wanglab/gogpt-training-data huggingface dataset:
Protein: Anthrax toxin receptor 2 (Q6DFX2)
Organism: Mus musculus (Mouse)
Function: Necessary for cellular interactions with laminin and the extracellular matrix.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P58335}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Anthrax toxin receptor 1
- Low-density lipoprotein receptor-related protein 6
Sequence:
MVAGRSRARSPGSWLFPGLWLLAVGGPGSLLQAQEQPSCKKAFDLYFVLDKSGSVANNWIEIYNFVHQLTERFVSPEMRLSFIVFSSQATIILPLTGDRYKIGKGLEDLKAVKPVGETYIHEGLKLANEQIQNAGGLKASSIIIALTDGKLDGLVPSYAENEAKKSRSLGASVYCVGVLDFEQAQLERIADSKDQVFPVKGGFQALKGIINSILAQSCTEILELSPSSVCVGEKFQVVLTGRAVTSISHDGSVLCTFTANSTYTKSEKPVSIQPSSILCPAPVLNKDGETLEVSISYNDGKSAVSRSLTITATECTNGIAAIVAILVLLLLLGAALMWWFWPLCCKVVIKDPPPPPSAPMEEEEEDPLPNKKWPTVDASYYGGRGVGGIKRMEVRWGDKGSTEEGARLEKAKNAVVMVPEEEIPIPSRPPRPRPTHQAPQTKWYTPIKGRLDALWALIMKQYDRVSLMRPQEGDEGRCINFSRVPHQ
Protein: Polar amino acid uptake family ABC transporter, periplasmic substrate-binding protein, putative (Q5LP13)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Polar amino acid uptake family ABC transporter, permease protein
- Glutamine ABC transporter, ATP-binding protein
- histidine kinase
- Polar amino acid uptake family ABC transporter, permease protein
Sequence:
MNRLFQILEAICLIGIMMRPVHAETWVVGSMEGFAPFNYSINGEYSGIDVQILNEAAERIGVTLDHRPLPWKRALLDFETGQLDAVFQLAPTPERFQKWNMVGPLRRTRTVFATLKGSPIQDIRSLSDLDGLVVGVVSGFTYEARFDSYQLLQREASLDDFTNLRKLLLGRSDLIVGGYETLHYVASELNALDKLKFLPTPLAEHARYIGFHRTPEGDDMARRLQAELERMQANRIPPEYLRYYFSR
Protein: Transcription factor protein (F7ABQ1)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHTDHANIGGASNPPTLLGGLGVSDETSYPILSNPFNDIEHGQGMNAGFTFGQNPDYFDYNDTSDNGSPSPCDGQRTPSTCNSWAASPYSALDTSLAISPQQSPCHPSMVEKLTHKLSLPERQTSLSIAIEVLGTCENPSLPFQNYDYPPTPTSNVSDDHFTPGDSPISAPPRLRTFSGFEARDWLKCDDVNNRTRSYSSNSASGGVVDLTNLMEPIVLPETYIHLNNNTTPHHTLPPHANQPSQPINPQSTCIETPTRPPTLQSLPSIVEDAIAQAKPFEMLEESSLDVHGMLDDIMDVGNTQQQNPSHDVVVIQEDHCYSSQTLTIVENPVEEVLAVKPDPVVDLTDAPSTSGVKVSRKRDRNNAACRESRKKKKMKLVEAEMEVVRLVEDNEVQRLKIARLEVEVKETKALLLSKMTGKTVKP
Protein: MADS-box protein AGL35 (MADS-box transcription factor family protein) (Q7XJK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Putative clathrin assembly protein At1g33340
- Ribosome biogenesis protein NOP53
- Putative clathrin assembly protein At5g65370
- Putative clathrin assembly protein At1g14686
- Putative clathrin assembly protein At1g14910
- Putative clathrin assembly protein At5g10410
- Putative clathrin assembly protein At4g25940
- Putative clathrin assembly protein At5g35200
- Reverse transcriptase
- Putative clathrin assembly protein At5g57200
Sequence:
MTRQKVKMTFIENETARKSTFKKRKKGLLKKAQELGILCGVPIFAVVNSPYELNPEVWPSREAANQVVSQWKTMSVMDKTKKMVNQETFLQQRITKATESWKKLRKENKELEMKNIMFDCLSGKTLVSSIEKTELRDFGYVIEQQLKDVNRRIEILKRNNEPSSALVPVAAPTTSSVMPVVEMGSSSVGFYDKVRDQIQITLNMKQTTNDLDLNKKQW
