wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (O46034)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATRGSGTRVQSQPKIFPSLLSKLHGAISEACVSQRLSTDKKTLEKTWKLMDKVVKLCQQPKMNLKNSPPFILDILPDTYQRLRLIYSKNEDQMHLLHANEHFNVFINNLMRKCKQAIKLFKEGKEKMFDENSHYRRNLTKLSLVFSHMLSELKAIFPNGVFAGDQFRITKADAADFWKSNFGNSTLVPWKIFRQELNKVHPIISGLEAMALKTTIDLTCNDFISNFEFDVFTRLFQPWVTLLRNWQILAVTHPGYVAFLTYDEVKARLQRYILKAGSYVFRLSCTRLGQWAIGYVTAEGEILQTIPQNKSLCQALLDGHREGFYLYPDGQAYNPDLSSAVQSPTEDHITVTQEQYELYCEMGSTFQLCKICAENDKDIRIEPCGHLLCTPCLTSWQVDSEGQGCPFCRAEIKGTEQIVVDAFDPRKQHNRNVTNGRQQQQEEDDTEV
Protein: Uncharacterized protein (Q8INU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP11594p
- IP02289p
- IP20609p
- Serpin 28F
- Accessory gland protein Acp53Ea
- Accessory gland-specific peptide 26Ab
- Accessory gland-specific peptide 26Aa
- Odorant binding protein b
- Accessory gland protein Acp29AB
- Lectin-29Ca
Sequence:
MKIIALLVLANLGFVLSESLAEMDRLATWRLHNISNKYKYLSTGNPEFYQWIERVNTVADEFNHYNKHRQRLEDQITERLITIRSIIAIRNASKRCLRFYLNQEAELESAYKSSNERKQQVLYQNSVRCPHGLDDGRLGDPYFVDYL
Protein: Mitochondrial protein YPR099C (O13548)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the functional mitochondria and respiratory growth.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:31374566}.
Interaction partners:
- Large ribosomal subunit protein mL43
- Uncharacterized membrane protein TOS7
Sequence:
MSPSESFNSFSLFSTLSMFKFLTQITFSRPFVYSALNKGCPDFLITSNCIHGNSWPHLSNLFEVKNFLMPSEDPPQLQNCKVIFLHGNTNAPTPLRPMEFRAIAFTTISPYIRVCVST
Protein: Platelet-activating factor receptor (PAF-R) (PAFr) (P25105)
Organism: Homo sapiens (Human)
Function: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1374385}; Multi-pass membrane protein {ECO:0000269|PubMed:1374385}.
Interaction partners:
- G-protein coupled receptor 135
- Guanine nucleotide-binding protein G
- Beta-arrestin-1
- Non-receptor tyrosine-protein kinase TYK2
- C-C chemokine receptor type 1
- N-formyl peptide receptor 2
- Signal transducer and activator of transcription 1-alpha/beta
- Signal transducer and activator of transcription 3
- Platelet endothelial cell adhesion molecule
- Toll-like receptor 4
Sequence:
MEPHDSSHMDSEFRYTLFPIVYSIIFVLGVIANGYVLWVFARLYPCKKFNEIKIFMVNLTMADMLFLITLPLWIVYYQNQGNWILPKFLCNVAGCLFFINTYCSVAFLGVITYNRFQAVTRPIKTAQANTRKRGISLSLVIWVAIVGAASYFLILDSTNTVPDSAGSGNVTRCFEHYEKGSVPVLIIHIFIVFSFFLVFLIILFCNLVIIRTLLMQPVQQQRNAEVKRRALWMVCTVLAVFIICFVPHHVVQLPWTLAELGFQDSKFHQAINDAHQVTLCLLSTNCVLDPVIYCFLTKKFRKHLTEKFYSMRSSRKCSRATTDTVTEVVVPFNQIPGNSLKN
Protein: Semaphorin-3G (Q4LFA9)
Organism: Mus musculus (Mouse)
Function: Has chemorepulsive activities for sympathetic axons. Ligand of NRP2.
Subcellular location: Secreted.
Interaction partners:
- Neuropilin-1
- Neuropilin-2
- Plexin-A3
- Plexin-D1
Sequence:
MDPSAWAICCLLGSLLFHVGIPSPGPSPSVPRLRLSYRDLLSTNRSAIFLGPRGSLDLQVMYLDEYRDRLFLGSRDALYSLRLDQAWPDPREVLWLPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTGAFQPICTFITVGHRGEHVLRLDASSVENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRSDSDQSLLHEPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGPGHVTISRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKSLEVYALFSTVSAVFQGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSKMTAQPGRPFGSTKDYPDEVLQFVRDHPLMFQPVRPRRGRPVLVKTHLAQRLRQIVVDRVEAEDGTYDVIFLGTDSGSVLKVIALQGGGLTEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQCETYGSACAECCLARDPYCAWDGTACARYRPSSGKRRFRRQDIRHGNPAVQCLGQGQSQNKAASGLMTRVFGTEHNSTFLECLPKSPQAAVRWFLQRPGDKGTDQVKTDERVVQTAQGLLFRRLSRHDAGNYTCTTLEHGFSQTVVRFALEVIAAVQLDSLFLRESRLEEPSAWGSLASASPKTWYKDILQLTGFANLPRVDEYCERVWCRGVGERSGSFRGKGKQAKGKSWAGLELGKKMKSRVLAEHNRTPREVEAT
Protein: Antimicrobial peptide defensin 3 (AgDef3) (Q5TWR9)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Antibacterial peptide mostly active against Gram-positive bacteria with atypical up-regulation of expression.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710}.
Interaction partners:
- AGAP009515-PA
Sequence:
MKFAVVSFLLVALLGLVAVGEAQLKNLACVTNEGPKWANTYCAAVCHMSGRGAGSCNAKDECVCSMT
Protein: Pre-mRNA-splicing regulator WTAP (Female-lethal(2)D homolog) (WT1-associated protein) (Wilms tumor 1-associating protein) (Q9ER69)
Organism: Mus musculus (Mouse)
Function: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR. Required for accumulation of METTL3 and METTL14 to nuclear speckle (By similarity). Acts as a mRNA splicing regulator (By similarity). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (By similarity). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q15007}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}.
Interaction partners:
- Protein virilizer homolog
- N
- N
- Zinc finger CCCH domain-containing protein 13
- E3 ubiquitin-protein ligase Hakai
- RNA-binding protein 15
- Putative RNA-binding protein 15B
- RNA N
- N
- Mothers against decapentaplegic homolog 2
Sequence:
MTNEEPLPKKVRLSETDFKVMARDELILRWKQYEAYVQALEGKYTDLNSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETRQQLAQYQQQQSQASAPSTSRTTSSEPVDQAEVTSKDCSRLANGPSNGSSSRQRTSGSGFHREGSTPEDDFPSSSGNGNKASNSSEERTGRGGSSYINPLSAGYESVDSPTGSENSLTHHSNDTDSSHDPQEEKAVSGKGNRTVGSRHVQNGLDSSVNVQGAVL
Protein: Protein RecA (Recombinase 1) (Recombinase A) (P43705)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. Plays a central role in DNA metabolism, participating in general homologous recombination, recombinational (postreplication) DNA repair, and prophage induction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- ATP-dependent DNA helicase RecQ
- LexA repressor
- Regulatory protein RecX
- Uncharacterized protein HI_1546
- Beta sliding clamp
- Uncharacterized protein HI_1564
- DNA topoisomerase 1
- DNA topoisomerase 3
- DNA repair protein RadA
Sequence:
MATQEEKQKALAAALGQIEKQFGKGSIMKLGDTKTLDVESISTGSLGLDVALGIGGLPMGRIVEIFGPESSGKTTLTLSVIAQAQKAGKTCAFIDAEHALDPIYAAKLGVDVKELFVSQPDNGEQALEICDALVRSGAIDVIIVDSVAALTPKAEIEGDMGDSHMGLQARLMSQALRKLTGQIKNANCLVVFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRTGSVKDGENIIGNETRVKVVKNKLAAPFRQVDFQILYGEGISKAGELLELGVKHKLVEKSGAWYSYNGEKIGQGKANSMKWLNENIEKSDELEARLRAELVANPEQALMADIEQSENNTESESDFE
Protein: Chaperone SurA (Peptidyl-prolyl cis-trans isomerase SurA) (PPIase SurA) (EC 5.2.1.8) (Rotamase SurA) (P0ABZ8)
Organism: Escherichia coli O157:H7
Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_01183}. Note=Is capable of associating with the outer membrane. {ECO:0000255|HAMAP-Rule:MF_01183}.
Interaction partners:
- Outer membrane protein assembly factor BamA
- Outer membrane protein assembly factor BamB
- Outer membrane protein assembly factor BamB
- Outer membrane protein assembly factor BamA
- Chaperone protein Skp
- LPS-assembly protein LptD
- Bis
- Ribosomal RNA small subunit methyltransferase A
- LPS-assembly protein LptD
- 4-hydroxythreonine-4-phosphate dehydrogenase
Sequence:
MKNWKTLLLGIAMIANTSFAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALTRLNKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRASAYVKILSN
Protein: Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)] (P07200)
Organism: Sus scrofa (Pig)
Function: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-1
- TGF-beta receptor type-2
- Decorin
- Latent-transforming growth factor beta-binding protein 1
- Mothers against decapentaplegic homolog 3
- Transforming growth factor beta-3 proprotein
- Integrin alpha-V
- Fibromodulin
- Transforming growth factor beta-2 proprotein
- Latent transforming growth factor beta binding protein 3.
Sequence:
MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGDVPPGPLPEAVLALYNSTRDRVAGESVEPEPEPEADYYAKEVTRVLMVESGNQIYDKFKGTPHSLYMLFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNDSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTRREAIEGFRLSAHCSCDSKDNTLHVEINGFNSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
Protein: 5'-AMP-activated protein kinase subunit gamma-2 (AMPK gamma2) (AMPK subunit gamma-2) (H91620p) (Q9UGJ0)
Organism: Homo sapiens (Human)
Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-1
- Calcium/calmodulin-dependent protein kinase kinase 2
- Serine/threonine-protein kinase STK11
- 5'-AMP-activated protein kinase subunit gamma-3
- Glycogen [starch] synthase, muscle
- Glycogen [starch] synthase, liver
Sequence:
MGSAVMDTKKKKDVSSPGGSGGKKNASQKRRSLRVHIPDLSSFAMPLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPRPSSPMSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESYKHEPERLENRIYASSSPPDTGQRFCPSSFQSPTRPPLASPTHYAPSKAAALAAALGPAEAGMLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Protein: Calmodulin-regulated spectrin-associated protein 1 (Q5T5Y3)
Organism: Homo sapiens (Human)
Function: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules. Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization. In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation. Through interaction with spectrin may regulate neurite outgrowth.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19508979}. Note=Associates with the minus-end of microtubules (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends (PubMed:24486153, PubMed:24706919). {ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin beta chain
- Tubulin alpha-1A chain
- Tubulin beta-2B chain
- Ubiquitin-associated domain-containing protein 1
Sequence:
MVDASGRAAAEGWRKMEAPPDGAADLVPLDRYDAARAKIAANLQWICAKAYGRDNIPEDLRDPFYVDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQVAALQGHQSVIQALSRKGIYVMESDDTPVTESDLSRAPIKMSAHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQLLESPAHQKVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYLNKCFYLTLEDMLYAPLVLKPNVMVFIAELFWWFENVKPDFVQPRDVQELKDAKTVLHQKSSRPPVPISNATKRSFLGSPAAGTLAELQPPVQLPAEGCHRHYLHPEEPEYLGKGTAAFSPSHPLLPLRQKQQKSIQGEDIPDQRHRSNSLTRVDGQPRGAAIAWPEKKTRPASQPTPFALHHAASCEVDPSSGDSISLARSISKDSLASNIVNLTPQNQPHPTATKSHGKSLLSNVSIEDEEEELVAIVRADVVPQQADPEFPRASPRALGLTANARSPQGQLDTSESKPDSFFLEPLMPAVLKPAKEKQVITKEDERGEGRPRSIVSRRPSEGPQPLVRRKMTGSRDLNRTFTPIPCSEFPMGIDPTETGPLSVETAGEVCGGPLALGGFDPFPQGPSTDGFFLHVGRADEDTEGRLYVSCSKSPNSHDSEPWTLLRQDSDSDVVDIEEAEHDFMGEAHPVVFSRYIGEEESAKLQEDMKVKEHEDKDDASGRSSPCLSTASQMSSVSMASGSVKMTSFAERKLQRLNSCETKSSTSSSQKTTPDASESCPAPLTTWRQKREQSPSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKKGKAEAAPPLRPEHFAKEYSQHNGEDCGDAVSKTEDFLVKEEQREELLHEPQDVDKESLAFAQQHKAKDPVALHELERNKVISAALLEDTVGEVVDVNECDLSIEKLNETISTLQQAILKISQQQEQLLMKSPTVPVPGSKNNSQDHKVKAPVHFVEPLSPTGVAGHRKAPRLGQGRNSRSGRPAELKVPKDRPQGSSRSKTPTPSVETLPHLRPFPASSHPRTPTDPGLDSALEPSGDPHGKCLFDSYRLHDESNQRTLTLSSSKDANILSEQMSLKEVLDASVKEVGSSSSDVSGKESVPVEEPLRSRASLIEVDLSDLKAPDEDGELVSLDGSADLVSEGDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQILEEQGLGKPKSKPKKPRPKSVHREESCSDSGTKCSSTPDNLSRTQSGSSLSLASAATTEPESVHSGGTPSQRVESMEALPILSRNPSRSTDRDWETASAASSLASVAEYTGPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTGPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPAVPKKAQTRK
Protein: Protein-S-isoprenylcysteine O-methyltransferase A (AtICMTA) (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase A) (Prenylated protein carboxyl methyltransferase A) (Prenylcysteine carboxyl methyltransferase A) (AtPCM) (Q9FMW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues, resulting in the modulation of the function of prenylated proteins. Involved in negative regulation of abscisic acid signaling. Carboxyl methylation is a reversible and potentially regulated step in the post-translational modification of prenylated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:18641086}; Multi-pass membrane protein {ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:18641086}.
Interaction partners:
- CAAX prenyl protease 1 homolog
- CAAX prenyl protease 2
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2
- Protein-S-isoprenylcysteine O-methyltransferase B
- Bifunctional riboflavin kinase/FMN phosphatase
- Pentatricopeptide repeat-containing protein At1g79490, mitochondrial
- FAD synthetase 2, chloroplastic
- Jacalin-related lectin 33
Sequence:
MTEIFSDTSIRQLSQMLLSLIFFHISEYILAITIHGASNVTLSSLLITKHYALAMLLSLLEYLTEIILFPGLKQHWWVSNFGLIMIIVGEIIRKAAIITAGRSFTHLIKINYEEHHGLVTHGVYRLMRHPSYCGFLIWSVGTQVMLCNPVSAVAFAVVVWRFFAQRIPYEEYFLNQFFGVQYLEYAESVASGVPFVN
Protein: histidine kinase (EC 2.7.13.3) (A0A0H3NUZ2)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
Sequence:
MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELANDPPNDLMWWRRLFRAIDKWAPPGQRLLLVTSEGRVIGAERSEMQIIRNFIGQADNADHPQKKKYGRVEMVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSSPLLLWLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLGTALLRRRGGESKELERIETEAQRLDSMINDLLVMSRNQQKNALVSETMKANQLWGEVLDNAAFEAEQMGKSLTVNYPPGPWPLYGNPNALESALENIVRNALRYSHTKIEVGFSVDKDGITITVDDDGPGVSPEDREQIFRPFYRTDEARDRESGGTGLGLAIVESAMQQHRGWVKADDSPLGGLRLTLWLPLYKRT
Protein: 6-methylsalicylic acid decarboxylase (EC 4.1.1.52) (Patulin biosynthesis cluster protein G) (A0A075TXZ1)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatG catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
Interaction partners:
- 3-hydroxyanthranilate 3,4-dioxygenase
Sequence:
MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILDKAKL
Protein: Bacteriocin-associated integral membrane protein (A0A0H2URQ1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MSQKMNHLDVGEFVLLLPEHLRSEEEHYKSVFEDDLTSRISSQDERQQMTATVGYLESGQDRFVYNTTPISYQQFLKDPIIIVITPQSTGPQSILFWIDAVQNYVLFNQLSDAQELIQRQGIENWVSEMQTGYHNYITLLDNIQRERWVMLAGAVLGIATSILLFNTMNRLYFEEFRRAIFIKRIAGLRFLEIHRTYLFAQLGVFLLGFVASVFLQVEIGVAFLVLLLFTGLSLLQLHVQMQKENKMSMLVLKGG
Protein: Histamine N-methyltransferase (HMT) (EC 2.1.1.8) (Q01984)
Organism: Rattus norvegicus (Rat)
Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1639806}.
Interaction partners:
- Diamine oxidase [copper-containing]
- Amine oxidase
- Amine oxidase
- Histidine decarboxylase
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Histamine H3 receptor
Sequence:
MASFMRSLFSDHSRYVESFRRFLNNSTEHQCMQEFMDKKLPGIIARIGETKAEIKILSIGGGAGEIDLQILSKVQAQYPGICINNEVVEPNAEQIVKYKELVAKTSNMENIKFAWHKETSSEYQKRVVEEDEEPPKWDFIHMIQMLYYVKDIPATLKFFHGLLAANAKILIILVSGTSGWEKLWKKYGFRLPRDDLCQYVTSSDLAQILDDLGIKYECYDLLSTMDITDCFIDGNENGDLLWDFLTETCNFIKTAPLDLKEEIMKDLQEPEFSVKKEGKVLFNNNLSFIVVEANV
Protein: Protein disulfide-isomerase (EC 5.3.4.1) (O48949)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Thioredoxin domain-containing protein
- protein disulfide-isomerase
- Calnexin
- Endoplasmic reticulum resident protein 29 C-terminal domain-containing protein
- Calreticulin
- Endoplasmic reticulum oxidoreductin 1
- Uncharacterized protein
- Uncharacterized protein
- 38 kDa RNA-binding protein
- Uncharacterized protein
Sequence:
MNRWNLLALTLGLLLVAAPFTKHQFAHASDEYEDDEEDDAPAAPKDDDVDVTVVTVKNWDETVKKSKFALVEFYAPWCGHCKTLKPEYAKAATALKAAAPDALIAKVDATQEESLAQKFGVQGYPTLKWFVDGELASDYNGPRDADGIVGWVKKKTGPPAVTVEDADKLKSLEADAEVVVVGYFKALEGEIYDTFKSYAAKTEDVVFVQTTSADVAKAAGLDAVDTVSVVKNFAGEDRATAVLATDIDTDSLTAFVKSEKMPPTIEFNQKNSDKIFNSGINKQLILWTTADDLKADAEIMTVFREASKKFKGQLVFVTVNNEGDGADPVTNFFGLKGATSPVLLGFFMEKNKKFRMEGEFTADNVAKFAESVVDGTAQAVLKSEAIPEDPYEDGVYKIVGKTVESVVLDETKDVLLEVYAPWCGHCKKLEPIYKKLAKRFKKVDSVIIAKMDGTENEHPEIEVKGFPTILFYPAGSDRTPIVFEGGDRSLKSLTKFIKTNAKIPYELPKKGSDGDEGTSDDKDKPASDKDEL
Protein: IP08087p (Uncharacterized protein, isoform A) (Q8INT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- Prolyl 4-hydroxylase alpha subunit domain-containing protein
- FI16633p1
- procollagen-proline 4-dioxygenase
- HDC01001
- SCP domain-containing protein
- Hat-trick, isoform D
- Sulfhydryl oxidase
- Uncharacterized protein, isoform A
Sequence:
MKDCVEIFEGEFEVLRVTPPLYDEVEELLVNISINYEFGCVIAKLKDSPLAIAELGKLIRHIISRGISFAIRHVESGRIVAAIANIIFNTKRKTSYYDICAQIKSPNMIKYMELWDAVDASFNVNEHCQVDSTGDVEYMATLPEFRRRGLGHILCQQSIQFASLLAQRKLPLEILNQLPEEMRIERPQAIVAITTSQSSQIMGRQLGMKTMHKWHFSELRSLCGAMAESNGAAQAFEYAELQVVKF