wanglab/gogpt-training-data huggingface dataset:
Protein: DH domain-containing protein (Putative GDP-GTP exchange factor) (Rho guanine nucleotide exchange factor FGD-1) (G5ECM5)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSLVQLPSQPSSAFQLDFDAVRNFQNVPPVDLEGGTLIDATEEEEIDPVDGCTVRVFTYRILSADEMEELTKTVRQKIKFDCTQTMRSLKMIGSEANVVEKSQRISGDIKGMKPIEFSNNSKQICLDQHSLQLDPNDEQDQQISRVLNQVPNTFMSLLSREKDMFVKLYPELFEKMRTESSLIPSTTTEIITNPDGSTTTRVKSSKSYSSHFSRQETYVNGVKKMSKSKFRAFVEYKGPDGGFQVKLSDGDEFELSEDEQEDDDTSLSQSCYSEIDSESDITGPSPKTDLDKRYQKAWYAAKELVDSEQRYVDKLKLLGDTFRNRLIKEELITNDKITRLLANVSSLYQFHNTHFLPQLLESIRDWHTTKRIANVVRKQAPFLKMYSEYTNNYDRATKLFEELKKKKKFADVVKEIEKQAECEGLPLGHHLICPVQRVMRYQLLLQEYKKHLQPSDVDFDDTTVALELVLQAAAHANEMMKKLDRFGKVIEVQEQLGNSISLVSPGRELLKSGSVQKISSTTEKTEERFIFLFNDLVILASERKMIGVSKYKLRAVFSASHMQVCEGDNLEREHSFYLRGSDGTGPKRCVELFTPTQKEKNDWVDSIFSIIDEAKAHSLTFTSSSRSSISENNNNSIESKHCADCDIEFGFLSRGSKCVKCSRRLCKKCFGRRRNESKKHRICDTCTKNMDLDGIPRSFSTQSNMRRNLLQLPAKGSGVLHSSQIRFRGSLGKLLDRFMVVRDDFCMYTYSSEEDICALAMLPLPGCEVKMCGEKFTFSVRVGARRMYTMTAEDEQTQMKWLAILDLAANAHLKNQRNSGSEQSE
Protein: NADH-quinone oxidoreductase subunit L (EC 7.1.1.-) (NADH dehydrogenase I subunit L) (NDH-1 subunit L) (P9WIW1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit M
Sequence:
MTTSLGTHYTWLLVALPLAGAAILLFGGRRTDAWGHLLGCAAALAAFGVGAMLLADMLGRDGLERAIHQQVFTWIPAGGLQVDFGLQIDQLSMCFVLLISGVGSLIHIYSVGYMAEDPDRRRFFGYLNLFLASMLLLVVADNYVLLYVGWEGVGLASYLLIGFWYHKPSAATAAKKAFVMNRVGDAGLAVGMFLTFSTFGTLSYAGVFAGVPAASRAVLTAIGLLMLLGACAKSAQVPLQAWLGDAMEGPTPVSALIHAATMVTAGVYLIVRSGPLYNLAPTAQLAVVIVGAVTLLFGAIIGCAKDDIKRALAASTISQIGYMVLAAGLGPAGYAFAIMHLLTHGFFKAGLFLGSGAVIHAMHEEQDMRRYGGLRAALPVTFATFGLAYLAIIGVPPFAGFFSKDAIIEAALGAGGIRGSLLGGAALLGAGVTAFYMTRVMLMTFFGEKRWTPGAHPHEAPAVMTWPMILLAVGSVFSGGLLAVGGTLRHWLQPVVGSHEEATHALPTWVATTLALGVVAVGIAVAYRMYGTAPIPRVAPVRVSALTAAARADLYGDAFNEEVFMRPGAQLTNAVVAVDDAGVDGSVNALATLVSQTSNRLRQMQTGFARNYALSMLVGAVLVAAALLVVQLW
Protein: Histidine biosynthesis trifunctional protein [Includes: Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphohydrolase (EC 3.6.1.31); Histidinol dehydrogenase (HDH) (EC 1.1.1.23)] (A0A1D8PKY7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Imidazole glycerol phosphate synthase hisHF
- Imidazoleglycerol-phosphate dehydratase
- 1-
- ATP phosphoribosyltransferase
