wanglab/gogpt-training-data huggingface dataset:
Protein: At5g05500 (Pollen Ole e 1 allergen and extensin family protein) (Q9FFG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein SEED AND ROOT HAIR PROTECTIVE PROTEIN
- Peroxidase 7
- Pollen Ole e 1 allergen and extensin family protein
- Expansin-A18
- Probable pectinesterase/pectinesterase inhibitor 46
- Expansin-A7
- Xyloglucan endotransglucosylase/hydrolase protein 14
- Peroxidase 44
- Peroxidase 73
- Endoglucanase 5
Sequence:
MDSRALPFSVLVILIATAVLANAYTPPPPPPTTAYPAVKTVEAAVEGMVYCQSCDKFGSWSLAGAEAIAGAKISIICKNHRQQVSFYKVFRTDSYGHFYGELKGFKMTPHFLDHPLHSCRAKLVSSPREDCNLFSNINNALDGAPLRYEEKRLKWTNYEAVIYAAGPLAFRPDHCPATAPPTY
Protein: Cell wall synthesis protein KNH1 (P50112)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell wall beta(1->6) glucan synthesis.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- Beta-glucan synthesis-associated protein KRE6
- Uncharacterized protein YIL029C
- Beta-glucan synthesis-associated protein SKN1
- Protein KRE1
- Killer toxin-resistance protein 5
- Protein ROT1
- Ras modification protein ERF4
Sequence:
MLIVLFLTLFCSVVFRTAYCDVAIVAPEPNSVYDLSGTSQAVVKVKWMHTDNTPQEKDFVRYTFTLCSGTNAMIEAMATLQTLSASDLTDNEFNAIIENTVGTDGVYFIQVFAQTAIGYTIHYTNRFKLKGMIGTKAANPSMITIAPEAQTRITTGDVGATIDSKSFTVPYNLQTGVVKYAPMQLQPATKVTAKTWKRKYATSEVTYYYTLRNSVDQHTTVTPGWSYIITADSNYATPAPMPADNGGWYNPRKRLSLTARKVNALRHR
Protein: polynucleotide adenylyltransferase (EC 2.7.7.19) (A1Z745)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDVYQIDDGFHSDGGTETPPPSPSSGSSIASTSDHGSLESVDTGGTQRLAVLSFEQVSKLHDVMDEKVAIHGRGNFPTLEVKLKDLVNLVRRKLEAEVNAGGAGVLVKDIRLNGGAASHVLASEDQPYNDLDLIFAIELSSPRVFDRVKVAVLNTLLDLMPEGVCKRRIYTCSLKEAYVGKMVKVNNNNDGDRWSLISLGNSPGHKNVELKFVDTMRRQFEFSVDSFQIVLDSLLLFYDCAALPISENFYPTVVGESVYGDFQEALYHLQKKLISTRQPEEIRGGGLLKYCNLLVRNYKAVDSQLIKTLERYMCSRFFIDFPDINTQTTKLEAYLRNHFWGVDEEPLQYQYLMHLREVVEMSTVCLMGHERRQSLHLIQSLAAQVLFNKQEKQQQQQAQEKYQQQQQQQQHQQNQQQQQQQRQHQFLDPAQQQQQQQQTQTQQQQAQQATTLTLVPQAPPTGQAQTIYVQQAAPAAVCCTSSADQTATAAPQTIQIQAGPPGLIYANGVYYAPVIPSTICTCNSTWLST
Protein: Fumigaclavine B O-acetyltransferase easN (EC 2.3.1.205) (Ergot alkaloid synthesis protein N) (Q4WZ64)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Fumigaclavine B O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Fumigaclavine A dimethylallyltransferase easL
Sequence:
MKKQVTFKPFRLSPVDHSLPKVYIFKSLYFRGVDDTGSLSRLQDGIDRLISCLPFLSGEVVPCADIPDKVGVLQVQMPCPSLQEIPMLLVKSYPNHTWPAASTSERWRNTALLDQSYRPLPDFIPPSKPRPVLRFQANFLADGLMLCMGYNHSVFDGTGAGNILEMLADCCRANPNSILALPTNGDIESELRGLLSSPGVAVANASQEAYAINCAHTEVEPEPSSAMLYCWPFLLSSEKIECLQEACNSLLPHIVRLYSGTQSSLINQDTNWPHILSSNDVLTALLAVSIEKAREATGALGHMSRSLAMAVNLRERLKPMPRHYLGNLVTTVWVSHHRPAVKDLETMVLPVPACNRHEIDRDDLLWITHVAFRIRLGLNAINEEHIRGLIHYLHSQDDWEQIGIHFTDPIFISSWRHLKVYELDFGPTIGHAEHFEMDVGTTDGVCVVMPANTRAVGKTKKAPWDIRIVLNPEVLQALIASAIFGWAMVKDAST
