wanglab/gogpt-training-data huggingface dataset:
Protein: Dibenzofuran dioxygenase alpha subunit (G8GV17)
Organism: Rhodococcus sp. p52
Interaction partners:
Sequence:
MTSISERPVDVAAAGLHDLVKPDEGSVSRTVFVDEAIYRKELDRVFTKTWLFIGHESQLSEPGDYLTNFMGEDPVIATRGADGVIRVMLNSCAHRGMAVCSTDAGSSKFFRCPYHGWTYSNNGDLIGVPRADTVYHGELDKSRLGLKAVPRVENYKGFIFANWDEDAIPLVDYLGADQLWYLDLAFEAPLGGLEVIGPTMKFRIKANWKLAAENFAGDDYHVLYTHGSAFQIGFLPDYDTLGDYIAYFGHGHGMGDISKPGRAYQNDVGMAQFLGPEAIEYVNAVHERLKARVSPLQAEMHGLGQGNIFPNLSWIKFGVFHVFGLFQWHPRGPGEIEVWQTALFDRDAPQSVKDFARTQMSQENAAAGIFGQDDGENFEQITESARGVVSQTRDFNYAMGLGHEGEIHEEGYPGHLGPHYSEQNHRNFYRYWLELMTTPGEQK
Protein: Ubiquinol-cytochrome c reductase complex assembly factor 1 (Basic FGF-repressed Zic-binding protein) (bFGF-repressed Zic-binding protein) (bFZb) (Ubiquinol-cytochrome c reductase complex chaperone CBP3 homolog) (Q9NVA1)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Involved in cytochrome b translation and/or stability.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24385928}. Cytoplasmic vesicle {ECO:0000250}. Note=Cytoplasmic vesicular structures. {ECO:0000250}.
Interaction partners:
- Ubiquinol-cytochrome c reductase complex assembly factor 2
- Growth/differentiation factor 5
- Cytochrome b
- Complex III assembly factor LYRM7
- Mitochondrial chaperone BCS1
- Ubiquinol-cytochrome-c reductase complex assembly factor 3
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase assembly protein COX20
Sequence:
MALLVRVLRNQTSISQWVPVCSRLIPVSPTQGQGDRALSRTSQWPQMSQSRACGGSEQIPGIDIQLNRKYHTTRKLSTTKDSPQPVEEKVGAFTKIIEAMGFTGPLKYSKWKIKIAALRMYTSCVEKTDFEEFFLRCQMPDTFNSWFLITLLHVWMCLVRMKQEGRSGKYMCRIIVHFMWEDVQQRGRVMGVNPYILKKNMILMTNHFYAAILGYDEGILSDDHGLAAALWRTFFNRKCEDPRHLELLVEYVRKQIQYLDSMNGEDLLLTGEVSWRPLVEKNPQSILKPHSPTYNDEGL
Protein: Polarity protein BemA (D1MYR7)
Organism: Epichloe festucae
Interaction partners:
Sequence:
MTLIQALRRSIKGDKKEQHHTSLGTKSAVAIIPPKKVIRALYDYEAQSSQELSFSKGDFFHVIGRENDEDWYEACNPALPDARGLVPVSFFQALGRTERDSAQSDGGRPPTAKSPDHDSGYSEHSPHPIATAMPISHRSTKSTDIDNKIFAIVMYDFEAQRADELGATKGEQIIIIAQSTAEWFVAKPIARLGGPGLIPVSYVEIRSVKTREVVPNALEAVRKAGVPSVEEWKKMAASYKNSSITLGKFEGGAGPGGGGGQQGIEQGMDRMSLQTGRQSAQNGSQPRAGQNNNVSQSNQFAPSQSTPQLYAPTRAWIPRYCFAEDKYWFVIVAVLDDGRHWELSRYYEDFYDFQIALLTEFPAEAGNAGGQKRTLPYMPGPVSYVTDAITEGRLHNLDAYVKNLLNQPEYISRCNLVKQFFAPREGDYEVDPNETEQEYRLSQGSQQSAESPGNNGSRSNLNGNGYAGHSATPRQTSNSQQGMPSQQQGGQAPQMKVKMYFNGDLIAIRVPSAADYQQLCDKVRERLKISQDDQLQLFYKDEPTGNKPSLMSDGDLDFALQRNEKLVLYVEVV
