wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 monooxygenase aba1 (EC 1.-.-.-) (Abscisic acid biosynthesis cluster protein 2) (A0A384JQG4)
Organism: Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MSNSILNLGSFACLLSLGSIVLWYTISAVLAWYPLRKIPAPSFLATFSYLWLAKTTYSGKQYWIQRDLHKKYGPLVRIGPTDIITDDPEIIKKISSARSSHRRGDWYLTGRFNPYYDNMFTMLEPGPHAKAKARTAAAYSGRDMPDLEVGVNAQLQTLIGLMRSKYASNTVKPHQPLLDLGQVSCFFTMDVITRLAFGEEFGYLKEETDQYGFLGEVRELWPRMSTSADTPWIRKFLFSPPFLKVLGPKPTDKTGFGALMAVAEHHVGKRFAPDAKKKEDMLGSFIRHGLNQQECEVEGLFMIVAGTESTASAIRSTLVHVMTCPRVYQKLKTEINLAVEEGKVSSPIKLEEAKLLPFLQAVIYEGIRMRPPLLGLFPKIVPDGGEEFHGMFIPAGTAICMNTSSLLRSTALFGDDAEVYRPERFMELEKSKRGEMERNVELAFGYGQYMCVGKTVAFMELNKSIFEILRAFDLQLLSPAKPCDVLSYGIFLESNMLVKVTESEGTEYK
Protein: Thrombospondin type-1 domain-containing protein 7A [Cleaved into: Thrombospondin type-1 domain-containing protein 7A, soluble form] (Q69ZU6)
Organism: Mus musculus (Mouse)
Function: Plays a role in actin cytoskeleton rearrangement.
Subcellular location: [Thrombospondin type-1 domain-containing protein 7A]: Cell membrane {ECO:0000269|PubMed:27214550}; Single-pass type I membrane protein {ECO:0000305|PubMed:27214550}. Cell projection {ECO:0000269|PubMed:27214550}. Note=Detected on podocyte foot processes. {ECO:0000269|PubMed:27214550}.; SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein 7A, soluble form]: Secreted {ECO:0000250|UniProtKB:Q9UPZ6}. Note=Proteolytic cleavage in the extracellular region generates a 210 kDa soluble form. {ECO:0000250|UniProtKB:Q9UPZ6}.
Interaction partners:
- Secretory phospholipase A2 receptor
Sequence:
MGLRAGRLASPSRGVLQLLRLPLLLLLLLSSGARGAAAQGDTEVPTLYLWKTGPWGRCMGDDCGPGGIQTRAVWCAHVEGWTTLHTNCKQAVRPSNQQNCFKVCDWHKELYDWRLGTWDRCQPVISKSLEKSRECVKGEEGIQVREIMCIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQKDCIVSEFSPWSECSRTCGSGLQHRTRHVVAPPQYGGSGCPNLTEFQVCQSNPCEEDESLYSLQVGPWSACSVPHTRQARQARRRGKNKEREKERGKAVKDPEARELIKKKRNRNRQNRQENRYWDIQIGYQTRDVTCLNRTGKSADLSFCQQERLPMTFQSCVITKECQVSEWLEWSPCSKTCHDVTSPTGTRVRTRTITQFPIGSEKECPALEEKEPCVSQGDGAVLCATYGWRTTEWTECHVDPLLSQQDKRRANQTALCGGGVQTREIYCIQTNDNMLSHGNTQKDKEASKPVDSKLCTGPVPNTTQLCHVPCPIECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGGSGATGNCPHLLEAIPCEEPSCYDWKSVRLGDCEPDNGKSCGPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSAWSSWSSCSHTCSGKTTEGKQTRARSILAYAGEEGGIRCPNISALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVICVRVNVGQVGPKKCPESLRPETVRPCLLPCRKDCVVTPYSDWTPCPSSCREGDSGARKQSRQRVIIQLPANGGKECSDPLYEEKACEAPPTCHSYRWKTHKWRRCQLVPWSIQQDVPGAQEGCGPGRQARAITCRKQDGGQASIQECLQYAGPVPALTQACQIPCQDDCQFTSWSKFSSCNGDCGAVRTRKRAIVGKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKAEVLLGMKVQGDSKECGQGYRYQAMACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYIWVTEPWSVCKVTFVDMRDNCGEGVQTRKVRCMQNTADGPSEHVEDYLCDPEDMPLGSRECKLPCPEDCVISEWGPWTCALPCNPSGSRQRSADPIRQPADEGRACPDAVEKEPCSLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKYCEELGLEKNWPMNTSCTVECPVNCQLSDWSSWSQCSQTCGLTGKMIRKRTVTQPFQGDGRPCPSLMEQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSAEDFSKVVDEEFCANTELIIDGNKQIVLEETCTQPCPGDCYLNDWSSWSLCQLTCVNGEDLGFGGIQVRSRAVIIQELENQHLCPEQMLETKSCDDGQCYEYKWVASAWKGSSRTVWCQRSDGINVTGGCLVVSQPDTDRSCNPPCSQPHSYCSEMKTCRCEEGYTEVMSSNSTLEQCTLIPVVVIPTVEDKRGDVKTSRAVHPTQPSINPAGRGRTWFLQPFGPDGRLKTWVYGVAAGAFVLLVFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
Protein: Steryl-sulfatase (EC 3.1.6.2) (Arylsulfatase C) (ASC) (Estrone sulfatase) (Steroid sulfatase) (Steryl-sulfate sulfohydrolase) (P08842)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of sulfated steroid precursors, such as dehydroepiandrosterone sulfate (DHEA-S) and estrone sulfate to the free steroid.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:2668275}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:2668275}; Multi-pass membrane protein.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Aldo-keto reductase family 1 member C3
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Sulfotransferase 2B1
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Cytochrome P450 3A4)
- Steroid 21-hydroxylase
- Cytochrome P450 1A1
- Cytochrome P450 1A2
Sequence:
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNGCFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQTLPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Protein: CG7093 (Q2XY50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GLAGHPHGLVGALAPPPPPPMKQPQMDIPSGKKQLQQLKGATVAASALEYQYQVMYAHCVQKEREREREHLPHSHPLPRQHRAVLVATTPYPHLPQYPTPPTLNSSSAFRPWGPDTTKAFLHAYGATLSSLPYACQEPPELQNPERVVRSTDKRYAERTYQPNVALAPRKSILSKERDKDRERMEREVMERQRLREKETDHQVVHIKQERSQTPTPPTASPPDGVVLPLDVVEPPHPSSSGSNSPLPAHLPAAPATAPPNAGGAPPTPTNLRNMRSPEEFSAGGSNEITSSTSPHHQQSSHHQVVQPTAGAPPPSQHIIATVNQHAKLLPSSSSLPNGNGSSSLAATNNEPSRIRINKNLMSQQPLVAVSGMTPHHHQHHPTHMHHFSHGYYKSQASSPTQSSSAGLNLSTHSSNVVSSPHHVTQPKTHHSSVGSGNHGLQNGKPHLGSEFELSTDTDDTDSLNGEPDSSAMLPPWEQAVESLRETRPKDRERVLLILQRLLQENDQYRYNNIQLSELLHKQDAHIADLTEQLQRYRRQFEEQVCKVDLRKMPFKHQTRLENVVEAGRGEAEEDEELEEEEMEDRANNNNQQELSPLIKAPTNGLRRSVTPPNCCASEGGDCEKPDEPESKRIKLQVGEKTEDKQVENEESPSNGTESHDLEKLEKDDDKTDPTNNPKSPQPSQISSDDEMEEDDEDEDEEDEDEEVQVEAPHSSALATPPTATTPLSPDSAATAGQLFDSSNSSDESSMKKAQMSACHALEKMSSNVGSDENNQRLAEESQEEEAEEDPEEEDSDDDEMPLQQRQQQQRQRVAPQNVLSGPSVAGHHPAPAHPPMATKASKKQTPPAPPTAAATTTASATTNSEL
Protein: Glutaredoxin-1 (Thioltransferase-1) (TTase-1) (P12864)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonucleoside-diphosphate reductase
- Thioredoxin
- glutathione-disulfide reductase
- peptide-methionine
- Thioredoxin, mitochondrial
- Thioredoxin reductase 1, cytoplasmic
- Glutathione peroxidase 1
- Glutathione peroxidase
- Glutathione peroxidase
- Glutathione peroxidase
Sequence:
AQEFVNSKIQPGKVVVFIKPTCPYCRKTQEILSQLPFKQGLLEFVDITATSDMSEIQDYLQQLTGARTVPRVFLGKDCIGGCSDLIAMQEKGELLARLKEMGALRQ
Protein: Dynein light chain roadblock-type 2 (Dynein light chain 2B, cytoplasmic) (Roadblock domain-containing protein 2) (Q8TF09)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Dynein light chain Tctex-type protein 2B
- Dynein light chain Tctex-type 1
- Dynein light chain Tctex-type 3
- Cytoplasmic dynein 2 intermediate chain 2
- Cytoplasmic dynein 2 intermediate chain 1
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 1 intermediate chain 1
- Dynein light chain 2, cytoplasmic
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 2 heavy chain 1
Sequence:
MAEVEETLKRIQSHKGVIGTMVVNAEGIPIRTTLDNSTTVQYAGLLHHLTMKAKSTVRDIDPQNDLTFLRIRSKKHEIMVAPDKEYLLIVIQNPCE
Protein: Mago nashi-like protein,putative (Q586G7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RRM domain-containing protein
- RNA-binding protein, putative
- C3H1-type domain-containing protein
- Probable eukaryotic initiation factor 4A
- MIF4G domain-containing protein
- RNA helicase
- RNA-binding protein, putative
- Nuclear cap-binding protein subunit 2
- Probable eukaryotic initiation factor 4A
- Cleavage and polyadenylation specificity factor subunit 5
Sequence:
MQSCLHYVRYFAGHTGRYGNEFLEFDIRDDGTLKYGNNSRYRNENIIKKQARISPAVLEEIKRLIILSGILERDDECWPQPDRNGRQELEIHLGDTHISFVTNKITSLSEVESPDKPKGLDTFYYFVRDIKALVLALVSLHFKIKAW
Protein: GTP-binding protein CIN4 (Chromosome instability protein 4) (P39110)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Implicated in yeast microtubule function.
Interaction partners:
- Chromosome instability protein 1
- Tubulin-specific chaperone C
- Protein PAC2
- Tubulin-specific chaperone A
- Tubulin-specific chaperone B
- Tubulin beta chain
- Tubulin alpha-3 chain
Sequence:
MGLLSIIRKQKLRDKEIRCLILGLDNSGKSTIVNKLLPKDEQNNDGIMPTVGFQIHSLMIKDVTISLWDIGGQRTLRPFWDNYFDKTQAMIWCIDVSLSMRFDETLQELKELINRDENRIGYECAVIVVLNKIDLVEDKSELHRRCLLVESELKCLFKPDIRIELVKCSGVTGEGIDNLRDRLVESCHFTQ
Protein: MMACHC-like protein (EC 1.16.1.-) (Cobalamin deficiency protein 1) (Cyanocobalamin reductase (cyanide-eliminating)) (Q7Z144)
Organism: Caenorhabditis elegans
Function: Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione-dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4U1}.
Interaction partners:
- Methylmalonic aciduria type A homolog, mitochondrial
- Corrinoid adenosyltransferase MMAB
- Methionine synthase reductase
- Probable methylmalonyl-CoA mutase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylmalonic aciduria and homocystinuria type D homolog
- Probable methionine synthase
- Propionyl-CoA carboxylase alpha chain, mitochondrial
Sequence:
MVTEMSHAESIKRVVDQKLSSHEGFESHMFKIGSYNEAVGESSPFALPYDDSTMALLILSTPDMFDVAFRKWVVQKTMDFGSFDEVCEMVSSPIQSFLEDRLEIMSEKLRKVEENFEILHDYSMTPQRRPKILMQTCGHVAGAAFYYQPCHFQEDGVTWPPAGRMGPNLKFIGLSLHPIYGGHFAFRSVLIFPNVKIPEFCEKEPRPILTASEDVRTALEKFNYNWKDSGFRDFGNPTRRYSTTQMEFFGRPVAERWEVLRPWVDGGAKNID
Protein: Parathyroid hormone (PTH) (Parathyrin) (P04089)
Organism: Rattus norvegicus (Rat)
Function: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone 2 receptor
- Tuberoinfundibular peptide of 39 residues
- Fibroblast growth factor 23
- Osteocalcin
- Tumor necrosis factor ligand superfamily member 11
- Extracellular calcium-sensing receptor
- Sclerostin
- Klotho
- Vitamin D3 receptor
Sequence:
MMSASTMAKVMILMLAVCLLTQADGKPVKKRAVSEIQLMHNLGKHLASVERMQWLRKKLQDVHNFVSLGVQMAAREGSYQRPTKKEENVLVDGNSKSLGEGDKADVDVLVKAKSQ
Protein: Uncharacterized protein C12orf50 (Q8NA57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEMQQNCSISCFWETQPLGCVKISCIFYHSKPRNINGLFLPPSSNITLQKEIQEGIPLQSQSQEPLKPQENISRPIHHPLVLKTNFEEEEEVDEQNDASSLWTKTPEEIEEKRAIKEMCYKSGEYYRFHTPPDILSSKSMTPTAEKQLEKPLENGSELQEGDSLTVPTKLSQYERQGEIKTSLHGKPKTDIAAFENGGGDCYVPQRVIFLGVDESEALTEEKEITISKCSNTKDNKDSPHPKHSLTTRLVPTTHVLNATENISMKCREDPSSMNDVQPVKKPHFKGVKKRKWIYDEPQNFPNSGMQRAVQAPRPQNKMSYHRNNKNRNAENASYIHVQRDAVRTVALNAPSRSRPTHGSYNKVHANREPKPNLSPDKYTSTSYNDSAWRKRIPFSKTYSKSEKIYPEPRRNGSK
Protein: 2'-5'olygoadenylate synthetase 1E, 42kD isoform (Q8K3L4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MARELFRTPIWRLDNFIEDQLLPDTTFLTELRADIDSISAFLKERCFQGATHPMRVSRVVMGGSYDEHNALKGRSEANMVVFFNDLTSFEDQLKWQQVFIEEIRKHLLQLQQEKPCKLKFEVQSSEEPNTRSLTFKLCSPERQQEVEFDVQPAYDALYEGGYCKSFESINYNKVYAQLIHECTTLEKEGEFSICFTDLHQSFLRYRAPKLWNLIRLVKHWYQLCKEKLRGPLPPQYALELLTVYVWEFGVQDSFGLHAAQCFRTVLELVTKYKCLLIYWTWFYDFRPEISDYLHGQIKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQTWIHSNFFRNCDMSLVNGWEVSPEKQ
Protein: At3g06330 (F24P17.21 protein) (RING/U-box superfamily protein) (Q9SQT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g21720
- AT3g17120/K14A17_24
- starch synthase
- Polypyrimidine tract-binding protein homolog 2
- Nucleosome assembly protein 1;4
- F-box/kelch-repeat protein At1g67480
- DEAD-box ATP-dependent RNA helicase 11
- Splicing factor U2af large subunit B
Sequence:
MKMQDSAAQEPEIAIIVGDSSSSSLHSSSQVTEKSTEDVPSCSHLDLSIQIPSRSLPFGNGRNPKGSLKSTPSFKSGTTSSPRGILRNLSLKKKVISQPESERSSLLSPGLMETAKKPNATGSTTSPYWKRCLSLPSRQAAKLSPVVSTQLSAGVPGDPPNKDYSRSLSMPGRNKVIVRSISFDNHKARVSSETSADQVSSVPPEETDEEIPEEEAVCRICLDVCEEGNTLKMECSCKGDLRLVHEACAMKWFSTKGTRTCDVCRQVVQNLPVTLVRVPTPNQQNNRRGSSQQNMPSQTVSAWQEFVVLVLISTVCYFFFLEQLLIRDLNKQAIYIAAPFSLTLGLLASIFAIVLAIREYIWTYAALEFALVGMLVHIFYATVRLSATYSILFAGILGFGIAVCLNSLYLHYFAWRVRVAQNSSPV
Protein: assimilatory sulfite reductase (ferredoxin) (EC 1.8.7.1) (O53674)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Nitrite reductase small subunit
- Nitrate/nitrite transporter
- Probable nitrate/nitrite transporter NarK2
- Nitrate reductase-like protein NarX
- Probable integral membrane nitrite extrusion protein NarK3
- Nitrate reductase alpha subunit
- Probable nitrite extrusion protein 1 NarK1
- Probable respiratory nitrate reductase
- Glutamine synthetase
- Nitrate reductase-like protein NarX
Sequence:
MPTAGSSRAPAAAREIVVVGHGMVGHRLVEAVRARDADGSLRITVLAEEGDAAYDRVGLTSYTESWDRALLALPGNDYAGDQRVRLLLNTRVTQIDRATKSVVTAAGQRHRYDTLVLATGSYAFVPPVPGHDLPACHVYRTFDDLDAIRAGAQRTLDGGHTDGGVVIGGGLLGLEAANALRQFGLQTHVVEMMPRLMAQQIDEAGGALLARMIADLGIAVHVGTGTESIESVKHSDGSVWARVRLSDGEVIDAGVVIFAAGIRPRDELARAAGLAIGDRGGVLTDLSCRTSDPDIYAVGEVAAIDGRCYGLVGPGYTSAEVVADRLLDGSAEFPEADLSTKLKLLGVDVASFGDAMGATENCLEVVINDAVKRTYAKLVLSDDATTLLGGVLVGDASSYGVLRPMVGAELPGDPLALIAPAGSGAGAGALGVGALPDSAQICSCNNVTKGELKCAIADGCGDVPALKSCTAAGTSCGSCVPLLKQLLEAEGVEQSKALCEHFSQSRAELFEIITATEVRTFSGLLDRFGRGKGCDICKPVVASILASTGSDHILDGEQASLQDSNDHFLANIQKNGSYSVVPRVPGGDIKPEHLILIGQIAQDFGLYTKITGGQRIDLFGARVDQLPLIWQRLVDGGMESGHAYGKAVRTVKSCVGSDWCRYGQQDSVQLAIDLELRYRGLRAPHKIKLGVSGCARECAEARGKDVGVIATEKGWNLYVAGNGGMTPKHAQLLASDLDKETLIRYIDRFLIYYIRTADRLQRTAPWVESLGLDHVREVVCEDSLGLAEEFEAAMQRHVANYKCEWKGVLEDPDKLSRFVSFVNAPDAVDSTVTFTERAGRKVPVSIGIPRVRS
Protein: Methyl-accepting chemotaxis protein PctB (Q9HW91)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Responds to L-Arg, L-Gln, L-Ala, L-Glu, L-Lys, L-Met and L-Tyr. Also involved in repellent responses to trichloroethylene (TCE), chloroform and methylthiocyanate.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chemotaxis protein methyltransferase 1
- Chemotaxis protein CheA
- Chemotaxis protein CheA
- Chemotaxis protein methyltransferase 2
- Probable chemoreceptor glutamine deamidase CheD
- Probable purine-binding chemotaxis protein
- Probable chemotaxis protein
- Chemotaxis protein CheW
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
- Chemotaxis protein CheA
Sequence:
MIKSLKFSHKILLAAALVVIATFSLFTLYNDSLQRASIREDLEDYLHEMGEITASNVQNWLSGRILLIENLAQTLARDHSPETTQALLEQPLLGSTFLFTYLGQTDGTYTARPTSDLPADYDPRRRPWYNAATSAGQTTLTEPYMEPAIHELVLTIASPARQGGQPFGVVGGDLSLQTVVKIINSLDFGGMGYAFLVSGDGKILVHPDKDQVMKSLSDVYPRNTPKIGSGFSEAELHGNTRILSFSPVKGLSGLDWYIGISVDKDKAYAMLTKLRTSAIVAALIAVVAIVLLLGMLIRVLMQPLTDMGRAMQDIAQGEGDLTKRLKVTSNDEFGALAISFNRFVERIHESIREVAGTARQLHDVAQLVVNASNSSMANSDEQSNRTNSVAAAINELGAAAQEIARNAADASHHASDANHQAEDGKQVVEQTIRAMNELSEKISASCANIEALNSRTVNIGQILEVIKGISEQTNLLALNAAIEAARAGEAGRGFAVVADEVRNLAHRAQESAQQIQKMIEELQIGAQEAVSTMTESQRYSLESVEIANRAGERLSSVTGRIAEIDGMNQSVATATEEQTAVVDSLNMDITEINTLNQEGVENLQATLRACGELETQAGRLRQLVDSFKI
Protein: Histone H2B.10 (HTB2) (Q9FFC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone H3.1
- Histone H3-like centromeric protein CENH3
- E3 ubiquitin-protein ligase BRE1-like 1
- E3 ubiquitin-protein ligase BRE1-like 2
- Probable histone H2A.3
- Histone H3.3
- Histone H2A.6
- Histone H3-like 5
- Histone H3-like 3
Sequence:
MAKADKKPAEKKPAEKTPAAEPAAAAEKKPKAGKKLPKEPAGAGDKKKKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAGESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
Protein: Probable NADPH dependent 2,4-dienoyl-CoA reductase FadH (2,4-dienoyl coenzyme A reductase) (4-enoyl-CoA reductase) (O50431)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Glutamate synthase large chain
- Electron transfer flavoprotein subunit beta
- Possible oxygenase
- Electron transfer flavoprotein subunit alpha
- Probable transcriptional regulator Rv1176c
- Probable respiratory nitrate reductase
- Possible electron transfer protein FdxB
- NADPH oxidoreductase
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- Probable oxidoreductase
Sequence:
MTNPYPNLLSPLDLGFTTLRNRVVMGSMHTGLEDRARHIDRLADYFAERARGGVGLIITGGYAPNRTGWLLPFASELVTSAQARRHRRITRAVHDSGAKILLQILHAGRYAYHPLAVSASPIKAPITPFRPRALSARGVEATIADFARCAQLARDAGYDGVEIMGSEGYLLNQFLAPRTNKRTDSWGGTPANRRRFPVEIIRRSRAAVGCDFIICYRLSMADYVAEGQSWDEIVALATEVEGAGATIINSGFGWHEARVPTIVTSVPGGAFVDISSAVAEHVTIPVVASNRINMPQAAERILAETQVRLISMARPMLSDPDWVLKAQSNRVDEINTCISCNQACLDHAFARKTVSCLLNPRAGRETQLVLSPTRRARSVAVVGAGPAGLATAANAAQRGHRVTLFEANDFIGGQFDMARRIPGKEEFSETIRYFSTILAKHGVEVRLGTRVAAQELTGYDEVVLATGVAPRIPAIPGIDHPMVLTYAEAITGVRPVGRTVAVVGAGGIGFDVTELLVTDSSPTLNLKEWKAEWGVADPREARGALTTPLPAPPAREVYLLQRTKGPQGKRLGKTTGWVHRASLKAKGVHQLSGVNYEQINDDGLHISFGPKRRRPQLLAVDNVVVCAGQEPVRDLESELRRHGINPHIIGGAAVAAELDAKRAIKQGTELAARL
Protein: Unextended protein (Putative metal transporter uex) (A0A0B7P9G0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable metal transporter (By similarity). Acts downstream of PRL-1 and protects the nervous system against olfactory carbon dioxide stimulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31404830}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- PRL-1 phosphatase
- Lethal
Sequence:
MNTYFISFITIIIFANGINGTSVDTSNKLLLQKANDFNLSQNLSSSRTRRTIANSFRIVGIRLEDETVETKNGIPTVLVDKEQQFRVFGSGLEENTAITFTNEKNDYGGPCLKPATDLFTPIEVSSNGFSALYSVKFPSFINEFFICAKTAEKTTNHSKAATTTPLEHQGNSDFLKIKTFEPLIPVWLAIIIIVTCLGFSALFSGLNLGLMSMDRTELKILRNTGTEKEKKYASKIAPVRDQGNYLLCSILLGNVLVNSTFTILLDGLTSGLFAVIFSTLAIVLFGEITPQAVCSRHGLAIGAKTILVTKTVMAITAPLSYPVSRILDKLLGEEIGNVYNRERLKELVRVTNDVNDLDKNEVNIISGALELRKKTVADVMTHINDAFMLSLDALLDFETVSEIMNSGYSRIPVYDGDRKNIVTLLYIKDLAFVDTDDNTPLKTLCEFYQNPVHFVFEDYTLDIMFNQFKEGTIGHIAFVHRVNNEGDGDPFYETVGLVTLEDVIEELIQAEIVDETDVFVDNRTKTRRNRYKKADFSAFAERREVQTVRISPQLTLATFQYLSTAVDAFKKDVISELILRRLLNQDVFHNIKTKGKSKDDPSLYIFTQGKAVDFFVLILEGRVEVTIGKEALMFESGPFTYFGTQALVPNVVIDSPTQMGSLQSLNMDSKIRQSFVPDYSVRAISDVIYITIKRVLYLTAKKATLLEKSRKSGTFSSETFDDEVERLLHSITENEKPSCFAQNQSTRRLSNRSINSSPTNMNRSPDFVYNSVDEAIQDDTKLKNIKHADNVTTSISLVAAELEDLHSGEQDTTAASMPLLPKLDDKFESKQSKP
Protein: AT-rich interaction domain 1B (A0A1B0GWZ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMMGPGGGGAASLSKAAAGAAAAAGGFQRFAGQNQHPSGATPTLNQLLTSPSPMMRSYGGSYPDYSSSSAPPPPSQPQSQAAAAAGAAAGGQQAAAGMGLGKDLGAQYAAASPAWAAAQQRNHPAMSPGTPGPTMGRSQGSPMDPMVMKRPQLYGMGTHPHSQPQQSSPYPGGAYGPPGAQRYPLGMQGRAPGALGGLQYPQQQMPPQYGQQGVSGYCQQGQQPYYNQQPQPSHLPPQAQYLQPQSQQRYQPQQDMSQEGYGTRAQPPLAPGKSNHEDLNLIQQERPSSLPDLSGSIDDLPTGTEATLSSAVSASGSTSSQGDQSNPAQSPFSPHASPHLSSIPGGPSPSPVGSPVGSNQSRSGPISPASIPGSQMPPQPPGSQSESSSHPALSQSPMPQERGNYSRTPTYSGVPSASYSGPGPGMGINANNQMHGQGPTQPCGAMPLGRMPSAGMQSRPFPGNMSSVPPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLVASSSPYSQPMNNNSNLMGTQAQPYSMTPTMVNSSTASMGLTDMMSPSESKLSVPLKADGKEEGVPQPESKSKDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSPKSSSSSTTGEKITKVYELGTEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKIERGEEPPPEVFSTGDAKKQPKLQPPSPANSGSLQGPQTPQSTGSSSMAEVPGDLKPPTPASTPHGQGTPMQSGRSSTVSVHDPFSDVSDSAYPKRNSMTPNAPYQQGMGMPDMMGRMPYEPNKDPFSGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGAMSNLGMGQRQQFPYGTSYDRRHEAYGQQYPGQGPPTGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYGSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYNRERMQGPGQMQPHGIPPQMMGGPMQSSSNEGPQQNMWATRNDMPYPYQNRQGPGGPAQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQSSYQTPPSLPNHISRAPSPASFPRSLESRMSPSKSPFLPAMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPVLKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQRALDHRTGKKDDSQSSEDDSGKEEDDAECLEEEEEEEEEEEEEEEEEEEEEEDSKKTESEGKSSSALAAPDTTADPKETPRQASKFDKLPIKIVKKNNLFVVDRSDRLGRVQEFNSGLLHWQLGGGDTTEHILTHFESKMEIPPRRRPPAPLSSTGKKKELAGKGDSEEQPEKSIIATIDDVLSARPGALPEDSNPGPQTESGKFPFGIQQAKSHRNIRLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDTLAARAIAVQKGSIGNLIGFLEDGVTMAQYQQSQHTLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
Protein: Diphosphomevalonate decarboxylase 2 (Mevalonate-5-pyrophosphate decarboxylase) (PgMVD) (EC 4.1.1.33) (F8QQQ7)
Organism: Panax ginseng (Korean ginseng)
Function: Performs the first committed step in the biosynthesis of isoprene-containing compounds such as sterols and terpenoids (By similarity). Component of the triterpenes (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Promotes the accumulation of stigmasterol and beta-sitosterol.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:O23722}.
Interaction partners:
Sequence:
MAKELQKWVVMVTAQTPTNIAVIKYWGKRDETLILPINDSISVTLDPDHLCTTTTVSVSPSFEQDRMWLNGKEISLLGGRFQSCLREIRSRACDLEDEKKGIKIKKMDWEKLRLHIASYNNFPTAAGLASSAAGLACFVFALAKLMNLNEDNGQLSAIARRGSGSACRSLYGGFVKWIMGKEENGSDSIAFQLADEKHWDDLVIVIAVVSARQKETSSTTGMQDSCKTSMLIQHRAKEVVPKRIIQMEDAIEKRDFPSFARLACADSNQFHAVCLDTSPPIFYMNDTSHKIISCVEKWNRSVGTPQVAYTFDAGPNAVLIARDRKIAALLLRRLLFHFPPTFQHCLNSYVIGDKSILQDVGVQDMKDIESLPPPPEIKDNIPAQKSNGDVSYFICTRPGRGPVLLPDSGALLNPETGLPK