Protein: Large ribosomal subunit protein eL32 (60S ribosomal protein L32) (P62911)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL1
Sequence:
MAALRPLVKPKIVKKRTKKFIRHQSDRYVKIKRNWRKPRGIDNRVRRRFKGQILMPNIGYGSNKKTKHMLPSGFRKFLVHNVKELEVLLMCNKSYCAEIAHNVSSKNRKAIVERAAQLAIRVTNPNARLRSEENE
Protein: Regulator of G protein signaling domain protein (AFU_orthologue AFUA_6G06860) (Q5B125)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Guanine nucleotide-binding protein alpha-3 subunit
- G-protein beta subunit
- Regulator of G protein signaling RgsB
- Intermediate filament, regulator of G-protein signaling
- Protein kinase domain-containing protein
- Developmental regulator flbA
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MLKKKSSHPPLLFWHSSPTSTPELSPTSSSSDTESDEDMDASGSRPLSLAVPQGTFCPMRPTLDEVLANTAPAPYTLGAFMAYLSQNHCLETLEFTLDAKRYRETYNELSRQLGQFPIEADCSESRHLRMLWQRLLSAYILPGSPREINVSSEVRDDILRHANSSIPPPPSMLDAAVKLVHDLMEESIFMPFLNAHSSSAHVYPLSEPLFSQDDGGVTIVSNPSLDEHAVKRVRSKGGRLSPRQSRELGSPISSSPPSSLSRSNFSLNAVTSLGKSSHRSSNQPSSASGESGSAGLSDDSGSMQSSAGEPMTPPTTPPSSEPSMQTGSPKNRMDNPWKKMGMKLGFKRRGGGSQSMRLPHEE
Protein: SusD-like protein BACOVA_02651 (A7LXT5)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Polysaccharide-binding protein present at the surface of the cell. Probably mediates xyloglucan-binding before xyloglucan transport in the periplasm for degradation.
Subcellular location: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MRIFMKSKLLVIATTALLFAACSDSFLDRAPEGNYVDATFYTSDEALEAATAPLYNRAWFDYNQRSIVPIGSGRANDMYSPWNYPQFVTFQVTALDENLSGAWSGFYSVVTMANSVINAVETQTQGSVSEAAKTKAIAEARLMRACAYFYMLRIWGPVILIEDNQKLVDNPVRPLNREEDVFQFIINDLNYAVDNLSEQSDKGRATSWAAKGILAKVYLARSGWNNGGTRDEGDLELARQYASDVCENSGLDLMTNYEDLFKYKNNNNQESLLAMQWVPLGEWYECNTLLSDLAFSTEVTGGVNCWSSYNGSIDMLQQYELADTLRRNATFFTKGSYYSYICIKDGGYTYKGTASPIKKGVPGGPDDDNDGKVKQMNSPLNTYILRLADVYLTYAEACLGNNSTLSDGRGLYFFNRVRERAKINKKSSITLDDIIRERRVEFGMEYSNWYDMVTWFRYLPDKMLNYFNNQWRGYRTDAIIKDEDGKLHFGKYDTDGTTFLEGPEYYTAPEFTINIEAEDIFLPYPESDVIQNPLLNEPPVPYTFNE
Protein: E4 ubiquitin-protein ligase UFD2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UFD2) (Ubiquitin conjugation factor E4) (Ubiquitin fusion degradation protein 2) (UB fusion protein 2) (P54860)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to RAD23 and DSK2, which target them to the proteasome. Has E3 ubiquitin-protein ligase activity, accepting ubiquitin from its cognate E2 ubiquitin-conjugating enzyme UBC4. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety. Promotes ubiquitin chain elongation at 'Lys-48' on the DOA10 substrate PEX29. Also involved in the proteolytic processing of the ER-bound transcription factor SPT23.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nuclear protein localization protein 4