- histidinol-phosphate transaminase
- phosphoserine phosphatase
- Polynucleotide 3'-phosphatase
- Histidinol-phosphatase
- Adenylosuccinate synthetase
- Protein ARG5,6
Sequence:
MIFPILPVISSPEDKQSIDEFSLVGQVLFPIESVSPKKHFIHQFPHDLDIFVNAIDNATTDQIVELLNVGIKQVFVNEKQYHDAIEAGSPSSRFVVAVDVPSTELLTSEASFVTSKPFSESDLKKYNANENRVIYIESNFTQDGAIELAKNYVPVIPSTKLTVKREEENKISISAVFVSTLTTDRPDGLYTTLITTPSPSYTALGIVYSSKDSIIAAIEEKVGVYQSRKRRDELWYKGKTSGATQKLVKLSKDCDSHVIQFMVEPRTGYGFCHRETKFTCFGDDIADSPARGLPKLDSTLQDRLENAPEVSYTKRLFDDEKLLIAKLKEELDELIEAKSKEEIAWECADLVYFAMVWCIKHGVRLADIEKNLDVKSLKVSRRKGDAKPQYQEAPVNSSYKLEIVSVDDAAAVERAMTRPVQKTADIMKLVLPIIEKVKSDGDKALIELTSKFDGVKLDAPVLQAPFPADLMDISEEMKAAIDLSMQNIEKFHAAQLPKEKVMTVETSPGVYCSRFAKPIENVGLYVPGGTAVLPSTAMMLGVPAKVAGCKNIIVASPPSRATGKLTPEVVYVAHKLGAKCIVMAGGAQAVTAMAYGTESVLKCDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADSNADADFVASDLLSQAEHGVDSQVILIGVGLSDEKLNEFQAAVERQAKVLPRKDIVAKCLAHSYILLAKTYKEAFDLSNQYAPEHLILQIDDAPSYVPDSIENAGSVFVGALSPESCGDYSSGTNHTLPTYGYARQYSGVNTATFQKFITSQEVTEKGLQNIGKAVMELARVEGLEAHRRAVEIRMERMAETK
Protein: Protein virB4 (P0A3W0)
Organism: Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Function: A possible function of virB4 might be to provide the energy, via hydrolysis of ATP, for translocation of virulence proteins of the transfer of a T-DNA-protein complex across the agrobacterium membrane.
Interaction partners:
Sequence:
MLGASGTTERSGEIYLPYIGHLSDHIVLLEDGSIMSIARIDGVAFELEEIEMRNARCRAFNTLLRNIADDHVSIYAHLVRHADVPSSAPRHFRSVFAASLNEAFEQRVLSGQLLRNDHFLTLIVYPQAALGKVKRRFTKLSGKRENDLAGQIRNMEDLWHVVAGSLKAYGLHRLGIREKQGVLFTEIGEALRLIMTGRFTPVPVVSGSLGASIYTDRVICGKRGLEIRTPKDSYVGSIYSFREYPAKTRPGMLNALLSLDFPLVLTQSFSFLTRPQAHAKLSLKSSQMLSSGDKAVTQIGKLSEAEDALASNEFVMGSHHLSLCVYADDLNSLGDRGARARTRMADAGAVVVQEGIGMEAAYWSQLPGNFKWRTRPGAITSRNFAGFVSFENFPEGASSGHWGTAIARFRTNGGTPFDYIPHEHDVGMTAIFGPIGRGKTTLMMFVLAMLEQSMVDRAGTVVFFDKDRGGELLVRATGGTYLALRRGTPSGLAPLRGLENTAASHDFLREWIVALIESDGRGGISPEENRRLVRGIHRQLSFDPQMRSIAGLREFLLHGPAEGAGARLQRWCRGHALGWAFDGEVDEVKLDPSITGFDMTHLLEYEEVCAPAAAYLLHRIGAMIDGRRFVMSCDEFRAYLLNPKFSAVVDKFLLTVRKNNGMLILATQQPEHVLESPLGASLVAQCMTKIFYPSPTADRSAYIDGLKCTEKEFQAIREDMTVGSRKFLLKRESGSVICEFDLRDMREYVAVLSGRANTVRFAARLREAQEGNSSGWLSEFMARHHEAED
Protein: Regulatory protein GAL4 (P04386)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.
Subcellular location: Nucleus.
Interaction partners:
- Galactose/lactose metabolism regulatory protein GAL80
- Galactokinase
- Protein GAL3
- Bifunctional protein GAL10
- Mediator of RNA polymerase II transcription subunit 15
- Galactose-1-phosphate uridylyltransferase
- Galactose transporter
- TATA-box-binding protein
- Meiotic mRNA stability protein kinase SSN3
- Proline utilization trans-activator
Sequence:
MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEQLFLLIFPREDLDMILKMDSLQDIKALLTGLFVQDNVNKDAVTDRLASVETDMPLTLRQHRISATSSSEESSNKGQRQLTVSIDSAAHHDNSTIPLDFMPRDALHGFDWSEEDDMSDGLPFLKTDPNNNGFFGDGSLLCILRSIGFKPENYTNSNVNRLPTMITDRYTLASRSTTSRLLQSYLNNFHPYCPIVHSPTLMMLYNNQIEIASKDQWQILFNCILAIGAWCIEGESTDIDVFYYQNAKSHLTSKVFESGSIILVTALHLLSRYTQWRQKTNTSYNFHSFSIRMAISLGLNRDLPSSFSDSSILEQRRRIWWSVYSWEIQLSLLYGRSIQLSQNTISFPSSVDDVQRTTTGPTIYHGIIETARLLQVFTKIYELDKTVTAEKSPICAKKCLMICNEIEEVSRQAPKFLQMDISTTALTNLLKEHPWLSFTRFELKWKQLSLIIYVLRDFFTNFTQKKSQLEQDQNDHQSYEVKRCSIMLSDAAQRTVMSVSSYMDNHNVTPYFAWNCSYYLFNAVLVPIKTLLSNSKSNAENNETAQLLQQINTVLMLLKKLATFKIQTCEKYIQVLEEVCAPFLLSQCAIPLPHISYNNSNGSAIKNIVGSATIAQYPTLPEENVNNISVKYVSPGSVGPSPVPLKSGASFSDLVKLLSNRPPSRNSPVTIPRSTPSHRSVTPFLGQQQQLQSLVPLTPSALFGGANFNQSGNIADSSLSFTFTNSSNGPNLITTQTNSQALSQPIASSNVHDNFMNNEITASKIDDGNNSKPLSPGWTDQTAYNAFGITTGMFNTTTMDDVYNYLFDDEDTPPNPKKE
Protein: Dipeptidase gliJ (EC 3.4.13.19) (Gliotoxin biosynthesis protein J) (Q4WMJ8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Interaction partners:
- Cytochrome P450 monooxygenase gliC
- Glutathione S-transferase gliG
- O-methyltransferase gliM
Sequence:
MSPSPIEEQATRLLKEVPLIDGHNDFPYMIRGWFRNDINGQDAHLYDMPIGQTDLQRLQKGLLGGQFWSAFVPCPKNPDKEVGSLEALRQTLQQLDVIHRLIERHPTILQFADSAASIWSSFRAGRVASLIGIEGLHQIADSVSALRMLHRLGVRYVTLTHNCHNAFADAATVSPELHGGLSRKGERLIRELNRMGMMIDLSHTSHEAQTQALRLSRAPVIYSHSSIYSLRAHARNVTDENLHLLHRNRGVVMICFLRELLASEADQATLAHVIDHIIYAGTRIGYEHVGIGSDFDGMLRGPDGLHDVSCYPALVAGLLERGVSEEDVKRVMGLNVIRVLEEVERVAAELQGAGEECLCDELDEVWNEDIKEQLTRERERVRKLGPQK
Protein: Regulator of G-protein signaling 18 (RGS18) (Q9NS28)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i) alpha-1, G(i) alpha-2, G(i) alpha-3 and G(q) alpha.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein G
- Pleckstrin
- Guanine nucleotide-binding protein G
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 1
- Regulator of G-protein signaling protein-like
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
