wanglab/gogpt-training-data huggingface dataset:
Protein: Xanthine dehydrogenase (XD) (EC 1.17.1.4) (Protein rosy locus) (P10351)
Organism: Drosophila melanogaster (Fruit fly)
Function: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
- Uricase
- Guanine deaminase
- purine-nucleoside phosphorylase
- Sulfite oxidase, mitochondrial
- 5-hydroxyisourate hydrolase
- RE54080p
- Molybdenum cofactor sulfurase
- Aldehyde oxidase 1
Sequence:
MSNSVLVFFVNGKKVTEVSPDPECTLLTFLREKLRLCGTKLGCAEGGCGACTVMVSRLDRRANKIRHLAVNACLTPVCSMHGCAVTTVEGIGSTKTRLHPVQERLAKAHGSQCGFCTPGIVMSMYALLRNAEQPSMRDLEVAFQGNLCRCTGYRPILEGYKTFTKEFACGMGEKCCKVSGKGCGTDAETDDKLFERSEFQPLDPSQEPIFPPELQLSDAFDSQSLIFSSDRVTWYRPTNLEELLQLKAKHPAAKLVVGNTEVGVEVKFKHFLYPHLINPTQVKELLEIKENQDGIYFGAAVSLMEIDALLRQRIEQLPESETRLFQCTVDMLHYFAGKQIRNVACLGGNIMTGSPISDMNPVLSAAGAQLEVASFVDGKLQKRSVHMGTGFFTGYRRNVIEAHEVLLGIHFRKTTPDQYIVAFKQARRRDDDIAIVNAAINVRFEEKSNIVAEISMAFGGMAPTTVLAPRTSQLMVGQEWSHQLVERVAESLCTELPLAASAPGGMIAYRRALVVSLFFKAYLAISLKLSKSGITSSDALPSEERSGAETFHTPVLKSAQLFERVCSDQPICDPIGRPKVHAAALKQATGEAIYTDDIPRMDGEVYLAFVLSTKPRAKITKLDASEALALDGVHQFFCYKDLTEHENEVGPVFHDEHVFAAGEVHCYGQIVGAIAADNKALAQRAARLVKVEYEELSPVIVTIEQAIEHKSYFPDYPRFVTKGNVEEALAQADHTFEGTCRMGGQEHFYLETHAALAVPRDSDELELFCSTQHPSEVQKLVAHVTALPAHRVVCRAKRLGGGFGGKESRGISVALPVALAAYRMGRPVRCMLDRDEDMLITGTRHPFLFKYKVGFTKEGLITACDIECYNNAGWSMDLSFSVLERAMFHFENCYRIPNVRVGGWVCKTNLPSNTAFRGFGGPQGMYAGEHIIRDVARIVGRDVVDVMRLNFYKTGDYTHYHQQLEHFPIERCLEDCLKQSRYDEKRQEIARFNRENRWRKRGMAVVPTKYGIAFGVMHLNQAGSLINIYGDGSVLLSHGGVEIGQGLNTKMIQCAARALGIPSELIHISETATDKVPNTSPTAASVGSDLNGMAVLDACEKLNKRLAPIKEALPGGTWKEWINKAYFDRVSLSATGFYAMPGIGYHPETNPNARTYSYYTNGVGVTVVEIDCLTGDHQVLSTDIVMDIGSSLNPAIDIGQIEGAFMQGYGLFTLEELMYSPQGMLYSRGPGMYKLPGFADIPGEFNVSLLTGAPNPRAVYSSKAVGEPPLFIGSSAFFAIKEAIAAAREDQGLSGDFPLEAPSTSARIRIACQDKFTELLEIPEPGSFTPWNIVP
Protein: MICOS complex subunit (F1SPZ9)
Organism: Sus scrofa (Pig)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363021}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MFKVIQRSMGPASLSLLTFKVYASPKKDSPHKAAVKVNELSLYSVPEGQSKYVEEPRTQLEENISHLRHYCEPYTSWCQEMYSQTKPKMQSLVQWGLGSKIKKLVYPPGFMGLAASLYYPQQAIVFAQVSGEKLYDWGLRGYIVVEDLWKENFQKPGNVKNPPGNK
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSR0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Exocyst complex protein EXO70
- Rho GDP-dissociation inhibitor
- Protein kinase C-like 1
- Candida glabrata strain CBS138 chromosome I complete sequence
- Exocyst complex component Sec8
- Actin
Sequence:
MAFLCGSSSSQSSGSKKPVERKIVILGDGACGKTSLLNVFTRGYFPEVYEPTVFENYIHDIFVDNRHITLSLWDTAGQEEFDRLRSLSYSDTHTIMLCFSIDSRDSLENVKNKWVGEITDHCEGVNLVLVALKCDLRNNENNVITPNNIQNNRNNNNNNNLITYEEGLAMAKQIGALRYLECSAKLNKGVNEAFTEAARVALTAKNATDNINSNSSSNEKDSFCTIC
Protein: Uncharacterized protein (Q57TS4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIRSLGYRLSNPVVTRYARSISLQVEKSCATLADKIVRGRATNVFYTHPSYVMAREKMLYTLWVDSGVFLLSLRAMLPFFCVALFFKA
Protein: Ornithine transcarbamylase, mitochondrial (OTCase) (EC 2.1.3.3) (Ornithine carbamoyltransferase, mitochondrial) (P00480)
Organism: Homo sapiens (Human)
Function: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3895227}.
