wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase B (DdHdaB) (Type-1 histone deacetylase 2) (EC 3.5.1.98) (Q55BW2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). May play a role in the regulation of the timing of gene expression during the development and in the definition aspects of the phenotype that mediate social behavior in genetically heterogeneous groups.
Subcellular location: Nucleus {ECO:0000269|PubMed:19576222}. Cytoplasm {ECO:0000269|PubMed:19576222}.
Interaction partners:
- Probable histone-binding protein rbbD
- NuA4 complex subunit EAF3 homolog
- PHD zinc finger-containing protein
- WD40 repeat-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Paired amphipathic helix containing protein
- Histone-lysine N-methyltransferase SETD7
- Polyubiquitin-D
- Polyubiquitin-A
Sequence:
MEYNTILNNTSKTRVCYFFDQDVGNYFYGPYHPMKPHRLCLTNNLVLNYGLHKKMHLYKARPADAEDMLKFHSEDYVDFLERVTPENINEWKDVKRFHIGEDCPVFPGLYDYCSIYSGGSIEGALKLNHRMYDIAINWSGGLHHARKDEASGFCYVNDIVLAILELLKFHARVLYIDIDVHHGDGVQEAFYLTDRVMTVSFHKFGGDFFPGTGDIDEIGAKTGKLYSVNVPLADGIDDKNYLNIFKPVIQGVMDYYRPSVIVLQCGADSLRFDRLGCFNLTIKGHAECVRFVKSFNIPTLVLGGGGYTVRNVARCWTYETSVCVDTEVNNELPYNDYIQFYSPDFQLIPDYTGLPFKYENANTKSYLESLRIKILENLRILQWAPSVQIQDVPPDIMPIDFDRDEDSKENMDKRKKKHNDFS
Protein: Subtilisin-like protease (Subtilase) (EC 3.4.21.-) (A0A0M3R8G2)
Organism: Petunia hybrida (Petunia)
Function: Required for arbuscular mycorrhiza (AM) development during AM symbiosis with AM fungi (e.g. Glomeromycota intraradices).
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:A9QY40}. Note=Accumulates in the intercellular spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal (AM) symbiosis. {ECO:0000250|UniProtKB:A9QY40}.
Interaction partners:
Sequence:
MTCICIFSIAFLLSFHLTTAQRSTGLQTYIVHVDKPDAQVLANSADLESYYNSFLPATVSGSEVPSRIIHSYHHVATGFAAKLSGEEVKEMEKKAGFVSAKLEKVLTLHTTHTPNFLGLYQNMGFWQESNYGKGVIIGLLDTGITPGHPSFSDVNMPSPPAKWKGKCEFTGNATCNKKIIGARNFISGSGVPPTDEEGHGTHTASTAAGNFVNDANVFGNANGTAVGMAPLAHIAMYKVCSEDGCSDADILAALDAAIDDGVDVLSLSLGGYSDPFYYDNIAIGAFAAIRKGIFVSASAGNDGPLNSTLSNEAPWILTVGASTHDRKIVATAVLGNGQQYDGESAFQPADFPHTLLPLVYPGTSDEEAAFCSSGSLDKFDVKGKVVVCDRGGDVARLEKSQTVKDAGGAAMILANLEIDGEGTFADAHVLPATHVGYAAGEMIKSYINSTSTPTAGILFKGTIIGFKSSPSVSSFSSRGPNLASPGIVKPDIIGPGVNILAAWPVSVENKTGTDLTFNIISGTSMSCPHLSGIVALLKSAHPDWSPAAIKSAIMTSADQSNLEGQPILDERNLPADIFATGAGHVNPSKASDPGLIYDIQLEDYIQYLCGLGYREKDIGLIVQETVKCESSISEAELNYPSFSIILGPKTQNYTRTVTNVGDASSTYTVNIAKTQGVDIVVEPATLVFTKMYQQATYTVSFTQSGDFTDRFVQGAISWSSNEYVVRSPISVKLE
Protein: Ig lambda-3 chain C region (P01845)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
QPKSTPTLTMFPPSPEELQENKATLVCLISNFSPSGVTVAWKANGTPITQGVDTSNPTKEDNKYMASSFLHLTSDQWRSHNSFTCQVTHEGDTVEKSLSPAECL
Protein: Sodium-dependent neutral amino acid transporter B(0)AT2 (Sodium- and chloride-dependent neurotransmitter transporter NTT73) (Solute carrier family 6 member 15) (Transporter v7-3) (Q8BG16)
Organism: Mus musculus (Mouse)
Function: Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for methionine and for the branched-chain amino acids, particularly leucine, valine and isoleucine. Can also transport low-affinity substrates such as alanine, phenylalanine, glutamine and pipecolic acid. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:16185194}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPKNSKVVKRDLDDDVIESVKDLLSNEDSVEEVSKKSELIVDVQEEKDTDAEDGSEADDERPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLLPYLILLLVIGIPLFFLELSVGQRIRRGSIGVWNYISPKLGGIGFASCVVCYFVALYYNVIIGWTLFYFSQSFQQPLPWDQCPLVKNASHTYVEPECEQSSATTYYWYREALDITSSISDSGGLNWKMTVCLLVAWVMVCLAMIKGIQSSGKIMYFSSLFPYVVLICFLIRSLLLNGSIDGIRHMFTPKLEMMLEPKVWREAATQVFFALGLGFGGVIAFSSYNKRDNNCHFDAVLVSFINFFTSVLATLVVFAVLGFKANIVNEKCISQNSEMILKLLKMGNISWDVIPHHINLSAVTVEDYRLVYDIIQKVKEEEFAVLHLNACQIEDELNKAVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLINLGLGSMFGTIEGIITPIVDTFKVRKEILTVICCLLAFCIGLIFVQRSGNYFVTMFDDYSATLPLLIVVILENIAVSFVYGIDKFIEDLTDMLGFAPSKYYYYMWKYISPLMLLTLLIASIVNMGLSPPGYNAWIKEKASEEFLSYPMWGMVVCFSLMVLAILPVPVVFIIRRCNLIDDSSGNLASVTYKRGRVLKEPVNLEGDDASLIHGKIPSEMSSPNFGKNIYRKQSGSPTLDTAPNGRYGIGYLMADMPDMPESDL
Protein: Chloroplast protein FOR GROWTH AND FERTILITY 1 (Q94A99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with CGF2, essential protein which supports female gametogenesis and embryogenesis, probably by securing local energy supply.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:32306898}; Multi-pass membrane protein {ECO:0000255}. Plastid membrane {ECO:0000269|PubMed:32306898}; Multi-pass membrane protein {ECO:0000255}. Note=Present in chloroplasts on green tissues as well as in plastids of roots and seeds. {ECO:0000269|PubMed:32306898}.
Interaction partners:
Sequence:
MERLLQPSSSSSSISPSKFPSRTSPFLPRLRSSGLSFVSTHRPESRRVSSISCNSSQIPSLYTPIGSNTTNNSFNGSPKSDESKPNPGFLTRIATSASEQRKTLSTGTVILISAVAVLLLNPLLAPPAFASFQTAAKSGWLTSAWTGFLAGCLHTLSGPDHLAALAPLSIGRSKMESAAVGALWGCGHDAGQVIFGLLFLLLKDRLHIEVLQTWGTRIVGLTLVIIGAMGIKEASEIPEPCVALETDISMVSTEKEALPLPKKKKIGFATFATGVVHGLQPDALMIVLPALALPSRLAGSAFLIMFLVGTVIAMGSYTAFIGSCSEALKEKVPRITEKLTWVSSLVAIGLGLGIVISPFFGFSLY
Protein: Zinc-type alcohol dehydrogenase-like protein C16A3.02c (EC 1.-.-.-) (O42909)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Zinc-type alcohol dehydrogenase-like protein C2E1P3.01
- Aldo-keto reductase yakc [NADP
- Uncharacterized oxidoreductase P32A8.02
- Putative S-
- Uncharacterized oxidoreductase C8E4.04
- NAD/NADP-dependent indole-3-acetaldehyde reductase
- Spore wall structural constituent isp3
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MSSETKSEFGTKSAWLYNRTGKPKDVLYLEKGLHIPNPAELGPYDVLVEVVATSINPLDYKLMNTYQMIAKALFKLPNIPGYDFAGRVLAVGSEVKEFSATQRVWGCQSFPRAGRQGGSCATHIVTGDKDVWHLPDGVSFNEGAGFGIAGLTAWEVLVRQMKVKPGTKLVIEGASGGVGTFAVALAKALECEVTTISSTENLDLCKSLGATHTLDYKKDNLVERLADLGPYDFVFDCVNDNVLYRASSKFVKPDGAFFGIGGDITLSYVGSRLSRTLRPRVLGGSSHSYYNILLHVDQEMLRDFVDFVMKHNIKTVIDSVYDFEDTVEAFNRLMTHRCKGKVIIKTD
Protein: Centromere protein M (CENP-M) (Interphase centromere complex protein 39) (Proliferation-associated nuclear element protein 1) (Q9NSP4)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres.
Subcellular location: Nucleus. Cytoplasm. Chromosome, centromere, kinetochore. Note=Nuclear in non-confluent cells and cytoplasmic in confluent or dividing cells (By similarity). Localizes in the kinetochore domain of centromeres. {ECO:0000250}.
Interaction partners:
- Centromere protein U
- Histone H3-like centromeric protein A
- Centromere protein O
- Centromere protein K
- Centromere protein T
- Centromere protein Q
- Centromere protein H
- Centromere protein N
- Centromere protein C
- Centromere protein L
Sequence:
MSVLRPLDKLPGLNTATILLVGTEDALLQQLADSMLKEDCASELKVHLAKSLPLPSSVNRPRIDLIVFVVNLHSKYSLQNTEESLRHVDASFFLGKVCFLATGAGRESHCSIHRHTVVKLAHTYQSPLLYCDLEVEGFRATMAQRLVRVLQICAGHVPGVSALNLLSLLRSSEGPSLEDL
Protein: Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24] (Q99PW6)
Organism: Rattus norvegicus (Rat)
Function: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin.
Subcellular location: [Matrix metalloproteinase-24]: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed matrix metalloproteinase-24]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000250}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 3
- Metalloproteinase inhibitor 4
Sequence:
MPRSRGGRAAPGQAARWSGWRAPGRLLPLLPALCCLAAAAGAGKPAGADAPFAGQNWLKSYGYLLPYESRASALHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERQPRPPRPPLGDRPSTPGAKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCKQKEVERRKERRLPQDDVDIMVTIDDVPGSVNAVAVVVPCTLSLCLLVLLYTIFQFKNKTGPQPVTYYKRPVQEWV
Protein: Acetate CoA-transferase YdiF (EC 2.8.3.8) (Short-chain acyl-CoA:acetate CoA-transferase) (Q8X5X6)
Organism: Escherichia coli O157:H7
Function: CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.
Interaction partners:
- Short chain acyltransferase
- Short chain acyltransferase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Acetaldehyde dehydrogenase
- Acetaldehyde dehydrogenase
- Probable acyl-CoA dehydrogenase YdiO
- Probable acyl-CoA dehydrogenase YdiO
- Transporter
- H repeat-associated protein
Sequence:
MKPVKPPRINGRVPVLSAQEAVNYIPDEATLCVLGAGGGILEATTLITALADKYKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWALCGHWGQSPRISDLAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKEYLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVVDPDQSQLYGGAPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEGCADDFILTVETGPIGGITSQGIAFGANVNTRAILDMTSQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSKKIIFCGTLTAGSLKTEIADGKLNIVQEGRVKKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGLHLIEIAPGVDLQKDILDKMDFTPVISPELKLMDERLFIDAAMGFVLPEAAH
Protein: Eukaryotic translation initiation factor 5A (eIF-5A) (A4GVE9)
Organism: Leishmania donovani
Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23301}.
Interaction partners:
Sequence:
MSDEDHDFSHQGGGDNASKTYPLPAGALKKGGYVCINGRPCKVIDLSVSKTGKHGHAKVSIVATDIFTGNRLEDQAPSTHNVEVPFVKTFTYSVLDIQPNEDPSLPSHLSLMDDEGESREDLDMPPDVALATQIKEQFDSGKEVLVVVVSAMGTEQVLQTKNAAEK
Protein: CWF19-like protein 1 (C19L1) (Q69YN2)
Organism: Homo sapiens (Human)
Interaction partners:
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SYF2
- Lariat debranching enzyme
- CWF19-like protein 2
- Pre-mRNA-splicing factor ISY1 homolog
- Tuftelin-interacting protein 11
- Pre-mRNA-splicing factor SYF1
- Coiled-coil domain-containing protein 12
- Crooked neck-like protein 1
Sequence:
MAQKPLRLLACGDVEGKFDILFNRVQAIQKKSGNFDLLLCVGNFFGSTQDAEWEEYKTGIKKAPIQTYVLGANNQETVKYFQDADGCELAENITYLGRKGIFTGSSGLQIVYLSGTESLNEPVPGYSFSPKDVSSLRMMLCTTSQFKGVDILLTSPWPKCVGNFGNSSGEVDTKKCGSALVSSLATGLKPRYHFAALEKTYYERLPYRNHIILQENAQHATRFIALANVGNPEKKKYLYAFSIVPMKLMDAAELVKQPPDVTENPYRKSGQEASIGKQILAPVEESACQFFFDLNEKQGRKRSSTGRDSKSSPHPKQPRKPPQPPGPCWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLRRFFKSRGKWCVVFERNYKSHHLQLQVIPVPISCSTTDDIKDAFITQAQEQQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRIKKNFPLQFGREVLASEAILNVPDKSDWRQCQISKEDEETLARRFRKDFEPYDFTLDD
Protein: FK506-binding protein-like (WAF-1/CIP1 stabilizing protein 39) (WISp39) (O35450)
Organism: Mus musculus (Mouse)
Function: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Cyclin-dependent kinase inhibitor 1
- G2 and S phase-expressed protein 1
- Ankyrin repeat domain-containing protein 49
Sequence:
METSPISPMNEKNTAQPQQREENAQQILNTAIPFRQRSPGLLPEALKVGVRPDPANQIVETQEIEHPVAGFEGDSDQFQVSTNEMAEHLQASDLWYCPDGSFVKKIIVPGHGLDKPKLGSKCQVLALGFPFGSGMPEGWTELTIGIGQWREKMWGELMEKCLESMRQGEEAKIHLPGSSAPLAKLRLDSFTNGRDSWEMEAMEKEALAKEEHRRGTELFRAGNPQGAARCYGRALRLLLTLPPPGPPERTTLYANLAACQLLLGHPQLAAQSCDRVLEREPGHLKALYRRGVARAALGDLEKATADFKKVLAVDPKNRAAKEELGKVVIQGRKQDAGLARGLRKMFS
Protein: Zinc-binding ribosomal protein family protein (F4JUQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVNIPKTKNTYCKNKECKKHTLHKVTQYKKGKDSLAAQGKRRYDRKQSGYGGQTKPVFHKKAKTTKKIVLRLQCQSCKHFSQRPIKRCKHFEIVLIESCAGKMVDEMIFSCVCCGGPGCCGDRGEGPVGGGIDNEPVNVVVVVVEPGSQRRKMW
Protein: Aspergillopepsin-1 (EC 3.4.23.18) (Aspartic protease pepA) (Aspergillopepsin F) (Aspergillopepsin I) (Aspergillopeptidase A) (P41748)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A (By similarity). Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin. Thought to play a significant role in virulence.
Subcellular location: Secreted {ECO:0000269|PubMed:7558282}.
Interaction partners:
- Alkaline protease 1
Sequence:
MVVFSKVTAVVVGLSTIVSAVPVVQPRKGFTINQVARPVTNKKTVNLPAVYANALTKYGGTVPDSVKAAASSGSAVTTPEQYDSEYLTPVKVGGTTLNLDFDTGSADLWVFSSELSASQSSGHAIYKPSANAQKLNGYTWKIQYGDGSSASGDVYKDTVTVGGVTAQSQAVEAASHISSQFVQDKDNDGLLGLAFSSINTVSPRPQTTFFDTVKSQLDSPLFAVTLKYHAPGTYDFGYIDNSKFQGELTYTDVDSSQGFWMFTADGYGVGNGAPNSNSISGIADTGTTLLLLDDSVVADYYRQVSGAKNSNQYGGYVFPCSTKLPSFTTVIGGYNAVVPGEYINYAPVTDGSSTCYGGIQSNSGLGFSIFGDIFLKSQYVVFDSQGPRLGFAPQA
Protein: AKT serine/threonine kinase 2 (M0QZK3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMND
Protein: Sucrose synthase 1 (AtSUS1) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 1) (P49040)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- alpha-D-xyloside xylohydrolase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Probable fructokinase-1
Sequence:
MANAERMITRVHSQRERLNETLVSERNEVLALLSRVEAKGKGILQQNQIIAEFEALPEQTRKKLEGGPFFDLLKSTQEAIVLPPWVALAVRPRPGVWEYLRVNLHALVVEELQPAEFLHFKEELVDGVKNGNFTLELDFEPFNASIPRPTLHKYIGNGVDFLNRHLSAKLFHDKESLLPLLKFLRLHSHQGKNLMLSEKIQNLNTLQHTLRKAEEYLAELKSETLYEEFEAKFEEIGLERGWGDNAERVLDMIRLLLDLLEAPDPCTLETFLGRVPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALEIEMLQRIKQQGLNIKPRILILTRLLPDAVGTTCGERLERVYDSEYCDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDAAVELSKELNGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLDDKYHFSCQFTADIFAMNHTDFIITSTFQEIAGSKETVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEEKRRLTKFHSEIEELLYSDVENKEHLCVLKDKKKPILFTMARLDRVKNLSGLVEWYGKNTRLRELANLVVVGGDRRKESKDNEEKAEMKKMYDLIEEYKLNGQFRWISSQMDRVRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCKGGPAEIIVHGKSGFHIDPYHGDQAADTLADFFTKCKEDPSHWDEISKGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRLEARRYLEMFYALKYRPLAQAVPLAQDD
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q9U458)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}.
Interaction partners:
Sequence:
MPPKKKNKEHKINGKEKKKDIQSFKKDVETDNHKIPVDELLERLKTDPNMGLSFVEAKLRLEINGPNILTPQPPTPKWIVFLKTMFGGFAILLWAGSFLCFVGYLIQLQTQHEPPDDNLYLGIALTVLVIVTGLFTYFQVHKSSSIMDSFKNLVPQYATVVREGEINTVTSDEIVKGDIVEVKFGDRVPADIRILEAHGLKVDNSSLTGESEPQVRSTEFTHENPLETKNLAFFSTNVLEGTCRGVVIATGDSTVMGRIANLAAGLDDVQSPISREIQLFIRFITIFAIILGLSFFAISLTLGYEFIDAVVFLIGIIVANVPEGLLVTVTVCLTLTAKRMASKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHLWYDQIIVESDTTESFRGSHFKIEDKSFNALFMCAALCNSAEFKGGQDDIPVFKKDVNGNASEAALLKFTETIFAGIGAFRQKHIKLTEIPFNSTEKYQVSVHEFNSSDGYFIVEMKGAPERILDRCSTIIIQGLSVELTPTLKLEFEEAYLEMGGMGERVLGFADLLLPMSKYPISYEFSADPPNFPLENLRFLGLISLIDPPRAAVPDAVAKCRSAGVRVIMVTGDHPITAKAIARSVGIITTPTAEDIAKQRGVTVLDIDSRQATAIVVHGGELREMKAEELDAVIYYHNEIVFARTSPQQKLIIVEACQRRGEIVAVSGDGVNDSPALKRADIGVAMGISGSDVSKQAADMILLDDNFASIVVGIEEGRIIFDNLKKSIAYTLTSNLPEIVPFLFFVIFDIPLARGTIAILCIDIGTDMLPAISLAYEKAESDIMARMPRDPFEDRLVNKRLILMAYLQIGVIQTVACFFTFFAIMAEHGFPPSRLKGIREDWDSKNVEDLEDGYGQEWTYRERKVLEYTAGTGFFVSIVVTQVFDLLICKTRRNSILQQGMGNHVLNFALVLEFIIACLLCYVPVFEKTLRMYSIKFIWWIYAFPFGLLIFFFDESRRFLIRRNPGGWVEQETYY
Protein: ATP-dependent RNA helicase HrpB (EC 3.6.4.13) (P37024)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein bS1
- Ribonuclease D
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS5
- Putative ankyrin repeat protein YahD
Sequence:
MSSLPVAAVLPELLTALDCAPQVLLSAPTGAGKSTWLPLQLLAHPGINGKIILLEPRRLAARNVAQRLAELLNEKPGDTVGYRMRAQNCVGPNTRLEVVTEGVLTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDDLKLLIMSATLDNDRLQQMLPEAPVVISEGRSFPVERRYLPLPAHQRFDDAVAVATAEMLRQESGSLLLFLPGVGEIQRVQEQLASRIGSDVLLCPLYGALSLNDQRKAILPAPQGMRKVVLATNIAETSLTIEGIRLVVDCAQERVARFDPRTGLTRLITQRVSQASMTQRAGRAGRLEPGISLHLIAKEQAERAAAQSEPEILQSDLSGLLMELLQWGCSDPAQMSWLDQPPVVNLLAAKRLLQMLGALEGERLSAQGQKMAALGNDPRLAAMLVSAKNDDEAATAAKIAAILEEPPRMGNSDLGVAFSRNQPAWQQRSQQLLKRLNVRGGEADSSLIAPLLAGAFADRIARRRGQDGRYQLANGMGAMLDANDALSRHEWLIAPLLLQGSASPDARILLALLVDIDELVQRCPQLVQQSDTVEWDDAQGTLKAWRRLQIGQLTVKVQPLAKPSEDELHQAMLNGIRDKGLSVLNWTAEAEQLRLRLLCAAKWLPEYDWPAVDDESLLAALETWLLPHMTGVHSLRGLKSLDIYQALRGLLDWGMQQRLDSELPAHYTVPTGSRIAIRYHEDNPPALAVRMQEMFGEATNPTIAQGRVPLVLELLSPAQRPLQITRDLSDFWKGAYREVQKEMKGRYPKHVWPDDPANTAPTRRTKKYS
Protein: Very-long-chain aldehyde decarbonylase CER1 (EC 4.1.99.5) (Protein ECERIFERUM 1) (F4HVY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex. Involved in epicuticular wax biosynthesis and pollen fertility.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19892830, ECO:0000269|PubMed:22773744}; Multi-pass membrane protein {ECO:0000269|PubMed:19892830, ECO:0000269|PubMed:22773744}.
Interaction partners:
- Alkane hydroxylase MAH1
- Fatty acyl-CoA reductase 3
- Protein ECERIFERUM 2
- Cytochrome b5 isoform B
- 3-ketoacyl-CoA synthase 6
- Cytochrome B5 isoform D
- Cytochrome b5 isoform E
- Cytochrome B5 isoform C
- Wax ester synthase/diacylglycerol acyltransferase 1
- Cytochrome b5 isoform A
Sequence:
MATKPGVLTDWPWTPLGSFKYIVIAPWAVHSTYRFVTDDPEKRDLGYFLVFPFLLFRILHNQVWISLSRYYTSSGKRRIVDKGIDFNQVDRETNWDDQILFNGVLFYIGINLLPEAKQLPWWRTDGVLMAALIHTGPVEFLYYWLHKALHHHFLYSRYHSHHHSSIVTEPITSVIHPFAEHIAYFILFAIPLLTTLLTKTASIISFAGYIIYIDFMNNMGHCNFELIPKRLFHLFPPLKFLCYTPSYHSLHHTQFRTNYSLFMPLYDYIYGTMDESTDTLYEKTLERGDDIVDVVHLTHLTTPESIYHLRIGLASFASYPFAYRWFMRLLWPFTSLSMIFTLFYARLFVAERNSFNKLNLQSWVIPRYNLQYLLKWRKEAINNMIEKAILEADKKGVKVLSLGLMNQGEELNRNGEVYIHNHPDMKVRLVDGSRLAAAVVINSVPKATTSVVMTGNLTKVAYTIASALCQRGVQVSTLRLDEYEKIRSCVPQECRDHLVYLTSEALSSNKVWLVGEGTTREEQEKATKGTLFIPFSQFPLKQLRRDCIYHTTPALIVPKSLVNVHSCENWLPRKAMSATRVAGILHALEGWEMHECGTSLLLSDLDQVWEACLSHGFQPLLLPHH