Protein: Semaphorin-6A precursor (Zgc:66106) (Q6P7E1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRAQALLLYLTLLQTAGAAFPEDTEPISIAHGNYTKQYPVFVGHKPGRNNTQRHKLDIQLIVIMNRTLYVAARDHIYTLDMETSSTEEIFFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLQQSEDSLFVCGTNAFNPSCRTYRMDSLDALGEEISGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAVDYEDFIYFFFREIAMEYNSMGKVVFPRVARVCKSDSGGSQRVLEKQWTSFLKTRLNCSIPGDSHFYFNILQAVTDVIHISGRDVVMATFSTPYNSIPGSAVCAYDMSEIALAFTGRFKEQKSPDSTWTPVPEERVPKPRPGVCAGSSSVEKFKVSSEFPDDSLSFIKAHPLMEEAVPAIANRPWFLKTMVRYRLTRIAVDNAAGPHSNHTVVFLGSERGIVLKFLAKIRSGALNDSLFLEELNVYNAEKCSIDGVEDKRIISMQIDSRSRSLFVAFSSCVVRVPLARCQRHGKCKKSCIASRDPYCGWVSEGACREITSDAKWPFEQDVEQGNTDGLGDCQNSFVALNGRVSSPSVSPAVVSVPLGRGRVLKDHQEPLVSGSSETQQESAGVIRETFHRDRDQMVPVTLLAIAVILAFSMGAIFSGILVYCVCDHHRRREFPMSGRKEKDCAASRRGSMNSVTKLTGLFETQAKDGRAEQMLTPLMNGRLVNGRMLIKAEQHLDLSALPTPESTPLQPRRKPSRGSREWERNQNLINACTKELSSMGSPVIPTELPLRASPGHISSVVVLPLPPHQSYQHEYVEHPQQRPDDPAATLEFQTLRSPCRGAEEEVVPPRVPQREASLVPPAVPQMGKRLDMHSSMYARGFPMSSGLKKQHNTNSSNSSHMSRNHSFRVETPPPAPQRVDSMQVSSPGLGLSHHPSLSSFGSLSRCGARQMKPDVPPKPSAVSYCSKATSGDSCT
Protein: Fructose-6-phosphate aldolase 1 (EC 4.1.2.-) (Fructose-6-phosphate aldolase A) (FSAA) (P78055)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Arabinose 5-phosphate isomerase KdsD
- Probable dehydratase YbiW
- Putative pyruvate formate-lyase 3-activating enzyme
Sequence:
MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDALKLRSIIADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI
Protein: Putative tRNA pseudouridine synthase C16C4.06c (EC 5.4.99.-) (O74451)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
- tRNA pseudouridine synthase 4
- Multisubstrate pseudouridine synthase 7
- tRNA
- tRNA
- tRNA-specific adenosine deaminase subunit tad2
- tRNA
- tRNA
- tRNA-dihydrouridine
- tRNA
- tRNA-dihydrouridine
Sequence:
MHSLLRPSRFSANQSVLCLLQRHRVFFSSISVKPRKRMVYCVVSYRGTGFAGLQYNANVKTIQDTLFQAFARVGAVVQVNADSPKKIRMCSAARTDKGVHAIVNVLGLKVLDNQPLPHVVNLVNDILPPCIRVWKMARTFNSFSPHTVCDSRVYEYWLPVSSLLTPRPCTLEAYVIAKASEKAFPINETLSHLANLSKQDCVANSLSEPFRLSKPKLDFLKHACTMFRGTHRFHSYTTEKGFSDASSRRFLLDVRVDNLHIDKLNRQWVKLIFHGQSFMKHQIRKMVGILIHLTRTGWNAQVLLNTFNNSYRIRIPRAPAEFLLLNQPIFQAFNKKCSRFDHEPVEWSCAQKGIDQFAHSFLRTPMFDCFISSESFQSFFILQKQFQLFQDLALLTSFDFLEPSSRRDILGEK
Protein: Probable methyltransferase PMT9 (EC 2.1.1.-) (Q8VZV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar-sorting receptor 5
- Transmembrane 9 superfamily member 9
- Probable pectinesterase/pectinesterase inhibitor 61
Sequence:
MKHFRTERVRATPKLFTYVLVGFIALLGLTCLYYGSSFAPGSRKSDEFDGSNNRVRTGIGSLRNRDIVLAVSRFEVPKSVPICDSRHSELIPCLDRNLHYQLKLKLNLSLMEHYEHHCPPSERRFNCLVPPPVGYKIPLRWPVSRDEVWKANIPHTHLAQEKSDQNWMVVNGDKINFPGGGTHFHNGADKYIVSLAQMLKFPGDKLNNGGSIRNVLDVGCGVASFGAYLLSHDIIAMSLAPNDVHQNQIQFALERGIPSTLGVLGTKRLPYPSRSFELAHCSRCRIDWLQRDGILLLELDRLLRPGGYFVYSSPEAYAHDPENRKIGNAMHDLFKRMCWKVVAKRDQSVIWGKPISNSCYLKRDPGVLPPLCPSGDDPDATWNVSMKACISPYSVRMHKERWSGLVPWPRRLTAPPPRLEEIGVTPEQFREDTETWRLRVIEYWKLLKPMVQKNSIRNVMDMSSNLGGFAAALNDKDVWVMNVMPVQSSPRMKIIYDRGLIGATHDWCEAFDTYPRTFDLIHAWNTFTETQARGCSFEDLLIEMDRILRPEGFVIIRDTTDNISYIKKYLTLLKWDKWSTETTPKGDPLSTKDEIVLIARKKLWSLPAISVS
Protein: RNA polymerase sigma factor sigB (Sigma factor B) (Sigma-B) (Protein ABERRANT CHLOROPLAST 1) (RNA polymerase sigma factor sig1) (Atsig1) (Sigma factor 1) (RNA polymerase sigma factor sig2) (Atsig2) (Sigma factor 2) (RNA polymerase sigma factor sigA) (Sigma factor A) (Sigma-A) (O22056)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the transition of plastids into chloroplasts by coordinating nuclear and chloroplastic genomes under light conditions. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Promotes the biosynthesis of plastid-encoded tRNAs (e.g. trnE-UUC and trnV-UAC).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:12602869}.
Interaction partners:
- Large ribosomal subunit protein bL28c
- Putative defensin-like protein 263
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein uL3c
- Large ribosomal subunit protein uL6c
- RNA-binding
- 50S ribosomal protein L33
- AT3G20230 protein
- Pentatricopeptide repeat-containing protein At3g26540
Sequence:
MSSCLLPQFKCPPDSFSIHFRTSFCAPKHNKGSVFFQPQCAVSTSPALLTSMLDVAKLRLPSFDTDSDSLISDRQWTYTRPDGPSTEAKYLEALASETLLTSDEAVVVAAAAEAVALARAAVKVAKDATLFKNSNNTNLLTSSTADKRSKWDQFTEKERAGILGHLAVSDNGIVSDKITASASNKESIGDLESEKQEEVELLEEQPSVSLAVRSTRQTERKARRAKGLEKTASGIPSVKTGSSPKKKRLVAQEVDHNDPLRYLRMTTSSSKLLTVREEHELSAGIQDLLKLERLQTELTERSGRQPTFAQWASAAGVDQKSLRQRIHHGTLCKDKMIKSNIRLVISIAKNYQGAGMNLQDLVQEGCRGLVRGAEKFDATKGFKFSTYAHWWIKQAVRKSLSDQSRMIRLPFHMVEATYRVKEARKQLYSETGKHPKNEEIAEATGLSMKRLMAVLLSPKPPRSLDQKIGMNQNLKPSEVIADPEAVTSEDILIKEFMRQDLDKVLDSLGTREKQVIRWRFGMEDGRMKTLQEIGEMMGVSRERVRQIESSAFRKLKNKKRNNHLQQYLVAQS
Protein: GM06978p (Q95S72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMPSPSGKSNSSTGSTATSSSSSASGQSGEEGYQRFSNIYEQVQPAPSTQPQEDATATPFQRSAPIYWTLQNRRSQPRPQPAGNVTCRDDLYATPIRRADRLPRPVAAAAATAAEGNRSNISPIVPRNRSGAFLTSTPTRSGEGERDSENTQLPPMKQPSRNWTDDAPERLNTCADRIGQSKTTLMDFKKLLLAKSAKASPVQRKVSAVELLKKPAQATATPPVVKPSGPGQKVASAGSKPTINTSLKLLDLSGSPKTFANRRMLRQGQFGSPSKTFAPKMRGPVNMVAAAAAPPRTDIMSTTIPEANSEEDHSNTSGGSRASSEAGETVPSSFDLKRNFFLQTEENNFMRGELKPSFARSNGAAGGGSTEGVNKYVAAPVANPPLPSFETAL
