wanglab/gogpt-training-data huggingface dataset:
Protein: Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10) (P50587)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Phosphoribosylformylglycinamidine synthase
- Bifunctional protein PyrR
- Ribose-phosphate pyrophosphokinase
- Ribonuclease PH
- Dihydroorotase-like protein
Sequence:
MQAYQRDFIRFAIERGVLRFGEFTLKSGRTSPYFFNAGLFDSGLALARLGRFYAEAVIDSGIDFDVLFGPAYKGIPLAATTAVALAEQHQRDLPWCFNRKEAKDHGEGGTLVGAPLSGRVLIIDDVITAGTAIREVMQIIDAQGARAAGVLIALNRQERGKGELSAIQEVERDFGMPVVSIVSLEQVLEYLAEDAELKKHLPAVEAYRAQYGI
Protein: Putative glycine cleavage system H protein, mitochondrial (Glycine decarboxylase complex subunit H) (Q9HDV9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable aminomethyltransferase, mitochondrial
- Putative glycine dehydrogenase
- Serine hydroxymethyltransferase, mitochondrial
- Putative lipoate-protein ligase A
- Probable serine hydroxymethyltransferase, cytosolic
- Dihydrolipoyl dehydrogenase, mitochondrial
- DASH complex subunit dad4
- Probable octanoyltransferase
- Probable pyruvate dehydrogenase protein X component, mitochondrial
- Methylenetetrahydrofolate dehydrogenase [NAD
Sequence:
MLARSALRSGFLPSLTSSVKTGFCLKAAAPTLSMKWSAVKYYSTKHFTKEHEWVKVDGDVGTVGITSYAANALGEVVFVELPEPETTVSVGDGIGAVESVKSASDVYSPVSGTVTSINESLGDSPDKVSSSPEEEGWICKIKLSSPDELKSLLNDESYAQFCKEEDASH
Protein: Putative head protein (H9C193)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MAQAVDEALIPVLRRNYTADSYLTDILKEAIWQASERFMNTAFQRNAERLSQRVVSRAESDSSAAFVEQINRAIGIDMTALMVNENLVDYVDASIESNVALIKSLSSDYFEDIQMQVFDGILRGDSLTTIVRNLQHSTGTAYNRAHLIARDQTAKIQADITSVRQQNAGIDRFRWSTSQDVRVSGNPAGKYPLAKISCFAISRIDVGMGAGVYLWSRGAKYNGQTDLFPGRAHIGCRCHAIPQIKGLDY
Protein: RecQ-mediated genome instability protein 2 (hRMI2) (BLM-associated protein of 18 kDa) (BLAP18) (Q96E14)
Organism: Homo sapiens (Human)
Function: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM.
Subcellular location: Nucleus {ECO:0000269|PubMed:18923082}. Note=Colocalizes with BLM at nuclear DNA repair foci.