METTLLFFSQINMCESKEKTFFKLIHGSGKEETSKEAKIRAKEKRNRLSLLVQKPEFHEDTRSSRSGHLAKETRVSPEEAVKWGESFDKLLSHRDGLEAFTRFLKTEFSEENIEFWIACEDFKKSKGPQQIHLKAKAIYEKFIQTDAPKEVNLDFHTKEVITNSITQPTLHSFDAAQSRVYQLMEQDSYTRFLKSDIYLDLMEGRPQRPTNLRRRSRSFTCNEFQDVQSDVAIWL
Protein: SH3 domain-containing protein (Q54NT2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- SH3 domain-containing protein
- Clathrin heavy chain
Sequence:
MSNKITTQFARTRQMLFTKTGHSEETIDVQYHYEKERTFSTEERLVKIQKNSKKLIELYKDLNKITTDIAQDACDLYDTQDPMWTPGSKLRDVATNNDKHLLDYTEQMAEPYTKPLSDYISQYKEARKRTEELTTRKVDMDRYKNEVGKLREKGAGSSSKAKLAPTEEKLRICKEGYDSLHEELLNDLPRLNEDKLIFIDYLVASLIKYQSEFHKKVSYEWSPLPSLTKHVDEYSGRDHQPVITSVERSAASINLRSDPVFKSNASIKMKPGAQDQQQYSTVDKDIHQSPNPSNLNLQKSTPNPYGGASAPPPLYGGGGSSTATALYDFTGVDSSELSFRAGDIITIHKSEGEWWEGELNGIYGFAPGSYLRMN
Protein: Aminodeoxychorismate lyase (EC 4.1.3.38) (4-amino-4-deoxychorismate lyase) (ADC lyase) (ADCL) (P28305)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Interaction partners:
- Aminodeoxychorismate synthase component 1
- Endolytic murein transglycosylase
- Aminodeoxychorismate synthase component 2
- Thymidylate kinase
- Dihydropteroate synthase
- DNA polymerase III subunit delta'
- Uncharacterized metal-dependent hydrolase YcfH
- Acyl carrier protein
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
Sequence:
MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFSSATLYEYLAPLCERPN
Protein: Mevalonate kinase (Q65XX8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHRNTTSQHGGLFVSAPGKIILFGEHAVVYGRTAIAGSIDLRTYVSLYTSADGRIYLSLPDLGVEKTWMLKDLLKAADRLAAEYPIEEDQPPSLEILVPIARKLSGSCEDQCGVQHLAILAFWYLLLGVAHRKRDLLAVKATVRFKLPSCVGLGSSGAYCVCIATSLLQTAGLIPPPSIVADEQGNLTWEEDHLDIIRKWATAAESLIHGRASGLDAAVCTFGGVASFKPGHRIEHLKNLPDLRVILVNSKVERNTARMVQTVKERLKKFPEVVDAMFGSIDAISLDAAKILHRPLLEENGGGDTGSTVQENGLGPFGGNMVEQDHHSLQPTRTASVRSSSLSSYVGGGKRNSSASVISATSEKGENVDTFSKLNDLCRINNQLLIALGVGHPKVDLICTTLARYGIHPKMTGAGGGGSVFAFLKPNTPQTLLDMIDGELRSHGFEVWQPPLGGPGVVEHQTRPELFQTPVSSTQCSTPASKHK
Protein: Thioredoxin-like protein (Q8IKL4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S11
- 40S ribosomal protein S5, putative
- 30S ribosomal protein S2, putative
- Small ribosomal subunit protein uS2
- Tubulin alpha chain
- Tubulin alpha chain
- Mitochondrial ribosomal protein L11, putative
- 60S ribosomal protein L12, putative
- Thioredoxin peroxidase 2
- Thioredoxin peroxidase 1
Sequence:
MKRTDDKIYVDINNEEEYKNLFDDKNDILYIIDIYTRWCGPCIFTFEMINKIYKNNLIFSENVKLFSICAQTVSSLKNYDNNCKPFYIILKNGEIIQQIQGCNIPLIFSFIDEHLMNKKIN
