wanglab/gogpt-training-data huggingface dataset:
Protein: D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein) (Q5RJG7)
Organism: Mus musculus (Mouse)
Function: Cytidylyltransferase required for protein O-linked mannosylation (By similarity). Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively (By similarity). Not involved in dolichol production (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A4D126}.
Interaction partners:
- Ribitol-5-phosphate transferase FKTN
- Beta-1,4-glucuronyltransferase 1
- Ribitol 5-phosphate transferase FKRP
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannosyl-transferase 2
- Protein O-mannosyl-transferase 1
Sequence:
MEPGPCSRPAEPGHCVSGPAGAGSAFPESPLSVAGAEPGNRPGTVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATRHRSIFNGLKALAEDQPDCKLTKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTECLQLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKEKISQEICVVMNTKDEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFIEQCYSFICVNVVSPDSQETRKLLRILEESSLPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQDEQKLQESLGQSAAIIAALVKERNSALVGQLLVA
Protein: Bile pigment transporter 1 (P14772)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12044871}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:12044871}.
Interaction partners:
- Metal resistance protein YCF1
- Oligomycin resistance ATP-dependent permease YOR1
Sequence:
MSSLEVVDGCPYGYRPYPDSGTNALNPCFISVISAWQAVFFLLIGSYQLWKLYKNNKVPPRFKNFPTLPSKINSRHLTHLTNVCFQSTLIICELALVSQSSDRVYPFILKKALYLNLLFNLGISLPTQYLAYFKSTFSMGNQLFYYMFQILLQLFLILQRYYHGSSNERLTVISGQTAMILEVLLLFNSVAIFIYDLCIFEPINELSEYYKKNGWYPPVHVLSYITFIWMNKLIVETYRNKKIKDPNQLPLPPVDLNIKSISKEFKANWELEKWLNRNSLWRAIWKSFGRTISVAMLYETTSDLLSVVQPQFLRIFIDGLNPETSSKYPPLNGVFIALTLFVISVVSVFLTNQFYIGIFEAGLGIRGSLASLVYQKSLRLTLAERNEKSTGDILNLMSVDVLRIQRFFENAQTIIGAPIQIIVVLTSLYWLLGKAVIGGLVTMAIMMPINAFLSRKVKKLSKTQMKYKDMRIKTITELLNAIKSIKLYAWEEPMMARLNHVRNDMELKNFRKIGIVSNLIYFAWNCVPLMVTCSTFGLFSLFSDSPLSPAIVFPSLSLFNILNSAIYSVPSMINTIIETSVSMERLKSFLLSDEIDDSFIERIDPSADERALPAIEMNNITFLWKSKEVLTSSQSGDNLRTDEESIIGSSQIALKNIDHFEAKRGDLVCVVGRVGAGKSTFLKAILGQLPCMSGSRDSIPPKLIIRSSSVAYCSQESWIMNASVRENILFGHKFDQDYYDLTIKACQLLPDLKILPDGDETLVGEKGISLSGGQKARLSLARAVYSRADIYLLDDILSAVDAEVSKNIIEYVLIGKTALLKNKTIILTTNTVSILKHSQMIYALENGEIVEQGNYEDVMNRKNNTSKLKKLLEEFDSPIDNGNESDVQTEHRSESEVDEPLQLKVTESETEDEVVTESELELIKANSRRASLATLRPRPFVGAQLDSVKKTAQKAEKTEVGRVKTKIYLAYIKACGVLGVVLFFLFMILTRVFDLAENFWLKYWSESNEKNGSNERVWMFVGVYSLIGVASAAFNNLRSIMMLLYCSIRGSKKLHESMAKSVIRSPMTFFETTPVGRIINRFSSDMDAVDSNLQYIFSFFFKSILTYLVTVILVGYNMPWFLVFNMFLVVIYIYYQTFYIVLSRELKRLISISYSPIMSLMSESLNGYSIIDAYDHFERFIYLNYEKIQYNVDFVFNFRSTNRWLSVRLQTIGATIVLATAILALATMNTKRQLSSGMVGLLMSYSLEVTGSLTWIVRTTVTIETNIVSVERIVEYCELPPEAQSINPEKRPDENWPSKGGIEFKNYSTKYRENLDPVLNNINVKIEPCEKVGIVGRTGAGKSTLSLALFRILEPTEGKIIIDGIDISDIGLFDLRSHLAIIPQDAQAFEGTVKTNLDPFNRYSEDELKRAVEQAHLKPHLEKMLHSKPRGDDSNEEDGNVNDILDVKINENGSNLSVGQRQLLCLARALLNRSKILVLDEATASVDMETDKIIQDTIRREFKDRTILTIAHRIDTVLDSDKIIVLDQGSVREFDSPSKLLSDKTSIFYSLCEKGGYLK
Protein: Ethylene-responsive transcription factor RAP2-1 (Protein RELATED TO APETALA2 1) (Q8LC30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEREQEESTMRKRRQPPQEEVPNHVATRKPYRGIRRRKWGKWVAEIREPNKRSRLWLGSYTTDIAAARAYDVAVFYLRGPSARLNFPDLLLQEEDHLSAATTADMPAALIREKAAEVGARVDALLASAAPSMAHSTPPVIKPDLNQIPESGDI
Protein: Putative acetolactate synthase large subunit IlvX (ALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase large subunit) (AHAS) (O53554)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Interaction partners:
- Putative acetolactate synthase small subunit
- Putative acetolactate synthase large subunit IlvB2
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydrogenase
- L-threonine dehydratase biosynthetic IlvA
- 2-isopropylmalate synthase
- Acetolactate synthase large subunit IlvB1
- Acetolactate synthase large subunit IlvG
- 2-oxoglutarate oxidoreductase subunit KorA
- 2-oxoglutarate oxidoreductase subunit KorB
Sequence:
MNGAQALINTLVDGGVDVCFANPGTSEMHFVAALDAVPRMRGMLTLFEGVATGAADGYARIAGRPAAVLLHLGPGLGNGLANLHNARRARVPMVVVVGDHATYHKKYDAPLESDIDAVAGTVSGWVRRTEAAADVGADAEAAIAASRSGSQIATLILPADVCWSDGAHAAAGVPAQAAAAPVDVGPVAGVLRSGEPAMMLIGGDATRGPGLTAAARIVQATGARWLCETFPTCLERGAGIPAVERLAYFAEGAAAQLDGVKHLVLAGARSPVSFFAYPGMPSDLVPAGCEVHVLAEPGGAADALAALADEVAPGTVAPVAGASRPQLPTGDLTSVSAADVVGALLPERAIVVDESNTCGVLLPQATAGAPAHDWLTLTGGAIGYGIPAAVGAAVAAPDRPVLCLESDGSAMYTISGLWSQARENLDVTTVIYNNGAYDILRIELQRVGAGSDPGPKALDLLDISRPTMDFVKIAEGMGVPARRVTTCEEFADALRAAFAEPGPHLIDVVVPSLVG
Protein: ATP-dependent 6-phosphofructokinase 3 (ATP-PFK 3) (Phosphofructokinase 3) (EC 2.7.1.11) (Phosphohexokinase 3) (Q94AA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:17485088}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- transaldolase
- Aldolase-type TIM barrel family protein
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
- Hexokinase-4
Sequence:
MSTVESSKPKIINGSCGYVLEDVPHLSDYLPGLPTYPNPLQDNPAYSVVKQYFVDADDSVPQKIVVHKDGPRGIHFRRAGPRQKVYFESDEVHACIVTCGGLCPGLNTVIREIVSSLSYMYGVKRILGIDGGYRGFYAKNTVSLDSKVVNDIHKRGGTILGTSRGGHDTTKIVDSIQDRGINQVYIIGGDGTQRGASVIFEEIRRRGLKVAVIGIPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEAESIENGIGVVKLMGRYSGFIAMYATLASRDVDCCLIPESPFYLEGEGGLFEYIEKRLKESGHMVLVIAEGAGQDLMSKSMESMTLKDASGNKLLKDVGLWLSQSIKDHFNQKKMVMNLKYIDPTYMIRAVPSNASDNVYCTLLAQSAVHGAMAGYTGYISGLVNGRQTYIPFYRITEKQNHVVITDRMWARLLSSTNQPSFLGPKDVFDNKEKPMSALLDDGNCNGVVDVPPVTKEITK
Protein: Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (EC 3.1.3.99) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77) (D3ZMY7)
Organism: Rattus norvegicus (Rat)
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (By similarity). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (By similarity). Through these activities regulates the purine nucleoside/nucleotide pools within the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}.
Interaction partners:
- 5'-nucleotidase, cytosolic IA
- Deoxycytidine kinase
- Purine nucleoside phosphorylase
- AMP deaminase 2
- Deoxycytidylate deaminase
- 5'-nucleotidase
- AMP deaminase 3
- Inosine-5'-monophosphate dehydrogenase 1
- AMP deaminase 1
- 7-methylguanosine phosphate-specific 5'-nucleotidase
Sequence:
MMTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLNFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE
Protein: General odorant-binding protein 69a (Odorant-binding protein 69a) (Pheromone-binding protein-related protein 1) (PBPRP-1) (P54191)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant-binding protein required for olfactory behavior and activity of pheromone-sensitive neurons in response to the male-specific pheromone cis-vaccenyl acetate (cVA). Modulates social responsivity differently in males and females, regulating male aggression and female receptivity respectively.
Subcellular location: Secreted {ECO:0000269|PubMed:29630598}. Note=Secreted in the lumen of olfactory hairs. {ECO:0000269|PubMed:29630598}.
Interaction partners:
- Pheromone-binding protein-related protein 6
- General odorant-binding protein 83a
- General odorant-binding protein 19a
- General odorant-binding protein lush
- General odorant-binding protein 84a
- General odorant-binding protein 28a
- Carboxylic ester hydrolase
- General odorant-binding protein 19d
- Antennal-specific protein OS-C
- Putative odorant-binding protein A5
Sequence:
MVARHFSFFLALLILYDLIPSNQGVEINPTIIKQVRKLRMRCLNQTGASVDVIDKSVKNRILPTDPEIKCFLYCMFDMFGLIDSQNIMHLEALLEVLPEEIHKTINGLVSSCGTQKGKDGCDTAYETVKCYIAVNGKFIWEEIIVLLG
Protein: Uncharacterized protein YggN (P0ADS9)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YgiM
- Putative type II secretion system M-type protein YghD
Sequence:
MMRKMLLAAALSVTAMTAHADYQCSVTPRDDVIVSPQTVQVKGENGNLVITPDGNVMYNGKQYSLNAAQREQAKDYQAELRSTLPWIDEGAKSRVEKARIALDKIIVQEMGESSKMRSRLTKLDAQLKEQMNRIIETRSDGLTFHYKAIDQVRAEGQQLVNQAMGGILQDSINEMGAKAVLKSGGNPLQNVLGSLGGLQSSIQTEWKKQEKDFQQFGKDVCSRVVTLEDSRKALVGNLK
Protein: cGMP-dependent protein kinase (EC 2.7.11.12) (Q8MMZ8)
Organism: Eimeria tenella (Coccidian parasite)
Function: Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305|PubMed:11897122}; Lipid-anchor {ECO:0000305|PubMed:11897122}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305|PubMed:11897122}.
Interaction partners:
Sequence:
MGACSSKAQHQTRDPEPREQQAAQEQKSTGPSGAPNDAPAPAEAERKMSGSSATAPKGEMPTASTGTPEQQQQQQQQQQQQQEQQQHPEHQQSEKQQQHGEEQQQERKPSQQQQNEEAAAPHKHGGERKVQKAIKQQEDTQAEDARLLGHLEKREKTPSDLSLIRDSLSTNLVCSSLNDAEVEALANAVEFFTFKKGDVVTKQGESGSYFFIVHSGEFEVIVNDKVVNKILTGQAFGEISLIHNSARTATIKTLSEDAALWGVQRQVFRETLKQLSSRNFAENRQFLASVKFFEMLTEAQKNVITNALVVQSFQPGQAIVKEGEKGDVLYILKSGKALVSIKNKEVRVLQRGEYFGERALLYDEPRSATITAEEPTVCVSIGRDLLDRVLGNLQHVLFRNIMLEALQQSKVFASFPTEQLSRLIGSVVVKDYPENYIILDRENRTRASASALFSAQGVRFFFVLEGEVSVFAYKDKSSSSSSSSSSSSSSSSAEGEMELHLIDTLKRGQAFGDEYVLSPNKPFAHCVKSNGPTKLALLTASALTATLGGQDIDETLDYNNKLAITKKMYIFRYLSEQQTQTLIKAFKTVRYTQGESIIREGEIGSRFFIIKLGEVVILKGEKRVRTLGRHDYFGERALLHDERRSATVAANSPEVDLWVVDKDVFLQIVKGPMLTHLEERIRMQDTKVEFKDLNVVRVVGRGTFGTVKLVQHIPTQMRYALKCVSRKSVVALNQQDHIRLEREIMAENDHPFIIRLVRTFRDKEFLYFLTELVTGGELYDAIRKLGLLGRYQAQFYLASIVLAIEYLHERNIAYRDLKPENILLDSQGYVKLIDFGCAKKMQGRAYTLVGTPHYMAPEVILGKGYTLTADTWAFGVCLYEFMCGPLPFGNDAEDQLEIFRDILAGKLIFPHYVTDQDAINLMKRLLCRLPEVRIGCSINGYKDIKEHAFFSDFDWDRLAGRDLSPPLLPKGEIYAEDAEEGGLDIEEDEGIELEDEYEWDKDF
Protein: Receptor-like protein 52 (AtRLP52) (Q7FZR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for defense against powdery mildew pathogen.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Receptor-like kinase
- Disease resistance protein
- RING-type E3 ubiquitin transferase
- Pathogenesis-related thaumatin superfamily protein
- Putative disease resistance protein At1g58400
- Heavy metal transport/detoxification superfamily protein
Sequence:
MTFLPLLFIFFFLTSIPFPAFSQYNDRSTLLNLKRDLGDPLSLRLWNDTSSPCNWPRITCTAGNVTEINFQNQNFTGTVPTTICNFPNLKSLNLSFNYFAGEFPTVLYNCTKLQYLDLSQNLFNGSLPDDINRLAPKLKYLDLAANSFAGDIPKNIGRISKLKVLNLYMSEYDGTFPSEIGDLSELEELQLALNDKFTPVKLPTEFGKLKKLKYMWLEEMNLIGEISAVVFENMTDLKHVDLSVNNLTGRIPDVLFGLKNLTELYLFANDLTGEIPKSISAKNLVHLDLSANNLNGSIPESIGNLTNLELLYLFVNELTGEIPRAIGKLPELKELKLFTNKLTGEIPAEIGFISKLERFEVSENQLTGKLPENLCHGGKLQSVIVYSNNLTGEIPESLGDCETLSSVLLQNNGFSGSVTISNNTRSNNNFTGKIPSFICELHSLILLDLSTNKFNGSIPRCIANLSTLEVLNLGKNHLSGSIPENISTSVKSIDIGHNQLAGKLPRSLVRISSLEVLNVESNKINDTFPFWLDSMQQLQVLVLRSNAFHGSINQNGFSKLRIIDISGNHFNGTLPLDFFVNWTAMFSLGKIEDQYMGTNYMRTNYYSDSIVVMIKGIALEMVRILNTFTTIDFSGNKFEGEIPRSVGLLKELHVLNLSNNGFTGHIPSSMGNLIELESLDVSQNKLSGEIPPELGKLSYLAYMNFSQNQFVGLVPGGTQFQTQPCSSFADNPRLFGLSLERVCVDIHKKTPQQSEMPEPEEDEEEVMNWTAAAIGSIPGISIGLTMGYILVSYKPEWLMNSGRNKRRIKPI
Protein: Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase) (Q9JHF7)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Prostaglandin-H2 D-isomerase
- Prostaglandin E synthase
- Thromboxane-A synthase
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase 3
- Prostacyclin synthase
- Prostaglandin G/H synthase 2
- Glutathione S-transferase theta-1
- Prostamide/prostaglandin F synthase
Sequence:
MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTIHQSLAIARYLTKNTDLAGKTALEQCQADAVVDTLDDFMSLFPWAEKDQDLKERMFNELLTHQAPRLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPGLLDIYPKLVSLRNKVQAIPAISAWILKRPQTKL
Protein: Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (P58137)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs. Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT). Is also able to hydrolyze CoA esters of dicarboxylic acids. It is involved in the metabolic regulation of peroxisome proliferation (By similarity).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:11673457}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000250|UniProtKB:O14734}.
Interaction partners:
- Sterol carrier protein 2
- Bile acid-CoA:amino acid N-acyltransferase
- Long-chain fatty acid transport protein 5
- Acyl-coenzyme A amino acid N-acyltransferase 1
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Acyl-coenzyme A thioesterase 3
- Acyl-coenzyme A thioesterase 13
- AN1-type zinc finger protein 2B
- Acyl-coenzyme A thioesterase 1
- Acyl-coenzyme A thioesterase 2, mitochondrial
Sequence:
MSAPEGLGDAHGDADRGDLSGDLRSVLVTSVLNLEPLDEDLYRGRHYWVPTSQRLFGGQIMGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQHQFSMPSVPPPEDLLDHEALIDQYLRDPNLHKKYRVGLNRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLKPQVSESKL
Protein: GATA transcription factor 28 (Protein TIFY 2A) (ZIM-like 2 protein) (Q8H1G0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein TIFY 4A
- Protein TIFY 8
- Protein FAR1-RELATED SEQUENCE 3
- Protein TIFY 4B
- WPP domain-interacting protein 3
- PLATZ transcription factor family protein
- Cryptochrome-1
- Cell differentiation, Rcd1-like protein
- Telomerase reverse transcriptase
- Armadillo repeat-containing protein LFR
Sequence:
MDDLHGSNARMHIREAQDPMHVQFEHHALHHIHNGSGMVDDQADDGNAGGMSEGVETDIPSHPGNVTDNRGEVVDRGSEQGDQLTLSFQGQVYVFDSVLPEKVQAVLLLLGGRELPQAAPPGLGSPHQNNRVSSLPGTPQRFSIPQRLASLVRFREKRKGRNFDKKIRYTVRKEVALRMQRNKGQFTSAKSNNDEAASAGSSWGSNQTWAIESSEAQHQEISCRHCGIGEKSTPMMRRGPAGPRTLCNACGLMWANKGAFRDLSKASPQTAQNLPLNKNEDANLETDHQIMITVANDISNSQ
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] GPDHC1, cytosolic (EC 1.1.1.8) (O22216)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cell redox homeostasis. Required for maintaining a steady state cellular NADH/NAD(+) ratio through a mitochondrial glycerol-3-phosphate redox shuttle. May function with the mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase SDP6 to shuttle reducing equivalents into the mitochondria for respiration.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- Glycerol-3-phosphate acyltransferase 9
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 2
- Putative lipid phosphate phosphatase 3, chloroplastic
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Glycerol kinase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 3
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
Sequence:
MVGSIEAKSLQSNGSVHHIGLNLEEKLDEFRRLLGKSEKDPLRIVSVGAGAWGSVFAALLQESYGGFRDKFQIRIWRRAGRAVDRETAEHLFEVINSREDILRRLIRRCAYLKYVEARLGDRTLYADEILKDGFCLNMVDTPLCPLKVVTNLQEAVWDADIVVNGLPSTETREVFEEISKYWKERITVPIIISLSKGIETALEPVPHIITPTKMIHQATGVPIDNVLYLGGPNIAAEIYNKEYANARICGAAKWRKPLAKFLRQPHFIVWDNSDLVTHEVMGGLKNVYAIGAGMVAALTNESATSKSVYFAHCTSEMIFITHLLAEEPEKLAGPLLADTYVTLLKGRNAWYGQMLAKGEINRDMGDSISGKGMIQGVSAVGAFYQLLSQSSLSILPSEEKKPVAPVESCPILKTLYKILITREQSTQAILQALRDETLNDPRDRIEIAQSHAFYRPSLLGQP
Protein: LexA repressor (EC 3.4.21.88) (Q9KVP9)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV
- DNA repair protein RecN
- O-methyltransferase-related protein
Sequence:
MKPLTPRQQEVFDLIKSKIDETGMPPTRAEIAKELGFRSANAAEEHLKALARKQVIEMVPGASRGIRILVDNAANEEEAETGLPLIGRVAAGEPILAQEHVEAHYQVDPSMFRPQADFLLRVHGESMKNIGILDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSKVFLHAENEEFAPIEVDLAAQSLTIEGIAVGVIRNSTWM
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (Large GTP-binding protein) (LargeG) (Optic atrophy protein 1 homolog) [Cleaved into: Dynamin-like GTPase OPA1, long form (L-OPA1); Dynamin-like GTPase OPA1, short form (S-OPA1)] (P58281)
Organism: Mus musculus (Mouse)
Function: Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion (By similarity). Binds lipid membranes enriched in negatively charged phospholipids, such as cardiolipin, and promotes membrane tubulation. The intrinsic GTPase activity is low, and is strongly increased by interaction with lipid membranes (By similarity). Plays a role in remodeling cristae and the release of cytochrome c during apoptosis. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. Plays a role in mitochondrial genome maintenance (By similarity).
Subcellular location: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000269|PubMed:11847212, ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:28746876}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000250|UniProtKB:O60313}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, short form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:20038678, ECO:0000269|PubMed:22433842}.
Interaction partners:
- Mitofusin-2
- Metalloendopeptidase OMA1, mitochondrial
- Mitofusin-1
- Serine/threonine-protein kinase PINK1, mitochondrial
- Mitochondrial fission 1 protein
- NAD-dependent protein deacetylase sirtuin-3
- Mitochondrial dynamics protein MID49
- Presenilin-associated rhomboid-like protein, mitochondrial
- Mitochondrial fission factor
- E3 ubiquitin-protein ligase parkin
Sequence:
MWRAGRAAVACEVCQSLVKHSSGIQRNVPLQKLHLVSRSIYRSHHPALKLQRPQLRTPFQQFSSLTHLSLHKLKLSPIKYGYQPRRNFWPARLAARLLKLRYIILGSAVGGGYTAKKTFDEWKDMIPDLSDYKWIVPDFIWEIDEYIDLEKIRKALPSSEDLASLAPDLDKITESLSLLKDFFTAGSPGETAFRATDHGSESDKHYRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQGRLKDTENAIENMIGPDWKKRWMYWKNRTQEQCVHNETKNELEKMLKVNDEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFIDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKVKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK