wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau) (P10636)
Organism: Homo sapiens (Human)
Function: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10747907, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:26014385}. Cell membrane {ECO:0000269|PubMed:10747907}; Peripheral membrane protein {ECO:0000269|PubMed:10747907}; Cytoplasmic side {ECO:0000269|PubMed:10747907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10747907}. Cell projection, axon {ECO:0000269|PubMed:10747907}. Cell projection, dendrite {ECO:0000269|PubMed:23666762}. Secreted {ECO:0000269|PubMed:32272059}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components (PubMed:10747907). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:10747907, ECO:0000269|PubMed:32272059}.
Interaction partners:
- Cyclin-dependent kinase 5
- Glycogen synthase kinase-3 beta
- Tubulin alpha-1B chain
- Amyloid-beta precursor protein
- Tubulin beta-2B chain
- Tyrosine-protein kinase Fyn
- Alpha-synuclein
- Apolipoprotein E
- Tubulin beta-3 chain
- Tubulin alpha-4A chain
Sequence:
MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Protein: Zinc transporter 2 (Q22541)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- SUppressor of activated let-60 Ras
- Histidine ammonia-lyase
- High zinc activated nuclear receptor protein
- Metallothionein-2
- ABC-type xenobiotic transporter
- Metallothionein-1
- SNAPIN protein homolog
- CaDmium Responsive
- Putative glucosylceramidase 3
- Gut granule loss protein 3
Sequence:
MISERAPLLENGVPHIYNTDEGRKTTVTYDNFHCHDEADSTDSHDSNRRATRILWLTVVLCLFFMVCEVIGGVLAGSLAIVTDAAHLLTDFASVLISLFSLYIARRPPSQKMSFGFHRAEVLGAFFSVFLIWIVTGVLVVLAIMRIVSGDYEVEGGIMALTAALGVVVNLVMLALLYFGGHSHSHGGGSSHGHSHGGGNGDNINVRAAFIHVLGDLLQSLGVLVAALFIYFQPSWVIIDPICTLVFSVIVLCTTIYILRDAMIVLLEGRPSNIDFAKVFSSLEDIEGVKKVHDLRIWSLTMDKIALSVHLEIDANSQSQSILRETRKMLKQTYNVHEITIQIEEFGANRSDCGKCDFPTK
Protein: IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 (G5EE44)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MFNARYRNIKEKKAAKMTYRAMIYNCLERPTGWKCFLYHFSVFLIVLICLILSVLSTVEEHSHFAAELLYILEIVLVVFFSVEFIVRLWSAGCRSKYIGVYGRLKFVRKPITLIDLVVVICSLFVICFGTEGQVFAASAMRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDHIGVDGRQAFTSYADALWWGVITMTTIGYGDVVPQTWLGRIVASCFSIFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAATLIQCLWRCHAAEKKVSATWNAHIDPLAHETKETHHWNGKKHASSMDSNNLTRKRQLFKKQSSLVNTFRRKGSPSTDVEMGELQQERLLRHERNSDTDDEKRIYRVGADIEIDYETEEPTTPTRPQGHISHVCELTDAHRNAIRAIRRVKYFVARRRFQQARKPYDVRDVIEQYSQGHLNMMVRIKELQRRLDQTLGKPGQYDGKGSRKGHPVTIGSRLSRLELQMSSLDRKVESSNRTLNALYRLMADRNSLTISPSPPALISRPVSPAACLSPRDQLSPTSISSQRSGSPGWQ
Protein: Heptahelical transmembrane protein 1 (PAQR family protein HHP1) (Q93ZH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a negative regulator of abscisic acid (ABA)-mediated osmotic stress signaling and function in cross-talk between cold and osmotic signaling.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Methyl-CpG-binding domain-containing protein 2
- Methyl-CpG-binding domain-containing protein 4
- Methyl-CpG-binding domain-containing protein 1
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 6
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
Sequence:
MDQNGHNDEAETVSCGNGNCKSKIVPGDDHGGDESSGTKRRKKRKTQQKTMKRRELMSYCELPEYMKDNEYILNYYRADWSIRDAFFSVFSFHNESLNVWTHLIGFIFFVALTVANIIHHDGFFPVDAKSPGNVTRWPFFVFLGGSMFCLLASSICHLFCCHSKELNVFLLRIDYAGITAMIITSFFPPIFYIFQCTPRWYFIYLAGITSMGIFTIITLFTPSLSAPKYRAFRALLFASMGLFGIVPAAHALVVNWGNPQRNVTLVYELLMAVFYLVGTGFYVGRVPERLKPGWFDRVGHSHQIFHVFVLLGALSHYAAALLFLDWRDHVGC
Protein: ATP-dependent protease ATPase subunit HslU2 (Mitochondrial proteasome-like protease HslVU ATPase subunit 2) (Q382V8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:18421378}. Note=Associated with kinetoplast DNA (kDNA).
Interaction partners:
- ATP-dependent protease subunit HslV
- ATP-dependent protease ATPase subunit HslU1
Sequence:
MIRFSWVRLCSSAMAAAAASPDVQAITRAQAMQLDDLSPRKIASILDSYIVGQAEGKRAVAISLRNRWRRRQIEDEGLRRDILPKNILLVGPTGVGKTEISRRMAKLTEAPFVKVEATKYTEVGFKGKDVESIIEDLYSNAKTKAKRRLEIEREKEAHELALEIVFNGWHSCRSASGSFGSSTRNSGSGDSSAEEDKNSSSRDNVTFEEFKEKYKTQFKDDMVVIDVTQQPKGNTKPNASINSVEMLSVGILLGLGSESRGVKTRVTKRVEEALPLATQEALSRLVDETQISALARTLAEQDGVVFIDEIDKVVTEPASANADVSSTGVQQDLLPLIEGSNVTLKDGSQISTDNILFICSGAFHTVKTSDMIAELQGRLPVRVEMHALKEEDIRRILCEPKFNLLLQQKALMKTENIDLEFTPDAVDELARVTTKVNANAQNIGARRLHTVVERVMDEYSFNCQDYEGKKVVIDAEVVRKATGSLMNNIDLAKYIL
Protein: Magnesium-chelatase subunit ChlI-2, chloroplastic (Mg-chelatase subunit I-2) (EC 6.6.1.1) (Mg-protoporphyrin IX chelatase subunit ChlI-2) (Q5XF33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. Possesses low affinity for ATP and may play a limited role in chlorophyll biosynthesis, and contributes to the assembly of the Mg-chelatase complex.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:18846282}.
Interaction partners:
- Magnesium-chelatase subunit ChlH, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Protoporphyrinogen oxidase 1, chloroplastic
- Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial
- Ferrochelatase-1, chloroplastic/mitochondrial
- Magnesium-chelatase subunit ChlD, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Ferrochelatase-2, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
- Probable E3 ubiquitin-protein ligase EDA40
Sequence:
MASLLGRSPSSILTCPRISSPSSTSSMSHLCFGPEKLSGRIQFNPKKNRSRYHVSVMNVATEINSVEQAKKIDSKESARPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPEITVVSGDPYNSDPRDPECMGKEVREKVQKGEELSVIETKINMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDAELRVKIVEERARFDSNPKEFRETYQEEQLKLQEQITTARSNLSAVQIDQDLKVKISKVCAELDVDGLRGDMVINRAARALAALQGRDQVTAEDVGIVIPNCLRHRLRKDPLESMDSGILVTEKFYEVFT
Protein: Sulfotransferase 2A1 (ST2A1) (EC 2.8.2.2) (Bile salt sulfotransferase) (EC 2.8.2.14) (Hydroxysteroid sulfotransferase) (HST) (P52842)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism (By similarity). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:31100221}.
Interaction partners:
- Cytochrome P450
- Cytochrome P450 1A1
- Cytochrome P450 family 1 subfamily B member 1
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
- NADPH--cytochrome P450 reductase
- Extracellular sulfatase
- Nuclear factor 1
- GATA binding protein 6.
- Steroid sulfatase
Sequence:
MSDDFLWFEGIAFPNMGFRSETLRKVRDEFVIKDEDVIILTYPKSGTNWLIEILCLIHSNGDPKWIQSVPIWERSPWVETEMGYKLLSEEEGPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVFVSGYFFWNSVKFVKKPKSWQQYFEWFCQGNVIYGSWFDHIHGWMPMREKKNFLLLSYEELKQDTRRTVEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNFSLLSVDFVEEKAQLLRKGISGDWKNHLTVAQAEAFDKLFQEKMTDLPRELFPWE
Protein: Recombination activating protein 2 (Q99NM1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
KIYIMSVACKNNKKVTFRCTEKDLVGDVPEARYGHSIDVVYSRGKSVGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLVDFEFGCATSYILPELQDGLSFHVSIARNDTIYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLP
Protein: Protein LAZY 2 (AtLAZY2) (Protein DEEPER ROOTING 3) (AtDRO3) (Protein LAZY1-LIKE 2) (Protein NEGATIVE GRAVITROPIC RESPONSE OF ROOTS 1) (AtNGR1) (Q58G53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of root gravitropism. Functions redundantly with LAZY3 and LAZY4 in the control of root gravitropism. Functions redundantly with LAZY1, LAZY3 and LAZY4 to control plant architecture by coupling gravity sensing to the formation of auxin gradients. Involved redundantly with LAZY1 and LAZY4 in the regulation of both shoot and root gravitropism. Mediates gravity signaling in statocytes downstream of amyloplast displacement, leading to the generation of asymmetric auxin distribution in gravity-responding organs. Regulates the direction of polar auxin transport in response to gravity through the control of asymmetric PIN3 expression in the root cap columella. Regulation of auxin flow by the three proteins LAZY1, LAZY2 and LAZY4 in statocytes influences plant architecture by controlling the growth angle of lateral shoots and lateral roots.
Interaction partners:
- Sm-like protein LSM4
- Sm-like protein LSM2
- Sm-like protein LSM5
- Sm-like protein LSM3B
- Sm-like protein LSM3A
- Protein GOLVEN 6
- Sm-like protein LSM6A
- Sm-like protein LSM7
- Sm-like protein LSM36B
- Sm-like protein LSM8
Sequence:
MKFFGWMQNKLNGDHNRTSTSSASSHHVKQEPREEFSDWPHALLAIGTFGTTSNSVSENESKNVHEEIEAEKKCTAQSEQEEEPSSSVNLEDFTPEEVGKLQKELMKLLSRTKKRKSDVNRELMKNLPLDRFLNCPSSLEVDRRISNALSAVVDSSEENKEEDMERTINVILGRCKEISIESKNNKKKRDISKNSVSYLFKKIFVCADGISTAPSPSLRDTLQESRMEKLLKMMLHKKINAQASSKPTSLTTKRYLQDKKQLSLKSEEEETSERRSSSDGYKWVKTDSDFIVLEI
Protein: Pro-P-factor [Cleaved into: P-factor; P-factor-like 1; P-factor-like 2] (Q09180)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: In h- cells under nutritional starvation, P-factor induces alteration of cell morphology toward mating, arrest of the cell cycle at the G1 phase prior to the initiation of DNA synthesis and indirect transcriptional activation of the sxa2 gene which down-regulates the signaling pathway.
Subcellular location: Secreted.
Interaction partners:
- Carboxypeptidase sxa2
- Pheromone M-factor receptor
- Pheromone P-factor receptor
- Mating factor M secretion protein mam1
- Dibasic-processing endoprotease
- M-factor
- Guanine nucleotide-binding protein alpha-1 subunit
- Mitogen-activated protein kinase spk1
- M-factor
Sequence:
MKITAVIALLFSLAAASPIPVADPGVVSVSKSYADFLRVYQSWNTFANPDRPNLKKREFEAAPAKTYADFLRAYQSWNTFVNPDRPNLKKREFEAAPEKSYADFLRAYHSWNTFVNPDRPNLKKREFEAAPAKTYADFLRAYQSWNTFVNPDRPNLKKRTEEDEENEEEDEEYYRFLQFYIMTVPENSTITDVNITAKFES
Protein: Diphosphoinositol polyphosphate phosphohydrolase aps1 (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase) (Ap6A hydrolase) (Diadenosine hexaphosphate hydrolase (ADP-forming)) (EC 3.6.1.-) (Q09790)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate). Also catalyzes the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A.
Interaction partners:
Sequence:
MLENNGSVILMEPDHLRTAVNRSMTSREGRTKNRFNPITGARLAAGVVALSADKRKVLLVSSAKKHPSWVVPKGGWEADESVQQAALREGWEEGGLVGHITRSLGSFKDKRPTDTIDRRKKYLKQLMSKSSGNDVSTNTELGAEAEKLLLPPRAECEFFEVIVERLEDNYPEMRKRRRKWMSYQEAKEALTSRKDILAALEKSSIIKEEN
Protein: Polyadenylate-binding protein 3 (PABP-3) (Poly(A)-binding protein 3) (Testis-specific poly(A)-binding protein) (Q9H361)
Organism: Homo sapiens (Human)
Function: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Binds poly(A) with a slightly lower affinity as compared to PABPC1.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Eukaryotic translation initiation factor 4 gamma 1
- Polyadenylate-binding protein 2
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-II
- Eukaryotic initiation factor 4A-I
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
Sequence:
MNPSTPSYPTASLYVGDLHPDVTEAMLYEKFSPAGPILSIRICRDLITSGSSNYAYVNFQHTKDAEHALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFVKNLDKSINNKALYDTVSAFGNILSCNVVCDENGSKGYGFVHFETHEAAERAIKKMNGMLLNGRKVFVGQFKSRKEREAELGARAKEFPNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRTFEQMKQDRITRYQVVNLYVKNLDDGIDDERLRKAFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAYLTNEYMQRMASVRAVPNQRAPPSGYFMTAVPQTQNHAAYYPPSQIARLRPSPRWTAQGARPHPFQNKPSAIRPGAPRVPFSTMRPASSQVPRVMSTQRVANTSTQTVGPRPAAAAAAAATPAVRTVPRYKYAAGVRNPQQHRNAQPQVTMQQLAVHVQGQETLTASRLASAPPQKQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLYMLESPESLRSKVDEAVAVLQAHQAKEATQKAVNSATGVPTV
Protein: Non-structural protein 1 (NSP1) (NCVP2) (Non-structural RNA-binding protein 53) (NS53) (A2T3M4)
Organism: Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Function: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities.
Subcellular location: Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04088}.
Interaction partners:
Sequence:
MATFKDACFHYRRLTALNRRLCNIGANSICMPVPDAKIKGWCLECCQIADLTHCYGCSLPHVCKWCVQNRRCFLDNEPHLLKLRTVKHPITKDKLQCIIDLYNIIFPINDKVIRKFERMIKQRKCRNQYKIEWYNHLLLPITLNAAAFKFDENNLYYVFGLYEKSVSDIYAPYRIVNFINEFDKLLLDDINFTRMSNLPIELRNHYAKKYFQLSRLPSSKLKQIYFSDFTKETVIFNTYTKTPGRSIYRNVTEFNWRDELELYSDLKNDKNKLIAAMMTSKYTRFYAHDNNFGRLKMTIFELGHHCQPNYVASNHPGNASDIQYCKWCNIKYFLSKIDWRIRDMYNLLMEFIKDCYKSNVNVGHCSSVENIYPLIKRLIWSLFTNHMDQTIEEVFNHMSPVSVEGTNVIMLILGLNISLYNEIKRTLNVDSIPMVLNLNEFSSIVKSISSKWYNVDELDKLPMSIKSTEELIEMKNSGTLTEEFELLISNSEDDNE
Protein: Zinc finger protein BRUTUS-like At1g18910 (F4IDY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable E3 ubiquitin-protein ligase that may regulate the response to iron deficiency and thus contributes to iron homeostasis.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q8LPQ5}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MGVGDPLPLPPEKNRREVNKPPDIASTSSSSASAVNNARLSDAPILLFVYFHKAFRAQLAELQFLAGDTVRSGSDLAVELRSKFEFLKLVYKYHSAAEDEVIFSALDTRVKNIVFNYSLEHDATDDLFTSVFHWLNVLEEEQGNRADVLREVVLCIGTIQSSICQHMLKEERQVFPLMIENFSFEEQASLVWQFICSVPVMVLEEIFPWMTSLLSPKEKSEVETCFKEVVPNELSLQLVINSWLIDDSQSSLTALTKIMKGVQSVEVSENMTNSQTNSSSSGVFQRFWQWSKKMSFSSPNTGHILVHGIHLWHNAIRKDLVDIQKGLCQLTFPSLSLDLNVLVVRLNFLADVLIFYSNAFKTFFYPVFEDMVDQQHSSSSKQFTIDGHVENFKKSLDLETRAGSDNFVITLQEKLESLILTVAKQFSIEETEVFPIISKNCNIEMQRQLLYRSIHFLPLGLLKCVIMWFSAQLPEDECQSIIHYLSSEDSFPNKPFAHLLLQWFRFGYSGKTPVESFWNELSFMFKPRCSFEEELTEEASGSFFQQSPQKLFKVSDPYSMDPPAGYMNETPYSSAMNQQILIPGKLRPLLHLPDLFGDKTIGEHLTMDLKPIDLIFYFHKAMKKDLDYLVRGSARLATDYSFLGEFQQRFHLIKFLYQIHSDAEDEIAFPALEAKGKLQNISQSYSIDHELEVEHLNKVSFLLNELAELNMLVLDHKNVKYEKLCMSLQDICKSIHKLLSEHLHREETELWCLFRDCFTIEEQEKIIACMLGRISGEILQDMIPWLMESLIPDEQHAVMSLWRQATRKTMFGEWLTEWYNSHAVEEETEEANKDPSENSDPLDVVWSYLFEGAADEYKGSICSKPLEETELKGIMNKPLGKAAPNNKVEFGNKEENHLEISGSKKVCTGADETKYKEQTDSNAQAFQMSHNTSQSGQDSRYECLLSMSQEDVEATIRRISRDSSLDPQKKSYIIQNLLMSRWIATQRIYNLEPSILSSNREAVPGQNPSYRDPHKLIFGCKHYKRSCKLLAPCCNKLYTCIRCHDEEVDHLLDRKQITKMMCMKCMIIQPVGASCSNISCSSSMGKYYCKICKLFDDDREIYHCPYCNLCRLGKGLSIDYFHCMKCNACMSRLIVEHVCREKCLEDNCPICHEYIFTSNSPVKALPCGHVMHSTCFQEYTCSHYTCPICSKSLGDMQVYFRMLDALLAEQKMPDEYLNQTQVILCNDCGRKGNAPYHWLYHKCSSCASYNTRLF
Protein: Pyruvate carboxylase subunit B (H2L2E4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSFNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLRGANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTDKSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECATTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAQFMVQNNLTRETLVDRADDLSFPKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLDAVKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQLLAEGKLNKRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP
Protein: Type 2 topoisomerase subunit B (EC 5.6.2.2) (DNA gyrase subunit B) (O67137)
Organism: Aquifex aeolicus (strain VF5)
Function: A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. If this subunit is reconstituted with GyrA from E.coli the hybrid enzyme supercoils relaxed plasmid DNA; if paired with E.coli ParC supercoiling is not restored. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
Interaction partners:
- Type 2 topoisomerase subunit A
- Beta sliding clamp
- Chromosomal replication initiator protein DnaA
- 4-hydroxythreonine-4-phosphate dehydrogenase
- DNA mismatch repair protein MutL
- UspA domain-containing protein
- Acetoin utilization protein AcuC
- Uncharacterized protein aq_1029
- Chromosome partition protein Smc
Sequence:
MKKRQSQTPQEYTAEAIKAVSGLEHVRLRPAMYIGDIGERGLHHLIWEILDNAVDEAVAGYARNISVTIHRDNSVTVEDDGRGIPVDIHPETGKPAVEMVFTMLGAGGKFEKKVYTYSGGLHGVGASVVNALSEWLIVEVYRDGKIYRMAFKRGEVVEPLHVVGETKKRGTKVSFKPDPEIFETTEIKFDIVEKRVRELAYLNPEVKFELTDERLGKHLIYKFDRGIEELVKYLNEGKEPLFKDIIRIQGEKEGVIVDIAFQYVKDYKERIESFVNNIKTVEGGTHVTGFRSGLSKAVIRMAQGLKLAKELKKSFTGEDVREGLTAVVACKVPNPQFEGQTKTKLGNQNVKQIVESITYDFLTSYFEKKRDVLKAIVEKAIEAALAREAAKKAKELVRRKSPLEEGVLPGKLADCSETDPSKCEIFLVEGDSAGGSAKQARDRRYQAILPLRGKIINVEKARIDKVLSNDEIKAIVSALGCGIGEDLDLKKLRYHKIILMTDADVDGSHIRTLLLTFFYRFMPKLVEEGYVYIAEPPLYRVKKGKKEIYIKDDKEFEHFLLNEIREKGRLVDAREKEFKGEELVRLLIDLKDYEDAYRALVKSKGENLVNFLLTHRVREEDLRNPARVKEITHLMEEELGDYRVDTKYNELEGAYDIIFYDDKLGTKTIIDVNFLSSLSYREVLEGIHLHLPVQVFFENKKVEINSLGEIYDKFMDFARSGMEVQRYKGLGEMNPEQLWETTMNPKTRRLKKVKIEDAAEADRIFTILMGEQVEPRREFIEAYAKEVKHLDV
Protein: Pertussis-like toxin subunit (Subtilase cytotoxin subunit B) (Typhoid-like toxin S-CDT binding subunit PltB) (Q8Z6A3)
Organism: Salmonella typhi
Interaction partners:
- Cytolethal distending toxin subunit B homolog
- Pertussis toxin-like subunit ArtA
- Glycoside hydrolase family 108 protein
Sequence:
MYMSKYVPVYTLLILIYSFNASAEWTGDNTNAYYSDEVISELHVGQIDTSPYFCIKTVKANGSGTPVVACAVSKQSIWAPSFKELLDQARYFYSTGQSVRIHVQKNIWTYPLFVNTFSANALVGLSSCSATQCFGPK
Protein: NADH-dependent fumarate reductase (EC 1.3.1.6) (Q57W38)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Electron transfer protein, putative
- Succinate dehydrogenase, putative
- 2-oxoglutarate dehydrogenase subunit, putative
- oxoglutarate dehydrogenase
- Reiske iron-sulfur protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MVDGRSSASIVAVDPERAARERDAAARALLQDSPLHTTMQYATSGLELTVPYALKVVASADTFDRAKEVADEVLRCAWQLADTVLNSFNPNSEVSLVGRLPVGQKHQMSAPLKRVMACCQRVYNSSAGCFDPSTAPVAKALREIALGKERNNACLEALTQACTLPNSFVIDFEAGTISRKHEHASLDLGGVSKGYIVDYVIDNINAAGFQNVFFDWGGDCRASGMNARNTPWVVGITRPPSLDMLRNPPKEASYISVISLDNEALATSGDYENLIYTADDKPLTCTYDWKAKELMKPSQSNIAQVSVKCYSAMYADALATACFIKRDPAKVRQLLDGWRYVRDTVRDYRVYVRENERVAKMFEIATEDAEMRKRRISNTLPARVIVVGGGLAGLSAAIEAAGCGAQVVLMEKEAKLGGNSAKATSGINGWGTRAQAKASIVDGGKYFERDTYKSGIGGNTDPALVKTLSMKSADAIGWLTSLGVPLTVLSQLGGHSRKRTHRAPDKKDGTPLPIGFTIMKTLEDHVRGNLSGRITIMENCSVTSLLSETKERPDGTKQIRVTGVEFTQAGSGKTTILADAVILATGGFSNDKTADSLLREHAPHLVNFPTTNGPWATGDGVKLAQRLGAQLVDMDKVQLHPTGLINPKDPANPTKFLGPEALRGSGGVLLNKQGKRFVNELDLRSVVSKAIMEQGAEYPGSGGSMFAYCVLNAAAQKLFGVSSHEFYWKKMGLFVKADTMRDLAALIGCPVESVQQTLEEYERLSTSQRSCPITRKSVYPCVLGTKGPYYVAFVTPSIHYTMGGCLISPSAEIQMKNTSSRAPLSHSNPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRASTILQRKSSALSFKVWTTVVLREVREGGVYGAGSRVLRFNLPGALQRSGLSLGQFIAIRGDWDGQQLIGYYSPITLPDDLGMIDILARSDKGTLREWISALEPGDAVEMKACGGLVIERRLSDKHFVFMGHIINKLCLIAGGTGVAPMLQIIKAAFMKPFIDTLESVHLIYAAEDVTELTYREVLEERRRESRGKFKKTFVLNRPPPLWTDGVGFIDRGILTNHVQPPSDNLLVAICGPPVMQRIVKATLKTLGYNMNLVRTVDETEPSGSSKI