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (J3KR55)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KRRRAASMNRLGCWPARSLPRSGRGSGQRSLGLGGHPSGPRHPGTPAAKRTWESPGVRARDCPLSTSWLSEPPLGPAPHLSMVQAHGGRSRAQPLTLSLGAAMTQPPPEKTPAKKHVRLQERRGSNVALMLDVRSLGAVEPICSVNTPREVTLHFLRTAGHPLTRWALQRQPPSPKQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAGQLPEEPSP
Protein: Interferon regulatory factor 3 (B5XBN4)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MQSCKPQFADWLIEQVRTEQYTGLFFMDNNKFRVPWKHNSRKDCSEDDRKIFRAWAVVSGKITEHPNDKAKWKTNFRSALNSLCRRFKMVEDHSKDSNDPHKVYLVINEYNYESPLIEEITLENYGIDHALTTTENTPPGMEHDILNFSNLTLNHLDLNQHTENYIPVHTHHPVPPVLIQQPYAQVNPDALLNLPATRSSLWDLEITISYRGSEMLKTQVSGPRVQLHYQCNALEPC
Protein: RE73736p (Spoonbill, isoform C) (Q7KVW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit 1
- Veneno
- UT01108p)
- cAMP-dependent protein kinase catalytic subunit 2
Sequence:
MTLPCRCCCCSGKVTIFQYSAKMVSGRPLLYLSLPGVAFILGVFWFRRRYKNCLDKPDDEDSSAINDSSIEPTVQARKANGVLQNGKLPQQSASKSMNINGTLVNGSGSGSGSSSDEKDSPTTMLYGKSAPIKIQSNGRTSNGKHQQQIDSEILKSKIQDAEHKTLCSIDEDFENLSSPRDLPDSVNTRVSFYNRKATQKTVEPVVIKATRTPKISPENSFLDTNYTNKECEQNNNCEPKEEPSKKEADQEELEQDQEQTVLKEEVVDSNGNQKRNVDAASPSLSICSVQSGDSGKGSSLPRSEATRVKTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQRLPAKRYPNFTMQRIHFALPQTIVPLSTESLYNLQLKLIEGINNDVVVSAVLSGSHIFIQHPLHPSHPSLPLLQKQLYDSYSTMEAPLLPSLELSAVCVIPINDVWYRVQIVDTDPEDEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIGGTWSIEAAEILNKLTKGIVLQAQVAGYNSHNLPEIFLFASLGPNNVIFINKELVGRKLAKWVEMSD
Protein: Cytochrome c biogenesis Fn (Q2F909)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSINEFSHYLLFPGLFVAFTYNKKQPPAFGAAPAFWCILLPFLGLSFRHIPNNLSNYNVLTANASFFYQISGAWSNHEGSILSWCWIPSFYGFLFCYRGRPQSHNVSKRRGYRETFIFSFVSNFVKNSILSLQQKSGAAPQLYTPFVRRTFVDSELRSQSKRPFNGPALFNAPLDPVLKMSFALLGAGRSRGSREGKRTNLLLHLARDEKERASSIDEQQIDGALGIALFFSSFLSASSDPFVRNFFVRTEPLAESNPVPQDPISAIHPPCIYAGDVASAMGFGLCRSKMMNGIVALHSPPMRKDAAEKNGTLLRSAGCVGSHIRSSLFTRSFKHFVGGAPALLLRSNRSLLMLLRRRFFAFSSLWTGALMDTGREQAKRVVRNGKKDTTTSPLCWTAGANTVVSDQDQEPIRIWILTCRLFLTVGISPGSWWAHHELGRGGWWFRDPVENASFMPRVLATARIHSVILPLLHSWTSLLNILTLPCCVSGTFSIRSGLLAPVHSSATDDTRGRFLWRFFLLITGISMTLFYQMKQEASVRRTYKKEMVVARSTLVHLRHSARAQPRPVMLWKNLAYCWAGYSEPATGCRISSRP
Protein: Ligand-dependent corepressor (LCoR) (Mblk1-related protein 2) (Q96JN0)
Organism: Homo sapiens (Human)
Function: May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' (By similarity). Repressor of ligand-dependent transcription activation by target nuclear receptors. Repressor of ligand-dependent transcription activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000269|PubMed:12535528}.