Protein: Glucosaminyl (N-acetyl) transferase 2 (Q6T5E0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MPPSMRHFFIVSVTTVIVFIVLYVLSFGGDQSYQKLNISDSAMLAQVCTSFTNGKNSFLWRNKLMIHEKPSCTEYVTQSHYITAPLSQEEVEFPLAYVMVIHHNFDTFARLFRAIFMPQNVYCVHVDEKATAEFKGAVEQLVNCFPNAFLASKTEPVVYGGISRLQADLNCIRDLSTSEVPWKYAINTCGQDFPLKTNKEIVQYLKGLKGKNLTPGVLPPAHAIGRTRYVHREHLSKEFSYVIRTAALKPPPPHNLTIYFGSAYVALSREFANFVLHDPRAVDLLHWSKDTFSPDEHFWVTLNRIPGVPGAMPNASWTGNLRAVKWKDMESQNGACHGHYVHDICIYGNGDLQWLINSQSLFANKFEVNTYPLTVECLELRLRERTLNQSDIALQPSWHF
Protein: Protein shisa-2 homolog (Transmembrane protein 46) (Q6UWI4)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MWGARRSSVSSSWNAASLLQLLLAALLAAGARASGEYCHGWLDAQGVWRIGFQCPERFDGGDATICCGSCALRYCCSSAEARLDQGGCDNDRQQGAGEPGRADKDGPDGSAVPIYVPFLIVGSVFVAFIILGSLVAACCCRCLRPKQDPQQSRAPGGNRLMETIPMIPSASTSRGSSSRQSSTAASSSSSANSGARAPPTRSQTNCCLPEGTMNNVYVNMPTNFSVLNCQQATQIVPHQGQYLHPPYVGYTVQHDSVPMTAVPPFMDGLQPGYRQIQSPFPHTNSEQKMYPAVTV
Protein: Protein YchN (P0AB52)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative HNH nuclease YajD
- Sulfurtransferase TusD
Sequence:
MQKIVIVANGAPYGSESLFNSLRLAIALREQESNLDLRLFLMSDAVTAGLRGQKPGEGYNIQQMLEILTAQNVPVKLCKTCTDGRGISTLPLIDGVEIGTLVELAQWTLSADKVLTF
Protein: Ras guanine nucleotide exchange factor V (RasGEF domain-containing protein V) (Q55FD8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Formin-I
- Formin-J
Sequence:
MGNINSICLNNNGKYRIDSISCSLEGCKLNSKELVENMVALVDKYPLTQLLIIRECKLKQIPVNITNLSNLSELILSDNKLSQLPWSLPPPFKPNTLLSMASITNENLVRLDLSNNRFTEFPSSVFVLPNLKQLILCNNQLTNMNVTLCGGTSNNNGAHQPHIACQLEELKLSNNNFTIFPSIIGDQLTTLKSLDLSGNTITSLPNSFSNLVSLTSLNLKSNKFTCFPPSLCTLDKLVHLNLSCNQILVSPSDHTLGVSLLPSLEKLELQHNRFAHFPMDILEIVSLRVLKLQDNDIDKIPDKIGNLLNLNELFLSENKITQLPSTIGELINLRKLYLEYNKIGSLPQEFSKLSKLNILILHNNDLKFVPDQLHSLSQLLRLSLDENQLSSSDQKLIKSEGSLALIKRKNKLNYGSTMNGTGTTSSSGSASTSTHGSINKTTDILLSSVTLNNSILNQINNNNNNNNNNNNNNNNNNNSSNNNSGTNSLSSTPNGTGKSKKKLTHLTISRSLFRGNSSNLESEKEDFINKKQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLGSTASPSTASPITSHITVNSTVLDFEDDIQKMQLGLEALSNLETSIGSNNSGGGDSMNGSGGNINNSGGSGSGCGTISGSTTKQRRGSVFLPPTNAFKLSPNVVSSSYNTLPASVMSGLLQQQNLENGGVGSGSGSGSPIISANSICNSNSSSSNSLLKPPIINTTNLSTSPNLLSQSSTSFLNLPPLNQSSTNSFLPPQHQHHHHHSNLSQSLSINNLAHRLPTSLSSSSLSSNNTYDSLQFQQQQQHHHHNHNNHQNSNQPLATIVPSFSKFKNSFDQLLEEQDFSKKKRETLQKLSKEQKWNLLLQYRNSTLNMLNMKEHSNNSNNNQSIKNSTIIASTTTTTTTNGESLDGSSIQQQITKNSNFQSSRFYIDNLTSKTDISLVKEVHDFLKESGPEVSIFIGMGGIESLLGILQFNLDNAQLQFDEEKVGYCLLCLKILVECTAKSVITTNNSLNLVTMFLTSASKYIIDIIIDIYDELLRLQVIGVSVVLDSLINFQKVKGLSSPYVPLVALLRNPIIEMPTKTTVFKIINFLIYSFSVLEERFSVICSLLKVGILEVIGMFRALPHTSYSLRFELDLFEEVLDSDESELVKKIGRKEVLKRMSNEDNDLSKQSSKQSMDFVRVVMVSAGYGDLKIDLDERTSYANVIDFIQSNYQIKYSIDRYGLFVPAIGSLVLDGSILQSSGSQSRWVDPSKSLIDNGLSNEIVEFKMKPMQIQVLQSVVVVVATNHQKEDIIKEFTIDPQLKCFEIVQYLRTRLDSSSPAFQRKISVLTEDEDEDYESDIYGVYCFSSLESYDQGSWYPLNSRFLDFNPTNTPTIIDVKLMERPLRVLFSGTEKLMKFNPYVPVSELIKEIKNEIHLKINIEDYGISYVPNVSSSNLSSLIIEETWLDPTKTLLDHNDMKCSVVQFKFKPRTVSVMVLVESGIEIPTTDTPYQFVNTNSISEIIEKICTPHQLNPLSHSLYISDCQGQKIKLLSRQNCLRDQQVNNGDHLIITSKQKDLPSDFNVWDEPNDSSETITYSKDRRVSSVTLNKLIEKLTSPEYTQDSEMKTIFLSSYRSIITPSVLLSKLMERHTIPTLVDKERGKLIQRKTRLLIKSWLELETTKNREEVITLLVQNMPAQSIEDDGLKELTELFVDLSTKSYSSILPIVIGELPKCKIPKIIDSYVTFADMDEIEIARQLSLLTFPLYSRIETSELLNQRWSKPGGGPNIMSVVGLFNKISNWVSFTIVNQPKLRDRAVVYGKMVKIANAFYELRNYHLLMAIISGLNASPVLRLKYTKGKLSKNLKDNLDTLEELMSTQSSMKNYRADLAAASPPAIPFMGFHLSDLVFIDEGNQQLCDSRINFKKLEMYKKTIATLQNFSLFPYQFTPVPIIQNYFLDYKIVADKPIYEMSLSAEPRNAERYDIQ
Protein: Transcription factor bHLH23 (Basic helix-loop-helix protein 23) (AtbHLH23) (bHLH 23) (Transcription factor EN 107) (bHLH transcription factor bHLH023) (Q9SVU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MTWKPKMLILSHDLISPEKYIMGEDDIVELLGKSSQVVTSSQTQTPSCDPPLILRGSGSGDGEGNGPLPQPPPPLYHQQSLFIQEDEMASWLHQPNRQDYLYSQLLYSGVASTHPQSLASLEPPPPPRAQYILAADRPTGHILAERRAENFMNISRQRGNIFLGGVEAVPSNSTLLSSATESIPATHGTESRATVTGGVSRTFAVPGLGPRGKAVAIETAGTQSWGLCKAETEPVQRQPATETDITDERKRKTREETNVENQGTEEARDSTSSKRSRAAIMHKLSERRRRQKINEMMKALQELLPRCTKTDRSSMLDDVIEYVKSLQSQIQMFSMGHVMIPPMMYAGNIQQQYMPHMAMGMNRPPAFIPFPRQAHMAEGVGPVDLFRENEETEQETMSLLLREDKRTKQKMFS
Protein: Dehydrogenase/reductase SDR family member 9 (EC 1.1.1.209) (EC 1.1.1.53) (3-alpha hydroxysteroid dehydrogenase) (3-alpha-HSD) (NADP-dependent retinol dehydrogenase/reductase) (RDH-E2) (RDHL) (Retinol dehydrogenase 15) (EC 1.1.1.105) (Short chain dehydrogenase/reductase family 9C member 4) (Short-chain dehydrogenase/reductase retSDR8) (Tracheobronchial epithelial cell-specific retinol dehydrogenase) (RDH-TBE) (Q9BPW9)
Organism: Homo sapiens (Human)
Function: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. Also plays a role in the biosynthesis of retinoic acid from retinaldehyde. Can utilize both NADH and NADPH.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:11294878, ECO:0000269|PubMed:11304534, ECO:0000269|PubMed:12618084}. Endoplasmic reticulum membrane {ECO:0000305}. Note=Associated with microsomal membranes.