- UV excision repair protein RAD23
- Ubiquitin fusion degradation protein 1
- Cell division control protein 48
- Ubiquitin thioesterase OTU1
- Ubiquitin domain-containing protein DSK2
- UBX domain-containing protein 2
- UBX domain-containing protein 1
- Protein DOA1
- Ubiquitin fusion degradation protein 4
Sequence:
MTAIEDILQITTDPSDTRGYSLLKSEEVPQGSTLGVDFIDTLLLYQLTENEKLDKPFEYLNDCFRRNQQQKRITKNKPNAESLHSTFQEIDRLVIGYGVVALQIENFCMNGAFINYITGIVSNVNSYTDFLSQIIQRAILEGTALDLLNAVFPTLLEYCNKHVSHFDLNESVIYNNVLTIFELFVTFKPIAEIFTKIDGFFADYSCKPQDFERKTILGPILSLSPIEAAVAIRNYGDNLLRSKQQTAMIHESLQAEHKVVIDRLFFIVDKLVRGSLNSRTDMISYFAHIANKNHLRRADHPPFKELSSNGFMSNITLLLVRFSQPFLDISYKKIDKIDANYFNNPSLFIDLSGETRLNSDFKEADAFYDKNRKTADSKPNFISDCFFLTLTYLHYGLGGTLSFEEKMGSEIKALKEEIEKVKKIAANHDVFARFITAQLSKMEKALKTTESLRFALQGFFAHRSLQLEVFDFICGASTFLIRVVDPEHEFPFKQIKLPLIPDQIGVENVDNADFLRAHAPVPFKYYPEFVVEGPVNYSLYISKYQTSPIFRNPRLGSFVEFTTMVLRCPELVSNPHLKGKLVQLLSVGAMPLTDNSPGFMMDIFEHDELVNKNLLYALLDFYVIVEKTGSSSQFYDKFNSRYSISIILEELYYKIPSYKNQLIWQSQNNADFFVRFVARMLNDLTFLLDEGLSNLAEVHNIQNELDNRARGAPPTREEEDKELQTRLASASRQAKSSCGLADKSMKLFEIYSKDIPAAFVTPEIVYRLASMLNYNLESLVGPKCGELKVKDPQSYSFNPKDLLKALTTVYINLSEQSEFISAVAKDERSFNRNLFVRAVDILGRKTGLASPEFIEKLLNFANKAEEQRKADEEEDLEYGDVPDEFLDPLMYTIMKDPVILPASKMNIDRSTIKAHLLSDSTDPFNRMPLKLEDVTPNEELRQKILCFKKQKKEEAKHKASE
Protein: Influenza virus NS1A-binding protein (NS1-BP) (NS1-binding protein) (Aryl hydrocarbon receptor-associated protein 3) (Kelch-like protein 39) (Q9Y6Y0)
Organism: Homo sapiens (Human)
Function: Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription. In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors. Inhibits pre-mRNA splicing (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9696811}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9696811}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9696811}. Note=Associated with actin filaments (By similarity). Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing (PubMed:9696811). Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm (PubMed:9696811). {ECO:0000250|UniProtKB:Q920Q8, ECO:0000269|PubMed:9696811}.
Interaction partners:
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Heterogeneous nuclear ribonucleoprotein K
- T-cell leukemia homeobox protein 2
- Phosphoribosyl pyrophosphate synthase-associated protein 2
- Proline dehydrogenase
- Serine/arginine-rich splicing factor 2
Sequence:
MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQF
Protein: Endochitinase A (EC 3.2.1.14) (ChitA) (Chitinase-A) (Seed chitinase A) (allergen Zea m 8) (P29022)
Organism: Zea mays (Maize)
Function: Defense against chitin-containing fungal pathogens. Hydrolyzes glycol chitin and tetra-N-acetylchitotetraose in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:28328103}.
