wanglab/gogpt-training-data huggingface dataset:
Protein: NACHT, LRR and PYD domains-containing protein 12 (Monarch-1) (PYRIN-containing APAF1-like protein 7) (Regulated by nitric oxide) (P59046)
Organism: Homo sapiens (Human)
Function: Plays an essential role as an potent mitigator of inflammation. Primarily expressed in dendritic cells and macrophages, inhibits both canonical and non-canonical NF-kappa-B and ERK activation pathways. Functions as a negative regulator of NOD2 by targeting it to degradation via the proteasome pathway. In turn, promotes bacterial tolerance. Inhibits also the RIGI-mediated immune signaling against RNA viruses by reducing the E3 ubiquitin ligase TRIM25-mediated 'Lys-63'-linked RIGI activation but enhancing the E3 ubiquitin ligase RNF125-mediated 'Lys-48'-linked RIGI degradation. Acts also as a negative regulator of inflammatory response to mitigate obesity and obesity-associated diseases in adipose tissue (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30902577}.
Interaction partners:
- NLR family CARD domain-containing protein 4
- Apoptosis-associated speck-like protein containing a CARD
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 6
- NACHT, LRR and PYD domains-containing protein 1
- NACHT, LRR and PYD domains-containing protein 3
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 7
- Pyrin
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MLRTAGRDGLCRLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQREDLVRDTPPGGPSSLGNQSTCLLEVSLVTPRKDPQETYRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHARTVGHQASPIKIETLFEPDEERPEPPRTVVMQGAAGIGKSMLAHKVMLDWADGKLFQGRFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQELIRVPERLLFIIDGFDELKPSFHDPQGPWCLCWEEKRPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSEAERKEYFYKYFHNAEQAGQVFNYVRDNEPLFTMCFVPLVCWVVCTCLQQQLEGGGLLRQTSRTTTAVYMLYLLSLMQPKPGAPRLQPPPNQRGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSFIHLSFQEFFAAMYYILDEGEGGAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVSPHIKMDLLQWIQSKAQSDGSTLQQGSLEFFSCLYEIQEEEFIQQALSHFQVIVVSNIASKMEHMVSSFCLKRCRSAQVLHLYGATYSADGEDRARCSAGAHTLLVQLPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLGICRLGSAACEGLSVVLQANHNLRELDLSFNDLGDWGLWLLAEGLQHPACRLQKLWLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLFGMDLNKMTHSRLAALRVTKPYLDIGC
Protein: Collagen type XI alpha 2 chain (A0A8I5ZY93)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPSVDVLRALRFPSLPDGVRKSKGVCPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRSGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHVLDDEVFEGDVQELLIVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQNQEPQQQYPTPGEEEGVLESSLLPSLEEEQTDLQVPPTADSFQAEEYGEGGTEPPAGFYDYTYGYGDDYREETELGPALSAETDHTGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPRGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGESGPMGERGHPGPPGPPGEQGLPGTAGKDGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPFGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGSQGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLMQDEEATPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPTRRGGVLLGPVCFMG
Protein: Arrestin domain-containing protein B (Q86KB1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Arrestin domain-containing protein E
- Arrestin domain-containing protein D
- Arrestin domain-containing protein F
Sequence:
MDNRGLRLFIVEGKELKGSDNGGSSSDPYVKLKFNGNSFKTETIKNTLSPVWNQSFDIGIINVNDPNAIIEVECLDWDRFGKHDSLGKVQLPIAILREAATFGQTDKWLNLDKKGYVRVGFQFNPPYPLQQHISPDGNPNIIQNQIQQQNLISSNGQLPPPVYYEPIYLKTHPTVLEAEFILPNDLYQKTIYVTGEPVRASLVLYVNQPIVVRSLFVSLKGKTSVCGKKQKELIQDLRNLLHTSIGPSSPNSQNQKVALDIGKHIYPFEFFIPKHCNSSIDGVGNYKVLYRFQFNADIVNLPDIQLEREITVVNIEDTVHRMTQSQIHEKCSKSPLTGGTIEMTITAPKNSYYPGEDIELQVHVNNSSKKKVKKIELELQRTISIQHEKGVPTQVLKVSKNFFPKIQQNQQSTQIVVMETPQTLLNSIYQSGIIKIEYKVRAVLDILDCIDLYTIFPVNIVLPDPKRVILPNPLDELSKIPRYIQDWTPRNLLSWLYFRMNCPEVVTSNPEFYQYCLSGNELLSIPDTILLEKVLKGAGTRTTEIHNAIKIEIDRVLSVRTILKDNQLPHLIQTFENELVTFDLLSSLSSIDLSHLTSTIGDRIRLQNAFEKLKLNN
Protein: Polyadenylate-binding protein 1 (E5RH24)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDT
Protein: Probable E3 ubiquitin-protein ligase dma1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase dma1) (Q10322)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable E3 ubiquitin-protein ligase which is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is compromised. Inhibits the septation initiation netwok (SIN) during spindle checkpoint activation. The effect appears to be mediated through preventing the SIN activator, plo1 kinase, from localizing to the SPB.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:12479804, ECO:0000269|PubMed:16823372}. Note=Also localizes at the division site in mitosis.
Interaction partners:
- Cell division control protein 16
- Septation initiation protein sid4
- Serine/threonine-protein kinase plo1
- 2-oxoglutarate dehydrogenase, mitochondrial
- Spindle pole body protein ppc89
- Protein byr4
- Septation initiation network scaffold protein cdc11
- Cell division control protein 7
- Polyubiquitin
- Serine/threonine-protein kinase ppk35
Sequence:
MTKSVEGYLKEQELAAETDSEKDDDKISIRLTNFVGPNAHSFSFDPLVRYWNRKQNNLPIYIGRYTERYNGGDVSAIVFRSKVVSRRHAQIFYENNTWYIQDMGSSSGTFLNHVRLSPPSKTSKPYPISNNDILQLGADYRGGHEVNYRCVRARVELNNSWKIKLSPYNLNEFKRMQELVLCGSSESGPPECCICLMPVLPCQALFVAPCSHSYHYKCIRPTLNESHPYFSCFICRKYHDLEAPVEEGDESLNDLLRNATVKDDASE
Protein: RNA polymerase-binding transcription factor DksA (Q9HT38)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}.
Interaction partners:
- CobW C-terminal domain-containing protein
- DUF1826 domain-containing protein
- RNA polymerase sigma factor RpoD
- Large ribosomal subunit protein bL31B
- Transcription elongation factor GreB
- Metal-pseudopaline receptor CntO
- RNA polymerase sigma factor RpoS
- GTP pyrophosphokinase
- DNA-directed RNA polymerase subunit omega
- Large ribosomal subunit protein bL36B
Sequence:
MTEQELLAQPDAAYMDEAQQDFFRDLLLRQRQELQARIEGEFGELRDLERPSDEADLASREEQRQWQLRLLEREKKLLDKIDEALERLARGDYGWCQETGEPIGLRRLLLRPTATLCIEAKERQEKRERHVRHN
Protein: Unconventional myosin-Id (Myosin heavy chain myr 4) (Q63357)
Organism: Rattus norvegicus (Rat)
Function: Unconventional myosin that functions as actin-based motor protein with ATPase activity. Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24903835, ECO:0000269|PubMed:8034741}. Perikaryon {ECO:0000269|PubMed:8034741}. Cell projection, dendrite {ECO:0000269|PubMed:8034741}. Early endosome {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26446290}. Note=Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane (PubMed:26446290). Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles (PubMed:8034741). {ECO:0000269|PubMed:26446290, ECO:0000269|PubMed:8034741}.
Interaction partners:
Sequence:
MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKVLNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIMISGESGAGKTEASKYIMQYIAAITNPSQRAEIERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLHSLHLQKSLSSYNYIRVGAQLKSSINDAAEFKVVADAMKVIGFKPEEIQTVYKILAAILHLGNLKFIVDGDTPLIENGKVVSVIAELLSTKADMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTVHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDGMFLEALNSKLGKHGHFSSRKTCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLVRVVLFLQKVWRGTLARMRYKRTKAALTIIRYYRRYKVKSYIHEVARRFHGVKNMRDYGKHVKWPTPPKVLRRFEEALQSIFNRWRASQLIKTIPASDLPQVRAKVAAMEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNRSGFILSVPGN
Protein: Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47) (Q8BY87)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER) (By similarity). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- DNA polymerase beta
- E3 ubiquitin-protein ligase TRIP12
Sequence:
MVPGEENQLVPKEDVFWRCRQNIFDEMKKKFLQIENAAEEPRVLCIIQDTTNSKTVSERITLNLPASTPVRKLFEDVANKVGYINGTFDLTRENGVTTADMAPLDHTSDKSLLDANFEPGKKNFLHLTDKDGEPPQMLLEDSNNVDDSVHDRFIGPLPREGSVASTNDYVSQNYSYSSILNKSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEDSEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFGWDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSFPEELDMSTFIDIEDEKSPQTESCTDSGAENEGSCHSDQMSNDFSTDDAVDEGICLESSSGSEKISKPGLEKNSLMYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKTHGGSSGSRGYYSSAFASSTNAYMLIYRLKDPTRNAKFLEVDEYPEHIKNLVQKERELEEQEKRQREIERNTCKIKLFCLHPVKQVMMENKLEVHKDKTLKEAVEMAYKMMDLEDVIPLDCCRLVKYDEFHDYLERSYEGEEDTPMGLLLGGVKSTYMFDLLLETRKPDQIFQSYKPGEVMVKVHVVDLKAETVAAPVTVRAYLNQTVTEFKQLISKATHLPADSMRIVLERCYNDLRLLSMPSKTLKAEGFFRSNKVFVESSETVDHQAAFTDSHLWKLLDRHANTIRLFVLLPEQSPGSYSKRTAYQKAGGDSGNVDDDCERVKGPAGNLKSVDAILEESTEKLKSLSLQQQQQDGDNGDSSKSTETSDFENIESPLNERGSSTSVDNRELEQHIQTSDPENFQSEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADSAQIPLANGLDSHSITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKSRGDMQYMYFKADPYTADEGSGEGHKWLMVHVDKRITLAAFKQHLEPFVGVLSSHFKVFRVYTSNQEFETVRLNETLSSFSDDNKITIRLGRALKKGEYRVKVCQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQCGLDLSIDRFRLRKKTWKNPGTVFLDYHIYEEDINISSNWEVFLEVLDGVEKMKSMSQLAILTRRWRPAEMKLDPFQELVLESNSVDELREKLSEISGIPLEDIEFAKGRGTFPCDISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDRTEEVMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKIYLDGAPNKDVAQD
Protein: Arylamine N-acetyltransferase 1 (EC 2.3.1.5) (Arylamide acetylase 1) (Monomorphic arylamine N-acetyltransferase) (MNAT) (N-acetyltransferase type 1) (NAT-1) (P18440)
Organism: Homo sapiens (Human)
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Cytochrome P450 2A6
- Arylamine N-acetyltransferase 2
- Liver carboxylesterase 1
- Xanthine dehydrogenase/oxidase
- Myeloperoxidase
- Arylacetamide deacetylase
- Glutamine amidotransferase-like class 1 domain-containing protein 3
- CDK-activating kinase assembly factor MAT1
Sequence:
MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI
Protein: Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i) (P40306)
Organism: Homo sapiens (Human)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-3
- Proteasome maturation protein
- Proteasome subunit beta type-8
- Proteasome subunit beta type-9
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-1
Sequence:
MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE
Protein: Alpha-glucan phosphorylase 1 (AtPHS1) (EC 2.4.1.1) (Alpha-glucan phosphorylase, L isozyme) (Starch phosphorylase L) (Q9LIB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). May be not required for the degradation of starch, but the phosphorolysis of starch may play an important role in water stress tolerance.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
Interaction partners:
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Isoamylase 1, chloroplastic
- Isoamylase 3, chloroplastic
- Phosphoglucomutase, chloroplastic
- Isoamylase 2, chloroplastic
- Probable phosphoglucomutase, cytoplasmic 2
- Probable phosphoglucomutase, cytoplasmic 1
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- Alpha-amylase 3, chloroplastic
Sequence:
MDTMRISGVSTGAEVLIQCNSLSSLVSRRCDDGKWRTRMFPARNRDLRPSPTRRSFLSVKSISSEPKAKVTDAVLDSEQEVFISSMNPFAPDAASVASSIKYHAEFTPLFSPEKFELPKAFFATAQSVRDALIMNWNATYEYYNRVNVKQAYYLSMEFLQGRALSNAVGNLGLNSAYGDALKRLGFDLESVASQEPDPALGNGGLGRLASCFLDSMATLNYPAWGYGLRYKYGLFKQRITKDGQEEAAEDWLELSNPWEIVRNDVSYPIKFYGKVVFGSDGKKRWIGGEDIVAVAYDVPIPGYKTKTTINLRLWSTKAPSEDFDLSSYNSGKHTEAAEALFNAEKICFVLYPGDESTEGKALRLKQQYTLCSASLQDIVARFETRSGGNVNWEEFPEKVAVQMNDTHPTLCIPELMRILMDLKGLSWEDAWKITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVEIIEKIDEELVRTIVSEYGTADPDLLEEKLKAMRILENVELPSAFADVIVKPVNKPVTAKDAQNGVKTEQEEEKTAGEEEEDEVIPEPTVEPPKMVRMANLAVVGGHAVNGVAEIHSEIVKQDVFNDFVQLWPEKFQNKTNGVTPRRWIRFCNPYLSDIITNWIGTEDWVLNTEKVAELRKFADNEDLQSEWRAAKKKNKLKVVSLIKERTGYTVSPDAMFDIQIKRIHEYKRQLLNILGIVYRYKKMKEMSASEREKAFVPRVCIFGGKAFATYVQAKRIVKFITDVASTINHDPEIGDLLKVIFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEENFFLFGAKADQIVNLRKERAEGKFVPDPTFEEVKKFVGSGVFGSNSYDELIGSLEGNEGFGRADYFLVGKDFPSYIECQEKVDEAYRDQKRWTRMSIMNTAGSFKFSSDRTIHEYAKDIWNIKQVELP
Protein: Cytochrome P450 monooxygenase patI (EC 1.-.-.-) (Patulin synthesis protein I) (m-hydroxybenzyl alcohol hydroxylase) (A1CFL6)
Organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Function: Cytochrome P450 monooxygenase; 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. PatI catalyzes the conversion of m-hydroxybenzyl alcohol into gentisyl alcohol. 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: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A075TMP8}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDFTQVPPSYILGVLLSSTSILFCLKYLLRSGYRPPELPSGPTTVPLFGNELQVPKADAHFQFTKWAKQYGGMFSLKRYMNTTIVITDRKLMKSLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGEEWRMLRKIIHQYFMEPNCEREHWKVQEAEAKQMLHDFLTMPEDHMLHPKRYSNSITNSLVFGIRTATVHDEYMDELFYLMDKWSLVQELGATPPVDSFGLLRILPQWMLGNWKNRAVEVGDLMQALYSKVLDQVRARRQRGVYRDSFMDRVLDNLEKTPLTENQLRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDAVVGSERSPSWSDFAQLPYINMIIKESHRWRPVSPLGVPHAVAEDDRVNNTLIPKGSTIVLNVWGMHHDPDRWSEPEHFQPDRFADYPALASTYAASGEWDKRDHYGYGAGRRICPGIHLAERNLFIGVAKLLWAFEFSEPLGSRSDISAESGASQGFLHCPKDYGCAIRLRAPEKRETIMREFEEAQGVFSRFD
Protein: Transmembrane protein (Q38C56)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDNQGSYITTTKLEEVRLLAVAGDRSAAVYAAHRRMEDNLAKLPAVLADTARYHPTSVDPWVAVFAAVDSLCRDVELCLQLFTIGAQVERSKGLPTVAVLYEQQKKPAARLQSFAATVQSAFTCKGVTIPVPASLMLRFAEAIRPFDSSQATKWLQCSFEEMFNRETTGEGAGNNYVASGPTAVAATPAHATQEPKGVVVAMLTLLIKWRAEDGEDVLWAQRKRKELSQLVEENVLESLIRFEVESVAAVARRKQRVQKKGERQATKRQVKPTPATEALPGSAVEATVPAQGVSTLGRLRRYVNDLLATNWSQNPSRAACVIIAIILLCILARKALCTVSLFGGFAGGTPRGGRKLIDL
Protein: JmjC domain-containing protein 8 (Jumonji domain-containing protein 8) (Q96S16)
Organism: Homo sapiens (Human)
Function: Functions as a positive regulator of TNF-induced NF-kappa-B signaling. Regulates angiogenesis and cellular metabolism through interaction with PKM.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:29133832}. Cytoplasm {ECO:0000269|PubMed:27199445}.
Interaction partners:
- GATOR2 complex protein WDR24
Sequence:
MAPASRLLALWALAAVALPGSGAEGDGGWRPGGPGAVAEEERCTVERRADLTYAEFVQQYAFVRPVILQGLTDNSRFRALCSRDRLLASFGDRVVRLSTANTYSYHKVDLPFQEYVEQLLHPQDPTSLGNDTLYFFGDNNFTEWASLFRHYSPPPFGLLGTAPAYSFGIAGAGSGVPFHWHGPGYSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLRDTYPALPPSARPLECTIRAGEVLYFPDRWWHATLNLDTSVFISTFLG
Protein: Probable E3 ubiquitin protein ligase C167.07c (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase C167.07c) (Q1K9C4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- 26S proteasome regulatory subunit rpn11
Sequence:
MPLSFEGTFKAKRNVNLGGKRVSNDRAQLLRKAAMERKNREEERKAENNSVAVQSLSRGFLARRKFKQDFRERWIYKYTKSGRTSIRFNTLEDIKCSISLLVLFAEPDIDLPFVSQVAHNILVWLENLIPLSNGMDDTPKSHLKVKILKVQETLSNSNDSWLWQRFSSLLLNCLVSSINSHRIEGTDTSAETSLLHCLAYVAPYLKSSELSTYYDSVMTFYAQIYPKQNMTNLEDIMSLSLLTPVSSKTDENANSSSAFLFHVLASDCFSSIENCIPPDLIIDKVFSSSLQLSEEACISSLLNLGMIKVFSLAGNCLHLLHTEYKNSSLWKFCSYILDALYVFSGESVNSRIQVVSDVDDDEDDENAFSQNYYSHLQMVAKHFSKNYANQSGIVQRSFAECISSTFITKAFKLVSSNTLQAMSHFYATMIKLFPSNRTSILMYISLVETNEGSLTRSFSRFSWDMFSESPVYQLFHKKFDVQNVLKNDSGYWFQLQLLIDVYSRMLFTMIDDEFHNDKQNPLYPVMAEFCTVLKNLVLGLYWDVQAAKDVDCKSVVDISQLRVSSTSLLQQLYRINSRKQFLPEDFFLMSEYFNLNEFEANALQESELASHAEAEINITYKFDNFSESRPRLNILNNCSFFLPFHFRIHLLQQLLLLDKQANGYAQPFGHLKHAVIRRNRIFDDGFDAFYNFGKLLKGPIRITFVDEHGVVEEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAHLLYPNTHAYAQDVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVENDMALNFTVVHEEFGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVPIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFGFS
Protein: Uncharacterized protein (Q38BQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEASVTTNEITAEPAANQMQLSNEYASSRFSLAVAEKVGNRSQEGSESRDVVDHWGQSVLQLSIVGLGGSRGSFGNFSIASELLSLGERNEEEQSVMQQRAPLTNPVGEVVHATSGARGFAFSPVQRIPSGVSQRNEASIGYNDDISRSSSCSSGSEVMRQEMRRGGVQRTEVKLHLSHSNADVDAEEEDISTIRATPTGGAVDTLNELYGIDRYFTFHYNPERVVTPIDCGDQCSGGGSGVSTVATAAGLESQRESDDNRVAMTHEEDEIVGVTAEGEFIYRRDIVEGPDRQRWQSFYQPINRRSSELGVNECVPSLIPSMTINSAPTRVESGPATTTEPYPQDQYNNRFHPLQSFERVATQLPHLSREAPHEGFTERESEWTEEERESYRLLMRYRLCENEEEFEYEKLLNSVSTLRETLHRKPIEMLQRRLEERQQFARSGLGMPLALRW