Interaction partners:
- Short-chain dehydrogenase/reductase 3
- Dehydrogenase/reductase SDR family member 4
- Aldo-keto reductase family 1 member C4
- Lecithin retinol acyltransferase
- Retinaldehyde dehydrogenase 3
- Cytochrome P450 26A1
- Aldehyde dehydrogenase 1A1
- Aldo-keto reductase family 1 member C2
- Retinal dehydrogenase 2
- Aldo-keto reductase family 1 member C3
Sequence:
MLFWVLGLLILCGFLWTRKGKLKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLKQKAELANPKAV
Protein: ATP synthase subunit H, mitochondrial (O59673)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit f
- ATP synthase subunit 4
- ATP synthase subunit J
- Uncharacterized protein C3B9.05
- ATP synthase subunit e, mitochondrial
- V-type proton ATPase subunit c
- V-type proton ATPase subunit c'
Sequence:
MSRILKSLSRSYSTTSPRLYVDVVQGLYISSLKSYKPKAVPSETAAEVKEWSMPSAPTAPKYDVDFTSALNSYKYEGETIPTKAAGESNKFDFLESYENEKEH
Protein: Class II, major histocompatibility complex, transactivator (A0A0G2JVN3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTCLSFSLLPGHTLCATMELGSPEGSYLELLNSDADPLHLYHLYDQMDLAGEEEIELNSETDMDTINCDQFSKLLQDMEMDEETREAYANIAELDQYVFQDTQLEGLSKDLFIQHIGPEEGFGENVEGPAESGEKPQKRRFPEEHAMDSKHRKLVPPSRTSLNYLDLPAGHIQIFTTLPQGLWQISGVGTGLSSVLVYHGEMPQVNQLLSSSSPTVPSLPESPDRPGSTSPFAPSTADLPGMPEPALTSRVNETEDTTPPSPCQEDPEPSIKLPKWPESVERFQHSLQDKYQALPGSPSGPLVAMELVRARLERGSNKSQERELATPDWTERQLAHGGLAEVLRVVGDSRRSRETQVVAVLGKAGQGKSHWARTVSHIWAQGQLPQYDFVFYVPCQCLDRPGDTYHLRDLLCPPNLQPLAMDDEVIDHIVRQPDRVLLILDAFEELEAQDSLLHGPCGPLSPEPCSLRGLLAGLFQRKLLRGCTLLLTARPRGRLAQSLSKADAIFEVPSFSTKQAQIYMRHYFENSGTAGSHDKALGLLEGQPFLLTHSHSPVLCSAVCQLSKALLDQGAEAQLPCTLTGLYVGLLGPAAQNSPPGALVELAKLAWELGRRHQSTLQETQFPSVEVKTWAVAQGLMQQTTEAQLAFSSFLLQCFLGAVWLAQCNEMKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLVFQPRAHCLGALVEPAMAAVADRKRKVLTRYLKRLKLGTLRAGRLLELLHCAHETQEPGIWKHVSHQLPGHLSFLGTRLTAPDVYVLGRALETASQDFSLDLRQTGIEPSRLGDLVGLSCVTSFRASLSDTMALWESLQHQGETQLLQAAEEKFTIEPFKAKSPKDVEDLDSLVQTQRLRNPSADAAKDLPAIRDLKKLEFALGPVLGPQAFPTLAKILPAFSSLQHLDLDSLSENKIGDKGVSKLSATFPQLKALETLNLSQNSITDVGACKLAEALPALAKSLLRLSLYNNCICDEGAKSLARVLPDMVSLRVMDVQFNKFTAVGAQQLTSSLQKCPQVETLAMWTPTIPFGVQEHLQQLDARISLR
Protein: Zinc finger protein 503 (Zinc finger protein Nolz-1) (Q7TMA2)
Organism: Mus musculus (Mouse)