Interaction partners:
- RecQ-mediated genome instability protein 1
- Fanconi anemia group M protein
- DNA topoisomerase 3-alpha
- RecQ-like DNA helicase BLM
- Fanconi anemia group A protein
- Fanconi anemia core complex-associated protein 100
- Centromere protein S
- Exonuclease 1
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA topoisomerase 3-beta-1
Sequence:
MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP
Protein: Putative syntaxin-4 (P91409)
Organism: Caenorhabditis elegans
Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Synaptobrevin-1
- Putative syntaxin-2
- Syntaxin-1A homolog
- Soluble NSF attachment protein 29
- Alpha-soluble NSF attachment protein
- Vesicle-trafficking protein SEC22b
- t-SNARE protein aex-4
- Putative syntaxin 6
- Synaptosomal-associated protein
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MHQISGINAASPEKNNSKLADVSLQQFLANVDEIRHVLTTLSADRHAIYMEQVESLAAGCSDTAKCRKLNDHVDKFIAQARGIRRRLADASEELVQYPESRVGSGRARHEQIQMLIVSLEGIMSQFADDQASYKAEAAKKIAAYLRKQNIEVTDSEIDGAIENGSLFQLTRNINLGVAQKKALFDDMKNRATDIMILEKQIREVEELFVDMQLLVQSQGETVDRIETSVIRAEEYAEQAQQNVRQAVVLRRKNRKWKIVTCIALIVLLLVVVYLLSHFLGAIIPGWK
Protein: Uncharacterized protein C21B10.08c (P78833)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSFPASTHVYIAKIIGKKGEGDKILDLLSKVNEHVLKSEPFTKTYYFARDAKNPDYIFGLELYDSKEVLENSHKTSNPFLAFANYLTSTHAPLAEPLQLLNFKVVDGHLDKDNLGPDAKDYVLYTEYTGDSATLKQQLTVNPKADTSLIIHSLDDPSLYAVVTRYSKSGIEPGPAEISGATSVSQQVIYSGVGFLNRP
Protein: Uncharacterized glutaminase C222.08c (EC 3.5.1.2) (Q9UTE4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit PDX1
- Isoamyl acetate-hydrolyzing esterase
- Probable pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase C18.10
- Putative pyridoxal kinase C6F6.11c
- Glutamine synthetase
- Putative glutamine amidotransferase-like protein C13C5.04
- Transaldolase
- Ribokinase
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
Sequence:
MSSASMFGSLKTNAVDESQLKARIGVLALQGAFIEHINIMNSIDGVISFPVKTAKDCENIDGLIIPGGESTTIGKLINIDEKLRDRLEHLVDQGLPIWGTCAGMILLSKKSRGGKFPDPYLLRAMDIEVTRNYFGPQTMSFTTDITVTESMQFEATEPLHSFSATFIRAPVASTILSDDINVLATIVHEGNKEIVAVEQGPFLGTSFHPELTADNRWHEWWVKERVLPLKEKKD
Protein: Mitochondrial import inner membrane translocase subunit Tim8 (Q9N408)
Organism: Caenorhabditis elegans
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane (By similarity). Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane (By similarity). Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). The ddp-1/tim-8-tim-13 complex mediates the import of some proteins while the predominant tim-9/tin-9.1-tim-10/tin-10 70 kDa complex mediates the import of much more proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O74700}; Peripheral membrane protein {ECO:0000250|UniProtKB:O74700}; Intermembrane side {ECO:0000250|UniProtKB:O74700}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit tim-13
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import receptor subunit TOM7 homolog
- HoloCentric chromosome binding Protein
- HoloCentric chromosome binding Protein
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import inner membrane translocase subunit Tim10B
- Cytochrome c oxidase copper chaperone
Sequence:
MDSADPQLNRFLQQLQAETQRQKFTEQVHTLTGRCWDVCFADYRPPSKMDGKTQTCIQNCVNRMIDASNFMVEHLSKMNGGHV
Protein: E3 ubiquitin protein ligase DRIP2 (EC 2.3.2.27) (DREB2A-interacting protein 2) (RING-type E3 ubiquitin transferase DRIP2) (Q94AY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the response to water stress. Mediates ubiquitination and subsequent proteasomal degradation of the drought-induced transcriptional activator DREB2A. Functionally redundant with DRIP1.
