wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-binding cassette subfamily G member 4 (EC 7.6.2.-) (ATP-binding cassette transporter White2) (Q91WA9)
Organism: Mus musculus (Mouse)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL). May play an important role in the removal of amyloid-beta peptides from brain, in a process that can be antagonized by desmosterol. However it is unclear whether ABCG4 can directly transport amyloid-beta peptides or whether peptide export may be facilitated due to changes in the membrane lipid environment. Induces apoptosis in various cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H172}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17916878}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:17916878}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Apolipoprotein A-I
Sequence:
MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSHLPKRSAVDIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAHGGRTVICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPMLFRAVQNGLCTMAEKKSSPGKNELPAHCPTCPPELDPIESHTFATSTLTQFCILFRRTFLSILRDTVLTHLRFMSHVLIGVLIGLLYLHIGDDASKVFNNTGFLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNYWYTLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALAIATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGLILTIYGMERGHLTCLDEQCPFRDPQIILRELDVEEAKLYMDFLVLGIFFLALRLLAYLVLRYRVKSER
Protein: Malate dehydrogenase 2, mitochondrial (EC 1.1.1.37) (Mitochondrial MDH2) (mMDH2) (Mitochondrial NAD-dependent malate dehydrogenase 2) (mNAD-MDH 2) (mtNAD-MDH2) (Q9LKA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Required for carbon dioxide and energy partitioning in leaves. May limit photorespiration during the dark phase. Can convert 2-ketoglutarate to L-2-hydroxyglutarate in vitro.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Malate synthase
- Fumarate hydratase 2
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Citrate synthase 1, peroxisomal
- Citrate synthase 2, peroxisomal
- Citrate synthase 5, mitochondrial
- Fumarate hydratase 1, mitochondrial
- NAD-dependent malic enzyme 2, mitochondrial
- NAD-dependent malic enzyme 1, mitochondrial
Sequence:
MFRSMIVRSASPVKQGLLRRGFASESVPDRKVVILGAAGGIGQPLSLLMKLNPLVSSLSLYDIANTPGVAADVGHINTRSQVSGYMGDDDLGKALEGADLVIIPAGVPRKPGMTRDDLFNINAGIVKNLSIAIAKYCPQALVNMISNPVNSTVPIAAEIFKKAGTYDEKKLFGVTTLDVVRARTFYAGKSDVNVAEVNVPVVGGHAGITILPLFSQASPQANLSDDLIRALTKRTQDGGTEVVEAKAGKGSATLSMAYAGALFADACLKGLNGVPNVVECSFVQSTITELPFFASKVRLGKNGVEEVLDLGPLSDFEKEGLEALKAELKSSIEKGIKFANQ
Protein: Teichoic acid poly(glycerol phosphate) polymerase (EC 2.7.8.12) (CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase) (CGPTase) (Major teichoic acid biosynthesis protein F) (Poly(glycerol phosphate) polymerase) (Tag polymerase) (P13485)
Organism: Bacillus subtilis (strain 168)
Function: Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of glycerol phosphate units from CDP-glycerol to the disaccharide linkage unit. Synthesizes polymers of approximately 35 glycerol phosphate units in length.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Teichoic acids export ATP-binding protein TagH
- Poly
- Glycerol-3-phosphate cytidylyltransferase
- Teichoic acid translocation permease protein TagG
- N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase
- Probable undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase
- Putative glycosyltransferase EpsH
- Uncharacterized glycosyltransferase EpsJ
- Teichoic acid glycerol-phosphate primase
- UDP-N-acetylglucosamine 2-epimerase
Sequence:
MSLVVDTNKRKQKGKSFYTEEQKKVMIENTVIKCILKSLKNNLGSLELLISIDSEHQFLEDYQLFLKLKERRSGTESEFPLQNTGSLEYKTEINAHVLPMPVEMGQTYDFYVEFRKKYEDAEQEPLLKRLSAEVNSIERAFHVDQTTELLILPYTTDKGNFSIKVKREAKIIRFDQIEISSEEISITGYAGYLSSENQYRIKNLNLILKKGGETPIEEKFPIKLERKTHGLENMRADGFVPELYDFEVKVPLKEIPFSNEKRYVYRLFMEYICNDDEGTDIQFNSTALVLGDRKNKLKGLVSIIKTNNAPVRYEVFKKKKKQTLGIRVNDYSLKTRMKYFIKGKKKRLVSKIKKITKMRNKLITKTYKSLFMMASRMPVKRKTVIFESFNGKQYSCNPRAIYEYMRENHPEYKMYWSVNKQYSAPFDEKGIPYINRLSLKWLFAMARAEYWVVNSRLPLWIPKPSHTTYLQTWHGTPLKRLAMDMEEVHMPGTNTKKYKRNFIKEASNWDYLISPNGYSTEIFTRAFQFNKTMIESGYPRNDFLHNDNNEETISLIKSRLNIPRDKKVILYAPTWRDDQFYAKGRYKFDLDLDLHQLRQELGNEYIVILRMHYLVAENFDLGPFEGFAYDFSAYEDIRELYMVSDLLITDYSSVFFDFANLKRPMLFFVPDIETYRDKLRGFYFDFEKEAPGPLVKTTEETIEAIKQISSPDYKLPVSFGPFYDKFCYLESGRSSEKVVNTVFKAE
Protein: Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.355) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1) (O54864)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43463}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
Interaction partners:
- Chromobox protein homolog 3
- DNA
- Chromobox protein homolog 5
- DNA
- NAD-dependent protein deacetylase sirtuin-1
- Methyl-CpG-binding protein 2
- Histone-lysine N-methyltransferase EZH2
- Histone deacetylase 1
- Polycomb protein Suz12
- DNA
Sequence:
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
Protein: Large ribosomal subunit protein bL32c (50S ribosomal protein L32, chloroplastic) (P0C452)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MAVPKKRTSMSKKRIRKNLWKKKTYFSIVQSYSLAKSRSFSGVSEHPKPKGFSRQQTNNRVLG
Protein: Large ribosomal subunit protein mL61 (54S ribosomal protein MRP49, mitochondrial) (P32388)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL61 is not essential in cells grown at 30 degree Celsius but is required for mitochondrial translation in cells grown at 18 degree Celsius.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein mL54
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL49
Sequence:
MSKVAQQLKFLNKISATTRLPQILVDPKKYSGLRLTFQTKNHNGHMGARVFWHNYLPTLQFYNPRMKFDVIRIKNEDKQKSVPCKLEILSHEGSVVETIDMRNKMHEDIMKDLLDKIEHVPLPENEIIRVGPQESII
Protein: Probable E3 ubiquitin-protein ligase DTX3 (EC 2.3.2.27) (Protein deltex-3) (Deltex3) (mDTX3) (RING-type E3 ubiquitin transferase DTX3) (Q80V91)
Organism: Mus musculus (Mouse)
Function: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 4
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 1
Sequence:
MSFVLSRMAACGGSCKNKVTVSKPVWDFLSKETPARLARLREEHRVSILIDGETSDIYVLQLSPQGPPPAPPNGLYLARKALKGLLKEAEKELKKAQRQGELMGCLALGGGGEHPELHRPGPPPLRAAPLLPPGARGLPPPPPPLPPPLPPRLREDAEEQETTCPICLGEIQNAKTLEKCRHSFCEGCITRALQVKKACPMCGRFYGQLVGNQPQNGRMLVSKDATLLLPSYEKYGTIVIQYVFPPGVQGAEHPNPGVRYPGTTRVAYLPDCPEGNKVLTLFRKAFDQRLTFTIGTSMTTGRPNVITWNDIHHKTSCTGGPQLFGYPDPTYLTRVQEELRAKGITDD
Protein: G-protein coupled receptor-associated sorting protein 2 (GASP-2) (Q96D09)
Organism: Homo sapiens (Human)
Function: May play a role in regulation of a variety of G-protein coupled receptors.
Interaction partners:
- Ribosome quality control complex subunit TCF25
- Ciliary microtubule-associated protein 3
Sequence:
MTGAEIEPSAQAKPEKKAGEEVIAGPERENDVPLVVRPKVRTQATTGARPKTETKSVPAARPKTEAQAMSGARPKTEVQVMGGARPKTEAQGITGARPKTDARAVGGARSKTDAKAIPGARPKDEAQAWAQSEFGTEAVSQAEGVSQTNAVAWPLATAESGSVTKSKGLSMDRELVNVDAETFPGTQGQKGIQPWFGPGEETNMGSWCYSRPRAREEASNESGFWSADETSTASSFWTGEETSVRSWPREESNTRSRHRAKHQTNPRSRPRSKQEAYVDSWSGSEDEASNPFSFWVGENTNNLFRPRVREEANIRSKLRTNREDCFESESEDEFYKQSWVLPGEEANSRFRHRDKEDPNTALKLRAQKDVDSDRVKQEPRFEEEVIIGSWFWAEKEASLEGGASAICESEPGTEEGAIGGSAYWAEEKSSLGAVAREEAKPESEEEAIFGSWFWDRDEACFDLNPCPVYKVSDRFRDAAEELNASSRPQTWDEVTVEFKPGLFHGVGFRSTSPFGIPEEASEMLEAKPKNLELSPEGEEQESLLQPDQPSPEFTFQYDPSYRSVREIREHLRARESAESESWSCSCIQCELKIGSEEFEEFLLLMDKIRDPFIHEISKIAMGMRSASQFTRDFIRDSGVVSLIETLLNYPSSRVRTSFLENMIHMAPPYPNLNMIETFICQVCEETLAHSVDSLEQLTGIRMLRHLTMTIDYHTLIANYMSGFLSLLTTANARTKFHVLKMLLNLSENPAVAKKLFSAKALSIFVGLFNIEETNDNIQIVIKMFQNISNIIKSGKMSLIDDDFSLEPLISAFREFEELAKQLQAQIDNQNDPEVGQQS
Protein: Relaxin family peptide receptor 2 (A0A8I5ZRR3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MWLLGFELRISGRAVNFTLAGSNMVAPLCPKGYFPCGNLTKCLPRAFHCDGVDDCGNGADEDNCGDTSGWTTIFGTVHGNVNKVTLTEECFLSRYPQHCYCRENELECVNADLKAVPKVSSNVTLLSLKKNKIHRLPVKVFSKYAELRKIFLQHNCITHISRRAFLGLHNLQILYLSHNCITSLRPGIFKDLHQLAWLILDDNPITRISQRSFTGLNSLFFLSMVSNRLEALPERLCAQMPQLNWVDLANNGIKFITNSTFLTCDSLTVLFLPRNQIGFVPEKTFSSLKNLGELDLSSNVIAKLPAHLFSDLHLLQKLNLSSNPLLYVHKNQFGSLKQLQSLDLERIEIPNINTGMFRPMKNLSHIYLKTFRYCSYVPHVRICMPSTDGISSSEDLLANSILRVSVWVIAFITCAGNFLVIAVRSLIKAENTTHAMSIKILCCADCLMGVYLFSVGVFDIKYRGQYQKYALLWMESVPCRLLGFLATLSTEVSVLLLTFLTLEKFLVIVFPFSNLRLGKRQTAVVLASIWVAGFLIAAVPFTSEDYFGNFYGKNGVCFPLHYDQAEDFGSRGYSLGIFLGVNLLAFLVITFSYVTMFCSIQKTALQTAEVRSHIGKEVAVANRFFFIVFSDAICWIPVFVVKILSLLQVEIPGTITSWIVVFFLPVNSALNPILYTLTTSLFKDKLKQLLHKHRRKSIFKVKKKSLSASIVWTDDSSLKLGVLNKIALGDSIMKPVSP
Protein: Uncharacterized protein (Q386P0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTCNVGTTAAADGCNDVGVRGIETLPYHTHGGVPPIQRGVSSSIFGRFAVEEADELRELLRVERCRLANSVQREEVLRQRLIVAEEGHVLYHLYFERLLELLRTDREETSTTSTKDDSPLITKEDLLKGLHEALRSVGAATAGGTISNADGEGCIRGINCSGASGETESISSDEQKMSGGAAAPFVNLSNATLLTASALQMRLANALELRRREKARKHELTKRALKDVLCVCVEEIEARHATVLLALRNAERRVESCDREVSAMLKYRVRQIQDPTENLEGLREKLVSLSQEHVRTLQELRLSQLEVAALKDDVVRAEARVTSLSSLNRAADSLEDARQGVCDFIRTTASDIRQRVHRGITLNEPFIQSMRSVALKIEAQVERLRPDDWHRDDNCSGVAGSVDTVVDSSNKTCLNSNEPCGVIALPIHGVPENGWAPRSNEQREKLRLPLASRRAEVRSESLVATALLEELARVMNNFCRLLENNMEQAAANTHSIMQAIDRFETAVVNKLTDMWDSTQSSLASCGLTSSPSAHGSTPCGTVERETFCTRNETHRCGRNDTSPAVQPHATPGKTITTTSAVLPSLMTSPQPEQAVASPHWQPEPPQRRLVLHERDSFGTPLCRVAIIQQ
Protein: Tight junction protein ZO-1 (H1UBK9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MYNPSGCTWQLLSVSLHRAANLGFGIAISGGRDNPHFTSGDPVVVISDVVPNGPAWGLLQVNDRILSANQVSFENIEYSSAVDIIKNKDHIDMIVKRRVAVPMLEYEQRTLKFTLSKSRKKDDFGIVVGCKFYIKEIRNPKLAEKDPGLKEGDSVLRINGQSLEGASLEEVNKWLERSRDKLCLVIQRDVRRGTSRWPSQNTVYERVGSVAATPRHSPSPMLPHMPITQRNSHEYVNSPRHRSDGSVERRVSSPANSQLSNFNGMASSQITTQDYDCYTRQPSRSIDANGVANIMFRKVGGSVGVRVIGGNEVGIFVSAVAADSPASLHGVSCGDRILEVNGRNMRGVTRESAVQLLLGLDDRVSLRLEHARQDFEHVRANQLGDNFYIRSHFSREKRDKASPLELSINEGDIFHVTDTLFGGTVGLWQAARVYSSSENKGEPVKGVIPNQATAEQIAKEWRVYVEAKQAKSGGSGTLLRRKFESRRTKSLPKNMICDPTELNLPLPAYERVALNTPSFHRPVVLFGPLADIARHQLLTQFSARFGSPESDGGVIRLSSVDHVIASMKHCVLDISIESVERLQLAQYAPIVVFLDVDGRSKIREIRKKCNAPHLSSRKLAENGNQIKKHHSHLLSATIDATHETGWFDALRELIGHLQQRRLWMPEFPPNLPLEDVLLFPLPKWDGDVDSLKSEYVDYQDSLPRKGGEKKWDSSPLQTPGDLPSEMREYSTMPRPQHHQLGQDFGGNRNRQSSNSQSTLSTFVTTASSSNPPRPLLTPTRDESASRTTTPHGYYHVKQLLDDDSLYQDARLANEIANARLREEAKLREERVNRQRSELSPSNMQHRLDNTTPSNFDFSNVQPSNSNPVPNGRYHPLTPSSMTSSSSGASRTAGQGQQQTAPPPRPPPVNSGNSSPYTQSYIRNKWNNDGAMDARGAENQTPPVVPARTNGSASPANASISLTVSNVPTGSSIASKSPTPRLDENENGQKSEEEEPTVVEESTALIGSLGGVIRCEKSNVELRIPAGAITEGQEHEIYVKVCREGDSSPIDRSKGETLLSPLVMCGPQGLKFEKQCELRMPHTGPVTADSDGQWSFSLKTGEGGEWKHMEIEQQQATNANLDQFLTVPITHF
Protein: Phosphatidylinositol 4-kinase type 2 (EC 2.7.1.67) (Q9VND3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}.
Interaction partners:
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 4-phosphate 5-kinase type-1 sktl
- EG:86E4.5 protein
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- phosphoinositide 5-phosphatase
- Putative 1-phosphatidylinositol 3-phosphate 5-kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Phosphatidylinositol 4-phosphate 5-kinase 59B, isoform E
Sequence:
MSGARDQTDPPLLQLEDEVDLIGDFAKDQPPPRNQLSPLLNGFESTSNQLTTKVEINTVGMGKRKTRRRGKKAREPMLLSVDDEDDEEEAQEERNHTNGLPPGEESAGGDAVIQKPQLDNLVMHYDDQIDDEDGEEAVLLKRSSNPRNQRLKGSAEDSIDSSSQQPPIICHIAPAKVASSALTSPLKTTSHTALARHPHDEADDICLVPEIDFEGMSTDAGSDNRESQPLLGGGNASHGSRISELLGGLGRGHDHVEFVSNTFGDDPLFSEIVAKAEGAIENGVLPERIYQGSSGSYFVKDASHQCLAVFKPKDEEPYGRLNPKWTKWMHKLCCPCCFGRACLIPNQGYLSESGASLVDRKLNLNVVPKTRVVRLVAESFNYARIDRQKAKLKKRIKEHYPSAHFNRMSLPLKTGSFQLFVEGYKDADYWLRRFESEPLPPSVAKSFQLQFERLVVLDYIIRNTDRGNDNWLIKYVAPKITTQVGGTGGRTMHGVVTPKLPNALGASKIVDLNEPPQASPKPTTGGRPSNHLAGGAATSAQQDSSSLASSEDEPSSRSPPTSEPDWNVVNSAFIRIAAIDNGLAFPFKHPDSWRAYPYHWAWLPQAKIPFSEEIKEQVLPQLSDMNFVEEICTELLYLFQQDRGFDKRLFERQMSVMRGQILNLTQALRDGKSPVQLVQMPAVIVERSSGSRFFSFTQRFQNKSPFFSWC
Protein: Dof zinc finger protein DOF5.7 (AtDOF5.7) (Q9LSL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- 2-oxoglutarate
- B3 domain-containing protein At3g06220
- AT-hook motif nuclear-localized protein 12
- Uncharacterized membrane protein At3g27390
- L-type lectin-domain containing receptor kinase IX.2
- Small ribosomal subunit protein mS81
- Lon protease homolog 3, mitochondrial
- B3 domain-containing protein REM1
- At1g64385
- Zinc finger CCCH domain-containing protein 66
Sequence:
MSSHTNLPSPKPVPKPDHRISGTSQTKKPPSSSVAQDQQNLKCPRCNSPNTKFCYYNNYSLSQPRHFCKSCRRYWTRGGALRNVPIGGGCRKTKKSIKPNSSMNTLPSSSSSQRFFSSIMEDSSKFFPPPTTMDFQLAGLSLNKMNDLQLLNNQEVLDLRPMMSSGRENTPVDVGSGLSLMGFGDFNNNHSPTGFTTAGASDGNLASSIETLSCLNQDLHWRLQQQRMAMLFGNSKEETVVVERPQPILYRNLEIVNSSSPSSPTKKGDNQTEWYFGNNSDNEGVISNNANTGGGGSEWNNGIQAWTDLNHYNALP
Protein: Uncharacterized protein, isoform D (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5) (X2J9G3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPINPLLITAFGLFITVCPRPSTAAAVIGRVDGAEGNKTAWELTEALYGTSGLRSFNGTWITDEEPTTLQPTDPSTNSMRPPRQM
Protein: Parthenolide synthase (Tp2116) (TpPTS) (EC 1.14.14.-) (Cytochrome P450 71CA1) (X2EVV9)
Organism: Tanacetum parthenium (Feverfew) (Matricaria parthenium)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti-cancer drugs highly active against colon cancer cells. Catalyzes the conversion of costunolide to parthenolide.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDTSTSFPSLFLPTLCTILISYIIIKYVLIWNRSSMAAFNLPPSPPKLPIIGNIHHVFSKNVNQTLWKLSKKYGPVMLIDTGAKSFLVVSSSQMAMEVLKTHQEILSTRPSNEGTKRLSYNFSDITFSPHGDHWRDMRKVFVNEFLGPKRAGWFNQVLRMEIKDVINNLSSNPLNTSINLNEMLLSLVYRVVCKFAFGKSYREEPFNGVTLKEMLDESMVVLAGSSADMFPTFGWILDKLYGWNDRLEKCFGNLDGFFEMIINEHLQSASETSEDEKDFVHSLVELSLKDPQFTKDYIKALLLNVLLGAIDTTFTTIVWAMSEIVKNTQVMQKLQTEIRSCIGRKEEVDATDLTNMAYLKMVIKETLRLHPPAPLLFPRECPSHCKIGGYDVFPGTCVVMNGWGIARDPNVWKEIPNEFYPERFENFNIDFLGNHCEMIPFGAGRRSCPGMKSATSTIEFTLVNLLYWFDWEVPSGMNNQDLDMEEDGFLVIQKKSPLFLIPIKHI
Protein: Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) (EC 3.4.17.-) [Cleaved into: Processed angiotensin-converting enzyme 2] (Q58DD0)
Organism: Bos taurus (Bovine)
Function: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity.
Subcellular location: [Processed angiotensin-converting enzyme 2]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BYF1}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R0I0}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:Q8R0I0}.
Interaction partners:
- Dipeptidyl peptidase 4
- Neprilysin
- renin
- Transmembrane protease serine 2
- Angiotensinogen
- Lysosomal Pro-X carboxypeptidase
- Transporter
- Meprin A subunit
- Xaa-Pro aminopeptidase 2
- Furin
Sequence:
MTGSFWLLLSLVAVTAAQSTTEEQAKTFLEKFNHEAEDLSYQSSLASWNYNTNITDENVQKMNEARAKWSAFYEEQSRMAKTYSLEEIQNLTLKRQLKALQHSGTSALSAEKSKRLNTILNKMSTIYSTGKVLDPNTQECLALEPGLDDIMENSRDYNRRLWAWEGWRAEVGKQLRPLYEEYVVLENEMARANNYEDYGDYWRGDYEVTGAGDYDYSRDQLMKDVERTFAEIKPLYEQLHAYVRAKLMHTYPSYISPTGCLPAHLLGDMWGRFWTNLYSLTVPFEHKPSIDVTEKMENQSWDAERIFKEAEKFFVSISLPYMTQGFWDNSMLTEPGDGRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPYLLRNGANEGFHEAVGEIMSLSAATPHYLKALGLLAPDFHEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKQQWMEKWWEMKREIVGVVEPLPHDETYCDPACLFHVAEDYSFIRYYTRTIYQFQFHEALCKTAKHEGALFKCDISNSTEAGQRLLQMLRLGKSEPWTLALENIVGIKTMDVKPLLNYFEPLFTWLKEQNRNSFVGWSTEWTPYSDQSIKVRISLKSALGENAYEWNDNEMYLFQSSVAYAMRKYFSEARNETVLFGEDNVWVSDKKPRISFKFFVTSPNNVSDIIPRTEVENAIRLSRDRINDVFQLDDNSLEFLGIQPTLGPPYEPPVTIWLIIFGVVMGVVVIGIVVLIFTGIRNRRKKNQASSEENPYGSVDLNKGENNSGFQNIDDVQTSL
Protein: Nucleolar protein 16 (Q57W06)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MGRIRVTPKGKAKKNIPITRSGRKKYLKRRFAHLHQIDKAGSNNYFTKKYFKRFSTASSNFKSLGLAKDPSITPKKIVDEPSQPTRRLEEENELEELRQQRKGTLQVRRISEEEAVTMANLIRKHQTDFKAMSLDRKLNPYQLNPRQLQRQVVNYLRWEKAAFPEAFAEAEANGWLSIEEYANPKNRHRKE
Protein: KHG/KDPG aldolase ((4S)-4-hydroxy-2-oxoglutarate aldolase) (EC 4.1.3.42) (2-dehydro-3-deoxy-phosphogluconate aldolase) (EC 4.1.2.14) (2-keto-3-deoxy-6-phosphogluconate aldolase) (KDPG aldolase) (2-keto-4-hydroxyglutarate aldolase) (KHG aldolase) (Ketohydroxyglutarate aldolase) (Entner-Douderoff aldolase) (Oxaloacetate decarboxylase) (EC 4.1.1.112) (Phospho-2-dehydro-3-deoxygluconate aldolase) (Phospho-2-keto-3-deoxygluconate aldolase) (P0A955)
Organism: Escherichia coli (strain K12)
Function: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphogluconate dehydratase
- 2-dehydro-3-deoxygluconokinase
- Glucose-6-phosphate 1-dehydrogenase
- Glucokinase
- Glucose-6-phosphate isomerase
- Isocitrate lyase
- HTH-type transcriptional regulator HexR
- Malate synthase A
- Glyoxylate/hydroxypyruvate reductase B
- Malate synthase G
Sequence:
MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAIAKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDYDRITKLAREAVEGAKL
Protein: Purine nucleoside phosphorylase (Q47QW5)
Organism: Thermobifida fusca (strain YX)
Interaction partners:
- Pyridoxal phosphate homeostasis protein
- Cell division protein SepF
- YggT family protein
- Pseudouridine synthase
- Cell division protein FtsZ
Sequence:
MTGTVVELAPGIHAGFTGRAGGVSGEPYATLNLGDHVGDDPAAVAENRRRAALGFGISPDRVVWMNQVHGATAVTVTGSGQAGDVDAVVTPEAGLALAVLVADCLPLLVADAAAGVIGAAHAGRPGMAAGVVPALVAEMARHGARPERCVALLGPAICGRCYEVPRDLQDRVARTVPEARCTTAEGTPGLDIRAGVTAQLTNLGVTNITHDSRCTRESADLFSYRRDATTGRFAGYVWRVP