Function: May function as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSTAPSLSALRSSKHSGGGGGGGGGGGSGGGSADPAWTSALSGNCSGHGPGSSPAGSTKPFVHAVPPSDPLRQANRLPIKVLKMLTARTGHILHPEYLQPLPSTPVSPIELDAKKSPLALLAQTCSQIGKPDPSPSSKLSSVASNGGGAGGAGNGAGGDKDAKSGPLKLSDIGVEDKSSFKPYSKPGSDKKEPGGGGGGGGGGGGGGGVAAEKSGFRVPSATCQPFTPRTGSPSSSASACSPGGMLPSAGGGPEGKDDKKDPEAGGGGSSKGSGGASADGVPAGLGHGRISCGGGINVDVNQHSEGGPGGKALGSDCGGSSSSSSGSGPSAPTSSSVLGSGLVAPVSPYKPGQTVFPLPPAGMTYPGSLAGAYAGYPPQFLPHGVALDPTKPGSLVGAQLAAAAAGSLGCSKPAGSSPLAGASPPSVMTASLCRDPYCLSYHCASHLAGAAAASASCAHDPAAAAAALKSGYPLVYPTHPLHGVHSSLTAAAAAGATPPSLAGHPLYPYGFMLPNDPLPHICNWVSANGPCDKRFATSEELLSHLRTHTAFPGTDKLLSGYPSSSSLASAAAAAMACHMHIPTSGAPGSPGTLALRSPHHALGLSSRYHPYSKSPLPTPGAPVPVPAATGPYYSPYALYGQRLTTASALGYQ
Protein: KAT8 regulatory NSL complex subunit 3 (NSL complex protein NSL3) (Non-specific lethal 3 homolog) (Serum inhibited-related protein) (Testis development protein PRTD) (Q9P2N6)
Organism: Homo sapiens (Human)
Function: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:20018852}. Mitochondrion {ECO:0000269|PubMed:27768893}.
Interaction partners:
- Microspherule protein 1
- KAT8 regulatory NSL complex subunit 2
- PHD finger protein 20
- KAT8 regulatory NSL complex subunit 1
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- WD repeat-containing protein 5
- Histone acetyltransferase KAT8
- Host cell factor 1
- PHD finger protein 20-like protein 1
- MSL complex subunit 3
Sequence:
MAHRGGERDFQTSARRMGTSLLFQLSVHERELDLVFLDHSYAKPWSAHPDASSARPTRMLFVTPRRQHESTIESDVPIDVETVTSTPMPLYDNQKARSVMNECERHVIFARTDADAPPPPEDWEEHVNRTGWTMAQNKLFNKILKALQSDRLARLANEGACNEPVLRRVAVDKCARRVRQALASVSWDTKLIQWLHTTLVETLSLPMLAAYLDALQTLKGKIPTLIDRMLVSSNTKTGAAGAEALSLLLKRPWDPAVGVLSHNKPSKLPGSPLILIASSGPSSSVFPTSRRHRFWQSQLSCLGKVIPVATHLLNNGSGVGVLQCLEHMIGAVRSKVLEIHSHFPHKPIILIGWNTGALVACHVSVMEYVTAVVCLGFPLLTVDGPRGDVDDPLLDMKTPVLFVIGQNSLQCHPEAMEDFREKIRAENSLVVVGGADDNLRISKAKKKSEGLTQSMVDRCIQDEIVDFLTGVLTRAEGHMGSEPRDQDAEKKKKPRDVARRDLAFEVPERGSRPASPAAKLPASPSGSEDLSSVSSSPTSSPKTKVTTVTSAQKSSQIGSSQLLKRHVQRTEAVLTHKQAQAQFAAFLKQNMLVRKALPPGTSSCLFVPISSEPPEEGEKEDLRVQLKRHHPSSPLPGSKTSKRPKIKVSLISQGDTAGGPCAPSQGSAPEAAGGKPITMTLGQASAGAKELTGLLTTAKSSSSEGGVSASPVPSVVSSSTAPSALHTLQSRLVATSPGSSLPGATSASSLLQGLSFSLQDISSKTSGLPANPSPGPAPQATSVKLPTPMQSLGAITTGTSTIVRTIPVATTLSSLGATPGGKPTAIHQLLTNGGLAKLASSLPGLAQISNQASGLKVPTTITLTLRGQPSRITTLSPMGSGAAPSEESSSQVLPSSSQRLPPAP
Protein: Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor 4) (p40-phox) (p40phox) (P97369)
Organism: Mus musculus (Mouse)
Function: Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15080}. Endosome membrane {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15080}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15080}. Membrane {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15080}. Note=Translocates to the membrane upon activation by phorbol myristate acetate (PMA). {ECO:0000250|UniProtKB:Q15080}.
Interaction partners:
- Neutrophil cytosol factor 1
- NADPH oxidase 2
- Ras-related C3 botulinum toxin substrate 2
- NADPH oxidase activator 1
- Neutrophil cytosol factor 2
- Cytochrome b-245 light chain
- NADPH oxidase 1
- NADPH oxidase organizer 1
- Ras-related C3 botulinum toxin substrate 1
- RAC-alpha serine/threonine-protein kinase
Sequence:
MALAQQLRSESDFEQLPDDVAVSANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYRQFYALQSKLEERFGPESKNSPFTCSLPTLPAKVYMGAKQEIAETRIPALNAYMKNLLSLPVCVLMDPDVRIFFYQSAYDAEQVPQALRRLRPRTRKIKGVSPQGAIMDRMEAPRAEALFDFTGNSKLELSFKAGDVIFLLSKINKDWLEGTSQGATGIFPGSFVKILKDFPEDEDTTNWLRCYFYEDTGKTIKDIAVEEDLSSTPLFKDLLALMRREFQREDIALSYQDAEGDLVRLLSDEDVGLMVKQARGLPSQKRLFPWKLHVTQKDNYSVYNTVP
Protein: Protein-tyrosine-phosphatase (Q9XVE7)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein F15G9.1
- ANK_REP_REGION domain-containing protein
- Myosin, essential light chain
Sequence:
MSRNVGVLGQMSEINDHLYLSGAGVLKPDKIKQRKINMIVNATTEEPSTYMQGVDTMKIRIEDHPYARLSEHFDVVADKIRNVKERGGKTLVHCMAGVSRSASLVMIYLVKHEHMTLRQAYHYVKAARPIIRPNVGFWKQMVDYEKRLRGTASVKMVQTPECDMPIPDVYADDIRRMQINREISRHSLPSAQSSASKQRAFSASTYRPSVSSASSLATSSLRRAYSPSSLPASSLALTTSYSLFSPAPTRKPRQSLFSMYSTSPRHNFFSAF
Protein: Prolyl endopeptidase (EC 3.4.21.-) (Q961N7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPSTLSAKLAYPVARKDESVAEDFHGTQIKDVYRWLEDPDSTETEEFVNAQNSISRPFLENGEEWKKLNTKLTKLWNYPKYGCPMRYGNYYYYFMNTGLQNQSVMYQQKSLGDESESKVFLDPNTLSEDGTIALTQKAFSEDGKYMAYGLSESGSDWIKILIRDAETGKDLSEVLEKVKFSEISWTKDNKGFFYGRYPDQDGKTDGSETKQNENQKLYYHRVGESQDKDTLVVEFPEEPSWRIQSTVSDCGKYLILAIVKDCRDNIVFYADLTPGAEITSKLNVKKIVEKFEADYDYITNEGSKIFFRTNKNAPNYQVIAIDFNNSAEDKWETLIAEHKSDVLDWVKCVDNDKLLVCYIRDVKSVLQVNSLKDGTLLREFDLDIGTIVGTSGEKKYSEIFYNFSSFLNPGSIYRYDFKTPDKSPSVFREIKLNLEGFRREDYAVEQIFYKSKDGTKVPMFIIRKKRDSVEPRPCLLYGYGGFNISMLPSFGLSGLMFIDTFDGVLAYPNLRGGGEYGEKWHNGGRLLNKQNVFDDFQAAAEYLIENKYTTKDRLAIQGGSNGGLLVGSCINQRPDLFGAAVAQVGVMDMLRFHKFTIGHAWCSDYGNPSEKEHFDNLYKFSPLHNVHTPKGAKRNTHRL
Protein: Uncharacterized HTH-type transcriptional regulator Rv0474 (P9WMH9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein TB16.3
- Conserved protein
- Cyclase
- Heparin-binding hemagglutinin
- Uncharacterized protein Rv0476
Sequence:
MSSEEKLAAKVSTKASDVASDIGSFIRSQRETAHVSMRQLAERSGVSNPYLSQVERGLRKPSADVLSQIAKALRVSAEVLYVRAGILEPSETSQVRDAIITDTAITERQKQILLDIYASFTHQNEATREECPSDPTPTDD