Protein: PcaQ transcriptional activator (Q92TL9)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MIDARVKFRHLQTFVEVARQKSVVKAAELLHVTQPAVTKTIRELEEVLGVAVFEREGRGIKITRYGEVFLRHAGAALTALRQGLDSVSQERSGEGPPIRVGALPTVSTRIMPRAIALFLKEKTGARIKIVTGENAVLLEQLRIGDLDLVVGRLAAPDKMTGFSFEHLYSEQVVFAVRAGHPLISGRQSLFAHLSDYPVLMPTRASIIRPFVEHFLIANGIAGLPNQIETVSDSFGRAFVRSSDAIWIISAGVVATDIADGVLAALPVDTSETRGPVGLTMRTDAIPSLPLSILMQTLREVAGTAMAAEAKRTA
Protein: Aladin (Q8GWR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP155
- Protein SEH1
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP35
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP85
- Nuclear pore complex protein GP210
Sequence:
MASFPHPGSVTVCEINRDLITAQNLSDERAQETYGKVLGMVFSPVSFDSTPSSLQENEGQENGDKASGESKGLVATLQMKVADSLKQILQPTDVTLLSEIDLQGVSWHQGKHIIAFISGANQVTIRDYEDKDEKEPCILTSDSQRNVKALEWRPNGGKSLSIACRGGICIWAASYPGNMALVRSGGSALRGSLSRGSGTRWILVDFLRCQNDEQISALSWSPCGRYLASASYDSSSFTIWDVSQGAGTPIRRGLGGISMLKWSPTGDYFFAARFDGTFCLWETNTWTSEPWSLSSGSGSVTGAIWDPEGRFILISFSKSSTLGSVHFSSKPPSLDAHLLPVELPEIASLTGCEGIEKIAWDASGERLAVSYKGGDENYKGLIAIYDTRRTPIVSASLVGFIRGPGENPKALSFSFHDKFKQGPLLSVCWSTGFCCTYPLIFRSHVLP
Protein: Phosphoglycerate mutase (EC 5.4.2.11) (EC 5.4.2.4) (Q7TP58)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Triosephosphate isomerase
- Triosephosphate isomerase.
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- Phosphoglycerate kinase 1
- Glucose-6-phosphate isomerase
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
- Alpha-enolase
- Beta-enolase
Sequence:
MSKHRLIILRHGEGQWNKENRFCSWVDQKLNSDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREKMALNHGEEQVRLWRRSYNVTPPPIEESHPFFHEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWKERISPEILKGKTVLISAHGNSSRALLKHLEVLSDGLSLENSLLRSYCLLLHLSVTVTRLSMLSSILPMKILSLKVIFLVELRMDFLCILDEHCPWATVPDHTGTEGSRRCWTPSGWSSGGYELQVSSGNWTWKSSISDEDIINITLPTGVPILLELDENLRAIRPHQFLGNQEAIQAAIKKVDDQGKSHGWALEKASENHSSTRPFDFPQPTAILFAVSKINFSQ
Protein: H/ACA ribonucleoprotein complex subunit 1 (GCR 101 snRNP) (Nucleolar protein family A member 1) (Ribonucleoprotein Gar1) (Q7KVQ0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P28007}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 4
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit 3
- rRNA 2'-O-methyltransferase fibrillarin
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 56
- Nucleolar protein 58
- IP08469p
- Protein SHQ1 homolog
- Telomerase Cajal body protein 1 homolog
Sequence:
MGFGKPRGGGGGGGRGFGGGGGGGGRGFGGGGGGRGGGGGRGGGGGFGRGGGGRGGGRGAFDTGPPERVIPLGNYVYSCQNDLVCKVDIQDVPYFNAPIFLENKEQVGKIDEIFGTVRDYSVSIKLSDNVYANSFKPNQKLFIDPGKLLPIARFLPKPPQPKGAKKAFTNNRGGGGGGGGFGGRGGGRGGGGRGGGGGRGGGGFRGGAGRNGGGGGGGGFNRGRGGGGGGGGGRGRW
Protein: Motility protein B (Chemotaxis protein MotB) (P0AF06)
Organism: Escherichia coli (strain K12)
Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:2447650}; Single-pass type II membrane protein {ECO:0000269|PubMed:2447650}. Note=The OmpA-like domain probably functions to anchor the complex to the cell wall.