Interaction partners:
- Putative E3 ubiquitin-protein ligase RING1b
- Putative E3 ubiquitin-protein ligase RING1a
- Dehydration-responsive element-binding protein 2A
- E3 ubiquitin-protein ligase AIRP1
- E3 ubiquitin-protein ligase SDIR1
- E3 ubiquitin-protein ligase RMA1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- E3 ubiquitin-protein ligase KEG
- E3 ubiquitin-protein ligase RHA2A
- Zinc finger A20 and AN1 domain-containing stress-associated protein 5
Sequence:
MEGDMVAKVKRETVVACMTCPLCDKLLRDATTISECLHTFCRKCIYEKITEDEIESCPVCDIDLGGTPLEKLRPDHILQDLRAKLFPLKRKKERAPEVVSSISLPAKRKERSISSLVVSTPRVSAQAGTTGKRTKAATRKDVRGSGSFTKRTVKKEEEFGDDHVESASSPETLKKFTQNKRQSSYANPNQSLSNRRNKDVDEPWDSKLHLWKPLNFLVDVANGTKDPKSELGNASHNDVQGSKTKTKDHKRKCKLEEEISNNGDPTTSETATLKRTRRTRRKRSSTFGDSRIPLLPGAASLKQERRNGHVWFSLVASSNQEGEASLPQIPANYLRIRDGNIPVSFIQKYLMRKLDLKSEDEVEITCMGEPVIPTLQLHSLVDLWLETTSKHQRVAASIGSSAKEFVMVLVYSRKLPECNN
Protein: Testis secretory sperm-binding protein Li 233m (A0A140VKA6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPRKVNELRAFVKMCKQDPSVLHTEEMRFLREWVESMGGKVPPATQKAKSEENTKEEKPDSKKVEEDLKADEPSSEESDLEIDKEGVIEPDTDAPQEMGDENAEITEEMMDQANDKKVAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALACKLDYDEDASAMLKEVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHERAQREEEARRQSGAQYGSFPGGFPGGMPGNFPGGMPGMGGGMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPANMSKYQSNPKVMNLISKLSAKFGGQA
Protein: Acyl-coenzyme A thioesterase 11 (Acyl-CoA thioesterase 11) (EC 3.1.2.-) (Acyl-CoA thioester hydrolase 11) (Adipose-associated thioesterase) (Brown fat-inducible thioesterase) (BFIT) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2) (Q8VHQ9)
Organism: Mus musculus (Mouse)
Function: Has an acyl-CoA thioesterase activity with a preference for the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in the mitochondrial beta-oxidation pathway.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8WXI4}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXI4}.
Interaction partners:
- Acyl-coenzyme A thioesterase 13
Sequence:
MIQNVGNHLRRGFASMFSNRTSRKSISHPESGDPPTMAEGEGYRNPTEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSEDLCSEKQWSVCKALATFVAHRELSKVKLKQVIPLTEEEKTEHGVAAERRRMRLVYADTIKDLLTHCVIQDDLDKDCSNMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETQRRHINSAFMTFVVLDKDDQPQKLPWIRPQPGEGERRYREASARKKIRLDRKYLVSCKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEDFLSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDNRNDLAPSLQTL
Protein: Forkhead box protein biniou (Forkhead box protein FoxF) (DmFoxF) (Q9VS05)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of a regulatory network controlling visceral mesoderm development and midgut morphogenesis. Transcriptional regulator involved in the activation of a large number of genes in the visceral mesoderm including betaTub60D, dpp and Hand. Binds to and regulates a number of enhancers driving expression in the visceral mesoderm in a temporally and spatially restricted manner. Also to binds to enhancers cooperatively with activators, such as bap or HLH54F, to coregulate expression of shared target genes in the visceral mesoderm. Binds to the Ndg enhancer and drives expression of Ndg in the late visceral musculature. May be involved in the transcriptional regulation of wupA in the visceral mesoderm. Plays an indirect role in the later stages of salivary gland positioning.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:11804790, ECO:0000269|PubMed:14523446}.