Interaction partners:
- Squamosa promoter-binding-like protein 15
Sequence:
MANAPRILALGLLALLCAAAGPAAAQNCGCQPNFCCSKFGYCGTTDAYCGDGCQSGPCRSGGGGGGGGGGGGGGSGGANVANVVTDAFFNGIKNQAGSGCEGKNFYTRSAFLSAVNAYPGFAHGGTEVEGKREIAAFFAHVTHETGHFCYISEINKSNAYCDASNRQWPCAAGQKYYGRGPLQISWNYNYGPAGRDIGFNGLADPNRVAQDAVIAFKTALWFWMNNVHRVMPQGFGATIRAINGALECNGNNPAQMNARVGYYKQYCQQLRVDPGPNLTC
Protein: Cation channel sperm-associated auxiliary subunit zeta (CatSper-zeta) (CatSperzeta) (Testis-expressed protein 40) (Q9NTU4)
Organism: Homo sapiens (Human)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for a distribution of the CatSper complex in linear quadrilateral nanodomains along the flagellum, maximizing fertilization inside the mammalian female reproductive tract. Together with EFCAB9, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:28226241}; Peripheral membrane protein {ECO:0000305}. Note=Specifically located in the principal piece of sperm tail (PubMed:28226241). Although it does not contain a transmembrane domain, localizes with the CatSper complex at the flagellum membrane (PubMed:28226241). {ECO:0000269|PubMed:28226241}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit gamma
- Cation channel sperm-associated auxiliary subunit TMEM262
Sequence:
MEEKPSKVSLKSSDRQGSDEESVHSDTRDLWTTTTLSQAQLNMPLSEVCEGFDEEGRNISKTRGWHSPGRGSLDEGYKASHKPEELDEHALVELELHRGSSMEINLGEKDTASQIEAEKSSSMSSLNIAKHMPHRAYWAEQQSRLPLPLMELMENEALEILTKALRSYQLGIGRDHFLTKELQRYIEGLKKRRSKRLYVN
Protein: Peroxiredoxin-4 (EC 1.11.1.24) (Thioredoxin-dependent peroxiredoxin 4) (Q555L5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}.
Interaction partners:
- Thioredoxin reductase
- Peroxinectin A
- Sestrin homolog
Sequence:
MRSATKLFKNLSKSVVQLKTVKPVSSLNFGYIKTRQFSTSTTDSSNLFLNNNNQFQNFTFPTKQQIRIRKPAPAFKGQAVVNGEFKEISLDDYKGKYLYLFFYPLDFTFVCPTEIIAFSNAAEEFKKAGCELVGCSIDSPFTHLAWINTPRKEGGLGGINIPLLSDLTHQISKDYGVYIEEDGHTIRGSILIDKEGLVRVITMNDNPVGRSVDEAIRTLKALKFTDQFGEVCPANWSEGDKSMKADPKGSKEYFEAVNK
Protein: RH21245p (Q8SZK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPPNAQAGAQSISDSLIAAASAAADAGQSPTKLQEDSTGVLFECDVETTDGGLVKDITVMKKAEKRRLKLVWRNIIAFGYLHLAALYGAYLMVTSAKWQTCILAYFLYVISGLGITAGAHRLWAHRSYKAKWPLRVILVIFNTIAFQDAAYHWARDHRVHHKYSETDADPHNATRGFFFSHVAGCCARSTRR
Protein: Rrp45p homologue (Q95Z11)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQYQRAALVIASPALTQREVEFTKSAWLAGLRPDQRTAQQMREVSVEFPLLSRDVVVVRCGGSVVTAAIATALVEPTPQRPKHGLLHFSVRRLHTEKDSPAADGSTQKNLVAFLERLVRTGGVIDTAGLCVLPGQKVWSLTVNVTIMNDEGNCNDAAVWAVIALLMHHRRPELTVRGSSVIVHPPHEREPVPLSVQHTPLPFTFAITMAPTEREKALNHQRALSATGSSSGPQPSSGVGNSIDTASAFAIDGTSPQPLGVVVDPTTAESLAAASSIVVAINAEGQVCTVVKAEGCSIHLKDLNACIEAAGTLAPRVLDLIKVAMEAHDERRKTAMKGQFAWAQKRSGVGKVEQTCVKKIKTET
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (Q4Q828)
Organism: Leishmania major
Interaction partners:
- Aminomethyltransferase
- Aminomethyltransferase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Glycine cleavage system P protein
- formate--tetrahydrofolate ligase
- Glycine cleavage system H protein
- Putative methylenetetrahydrofolate reductase
- Putative beta eliminating lyase
- 2-oxoglutarate dehydrogenase, e3 component,lipoamidedehydrogenase-like protein
- Putative dihydrolipoamide dehydrogenase
Sequence:
MILRAAPASTHRHRSPSLPGNISLRDHDPEVHQLIQREMRRQIEGLELIASENFTSRAVLDCLGSVLTNKYAEGLPGNRYYGGTEVVDELENLCVRRARAAFCLDAALWGVSVQPYSGSPANLAVYTALLRPHDRMMGLSLQAGGHLTHGFYTATKRLSASSIFFESLPYSITPKGLVDYDQLAYLADIYKPRLIIAGGSAYPRDWDYKRYREICDSVGAYFMVDMSHFSGLVAAREHNDPFEYADVVTTTTHKTLRGPRSGMIFFKKSIKQGKENVCVEDSINNAVFPALQGGPHLHQIAGIATQLKEVASPEWRTYIKQVKANARALAAVLTEGGETLVSGGTDNHLLLWNLRPHGLTGSKLEKLLDMVNITVNKNTIFGDRSAQAPYGIRLGTPALTTRGLQEEDFRRVGQLLIRSVQLSKEVQKSAGSTKLVDFVKAAETSKALQEMAEEVKAYARQFPYPGLESAYPIQ
Protein: Putative N-acetyltransferase subunit NAT1 (Q9NFL7)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MATTLPLQQQRLFDKLARDFDAREYAKGLRTADSILSVVPNHADTLALKGLTLHHMGRKEEGREIIESALGFNDTSTVVWHSLGMCHRADDNHVEALHAFQKAHEYGPSNVNVLRDISSICVQLREWEQFVDVRRKMVTLRPGVRANWIALSCGHRMLGNKELAAAVIDVMTTIMEAGDNRAEKSEVRLYQVELELACNAPARALDLLKKHSQEIIDEYEKASLRAKTHALLGQKVEAEKWYMELITRGMAEADCVAAIAQLRKIPLDAARRPKRDVDKYLELLKQVQEVNPKSNYAKRQVLECVPIEQFRDQLREYAGMFIVKTIPSLFSVLKSLYQCPDRTQHIGEVFHQWEEELMAGDFSSFGGKKDPTFILWVWMYLASHYCRIREFGRALEYIGRAIDHTPTFDLLYLMKAKIQAKNNQLDEAAKTADMARRLDLQDKYLNGKAAKYFFRANKIREGEALMQMFYKTTEVPDDTYLTALESQCAWYEREVGDAYYRMGDYISALSNYLMCESHHQRNHNELSEFHNYVFRRCTMRAWFNVIACDDNLEENKFFQKLCPRIVRTYMKIHEEGEEAVRAKYAPRPEVGKYSDVEEGKRIGNLRRTFYLHNVDISDPLKKAGRYLQASLLHNALSSEVHLLAVEFYTMCRMPFLVARELLILAKLKCPSTNELVTQFENNLFREMASSMDPRVESIIKETLTTALEKLN
Protein: Acetyl CoA carboxylase (A6MUS7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
LPENSCDPRAAISGALDSSGNWKGGIFDRDSFVETLEGWARTVVTGRAKLGGIPVGIVAVETQTVMQVIPADPGQLDSHERVVPQAGQVWFPDSATKTAQAIMDFNREELPLFILANWRGFSGGQRDLFEGILQAGSTIVENLRTYKQPVFV
Protein: 26S proteasome non-ATPase regulatory subunit 7 homolog A (26S proteasome regulatory subunit RPN8a) (AtRPN8a) (Protein ASYMMETRIC LEAVES ENHANCER 3) (Protein MOV34) (AtMOV34) (O24412)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Required for innate immunity.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit 6A homolog A
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 13 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
Sequence:
MDVIKTQQISARTIEKVVVHPLVLLSIVDHYNRVAKDSSKRVVGVLLGSSSRGVVDVTNSYAVPFEEDDKDPSIWFLDHNYHESMFHMFKRINAKEHVVGWYSTGPKLRENDLDVHALFNGYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVSTEIAAHEVEEIGVEHLLRDVKDTTISTLATEVTAKLTALKGLDARLREIRSYLDLVIEGKLPLNHEILYHLQDVFNLLPNLNVNELVKAFSVKTNDMMLVIYLSSLIRSVIALHNLINNKLLNKEHEKAEDSKPVAIPATS
Protein: T-box transcription factor TBX20 (T-box protein 20) (Q8AXW8)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional regulator that may be involved in heart developmental processes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MEYTPSPKPQLSSRANAFSIAALMSSGTPKDKEAQESTIKPLEQFVEKSSCSQPIGDISIVDSHGEFTNSPSSLCTEPLIPTTPIIPSEEMAKISCSLETKELWDKFHDLGTEMIITKSGRRMFPTIRVSFSGVDADAKYIVLMDIVPVDNKRYRYAYHRSAWLVAGKADPPLPARLYVHPDSPFTGEQLLKQMVSFEKVKLTNNELDQHGHIILNSMHKYQPRVHIIKKKDHTASLLNLKSEEFRTFIFQETVFTAVTAYQNQLITKLKIDSNPFAKGFRDSSRLTDIERESVESLIQKHSYARSPIRTYGGDEDVLSEDGQVVQCRGSAFTTSDNLSLSSWVSSTSGFSGFQHPQSLTALGTSTASLATPIPHPIQGSLPPYSRLGMPLTPSALASSMQGSGPTFPSFHMPRYHHYFQQGPYAAIQGLRHSSTVMTPFV
Protein: Uncharacterized protein (Q388F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSADTICRDHAAQTSQDRPCQTGCPAGYIAGAATRVAGNVIPPCHNGPLYRVPCCCEVAHDVCPATASDHSCCHCCFGCSRDNVPYQHHQGRPYSGGGVGVLPVAHGSRLCAFCVPEREQLREYEHHEKRQRYLAVRADRENLLQALGGKVVGTHGESRGHYKSNMTHLMRHARGTIHQQAAMAEQQRRRQELRREVEERRRELGGRGYRQLVGPVEDRRTSRVVARPRKETPAYYYTPVPHCGTGQMRQHSLARNTVAHVAPRAEGKCVAAHKERRAAAPRVTNNEDNVPENTQPPKKSKATDARPAQVSRSTSFIKKGSEPNQHPQVVLQCCCHAVCRCRPCKCFAPCRCNNNVPAKDPGTAPSAVVAKSEKEEPPAAKTPRPTNEFKKSVANSPVARSSSVKHGRKIFITDHAHSDRRSQVINRLEEDGYLRPVPPTTRSPSAPLAEKAKKWETTRSTSAHHL
Protein: LD16191p (Q8MZH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQMRVTELPAVQLLLPLILIGLASGQRVAPGVNPQHYQQVPQQVPQHHPPPPPQHHQPQYQQQVHSAPGVPPQQYQYEQVQVPVQQQAPVQYQQVPVQQQQQQHQPIHQQPTMQQQQQPQQGHHQQAGGHHHGQPQQVLNTGNIQQERAHIQEHMQLPIDTSKMSEAELQFHYFKMHDSDNNNKLDGCELIKSLIHWHEQGSKEQPNGEKPHVEEKVFSDEELVALIDPILQMDDTSRDGYIDYPEFIKAQQKAAEKQQQQQQQQQQPHEQQQQQQQQPVH
Protein: UI (Urotensin 1) (W5U9F7)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKPVASVLLIAAVLLSTHIPTSICRPRDLSLFDHHDDYKNQLDEVFLRVGKGETMSFLSGGNGREHELRIGSRSPTSPSPNSLEELIGFTKRNDDPPISIDLTFHLLRNMIEMARIENQREQAELNRKYLDEVGK
Protein: Dihydroneopterin aldolase 1 (DHNA1) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) (AtFolB1) (Q9SF23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of 7,8-dihydroneopterin into 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin tetrahydrofolate. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin.
Interaction partners:
- Folate synthesis bifunctional protein
- Folate synthesis bifunctional protein
- GTP cyclohydrolase 1
- Dihydrofolate synthetase
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Aminodeoxychorismate synthase, chloroplastic
- Folylpolyglutamate synthase
- D-amino-acid transaminase, chloroplastic
- Dihydroneopterin aldolase 2
Sequence:
MHSSLETTAPATLERRESNLGDKLILKGLKFYGFHGAIAEERTLGQMFLVDIDAWVSLKKAGESDNLEDTISYVDIFSLAKEIVEGSPRNLLETVAELIASKTLEKFHQINAVRVKLSKPNVALIKSTIDYLGVDIFRQRNTSSKN