Interaction partners:
- Motility protein A
- Chemotaxis protein CheA
- Chemotaxis protein CheW
- Flagellar motor switch protein FliG
- Flagellar M-ring protein
- Flagellar hook-associated protein 1
- Flagellar motor switch protein FliM
- Flagellar transcriptional regulator FlhC
- Flagellar basal-body rod protein FlgC
- Protein phosphatase CheZ
Sequence:
MKNQAHPIIVVKRRKAKSHGAAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGDRISNSESPIPGGGDDYTQSQGEVNKQPNIEELKKRMEQSRLRKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFRTGSADVEPYMRDILRAIAPVLNGIPNRISLSGHTDDFPYASGEKGYSNWELSADRANASRRELMVGGLDSGKVLRVVGMAATMRLSDRGPDDAVNRRISLLVLNKQAEQAILHENAESQNEPVSALEKPEVAPQVSVPTMPSAEPR
Protein: Retinol dehydrogenase 1 (All trans) (Retinol dehydrogenase type 1) (Q8CGV4)
Organism: Mus musculus (Mouse)
Interaction partners:
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol 13,14-reductase
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Selection and upkeep of intraepithelial T-cells protein 8
- Diacylglycerol O-acyltransferase 1
Sequence:
MWLYLVALVGLWTLLRFFRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTKMIWDKASSEVKEIYGEKFLLFYLKNLNELDKRCNKDLSVVTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALLYWTSMKPEKAL
Protein: Tubulin alpha chain (F8VQQ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTE
Protein: RNA polymerase sigma factor sigA (Sigma factor A) (Sigma-A) (RNA polymerase sigma factor sig1) (Atsig1) (Sigma factor 1) (RNA polymerase sigma factor sig2) (Atsig2) (Sigma factor 2) (RNA polymerase sigma factor sigB) (Sigma factor B) (Sigma-B) (O24629)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Controls the transcription of the psaA gene and thus modulates photosystem stoichiometry. Thereby maintains a harmonious electron flow and photosynthetic efficiency.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:9405719}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II and V subunit 6B
- Dynein beta chain, ciliary protein
- DNA-directed RNA polymerase I subunit 1
- DNA-directed RNA polymerase III subunit 1
- Orf03 protein
- Chloroplast sensor kinase, chloroplastic
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MATAAVIGLNTGKRLLSSSFYHSDVTEKFLSVNDHCSSQYHIASTKSGITAKKASNYSPSFPSSNRHTQSAKALKESVDVASTEKPWLPNGTDKELEEECYDDDDLISHSVEAILLLQKSMLEKSWNLSFEKAVSSEYPGKGTIRKKKIPVITCSGISARQRRIGAKKKTNMTHVKAVSDVSSGKQVRGYVKGVISEDVLSHVEVVRLSKKIKSGLRLDDHKSRLKDRLGCEPSDEQLAVSLKISRAELQAWLMECHLAREKLAMSNVRLVMSIAQRYDNLGAEMSDLVQGGLIGLLRGIEKFDSSKGFRISTYVYWWIRQGVSRALVDNSRTLRLPTHLHERLGLIRNAKLRLQEKGITPSIDRIAESLNMSQKKVRNATEAVSKVFSLDRDAFPSLNGLPGETHHSYIADTRLENNPWHGYDDLALKEEVSKLISATLGEREKEIIRLYYGLDKECLTWEDISKRIGLSRERVRQVGLVALEKLKHAARKRKMEAMILKN
Protein: Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III) (P49243)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. KAS III catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities (By similarity).
Subcellular location: Plastid, chloroplast.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- EMBRYO DEFECTIVE 3147
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
- Biotin carboxylase, chloroplastic
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 1, chloroplastic
Sequence:
MANASGFFTHPSIPNLRSRIHVPVRVSGSGFCVSNRFSKRVLCSSVSSVDKDASSSPSQYQRPRLVPSGCKLIGCGSAVPSLLISNDDLAKIVDTNDEWIATRTGIRNRRVVSGKDSLVGLAVEAATKALEMAEVVPEDIDLVLMCTSTPDDLFGAAPQIQKALGCTKNPLAYDITAACSGFVLGLVSAACHIRGGGFKNVLVIGADSLSRFVDWTDRGTCILFGDAAGAVVVQACDIEDDGLFSFDVHSDGDGRRHLNASVKESQNDGESSSNGSVFGDFPPKQSSYSCIQMNGKEVFRFAVKCVPQSIESALQKAGLPASAIDWLLLHQANQRIIDSVATRLHFPPERVISNLANYGNTSAASIPLALDEAVRSGKVKPGHTIATSGFGAGLTWGSAIMRWR
Protein: AT4g03150/F4C21_7 (Plant/protein) (Q944G6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSWVCSSVTRNVVKSHPLSLTKHLDFPATIRRRSVSFPATIRRRSVSFPITSAPKFPSLKLQKSQSSIHEGEEDSESAVQALTIPEEWLLPSRAIEESEWLRVTLHKWLDDEYCPEPTNVEISEVAAKSYYSSLLEKESDMGEILLKMAQDLTSISYQESFHGAFTSANAAINLIVDRIETGLV
Protein: Integral membrane protein 2C (Transmembrane protein BRI3) [Cleaved into: CT-BRI3] (Q91VK4)
Organism: Mus musculus (Mouse)
Function: Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:14592447}; Single-pass type II membrane protein {ECO:0000269|PubMed:14592447}. Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MVKISFQPAVAGIKADKADKAAASGPASASAPAAEILLTPAREERPPRHRSRKGGSVGGVCYLSMGMVVLLMGLVFASVYIYRYFFLAQLARDNFFHCGVLYEDSLSSQIRTRLELEEDVKIYLEENYERINVPVPQFGGGDPADIIHDFQRGLTAYHDISLDKCYVIELNTTIVLPPRNFWELLMNVKRGTYLPQTYIIQEEMVVTEHVRDKEALGSFIYHLCNGKDTYRLRRRSTRRRINKRGGKNCNAIRHFENTFVVETLICGVV
Protein: Beta-defensin 4 (BD-4) (mBD-4) (Defensin, beta 4) (P82019)
Organism: Mus musculus (Mouse)
Function: Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria. May act as a ligand for C-C chemokine receptor CCR6. Can bind to mouse (but not human) CCR6 and induce chemotactic activity of CCR6-expressing cells.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-defensin 14
- Beta-defensin 1
- Late cornified envelope 3B
Sequence:
MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTNGAICWGPCPTAFRQIGNCGHFKVRCCKIR
Protein: LD41072p (Q960P7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVIKKEEDDLRGLEELYYGISDGTDEYHEIFPYSTPRTVHNELAKTVECPICLNGDSFDSNEKLQTHLVSHISPEGKQHQFQCLFCLEKHPTESVLAKHNQIMHPTETKTEGSPSYYCLICQQRHNSLHLLTAHLQKVHSTLELPYWCHSCGYRSSSHRDLVRHFYDDHKHQNFLQCPYCLDIFYFSKLGVVNQLRIEHYFMHLDEHINKRDPSLRCQKCSLSFLEKGDLKQHAVQHHVSMTKTNRPVRLLLNNSMLIPPPKIRTHHREQPPFSTYKRPVFFAFLEGKTCAECNTDFASEETHYTGWLHCVKCNYQTCCERAQFRHGVECNGNFVDAMEVNMPQEMHCICGFATGNGNKMAQHLANCGLSTCYPSLEAASENAVKRNMLDMLGLVRRDGETSGEGADISETADDVADQSSDMLPPQEDHHLQQHHQQVGHQQQMQGQPNEPQAELQQEYLSAPVEHEPVQNMPVHQSMPVQQTGPIQFGEMEAAPVLLDTQQQVQPTPDYAQVSVVQQHQQQQPYGLSNYGQSSLATDIDMPLIGELSEPNAPPTPQFLGEVHTPMFDAVAAAEQQHYHAQHHHHPQ
Protein: Arginase (EC 3.5.3.1) (Q12611)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Ornithine aminotransferase
- Ornithine decarboxylase
- argininosuccinate lyase
- Ornithine carbamoyltransferase, mitochondrial
- SPEE_NEUCR Spermidine synthase
- Putative urea carboxylase
- Arginine biosynthesis bifunctional protein ArgJ
- Probable carboxypeptidase AN5749
- Urease
- Hypothetical arginase family protein
Sequence:
MTSPSTIKQRFLSKPNQLGVVAVGFNGGQCKLGVEAAPMALVEAGLLDQLRDDLDYEIHYDNTVHYYEKEIPAEDPDHRGMKKPRAVSAVTETLSSQVYEHSKEGKFTLTLGGDHSIAIGSISGIAKATRERLGREIGVIWVDAHADINIPEMSPSGNIHGMPMAFLTRLATEEKKDIFGWLQEEHKVNLRKLVYIGLRDVDRGEKKLLREHGIKAFSMHDVDRHGIGRVVEMALAHIGNDTPIHLSFDVDALDPQWAPSTGTPVRGGLTLREGDFICECVHETGNLISMDLVEVNPSLEAVGASDTIRTGCSLVRSALGDTLL
Protein: L-ascorbate peroxidase 1, cytosolic (AP) (AtAPx01) (EC 1.11.1.11) (Q05431)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in hydrogen peroxide removal. Constitutes a central component of the reactive oxygen gene network.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase DHAR1, mitochondrial
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione S-transferase DHAR2
- Monodehydroascorbate reductase 3
- Glutathione S-transferase DHAR3, chloroplastic
- Monodehydroascorbate reductase 1, peroxisomal
- Monodehydroascorbate reductase 2
- Superoxide dismutase 1, chloroplastic
- Glutathione reductase, chloroplastic
- Monodehydroascorbate reductase, chloroplastic/mitochondrial
Sequence:
MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA
Protein: Leucine-rich repeat-containing protein 38 (BK channel auxiliary gamma subunit LRRC38) (Q5VT99)
Organism: Homo sapiens (Human)
Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-1
Sequence:
MRPRAPACAAAALGLCSLLLLLAPGHACPAGCACTDPHTVDCRDRGLPSVPDPFPLDVRKLLVAGNRIQRIPEDFFIFYGDLVYLDFRNNSLRSLEEGTFSGSAKLVFLDLSYNNLTQLGAGAFRSAGRLVKLSLANNNLVGVHEDAFETLESLQVLELNDNNLRSLSVAALAALPALRSLRLDGNPWLCDCDFAHLFSWIQENASKLPKGLDEIQCSLPMESRRISLRELSEASFSECRFSLSLTDLCIIIFSGVAVSIAAIISSFFLATVVQCLQRCAPNKDAEDEDEDKDD
Protein: Slit-3 (Q90XG4)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
QTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSNPRRLANKRISQIKSKKFRCSGSEDYRSKFTGKCFMDLVCPEKCRCEGTVVDCSNQKLTRLPSHLPEYTTDLRLNDNDISVLEAIGLFKKLPNLRKINLSNNKIKEIREGTFDGASGVQELILTENQLESVHGRMFRGLTGLKTLMLRSNSISCINNDTFAGLSSVRLLSLYDNHISTITPGAFSTLVSLSTINLLANSFNCNCHLAWLGKWLRKKRIVSGNPRCLKPFFLKDIPIQDVDAQDFTCEGNDESSCLLSPPCPSQCTCVDSVVRCSNKGLRVMPKGIPKDVTELYLEGNHLTAVPKGLSAFRHLTLIDLSNNSISVLANYTFSNMTQLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPEGSFNDLVSLSHLALGTNPLHCDCNLRWLSEWVKAGYKEPGIARCSGPEAMVDRLLLTTPTHHFQCKEPVDISVVSKCNPCLSNPCKNNGTCSNDPVEFYQCTCPFGFKGRDCSVPINSCIQNPCQNGGTCHLTEANKDGFSCSCPLGYEGERCEINPDDCEDNDCENNSTCVDGINNYVCLCPPNYTGELCDEVINHCIPELNPCQHESKCVPLDKGSRCECLPGYSGKHCEIDDDDCVGHKCRHGAVCVDAVNGYTCVCPQGFSGLFCETPPPMVLLQTSPCDNYECQNGAQCIVAHQEPVCRCLAGFAGQKCEKLITVNFVGKDSYVELPSAKIRPQANISLQVATDKDNGILLYKGDNDPLALELYQGHVRLIYDTLNSPPTTVYSVETVNDGQFHSVELVMLNQTLNLVVDKGTPKSLGKLQKQSSVSLNTPLYIGGIPTSTGLSSLRQGADKTPNGFHGCIHDVRINNELQDFKDLPQQSIGVLPGCKSCNICKHGICRSLEKTSVVCECHPGWTGPLCDQEIGDPCLNHKCLHGKCMAANVAYTCKCMEGYTGTYCDKKNNSSNPCRILKCNHGQCKISEHGEPYCECDPNYSGDHCDRENLCQGEIIREVVRKQQGYTTCVTASKVPRMECHGSCGSGQCCVPLRSKRRKYFFQCVDGSTFTEELERHVECGCSKCS
Protein: Protein Frey (Frey regulator of sperm-oocyte fusion 1) (FREY1) (Q8CF31)
Organism: Mus musculus (Mouse)
Function: Key regulator for male fertility expressed transiently in round spermatids where it recruits IZUMO1 at the endoplasmic reticulum (ER) membrane and coordinates the oolemmal binding multimeric complex (IZUMO1 complex) assembly. Upon complete assembly of the IZUMO1 complex, its ER retention is released, facilitating IZUMO1 complex export to the acrosome. Through the interaction with SPPL2C, inhibits its intramembrane protease activity directly accessing the catalytic center of an I-CLiP.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35960805}; Single-pass type II membrane protein {ECO:0000269|PubMed:35960805, ECO:0000269|PubMed:36050562}.
Interaction partners:
Sequence:
MVLAMLGALYPRAGLSLFLFYLILAGALLRPQPQRSQQSVPEEFSAPLELLQPLSGLVDDYGLRPKHPRPGGPRPLLSQAQQRKRDGPNMADYYYDVNL
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (P20445)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in osmoadaptation.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase
- Multifunctional tryptophan biosynthesis protein
- Transaldolase
- Orotidine 5'-phosphate decarboxylase
- Phosphoketolase, putative
Sequence:
MAPKVGINGFGRIGRIVFRNAIEAGTVDVVAVNDPFIETHYAAYMLKYDSQHGQFKGTIETYDEGLIVNGKKIRFHTERDPANIPWGQDGAEYIVESTGVFTTQEKASAHLKGGAKKVVISAPSADAPMFVMGVNNETYKKDIQVLSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHSYTATQKVVDGPSAKDWRGGRTAATNIIPSSTGAAKAVGKVIPSLNGKLTGMAMRVPTSNVSVVDLTVRTEKAVTYDQIKDAVKKASENELKGILGYTEDDIVSTDLNGDTRSSIFDAKAGIALNSNFIKLVSWYDNEWGYSRRVVDLITYISKVDAQ
Protein: Actin-11 (EC 3.6.4.-) (P53496)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-depolymerizing factor 6
- Tubulin alpha-5 chain
- Actin-related protein 9
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Actin-related protein 4
- Actin-related protein 2
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Actin-related protein 2/3 complex subunit 3
- Tubulin alpha-6 chain
- Tubulin alpha-2 chain
Sequence:
MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELPDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
Protein: Coiled-coil domain-containing protein 136 (Q3TVA9)
Organism: Mus musculus (Mouse)
Function: May play a role in acrosome formation in spermatogenesis and in fertilization.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:27076447}; Single-pass membrane protein {ECO:0000305}. Note=Exclusively localized on a peripheral part of acrosome membrane (Golgi phase), localized on the equatorial segment of the acrosome (maturation phase). {ECO:0000269|PubMed:27076447}.
Interaction partners:
Sequence:
MQAMDGEVLLPALYEEEEEEEEEEEEVEEEQVEKGGSLGSLSMGKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQLRLLRCTPVESQSEKELMCRLQKLQAQHQCSVNEKEQLLEVQHHLHDKLRCHESEVHRLRSMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEENGNCSNKCDALLARLTELQDKFKASQEEIGHLQMEQCELLEDQRRLQEEQGQLQEELHRLTFPQPKCGILQKSQELLSKLQDLCEMQLLYQNMQEQQRKLTQNQECVLKEQLEAHKHLRGFKESHFQEVLANPQDARGPKSSSCENKFKVLMDQLQALQVLYDTSQKQQEVLQREHGRLMEERKRLQAELQLCMEEMQVLQTQSPMIKRSFEYCGKNSGSRAPSTENFHRSYESSIDENEGYQKSYVSSQPSTETFLKSYDSSTSANEAFEKSYCSSSTSVSYKKSYGSVSSGETLHRSYASSSTDEDPAEPEDLEHFEETVAKVLTKLQAVKALYQVSQEEHCQLQQRMHRLLAKQKELTEELQCCEKELRECMESLGKPLPPQSDKCEIKELQTKLRELQLQYQASMDEQGRLLAVQEQLEGQLQCCQEELRQLKENRPSISSEARGKNVNKNMNKNANGVRNKKLSMACSEDLENGFENEKNLEVMLYYKASQRRLDELMKEEKEIEEARKKEREKKAKKDLCKLATNPAADPRAEPEPTEDEEENFEEYREGEDESCEAAEEGNPLKLSESKKPSPAPDPPIFSLPLVGLVVISALLWCWWAETSS