Interaction partners:
- Homeobox protein bagpipe
- Muscle-specific homeobox protein tinman
- Homeobox protein abdominal-A
- GATA-binding factor A
Sequence:
MIKSEEASDRSVMTMDQLGGYYHDPRAHPPFSHPHAHSHPHQHTHTGHPYRAGNLLTGGNYQAMGGGESPTELIDEKPNIGYMELKHYMDATPTATPVSAAQHYSLSALHSMGTPPASSSPIPPYGVLMTAHSAGSASPQSNSKTPTDLPQDLQYASSSTSTAKVQPLQVQLQPLNHQYASTIKYCSNNTILSANDYQLLTSQEQAGQQQPQQLPAQQLQHSPGGGYMSRISTSPSQVISNAHGMPVLNYSSSSSSPAKSLNGSESSPPSQNHLENKVSGSAVVGTGGSSQQDAPSTPDTTKKSGTRRPEKPALSYINMIGHAIKESPTGKLTLSEIYAYLQKSYEFFRGPYVGWKNSVRHNLSLNECFKKLPKGMGVGKPGKGNYWTIDENSAHLFEDEGSLRRRPRGYRSKIKVKPYAGHANGYYASGYGDAGMDNGNYYASPAFASYDYSAAGATGVSPAGGQGFADPWNAHAAHSGSSSVGVGMGVGPLPQYTNISCLAAGGNVNGSATTPPLAHSALGMAPSASSSSSPLGAAATLQSDYAPTASLVAAGYSYATSAGSLDNGLRSISLQQLPGLSSIQHAQAQAQAQAHHHHHQHHASHPSHSHQGHGSMHQNHGTSSTTPPPSQSGGSHGIDHSPIDRKPAYLPPISPPPMMVALNGGGGYYEGLKYAN
Protein: KOW domain-containing protein (Q57ZE0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Ribosomal protein L11, putative
- 50S ribosomal protein L13, putative
- Uncharacterized protein
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- 50S ribosomal protein L17, putative
- 50S ribosomal protein L2, putative
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL29m
Sequence:
MCVFSSPFWCLCCNIGSITLVGSRYAGNSVASTIMYARFRTRSKFYFRPARPALAYNVDPNVMRRPKVKRGLLKGTYSDETVDLRDRERLELLESMRHPRERDFYQDHTYHNQWLRRDLEKHQKQQLAARYKYFAPDFEISPWIWYPGDIVEVVSGEGIGQRGTIIAVIKYKNEIVVQNINVQDVVIPASESRPEQIVQREHPISVTRVRHVDPSTNEICNIEMVKVRNKETGEMEEKRMSLESGILMSIPPVNDELEVGDPLKDTPIQDADEATYDREAEQAVLVDKRLEAMEEHFVQSLKHSYEFHEPLRRKNAEDMRQFQTDVIDMACAMLGERLLDTVNASDTSSLPAEWQEAIAMHVEEIEAEMEEVAAKEMAEAKEGVATENEQHDDDLDDDEDELDTSEESVKHV
Protein: Cation transporter, putative (Q384C6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MANVNNETTECGALLSNITSLQTTLTSMGCQVPVLHHHHRDNHTHGVVDDGIDGDTHGGCESGHGTYSIGLHVVAIFVVLIASFLGTLIPIIGKYVPALRLPPFALVLGKCIAAGVLLSVSTIHMINESILQLQEDCVPESFRESYEAYAFLFAVAGALLMQMVDVIVDKYVTNKSDSSTNKPEGQPDAEEAQAAPAALDAYDGHHCHYAVGMPQSRTKRLVAAMFMEFAVTVHSVFVGLAVGIARDAETKTLLVALVFHQMLEGLALGARLVDAELSLKLEMLFALLFSVSAPLGTAIAVGTIAIWNVSMVGTAFVITQAVTSAVCGGMLLYLAFCLMLSDFPSDMQKHAGKDKVRRFFRCFGMFAALWFGAALMAFIGKWI
Protein: Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i) (P28063)
Organism: Mus musculus (Mouse)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. May participate in the inflammatory response pathway. Required for adipocyte differentiation. May be involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-1
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-10
- Proteasome subunit beta type-9
Sequence:
MALLDLCGAARGQRPEWAALDAGSGGRSDPGHYSFSAQAPELALPRGMQPTAFLRSFGGDQERNVQIEMAHGTTTLAFKFQHGVIVAVDSRATAGSYISSLRMNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMLQYRGMGLSMGSMICGWDKKGPGLYYVDDNGTRLSGQMFSTGSGNTYAYGVMDSGYRQDLSPEEAYDLGRRAIAYATHRDNYSGGVVNMYHMKEDGWVKVESSDVSDLLYKYGEAAL
Protein: Sodium-dependent nutrient amino acid transporter 1 (B4NDL8)
Organism: Drosophila willistoni (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELKNIEQQPQLQNGNGTATENNEKGEQKPTEGGERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIIGQFTSQGSVKIWSICPSFLGVGYGQAFATVCIISYYSSLLALTLYYLFVSFQSVLPWSYCRDEWTNCVNSRPEDYSSTMLEAARNATSSLLIGNETTSLADNDSVQLQSSSELYFLNVVIKEKLDISDGVGAPDWKLTLALLVSWIVTFLVIMRGVKSSGKAAYFLAIFPYVVLFVLLGRAVTLEGAVDGIIFFLQPQWGELLNPTVWKEAVVQCFFSLAVSCGPIIMFASYNRFDHSIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQVDNIREVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKSWKYWKVALVTSICGFLLGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWIYGLQNFCDDIEFMCNKRVSLYWRVCWSFFTPVMMIIIFIYSMATIEPLKYSDLYFPLAGDIAGWIVFAIGTAQFPLWGIWYISHHRNGNLWQSFVSCLKPNENWGPANPETKQAWLLFKSEKARQRASKTQSSKMGQFWQKVGNFCGSST
Protein: Transcription factor TGAL7 (bZIP transcription factor 70) (OsbZIP70) (Q6H434)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Os01g0104800 protein
- Os04g0662100 protein
- Os12g0166500 protein
- U3 small nucleolar RNA-associated protein 18 homolog
- Pre-mRNA-splicing factor SLU7
- DEAD-box ATP-dependent RNA helicase 36
- Os03g0598200 protein
- Os05g0295100 protein
- Os03g0343300 protein
- Os01g0581900 protein
Sequence:
MGGSREEDRQHHNHLPSELPLGFRSSSPTTMIASSSMSKESSNYDMADFDQASLFLYLDSHDQQSIQEQRQTLNIFPSQPMHVADPAHEAKSAGVAMAMLPNGNQLQVLPSHPSKKPDQQGGQKINSSVPTNPPGPNLPLPNSAKDNKNSSLIKKEGSSSGKGATTSNDPEREGRRTLDPKTLRRLAQNREAARKSRLRKKAYIQQLESSRIRLSQLEQQVHVARVQGAMLGAGDQHQGLPSGPSAASLFDLEYGRWVEEHSKLIFQLRAALNEQMADSQLQVFVNGAMAQHDELLSLKGAIARADIFHLLCGVWATPAERCFLWLGGFRPSEAIKVMLKQVEPLSEGQLMSIYELQQAAKGTEDALSHAMDGLQQSLSDTVAAPDVAAAGGFMGHMSLAMNKISAMEDIVRQADGLRQQTLHKLQHMLTIRQAARCFVAISDYFHRLRALSTLWVARPRPEEGPAM
Protein: Ubiquinone biosynthesis protein COQ9, mitochondrial (O75208)
Organism: Homo sapiens (Human)
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}. Note=Associates with cardiolipin-rich membranes which leads to the lipid bilayer deformation and then accessing to membrane-bound lipids. {ECO:0000269|PubMed:30661980}.
Interaction partners:
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- Atypical kinase COQ8B, mitochondrial
Sequence:
MAAAAVSGALGRAGWRLLQLRCLPVARCRQALVPRAFHASAVGLRSSDEQKQQPPNSFSQQHSETQGAEKPDPESSHSPPRYTDQGGEEEEDYESEEQLQHRILTAALEFVPAHGWTAEAIAEGAQSLGLSSAAASMFGKDGSELILHFVTQCNTRLTRVLEEEQKLVQLGQAEKRKTDQFLRDAVETRLRMLIPYIEHWPRALSILMLPHNIPSSLSLLTSMVDDMWHYAGDQSTDFNWYTRRAMLAAIYNTTELVMMQDSSPDFEDTWRFLENRVNDAMNMGHTAKQVKSTGEALVQGLMGAAVTLKNLTGLNQRR
Protein: Peroxisomal membrane protein PEX14 (Peroxin-14) (Q9HG09)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX20 receptors. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 (or PEX20) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:11329173}; Peripheral membrane protein {ECO:0000269|PubMed:11329173}; Cytoplasmic side {ECO:0000269|PubMed:11329173}.
