSAKRHTPSDGQSTQEVSGRYDPNFDASRNLATAGQSQLGQHSDMSGMAGMQGSQQTPHSQPSLGGAIDAIHLNHFNTLNDSNRPQMSVPDLRSLQMLHPSGANTRSPSGALPPQGMNSGYNDGAYSLMNASEANHPSINQYRLGNSAENPPAPFLGLSPPAQSPGWLSLPSPSPANFASFSMPPFSSTLRYPVLQPVLPHIASIIPQSLACDLLDVYFTSFSPSHLSPQSPYVVGYIFRKQSFLHPTKPRVCSPGLLASMLWVAAQTSDAAFLTSPPSARGRVCQKLLELTVGLLRPLIHGPAPGETSPNYAANMVINGVALGGFGVSMDQLGAQSSATGAVDDVATYVHLATVISASEYKAASMRWWTAAWSLARELKLGRELPPNAPQPRQDGEPEDDTDVDMSKRNLPPLITSVGGNSGSTILNVTEEEREERRRLWWLLYATDRHLALCYNRPLTLLDKECEGLLQPMNDDLWQAGDFAGATYRQVGPQVECTGHSMFGFFLPLMTILGEIVDLQQAKEHPRFGRVFRNSADWDHQVLEITRQLDTYAQSLKEFEARYTSSLALGAGESEAAIEGSHLDHVSPSGRSTSTAGSRVNESIVHTKMVVAYGTHIMHVLHVLLAGKWDPINLLEDHDLWISSESFIAAMSHAVGAADAAADILEYDPDITFMPFFFGIYLLQGSFLLLLAADKLQGDVSPSVVRACETIVRAHEACVVTLNTEYQRTFRKVMRSALAQVRGRMPEDFGEQQQRRREVLALYRWTGDGSGLAL
Protein: Glutamate 5-kinase (LdG5K) (EC 2.7.2.11) (Gamma-glutamyl kinase) (A0A0R6Y3I5)
Organism: Leishmania donovani
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. May be important for growth and survival.
Interaction partners:
Sequence:
MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS
Protein: BTB/POZ and MATH domain-containing protein 6 (Protein BTB-POZ AND MATH DOMAIN 6) (AtBPM6) (A1L4W5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:19843165}. Cytoplasm {ECO:0000269|PubMed:19843165}.
Interaction partners:
- Cullin-3A
- Cullin-3B
- Homeobox-leucine zipper protein ATHB-6
Sequence:
MSKLMTRTSGSSSPNTIPDQIESPTSSRSVTQTTNGSHQFVIQGYSLAKGIGVGKHIASDNFSVGGYQWTIFVYPDGKNPEDNSSYVSVFIVLASECTEVRALFELSLVDQSGKGKHKVHSHFNRSLDGGPYTLKYRGSMWGYKRFFRRSLLETSDYLKDDCLKINCTVGVVVSEMHCPRLLSIHVPDSELGSHFGKLLDTLQGSDVTFDVAGEKFQAHKLVLAARSQFFRSMFYNTLAENNSDVVISDLEPKVFKALLHFMYKDSLPGDVEPLTAHSFDLLRPSEIDDTLIVKLLAAAEMYNLSRLRLLCESHICKGISISSVSKILALSDKYNASELKSVSLKFTAENLAAVLQTKAYEDLKDDCPNLQSELLKAVAGYDDTSSSGGGKSQSVWAQLSNGGETSSRRVRQRTT
Protein: Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (Centaurin-delta-3) (Cnt-d3) (Q8WWN8)
Organism: Homo sapiens (Human)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia. {ECO:0000250}.
Interaction partners:
- Transforming protein RhoA
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- SH3 domain-containing kinase-binding protein 1
- ADP-ribosylation factor 6
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
Sequence:
MAAPQDLDIAVWLATVHLEQYADTFRRHGLATAGAARGLGHEELKQLGISATGHRKRILRLLQTGTEEGSLDPKSDSAMEPSPSPAPQAQPPKPVPKPRTVFGGLSGPATTQRPGLSPALGGPGVSRSPEPSPRPPPLPTSSSEQSSALNTVEMMPNSIYFGLDSRGRAQAAQDKAPDSSQISAPTPALRPTTGTVHIMDPGCLYYGVQPVGTPGAPDRRESRGVCQGRAEHRLSRQDLEAREDAGYASLELPGDSTLLSPTLETEETSDDLISPYASFSFTADRLTPLLSGWLDKLSPQGNYVFQRRFVQFNGRSLMYFGSDKDPFPKGVIPLTAIEMTRSSKDNKFQVITGQRVFVFRTESEAQRDMWCSTLQSCLKEQRLLGHPRPPQPPRPLRTGMLELRGHKAKVFAALSPGELALYKSEQAFSLGIGICFIELQGCSVRETKSRSFDLLTPHRCFSFTAESGGARQSWAAALQEAVTETLSDYEVAEKIWSNRANRQCADCGSSRPDWAAVNLGVVICKQCAGQHRALGSGISKVQSLKLDTSVWSNEIVQLFIVLGNDRANRFWAGTLPPGEGLHPDATPGPRGEFISRKYRLGLFRKPHPQYPDHSQLLQALCAAVARPNLLKNMTQLLCVEAFEGEEPWFPPAPDGSCPGLLPSDPSPGVYNEVVVRATYSGFLYCSPVSNKAGPSPPRRGRDAPPRLWCVLGAALEMFASENSPEPLSLIQPQDIVCLGVSPPPTDPGDRFPFSFELILAGGRIQHFGTDGADSLEAWTSAVGKWFSPLSCHQLLGPGLLRLGRLWLRSPSHTAPAPGLWLSGFGLLRGDHLFLCSAPGPGPPAPEDMVHLRRLQEISVVSAADTPDKKEHLVLVETGRTLYLQGEGRLDFTAWNAAIGGAAGGGGTGLQEQQMSRGDIPIIVDACISFVTQHGLRLEGVYRKGGARARSLRLLAEFRRDARSVKLRPGEHFVEDVTDTLKRFFRELDDPVTSARLLPRWREAAELPQKNQRLEKYKDVIGCLPRVNRRTLATLIGHLYRVQKCAALNQMCTRNLALLFAPSVFQTDGRGEHEVRVLQELIDGYISVFDIDSDQVAQIDLEVSLITTWKDVQLSQAGDLIMEVYIEQQLPDNCVTLKVSPTLTAEELTNQVLEMRGTAAGMDLWVTFEIREHGELERPLHPKEKVLEQALQWCQLPEPCSASLLLKKVPLAQAGCLFTGIRRESPRVGLLRCREEPPRLLGSRFQERFFLLRGRCLLLLKEKKSSKPEREWPLEGAKVYLGIRKKLKPPTPWGFTLILEKMHLYLSCTDEDEMWDWTTSILKAQHDDQQPVVLRRHSSSDLARQKFGTMPLLPIRGDDSGATLLSANQTLRRLHNRRTLSMFFPMKSSQGSVEEQEELEEPVYEEPVYEEVGAFPELIQDTSTSFSTTREWTVKPENPLTSQKSLDQPFLSKSSTLGQEERPPEPPPGPPSKSSPQARGSLEEQLLQELSSLILRKGETTAGLGSPSQPSSPQSPSPTGLPTQTPGFPTQPPCTSSPPSSQPLT
Protein: PAR domain protein 1-delta (PAR-domain protein 1, isoform I) (Q24217)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDRERSSPTLIETGLKNLIGGRDGNYPLISGINGKSTSNSKEIICPDDKYKEEGDIWNVEAQTAFLGPNLWDKTLPYDADLKVTQYADLDEFLSENNIPDGLPGTHLGHSSGLGHRSDSLGHAAGLSLGLGHITTKRERSPSPSDCISPDTLNPPSPAESNELKDDKYWARRRKNNIAAKRSRDARRQKENQIAMRARYLEKENATLHQEVEQLKQENMDLRARLSKFQDV
Protein: Tektin-1 (Q969V4)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q32KZ9}.
Interaction partners:
- Protein Flattop
- Piercer of microtubule wall 1 protein
- Cilia- and flagella-associated protein 52
- Tektin-4
- Tektin-2
- EF-hand domain-containing protein 1
- Cilia- and flagella-associated protein 45
- EF-hand domain-containing family member C2
- Cilia- and flagella-associated protein 276
- Cilia- and flagella-associated protein 95
Sequence:
MAKLLQPPPKFLPSEWHIANKNQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSDVNKKLEQRLEEVQFWKKELDDKLEQLVNVTDDLLIYKIRLEKALETLKEPLHITETCLAYREKRIGIDLVHDTVEHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDLKDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVEKADKQRNNSLMLKALVDRILSQTANDLRKQCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEGPAKVAHTRLETRTHRPNVELCRDVAQYRLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYIDEVLCMQMRKSIPLRDGEDHGVWAGGLRPDAVC
Protein: Liquid facets, isoform I (M9PBU6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRKQKDDMQVNVAGLRRNIKNLAHNYSDAQVKVREATSNDPWGPSAAIMSEIAELTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKDDERLKNERVKAQKAKERFAQNPSGFGSDGYIDGPSQRDLPPGWQEEPPKSVSELEMVRPQTAGEEELQLQLAMAMSREEAEQEEAKRRSDDVRLQLALSQSEQDFKDPNGRPIPAPKKEEQQSHLLDLLDISLGATSISSPPLGAAGGAPTAVVDPWAMPGPRAPSQLSDPWSGTSSPQVDPWNPSAAPRTILGAGVPMTSAPLGAGNDAWGARTQSPSVASGSSNEGWLQSNGNANQNGRGATPAGPPAEGWLIKSTAVGALGAAPINHAANNGSSSSDPWLAEPAASAAGGAAAVGLADPWAPGAASQTGAGALDDPWKALGTGAIKKQSPEFDEFDLITNRNKSEHSNSNASNNNNASLLDDMDPLSANYGNGGINSSMHPSTGATAKKSIKDAHSFLGENSALVNLDNLIKPIAPQTQTGNQPAYNPFSDNVVPPKTNLFQQQQPAVPSINQLKQQAPFSVSMNQDPWAPVMGGVSTTSQPSMEAWTLK