Interaction partners:
- C-terminal-binding protein 1
- Metal-response element-binding transcription factor 2
- PHD finger protein 1
- Histone-lysine N-methyltransferase EZH2
- C-terminal-binding protein 2
- Estrogen receptor
- Polycomb protein SUZ12
- PHD finger protein 19
- Histone-lysine N-methyltransferase EZH1
- Elongin BC and Polycomb repressive complex 2-associated protein
Sequence:
MQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASWAKPHYEFNLSRMKFRGNGALSNISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
Protein: Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) (DES-1) (Dihydroceramide desaturase-1) (Q94515)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has sphingolipid-delta-4-desaturase activity. Converts sphinganine-containing sphingolipids (such as N-acylsphinganines or dihydroceramides) into sphingolipids containing the delta-4-desaturated sphingoid base (E)-sphing-4-enine (such as N-acylsphing-4-enines or ceramides), which are required for many different functions (structural functions as well as signaling). Required to initiate spermatid differentiation among other signals. Required for central spindle assembly and cytokinesis during male meiosis, may act as part of an anchoring mechanism that links membrane-bounded cellular compartments to components of the cytoskeleton.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein {ECO:0000305|PubMed:9819060}. Mitochondrion {ECO:0000269|PubMed:9819060}.
Interaction partners:
- LD18904p
- sphingosine kinase
- ceramide glucosyltransferase
- serine C-palmitoyltransferase
- Putative neutral sphingomyelinase
- Ceramide kinase, isoform A
- 3-dehydrosphinganine reductase
- Alkaline ceramidase
- Neutral ceramidase
- sphingosine kinase
Sequence:
MGQKVSRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINHSLMLAVHEISHNLAFGHSRPMHNRILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLWVCLQPFFYIFRPLIINPKPPTRLEIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFAKGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRRQRGLAS
Protein: rRNA 2'-O-methyltransferase fibrillarin (Histone-glutamine methyltransferase) (J9VR32)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Interaction partners:
Sequence:
MAFGDRGGRGGGRGGPRGGGRGGAGGRGGFGGGRGGGAARGGAGGRGRGAPRGRGAPGGRGGGRGGKAGLGRKGPGAVTLEPHKHEGVYIAKGKEHLLVTRNMTPGESVYGEKRISIATTNADGEEEKVEYRVWNPFRSKLAAGILGGLDNIHIKPGAKVLYLGAASGSSVSHVSDIVGPDGVVYAVEFSHRPGRELIGMAKKRTNVVPIVDDARHPQKYRMLVQMVDVIFADVAQPDQARIIALNAHHFLKNGGAIVISIKANCIDSTAPAAQVFASEVNNMRKEGIKPKEQLTLEPYERDHAMVVGIYQRHT
Protein: Circadian clock oscillator protein KaiB1 (P74645)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in output regulators CikA and SasA. KaiB switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from KaiC, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation.
Interaction partners:
- Circadian clock oscillator protein KaiA
- Circadian clock oscillator protein KaiC 1
- Circadian clock protein KaiC2
- Circadian clock protein KaiC3
- Protein RecA
- Amidophosphoribosyltransferase
Sequence:
MSPFKKTYVLKLYVAGNTPNSVRALKMLKNILEQEFQGVYALKVIDVLKNPQLAEEDKILATPTLAKILPPPVRKIIGDLSDREKVLIGLDLLYDEIREREAEDQ
Protein: Kinase suppressor of ras (Q8ISD8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSNSNAPASAPDTGSTNANDPISGSLSVDSNLVIIQDMIDLSANHLEGLRTQCAISSTLTQQEIRCLESKLVRYFSELLLAKMRLNERIPANGLVPHTTGNELRQWLRVVGLSQGTLTACLARLTTLEQSLRLSDEEIRQLLADSPSQREEEELRRLTRAMQNLRKCMESLESGTAASNNDPEQWHWDSWDRPTHIHRGSVGNIGLGNNSTASPRTHHRQHGVKGKNSALANSTNFKSGRQSPSATEELNSTQGSQLTLTLTPSPPNSPFTPSSGLSSSLNGTPQRSRGTPPPARKHQTLLSQSHVQVDGEQLARNRLPTDPSPDSHSSTSSDIFVDPNTNASSGGSSSNVLMVPCSPGVGHVGMGHAIKHRFTKALGFMATCTLCQKQVFHRWMKCTDCKYICHKSCAPHVPPSCGLPREYVDEFRHIKEQGGYASLPHVHGAAKGSPLVKKSTLGKPLHQQHGDSSSPSSSCTSSTPSSPALFQQRERELDQAGSSSSANLLPTPSLGKHQPSQFNFPNVTVTSSGGSGGVSLISNEPVPEQFPTAPATANGGLDSLVSSSNGHMSSLIGSQTSNASTAATLTGSLVNSTTTTSTCSFFPRKLSTAGVDKRTPFTSEYTDTHKSNDSDKTVSLSGSASTDSDRTPVRVDSTEDGDSGQWRQNSISLKEWDIPYGDLLLLERIGQGRFGTVHRALWHGDVAVKLLNEDYLQDEHMLETFRSEVANFKNTRHENLVLFMGACMNPPYLAIVTSLCKGNTLYTYIHQRREKFAMNRTLLIAQQIAQGMGYLHAREIIHKDLRTKNIFIENGKVIITDFGLFSSTKLLYCDMGLGVPHNWLCYLAPELIRALQPEKPRGECLEFTPYSDVYSFGTVWYELICGEFTFKDQPAESIIWQVGRGMKQSLANLQSGRDVKDLLMLCWTYEKEHRPQFARLLSLLEHLPKKRLARSPSHPVNLSRSAESVF
Protein: adenylate cyclase (EC 4.6.1.1) (B7UCF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MELSEVRCSSASEELYTINKTPSSSSSSSNNGNRPKRLLWQNAVRHITEQRFIHEHSPKPASPDEAHTQGSRKHSAGRTSVSDRHNNGGTKVFPERSSSDLGFLQIDCAPSNSDFFLSWGYTYRGVIFPTLRYAFKSRDLERLYQRYFLGQRRKSVVVMNILDVVTKLTLLVLHLTLASTPMDPIKGMLLGFFTGIEVVICALVVVRKDTSSHGYLQYSGAVTWVAMATQILATGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAIVAGLLTSALHIALQLLVPPRAQISTNQLLAQVLLFLCINTAGMFISYLSDRAQRQAFLETRRCIEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDETLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRPDHAHCCVEMGLSMIKTIRYVRSRTKHDIDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKAALDCLNGDYEVEEGHGKDRNDFLRRHNIETFLIKQPEESLLTLPEDIMRDSTNQSDHRTSNTSFTEGTWSPELPFHNIVGKQNTLAALTRHSINLLPNHLAQALHVRAGSQEINARMQSTIALRSGDKLRQEHISPFSLTFREALLEHKYSQMRDEVFKSNLVCAFIVLFFITGIQSLLPSARMVTMLIQFSVLILLHCCLVVVTTAEDYKCLPLVLRKACCWVNETYAARNVVIFLSILINFLAAMINILWCDFDKSGSFRNQTFNASASIPDICFYPEYFVFTGVLAMVTCAVFLRLNSVLKLAILLIMIAIYAVLTEAFYTPLFIRYDTLTLNQSKSFLGTKETSLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMRELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDTVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEERFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFAIALNESIQEINKHSFNNFQLRIGMAHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGKIQLPEETYAILNERGFAFEYRGEIYVKGISEQEGKIRTHFMIGRVQPNPLILQPRKLTGQYSLAAVVLGLVQSLNRQKQKQILNENNNSGIMKGHYNRRTLLAPGGSDTSHAEVTDKSDLA