Interaction partners:
Sequence:
MSSIREEMVTSAVEFLKNPQIADSPLAKKIEFIESKGLNEAEVKEALLRSQGGNGSSSVASQVSSYSPSASQSSVAPSPPPFPDHYRNAPPLPERDWKDYFVMATATAGVSFGLYKVISNYVLPKLLPPSKEAIELDKEAIDREFTRVEALLNTFEEDQKAFYEEQREKSGKIEDTLTEIDAIISKTNEKNLNNEESLKYLKLEIESIKNTLMKNIDSQKSTISSELGSIEAQLDELKKLIVAKPEDEPIRAAPQPSLTTGANSLTSESSGRSSIPHSQSVPIRTQLTTPPSDSDTSGPAKLHIPPATSIPSLKDILRKEKNRTVDTFSKSNLGKDLESVAQSDPDKVEKYEGRRDLKSLERPEEDEKKEDDVEDGGDKDKLASSLESVKLPPSSEQVQAPAPKERTSSSSSRSGIPAWQLAAQS
Protein: Snaclec purpureotin subunit alpha (P0DJL2)
Organism: Trimeresurus purpureomaculatus (Mangrove pit viper) (Cryptelytrops purpureomaculatus)
Function: Snaclec that induces platelet aggregation without any cofactor in a dose-dependent manner. Its platelet aggregation effect is blocked by echicetin, suggesting it is a GPIb-binding protein which binds to the same or a closely related GPIb site on platelets as echicetin.
Subcellular location: Secreted.
Interaction partners:
Sequence:
DCPSDWSSFKQYCYQIIKQLKTWEDAERFCLDQMKGAHLVSIESYREAVFVAELLSENVKTTKYHVWIGLSVQNKGQQCSSEWSDGSTVSYENLVKPNPKKCFVLKKESEFRTWSNVYCEQKHIFMCKFLGSR
Protein: Gallinacin-10 (Gal-10) (Beta-defensin 10) (Gallinacin-8) (Gal-8) (Q6QLQ9)
Organism: Gallus gallus (Chicken)
Function: Has bactericidal activity.
Subcellular location: Secreted. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- Gallinacin-9
- Gallinacin-8
- Gallinacin-12
- Gallinacin-1
- Gallinacin-3
- Gallinacin-14
- Gallinacin-6
- Gallinacin-11
- Gallinacin-13
- Gallinacin-4
Sequence:
MKILCLLFAVLLFLFQAAPGSADPLFPDTVACRTQGNFCRAGACPPTFTISGQCHGGLLNCCAKIPAQ
Protein: Neuronal acetylcholine receptor subunit beta-4 (Neuronal acetylcholine receptor non-alpha-3 chain) (N-alpha 3) (P26153)
Organism: Gallus gallus (Chicken)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-6
- Acetylcholine receptor subunit alpha
Sequence:
STAADAEEKLMNHLLSPDRYNKLIRPAVNSSQLVSIELQVSLAQLISVNEREQIMTTNVWLNQEWIDYRLAWKPSDYEGINMLRIPAKHIWLPDIVLYNNADGTYEVSLYTNAIVQNNGSIRWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKTSMASMDDFTPSGEWDIVALPGRRTENPLDPNYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMPPWVKLVFLERLPAYLFMKRPENNSPRQKPANCKKTRAENLCMDPADFYKNSTYFVNTASAKKYDMKITDTLDNVSSHQDFRLRTGTKFSPEVQEAIDGVSFIAEHMKSDDNDQSVIEDWKYVAMVVDRLFLWIFVLVCVLGTVGLFLQPLFQNHIAATNP