Interaction partners:
- Argininosuccinate synthase
- Carbamoyl-phosphate synthase, mitochondrial
- Arginase-1
- Arginase-2, mitochondrial
- Ornithine aminotransferase, mitochondrial
- 1,4-alpha-glucan-branching enzyme
- N-acetylglutamate synthase, mitochondrial
- Multifunctional protein CAD
- Aminoacylase-1
- Argininosuccinate lyase
Sequence:
MLFNLRILLNNAAFRNGHNFMVRNFRCGQPLQNKVQLKGRDLLTLKNFTGEEIKYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPCFLTTQDIHLGVNESLTDTARVLSSMADAVLARVYKQSDLDTLAKEASIPIINGLSDLYHPIQILADYLTLQEHYSSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDASVTKLAEQYAKENGTKLLLTNDPLEAAHGGNVLITDTWISMGQEEEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPQLQKPKF
Protein: Peroxisomal trans-2-enoyl-CoA reductase (TERP) (EC 1.3.1.38) (2,4-dienoyl-CoA reductase-related protein) (DCR-RP) (HPDHase) (Short chain dehydrogenase/reductase family 29C member 1) (pVI-ARL) (Q9BY49)
Organism: Homo sapiens (Human)
Function: Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity.
Subcellular location: Peroxisome {ECO:0000269|PubMed:11669066}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- Peroxisomal acyl-coenzyme A oxidase 1
- Sterol carrier protein 2
- Peroxisomal multifunctional enzyme type 2
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYNLTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVSSVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEKAKL
Protein: Genetic interactor of prohibitin 7, mitochondrial (P53171)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in respiratory growth and required for cell survival in the absence of prohibitins or GEM1.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}; Single-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Uncharacterized protein YBL059W
Sequence:
MVLSNVKIFRLKSHRAFRIGPMIKAVAGNLLVKRFYQPKLERIPPASLLLKQKIRLAQNGSTTSTENPISFSQTMSEIFSVLQPSAPDLDEDETSGLKRDHLLTERLNNGELGVIMNKFFNPSSTHNNQLIDTNILLQNFPKLSGNDLDLLDFAINEKMRGNWNDLKQDFIQLWYYKSFGFLGPRTQFVLTNSSPSVRSQFLKLPFIEYNWFLLQNNKNANILPADVQNVVKVFHLDDKRFTWKSIDPFSKAIISFVVFVSIYVWLDESAKQKTKELPAQKSTVISE
Protein: Leucine-rich repeat receptor-like protein kinase TDR (EC 2.7.11.1) (Protein PHLOEM INTERCALATED WITH XYLEM) (Tracheary element differentiation inhibitory factor receptor) (AtTDR) (TDIF receptor) (Q9FII5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts with CLE41p and CLE44p peptides as a ligand-receptor pair in a signal transduction pathway involved in the regulation of procambium maintenance and polarity during vascular-tissue development. Mediates repression of tracheary element differentiation and the promotion of procambial cells formation and polar division adjacent to phloem cells in the veins.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18812507, ECO:0000269|PubMed:27498761}; Single-pass type I membrane protein {ECO:0000269|PubMed:18812507}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- Somatic embryogenesis receptor kinase 2
- WUSCHEL-related homeobox 4
- WUSCHEL-related homeobox 14
- CLAVATA3/ESR
- Protein CLAVATA 3
- Dof zinc finger protein DOF5.3
- Homeobox-leucine zipper protein ATHB-8
- Shaggy-related protein kinase eta
Sequence:
MKKKNISPSLVLHPLLLLLLPFFAFNSLALKFSPQLLSLLSLKTSLSGPPSAFQDWKVPVNGQNDAVWCSWSGVVCDNVTAQVISLDLSHRNLSGRIPIQIRYLSSLLYLNLSGNSLEGSFPTSIFDLTKLTTLDISRNSFDSSFPPGISKLKFLKVFNAFSNNFEGLLPSDVSRLRFLEELNFGGSYFEGEIPAAYGGLQRLKFIHLAGNVLGGKLPPRLGLLTELQHMEIGYNHFNGNIPSEFALLSNLKYFDVSNCSLSGSLPQELGNLSNLETLFLFQNGFTGEIPESYSNLKSLKLLDFSSNQLSGSIPSGFSTLKNLTWLSLISNNLSGEVPEGIGELPELTTLFLWNNNFTGVLPHKLGSNGKLETMDVSNNSFTGTIPSSLCHGNKLYKLILFSNMFEGELPKSLTRCESLWRFRSQNNRLNGTIPIGFGSLRNLTFVDLSNNRFTDQIPADFATAPVLQYLNLSTNFFHRKLPENIWKAPNLQIFSASFSNLIGEIPNYVGCKSFYRIELQGNSLNGTIPWDIGHCEKLLCLNLSQNHLNGIIPWEISTLPSIADVDLSHNLLTGTIPSDFGSSKTITTFNVSYNQLIGPIPSGSFAHLNPSFFSSNEGLCGDLVGKPCNSDRFNAGNADIDGHHKEERPKKTAGAIVWILAAAIGVGFFVLVAATRCFQKSYGNRVDGGGRNGGDIGPWKLTAFQRLNFTADDVVECLSKTDNILGMGSTGTVYKAEMPNGEIIAVKKLWGKNKENGKIRRRKSGVLAEVDVLGNVRHRNIVRLLGCCTNRDCTMLLYEYMPNGSLDDLLHGGDKTMTAAAEWTALYQIAIGVAQGICYLHHDCDPVIVHRDLKPSNILLDADFEARVADFGVAKLIQTDESMSVVAGSYGYIAPEYAYTLQVDKKSDIYSYGVILLEIITGKRSVEPEFGEGNSIVDWVRSKLKTKEDVEEVLDKSMGRSCSLIREEMKQMLRIALLCTSRSPTDRPPMRDVLLILQEAKPKRKTVGDNVIVVGDVNDVNFEDVCSVDVGHDVKCQRIGV
Protein: Cytochrome P450 86A2 (EC 1.14.14.1) (Protein ABERRANT INDUCTION OF TYPE THREE 1) (O23066)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18. Plays a major role in the biosynthesis of extracellular lipids. Involved in the biosynthesis of hydroxylated fatty acids required for cutin biosynthesis, cuticle development and repression of bacterial type III gene expression.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein HOTHEAD
- Very-long-chain enoyl-CoA reductase
- Omega-hydroxypalmitate O-feruloyl transferase
- Long chain acyl-CoA synthetase 2
- F21B7.2
- Fatty alcohol:caffeoyl-CoA acyltransferase
- 3-ketoacyl-CoA synthase 6
- Glycerol-3-phosphate 2-O-acyltransferase 4
- ABC transporter G family member 12
- Probable glycerol-3-phosphate acyltransferase 8
Sequence:
MDVSNTMLLVAVVAAYWLWFQRISRWLKGPRVWPVLGSLPGLIEQRDRMHDWITENLRACGGTYQTCICAVPFLAKKQGLVTVTCDPKNIEHMLKTRFDNYPKGPTWQAVFHDFLGQGIFNSDGDTWLFQRKTAALEFTTRTLRQAMGRWVNRGIKLRFCPILETAQNNYEPVDLQDLILRLTFDNICGLAFGKDTRTCAPGLPENGFASAFDRATEASLQRFILPEFLWRLKKWLGLGLEVSLSRSLGEIDGYLDAVINTRKQELLSQRESGVQRHDDLLSRFMKKKDQSYSETFLRHVALNFILAGRDTSSVALSWFFWLITTHPTVEDKIVREICSVLIETRGTDVSSWTAEPLEFDEVDRLVYLKAALSETLRLYPSVPEDSKHVVNDDILPDGTFVPAGSSVTYSIYAAGRMKSTWGEDCLEFKPERWISPDDGKFVNHDQYRFVAFNAGPRICLGKDLAYLQMKTIAAAVLLRHRLTVAPGHKVEQKMSLTLFMKNGLLVNVHKRDLEVMMKSLVPKERNDVVVLNGKCNGGIGEGVAVNAAVAVAV
Protein: Hydrolase family protein / HAD-superfamily protein (Q9M169)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNHLLILARNSLRRRNFNLRPPSRSFSSTISPESNRSSFGIAFDIDGVILLGSSPVGGSPSALRRLYDDSGALKIPFLFLTNGGGLPESKRASEMSHLLGVQVSPLQVIQAHSPFRKLVNRFENELVVAAGKGEPAAVMSNYGFKNVISMDEYASYFDNIDPLAPYKKLMFRQDGHKELRSREDVLSQRVQAAFIVSDPVDWSRDIQVLCDILRTGGLPGKEIGPQPHLYIANDDLDYQTEFPTERLGMGAFRIALESIFNRIHEKPLEYTSFGKPNPFVFKNAEDVLKEIATSPYSSNQGSHHFKTLYMIGDNPKIDIRGARQAGTPWFSILTRTGVFKGKDNHSEFPADLVVDTVEEAVDFILTRESAKQSLLS
Protein: Decapping nuclease din1 (EC 3.6.1.-) (Dhp1-interacting protein 1) (NAD-capped RNA hydrolase Rai1) (DeNADding enzyme Rai1) (spRai1) (EC 3.6.1.-) (O13836)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective m7G cap and is part of a pre-mRNA capping quality control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P53063}.
Interaction partners:
- 5'-3' exoribonuclease 2
- UPF0400 protein C337.03
- Exosome complex component rrp42
- Polynucleotide 5'-hydroxyl-kinase grc3
- U3 small nucleolar ribonucleoprotein protein imp3
- Exosome complex component ski6
- Pre-rRNA-processing protein las1
- Exosome complex component mtr3
- Exosome complex component rrp43
- Large ribosomal subunit protein uL30C
Sequence:
MLREFSFYDVPPAHVPPVSEPLEIACYSLSRDRELLLDDSKLSYYYPPPLFSDLNTGFPNRFHPPKSDPDPISIVKDVLMTKGIQMNSSFLTWRGLITKIMCAPLDPRNHWETYLVMDPTSGIIMMEERTRSETSYANQDRMCYWGYKFEAISTLPEIWDACSRDQIEQRDNQDVVPDEQYCSIVKINIGKSKLILAGEVDCIWDKKPCSAKESDVHSDDGTIEEDASNAENPNLHYVELKTSKKYPLENYGMRKKLLKYWAQSFLLGIGRIIIGFRDDNGILIEMKELFTHQIPKMLRPYFKPNDWTPNRLLVVLEHALEWIKQTVKQHPPSTEFTLSYTGGSKLVLRQII
Protein: Transcription factor AP-2-delta (AP2-delta) (Activating enhancer-binding protein 2-delta) (Q91ZK0)
Organism: Mus musculus (Mouse)
Function: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSTTFPGLVHDAEIRHDGSNSYRLMQLGCLESVANSTVAYSSSSPLTYSTTGTEFASPYFSTNHQYTPLHHQSFHYEFQHSHPAVTPDAYSLNSLHHSQQYYQQIHHGEPTDFINLHNARALKSSCLDEQRRELGCLDAYRRHDLSLMSHGSQYGMHPDQRLLPGPSLGLAAAGADDLQGSVEAQCGIVLNGQGGVIRRGGTCVVNPTDLFCSVPGRLSLLSSTSKYKVTIAEVKRRLSPPECLNASLLGGILRRAKSKNGGRCLREKLDRLGLNLPAGRRKAANVTLLTSLVEGEALHLARDFGYTCETEFPAKAVGEHLARQHMEQKEQTARKKMILATKQICKEFQDLLSQDRSPLGSSRPTPILDLDIQRHLTHFSLITHGFGTPAICAALSTFQTVLSEMLNYLEKHTTHKNGGAADSGQGHANSEKAPLRKASEAAVKEGKTEKTD
Protein: Tryptophan decarboxylase TDC1 (EC 4.1.1.105) (P93082)
Organism: Camptotheca acuminata (Happy tree)
Function: Involved in the biosynthesis of tryptamine. Supplies tryptamine for the indole moiety of camptothecin (CPT), an anti-cancer monoterpene alkaloid. Represents a key step in monoterpene indole alkaloid biosynthesis. Is specific for tryptophan, and inactive against tyrosine, phenylalanine and 3,4-dihydroxyphenylalanine (dopa).
Interaction partners:
Sequence:
MGSLDSNYDTESPASVGQFNPLDPEEFRKQAHCIVDFIADYYKNIESYPVLSQVDPGYRHSRLGKNAPYRSEPFESILKDVQKDIIPGMTHWMSPNFFAHFPATVSSAAFVGEMLCTCFNSVGFNWLASPAATELEMVVIDWLANMLKLPKSFMFSGTGGGVLQGTTSEAILCTLIAASPMHFEIVGVKTSTSFVVYGSDQTHSTYAKACKLAGILPCNIRSIPTTADSNFSVSPLLLRRAIEADKAAGMVPLYICATVGTTSTTAIDPLSSLADVANDYGVWFHVDAAYAGSACICPEFRHYLDGIERADSLSLSPHKWLLSYLDCCCLWVKSPSLLVKALSTDPEYLKNQPSESKSVVDYKDWQVGTGRRFKALRLWFVMRSYGVANLQSHIRTDVQMAKMFEGFVKSDPRFEILVPRVFSLVCFRLNPISGSDPTGTEALNRKLLDWVNSTGRVYMTHTKVGGIYMLRFAVGATLTEKRHVSSAWKLIKEGADVLLKED
Protein: Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone) (O14618)
Organism: Homo sapiens (Human)
Function: Delivers copper to copper zinc superoxide dismutase (SOD1).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9726962}.
Interaction partners:
- Superoxide dismutase
- Copper-transporting ATPase 1
- Copper-transporting ATPase 2
- Copper transport protein ATOX1
- Extracellular superoxide dismutase
- Cytochrome c oxidase copper chaperone
- High affinity copper uptake protein 1
- Protein SLC31A2
Sequence:
MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAIFRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
Protein: RH49436p (Q8MS04)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLFENPAVAAKLPFPYNVPPPLQAAAAAAAAVPNLRFQTPIKAFACLTAATRSVSEMNATSLYAGNPMENAAAAAAAAAAGLIDPHHNRDLHQALVASIANNSVAAIGGGLTTAAVLKSAAQQSQQAVQQNQNAVVVTPGLEQPKQEPAQQAALALLKENVNASAGAGQNNGQAAMGGSNKSGSSGRSTPSLSGGSGSDPAPGKLFVGGLSWQTSSDKLKEYFNMFGTVTDVLIMKDPVTQRSRGFGFITFQEPCTVEKVLKVPIHTLDGKKIDPKHATPKNRPRQANKTKKIFVGGVSQDTSAEEVKAYFSQFGPVEETVMLMDQQTKRHRGFGFVTFENEDVVDRVCEIHFHTIKNKKVECKKAQPKEAVTPAAQLLQKRIMLGTLGVQLPTAPGQLIGARGASVATMNPLAMLQNPTQLLQSPAAAAAAQQAALISQNPFQVQNAAAAASIANQAGFGKLLTTYPQTALHSVRYAPYSIPASAATANAALMQAHQAQSVAAAAHHHQQQQQQQHHHQQQTHNAHVAAAQQQQQSHHNAVSNPASQAHSAAAAAALAANAANGAGAAGAHSLAAAAQQAGLMAGNPLNAAAAAAAAAANPAAAYSNYALANVDMSSFQGVDWSTMYGMGMYV
Protein: Truncated inactive ribonuclease PH (Truncated inactive RNase PH) (Inactive RNase PH) (Truncated RNase PH) (P0CG19)
Organism: Escherichia coli (strain K12)
Function: This an expressed but non-active exoribonuclease allele. The catalytically inactive protein translated in strain K12 MG1655 inhibits the 5'-processing of primary pre-tRNAs with short (<5 nucleotide) leaders in a dominant-negative effect when RNA pyrophosphohydrolase (rppH) is also inactive; perhaps inactive Rph inhibits interaction with RNase P which is exacerbated when RppH cannot cleave the triphosphate of the primary transcript.
Interaction partners:
Sequence:
MRPAGRSNNQVRPVTLTRNYTKHAEGSVLVEFGDTKVLCTASIEEGVPRFLKGQGQGWITAEYGMLPRSTHTRNAREAAKGKQGGRTMEIQRLIARALRAAVDLKALGEFTITLDCDVLQADGGTRTASITGACVALVDALQKLVENGKLKTNPMKGMVAAVSVGIVNGEAVCDLEYVEDSAAETDMNVVMTEDGRIIEVQGTAEGEPFTHEELLILLALARGESNPL
Protein: Forkhead box protein I1 (Q922I5)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator required for the development of normal hearing, sense of balance and kidney function. Required for the expression of SLC26A4/PDS, JAG1 and COCH in a subset of epithelial cells and the development of the endolymphatic system in the inner ear. Also required for the expression of SLC4A1/AE1, SLC4A9/AE4, ATP6V1B1 and the differentiation of intercalated cells in the epithelium of distal renal tubules.
Subcellular location: Nucleus.
Interaction partners:
- Pendrin
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 116 kDa subunit a 4
Sequence:
MSSFDLPAPSPPRCSPQFPSIGQEPPEMNLYYENFFHPQGMPSPQRPTSFEGGGEYGTTPNPYLWLNGPAMTPPPYLPGTNASPFLPQAYGMQRQLLPSDLGWLPIPSQEELMKLVRPPYSYSALIAMAIHGAPDQRLTLSQIYQYVADNFPFYNKSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRKSDSSSSTSSLASEKTENGLLASSPKPTEPQEVLDTASPDTTTSSPEKRSSPAPSGTPCLNNFLSTMTAYVSGTNPISRSVATPGLSSEPIDKMGQNSLNFNSYTPLTNLSSHGNGGEWANPVATNALGYGGSVFNQFSPHFYNSINTNGILFPREGTEV
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase (EC 2.5.1.54) (C8VTT5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Pentafunctional AROM polypeptide
- Uncharacterized protein
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Uncharacterized protein
Sequence:
MSSFFLPNPNLGDSNHLEDSRIRGYNPLTPPNLLQHEIALTEKARQTVLQGRAEAIAVAHGTDTDKRRLLVVIGPCSIHDPEMALEYCDRLLKLKEKYKDELLIVMRSYLEKPRTTVGWKGLINDPDIDNSFNINKGLRISRQLFVDLTNKGMPIASEMLDTISPQFLADCLSVGAVGARTTESQVHRELASGLSFPVGFKNGTDGSLDVAVDAIGSVKHPHHFLSVTKPGVVAIVGTVGNPDCFVILRGGKKGPNYDAASITEAKEKLIAKGLAPRLMVDCSHGNSQKDHKNQPKVAAVLAEQIAAGETAIMGVMIESNINEGNQKVPPEGKAGLKYGVSITDACINWEDTESTLETLAKAVATRREKLAPSS
Protein: Tubulin-specific chaperone D (Beta-tubulin cofactor D) (tfcD) (SSD-1) (Tubulin-folding cofactor D) (Q9BTW9)
Organism: Homo sapiens (Human)
Function: Tubulin-folding protein implicated in the first step of the tubulin folding pathway and required for tubulin complex assembly. Involved in the regulation of microtubule polymerization or depolymerization, it modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Acts as a GTPase-activating protein (GAP) for ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. Required for correct assembly and maintenance of the mitotic spindle, and proper progression of mitosis. Involved in neuron morphogenesis.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q28205}. Lateral cell membrane {ECO:0000250|UniProtKB:Q28205}. Cytoplasm {ECO:0000250|UniProtKB:Q28205}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q28205}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27666370}. Note=Localized in cell-cell contacts. {ECO:0000250|UniProtKB:Q28205}.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- Tubulin-specific chaperone E
- Tubulin-specific chaperone E
- Tubulin-folding cofactor B
- Tubulin beta-2A chain
- Tubulin-specific chaperone cofactor E-like protein
- Tubulin-specific chaperone C
- Tubulin-specific chaperone A
- Carboxypeptidase N catalytic chain
- Tubulin beta-2B chain
Sequence:
MALSDEPAAGGPEEEAEDETLAFGAALEAFGESAETRALLGRLREVHGGGAEREVALERFRVIMDKYQEQPHLLDPHLEWMMNLLLDIVQDQTSPASLVHLAFKFLYIITKVRGYKTFLRLFPHEVADVEPVLDLVTIQNPKDHEAWETRYMLLLWLSVTCLIPFDFSRLDGNLLTQPGQARMSIMDRILQIAESYLIVSDKARDAAAVLVSRFITRPDVKQSKMAEFLDWSLCNLARSSFQTMQGVITMDGTLQALAQIFKHGKREDCLPYAATVLRCLDGCRLPESNQTLLRKLGVKLVQRLGLTFLKPKVAAWRYQRGCRSLAANLQLLTQGQSEQKPLILTEDDDEDDDVPEGVERVIEQLLVGLKDKDTVVRWSAAKGIGRMAGRLPRALADDVVGSVLDCFSFQETDKAWHGGCLALAELGRRGLLLPSRLVDVVAVILKALTYDEKRGACSVGTNVRDAACYVCWAFARAYEPQELKPFVTAISSALVIAAVFDRDINCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVGNRSNCFLVISVFIAGFPEYTQPMIDHLVTMKISHWDGVIRELAARALHNLAQQAPEFSATQVFPRLLSMTLSPDLHMRHGSILACAEVAYALYKLAAQENRPVTDHLDEQAVQGLKQIHQQLYDRQLYRGLGGQLMRQAVCVLIEKLSLSKMPFRGDTVIDGWQWLINDTLRHLHLISSHSRQQMKDAAVSALAALCSEYYMKEPGEADPAIQEELITQYLAELRNPEEMTRCGFSLALGALPGFLLKGRLQQVLTGLRAVTHTSPEDVSFAESRRDGLKAIARICQTVGVKAGAPDEAVCGENVSQIYCALLGCMDDYTTDSRGDVGTWVRKAAMTSLMDLTLLLARSQPELIEAHTCERIMCCVAQQASEKIDRFRAHAASVFLTLLHFDSPPIPHVPHRGELEKLFPRSDVASVNWSAPSQAFPRITQLLGLPTYRYHVLLGLVVSLGGLTESTIRHSTQSLFEYMKGIQSDPQALGSFSGTLLQIFEDNLLNERVSVPLLKTLDHVLTHGCFDIFTTEEDHPFAVKLLALCKKEIKNSKDIQKLLSGIAVFCEMVQFPGDVRRQALLQLCLLLCHRFPLIRKTTASQVYETLLTYSDVVGADVLDEVVTVLSDTAWDAELAVVREQRNRLCDLLGVPRPQLVPQPGAC
Protein: tRNA-uridine aminocarboxypropyltransferase 1 (EC 2.5.1.25) (DTW domain-containing protein 1) (Q38CZ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- tRNA-uridine aminocarboxypropyltransferase
Sequence:
MKRARKVYSDDDEERCKKVVDFIRSLRFSIPLYRLREQNDRRLCPKCGRRRQYYCYDCLIVVHPESQPPPLKLPLNVYVILHPGETRGKSTSLAASTISPDLHIIDYPHVPTDLEPKATLLLYPSTDSTELESLENLDSCKNVVFIDGTWQQSKAMARDERLSKFRHVRIKAQTSLFWRFQNNDPTYLATVEAIYYFLREFISQNNKRRAGCQPPYYNGDVDDILYYYINQYIAVQQRYCKSELEYTTRHFDSYIIRCFSWDQLVAKPSESAPVVNHRTS
Protein: Calmodulin (CaM) (P02599)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Subcellular location: Contractile vacuole {ECO:0000269|PubMed:1629238}.
Interaction partners:
- AP-1 complex subunit gamma
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
- Nucleomorphin
- Ras GTPase-activating-like protein gapA
- Inositol 1,4,5-trisphosphate receptor-like protein A
Sequence:
MASQESLTEEQIAEFKEAFSLFDKDGDGSITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGNIDFPEFLTMMARKMQDTDTEEEIREAFKVFDKDGNGYISAAELRHVMTSLGEKLTNEEVDEMIREADLDGDGQVNYDEFVKMMIVRN
Protein: Actin (EC 3.6.4.-) (P53498)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MADEGEVSALVCDNGSGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFFNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILMERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATALSSSALEKTYELPDGQMITIGNERFRCPEVLFNPNMIGMEAVGIHDTTFNSIMKCDVDIRKDLYNNIVLSGGTTMFPGIADRMSKEITALAPSAMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKSEYDESGPSIVHRKCF