wanglab/gogpt-training-data huggingface dataset:
Protein: Spindle pole body component (C8UZY3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000256|RuleBase:RU363050}.
Interaction partners:
- Gamma-tubulin complex protein 3
- Tubulin gamma chain
- Spindle pole body component
- Spindle pole body component
- Spindle pole body component
- Mitotic-spindle organizing protein 1
- DASH complex subunit ASK1
Sequence:
MNPPRPRVASSRVADAEEAGLRGGTAPLQAENMDHRGSTSTQKSKVPREHVTSEKRTERVVIQTKEKMQGRTRNPVRESPSAGNRGEGDKSRSRRANTAGPLSPNLRKKEKETPDAPWNPHASLMPYTTAPLASRVSVPPLSSTLPQSLQPKPLRDLSTDAQEKAILEDLLFVFMGFEGQYIQYQAQYDPTAEKDRLTGPAFQLPSGLDPTLRDLTRSMLKMATHYSALEAFVEVQSRAEYGAVSHALCATIRKLLKDYLILVAQLETQLLNNPNFTLHVLHLHTMPTSQCLAQLYSLGQELLRRNGLLDQDIDESIDDFDDVDNILEQLREGGDLIPGAMSSKKICKGGNVLRLLTERLATFSGDPTTKALLETLLRESSRPYMTMLNEWLHHGVIKDPHAEFLVKEQKWIKREKLEEDYTDEYWEKRYTIRDNEVPPQLDSVRDKVLLAGKYLNVVRECGGVDVSKAVKDVPKTFDDPRFLENVNAAYTYANASLLNLLLTKNSLTTRFRSLKHYFFLDRSDFFSYFLELGASELRKPAKNVNESKLQSLLDLVLRQPGSIAAQDPFKEDVKVRMNKIGLTKWLMQVVSVSGIDQDNPEAALEKYQAPQAGSEDDKDIVGFDALELDYTVPFPLSLVISRKTVLRYQLIFRHLLSLRHLESMLSSAWLDQSKILGWRHKSTDRRLELWKRRAWNLRAKMLVFIQQLLYFCTAEVVEPNWQSLMDRVNGTDADGSEVTVNGTKQVNRTVDELMQDHVDFLDTCLKECMLTQAKLLKIHSKLLTCCTMFASWTAAPLGRALISADPGLSANPATSDGRGYDPARIGKLEDTLKRYEDHFGRHLRILMDSLNYFAATESVVLLKLAHALSSISKED
Protein: Demethyldecarbamoylnovobiocin O-methyltransferase (EC 2.1.1.285) (Novobiocin biosynthesis protein P) (Q9L9F2)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: S-adenosyl-L-methionine-dependent O-methyltransferase that methylates at 4-OH of the noviose moiety, the penultimate step in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Interaction partners:
Sequence:
MAPIVETAKETNSDSSLYLDLMIKVLAGTVYEDPAHRENFSHRDSTYREEVRNEGRDWPANAHTMIGIKRLENIRQCVEDVIGNNVPGDLVETGVWRGGACILMRGILRAHDVRDRTVWVADSFQGIPDVGEDGYAGDRKMALHRRNSVLAVSEEEVRRNFRNYDLLDEQVRFLPGWFKDTLPTAPIDTLAVLRMDGDLYESTWDTLTNLYPKVSVGGYVIVDDYMMCPPCKDAVDEYRAKFDIADELITIDRDGVYWQRTR
Protein: 5'-3' exoribonuclease 1 (A0A8I5XWP1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGVPKFYRWISERYPCLSEVVKEHQIPEFDNLYLDMNGIIHQCSHPNDDDVHFRISDDKIFTDIFHYLEVLFRIIKPRKVFFMAVDGVAPRAKMNQQRGRRFRSAKEAEDKIKKAIEKGETLPTEARFDSNCITPGTEFMARLHEHLKYFVNMKISTDKSWQGVTIYFSGHETPGEGEHKIMEFIRSEKAKPDHDPNTRHCLYGLDADLIMLGLTSHEAHFSLLREEVRFGGKKTQRVCAPEETTFHLLHLSLMREYIDYEFSALKEKITFKYDIEKIIDDWILMGFLVGNDFIPHLPHLHINHDALPLLYGTYIAILPELGGYINESGHLNLPRFERYLVKLSDFDREHFSEVFVDLKWFESKVGNKYLNEAAGAAAEEAKSCKDKRKVKGQENSLSWAALDKREGEGVASRDNFEDETEDDDLFETEFRQYKRTYYMTKMGVDVVSDEFLADQAACYVQAIQWILHYYYHGVQSWSWYYPYHYAPFLSDIRNISTLKIHFELGKPFKPFEQLLAVLPSASKTLLPTCYQHLMTSEDSPIIEYYPPDFKTDLNGKQQEWEAVVLIPFIDEKRLLEAMETCNHSLKKEERKRNQHSECLMCWYDSDTEFTYSSPWPEKFPAIERCSTRFYMEEPPGTQKVYLGKTAPPCKVIQLSDKEQSNWTKEIQGISEQYLRRKGIMINETSAVVYAQLLTGRRYQVNQNGEVRLEKQWSKQSLPFVYQTIVKDVRAFDSRFSNIKTLDDLFPPRSVVFMLGTPYYGCTGEVQDSGDVITEGRIRVVFSIPCEPNLDALIQNQHKYSIKYNPGYVLAGRLGVSGYLVSRFTGSIFIGRGSRRNPHGDHKANVGLNLKFNKKNEEVPGYTKRVGSEWMYSSAAEQLLAEYIERAPELFSYIAQNSQEDVFYEDDIWPGESESGAEKVQEIITWLKGHPVSTLSRSSCDLHILDAAIVEKIEEEVEKCKVLTLRNHVS
Protein: Tumor necrosis factor receptor superfamily member 14 (Herpes virus entry mediator A) (Herpesvirus entry mediator A) (HveA) (Tumor necrosis factor receptor-like 2) (TR2) (CD antigen CD270) (Q80WM9)
Organism: Mus musculus (Mouse)
Function: Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (By similarity). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation. Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (By similarity). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response. In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and pro-inflammatory cytokines. Upon binding to CD160 on activated CD4+ T cells, down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). May interact in cis (on the same cell) or in trans (on other cells) with BTLA. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15568026}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92956}.
Interaction partners:
- B- and T-lymphocyte attenuator
- Tumor necrosis factor ligand superfamily member 14
- CD160 antigen
- Lymphotoxin-alpha
- TNF receptor-associated factor 2
- Tumor necrosis factor
- Tumor necrosis factor ligand superfamily member 15
- Nectin-1
- Tumor necrosis factor ligand superfamily member 18
- CD70 antigen
Sequence:
MEPLPGWGSAPWSQAPTDNTFRLVPCVFLLNLLQRISAQPSCRQEEFLVGDECCPMCNPGYHVKQVCSEHTGTVCAPCPPQTYTAHANGLSKCLPCGVCDPDMGLLTWQECSSWKDTVCRCIPGYFCENQDGSHCSTCLQHTTCPPGQRVEKRGTHDQDTVCADCLTGTFSLGGTQEECLPWTNCSAFQQEVRRGTNSTDTTCSSQVVYYVVSILLPLVIVGAGIAGFLICTRRHLHTSSVAKELEPFQEQQENTIRFPVTEVGFAETEEETASN
Protein: ATP-dependent Clp protease proteolytic subunit-related protein 2, chloroplastic (ClpR2) (nClpP2) (Q9XJ36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for chloroplast development and integrity. Involved in the regulation of plastoglobules formation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14593120}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 4, chloroplastic
- Chloroplastic ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease proteolytic subunit 4, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- ATP-dependent Clp protease ATP-binding subunit CLPT2
- Clp protease adapter protein ClpF
Sequence:
MAVSFNTTLHQPSLSPSCSIKLYSGLKPQSASFLASGYQNLNKEFYGRVYKSLQSGTGKASRSRVKMMPIGTPRVPYRNREEGTWQWVDIWNALYRERVIFIGQNIDEEFSNQILATMLYLDTLDDSRRIYMYLNGPGGDLTPSLAIYDTMKSLKSPVGTHCVGLAYNLAGFLLAAGEKGHRFAMPLSRIALQSPAGAARGQADDIQNEAKELSRIRDYLFNELAKNTGQPAERVFKDLSRVKRFNAEEAIEYGLIDKIVRPPRIKEDAPRQDESAGLG
Protein: Fatty acyl-CoA reductase 1 (FAR1) (EC 1.2.1.84) (Male sterility domain-containing protein 2) (Q8WVX9)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols. It plays an essential role in the production of ether lipids/plasmalogens which synthesis requires fatty alcohols. In parallel, it is also required for wax monoesters production since fatty alcohols also constitute a substrate for their synthesis (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:24108123}; Single-pass membrane protein {ECO:0000269|PubMed:24108123}.
Interaction partners:
- Dihydroxyacetone phosphate acyltransferase
- Fatty acyl-CoA reductase 2
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Fatty acid synthase
Sequence:
MVSIPEYYEGKNVLLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEVLSGKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEVIIDSTNIIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTIRASNNALADLVPVDVVVNMSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTENVNMLMNQLNPEDKKTFNIDVRQLHWAEYIENYCLGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWRIFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY
Protein: Arginine N-methyltransferase, putative (Q38BP3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- type I protein arginine methyltransferase
- Small ribosomal subunit protein uS5
- Protein arginine N-methyltransferase 7
- Histone H2A
Sequence:
MQQFFFLTLILLKKGGEDDYEVYVRSIRTDEIFGTRAGLKGVKIEMSPKKNSASRPSNNGGGGKTGGGNGNVSHRTDNEQSGNNLSERIIANESLLATESERHATSKSLYGDCTARISGNLSCIHDRVRLRAYESVLRSIKGKSVLHLGCGMGLVSMIAARSLASAVVAVDRSAIVDAAQVVAKKNGLNNISFFRGALVDVVQNFPVRQFDVIICEWMGPFLINDPLLEEALYARNNLLASNGVMCPDSSSIHVVGVSDYCFHMDTVEFWGNVYGFKMEPMKALVQREVEMCRVPTSSIVTTTCLAHTVNIASINNLDDKSSLNDFVVPFSVRATKDTTVNFLTFYIDARFTNPHDPGANFVLGVRPGGTNPWTETSVALHEPLPLKGGEVLSGELKVCLLNPTRGITTVEVTARTSGNVVNIETKGTYNYQRY
Protein: ABC transporter B family member 9 (ABC transporter ABCB.9) (AtABCB9) (Multidrug resistance protein 9) (P-glycoprotein 9) (Q9M0M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- At1g01310 superfamily protein)
- CAP superfamily protein
- CAP superfamily protein
Sequence:
MEEKSSKKNDGGNQKVSFFKLFSFADKTDVVLMTVGTIAAAGNGLTQPFMTLIFGQLINAFGTTDPDHMVREVWKVAVKFIYLAVYSCVVAFLQVSCWMVTGERQSATIRGLYLKTILRQDIGYFDTETNTGEVIGRMSGDTILIQDAMGEKVGKFTQLLCTFLGGFAIAFYKGPLLAGVLCSCIPLIVIAGAAMSLIMSKMAGRGQVAYAEAGNVVEQTVGAIRTVVAFTGEKQATEKYESKLEIAYKTVVQQGLISGFGLGTMLAVIFCSYGLAVWYGAKLIMEKGYNGGQVINVIFAVLTGGMSLGQTSPSLNAFAAGRAAAFKMFETIKRSPKIDAYDMSGSVLEDIRGDIELKDVYFRYPARPDVQIFAGFSLFVPNGKTVALVGQSGSGKSTVISLIERFYDPESGQVLIDNIDLKKLQLKWIRSKIGLVSQEPVLFATTIKENIAYGKEDATDQEIRTAIELANAAKFIDKLPQGLDTMVGEHGTQMSGGQKQRLAIARAILKNPKILLLDEATSALDAESERIVQDALVNLMSNRTTVVVAHRLTTIRTADVIAVVHQGKIVEKGTHDEMIQDPEGAYSQLVRLQEGSKEEATESERPETSLDVERSGSLRLSSAMRRSVSRNSSSSRHSFSLASNMFFPGVNVNQTDEMEDEENNVRHKKVSLKRLAHLNKPEIPVLVLGSIAAMVHGTVFPIFGLLLSSSINMFYEPAKILKKDSHFWALIYIALGLTNFVMIPVQNYFFGIAGGKLIKRIRSMCFDKVVHQEISWFDDTANSRSLVGDALALIVQNIATVTTGLIIAFTANWILALIVLALSPFIVIQGYAQTKFLTGFSADAKAMYEEASQVANDAVSSIRTVASFCAEEKVMDLYQQKCDGPKKNGVRLGLLSGAGFGFSFFFLYCINCVCFVSGAGLIQIGKATFGEVFKVFFALTIMAIGVSQTSAMAPDSNKAKDSAASIFDILDSTPKIDSSSDEGTTLQNVNGDIEFRHVSFRYPMRPDVQIFRDLCLTIPSGKTVALVGESGSGKSTVISMIERFYNPDSGKILIDQVEIQTFKLSWLRQQMGLVSQEPILFNETIRSNIAYGKTGGATEEEIIAAAKAANAHNFISSLPQGYDTSVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLTTIKNADVIAVVKNGVIAEKGRHETLMKISGGAYASLVTLHMSAN
Protein: Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Group XVI phospholipase A2) (H-rev 107 protein homolog) (HRAS-like suppressor 3) (HRSL3) (Rat LRAT-like protein-3) (RLP-3) (P53817)
Organism: Rattus norvegicus (Rat)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2), ccatalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8290259}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:8290259}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8290259}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000250|UniProtKB:Q8R3U1}.
Interaction partners:
- Phospholipase A2, group III
- Group 10 secretory phospholipase A2
- Cytosolic phospholipase A2
- Lysophosphatidylcholine acyltransferase 1
- Phospholipase A2 group V
- Phospholipase B1, membrane-associated
- Cholinephosphotransferase 1
- Phospholipase A2 group IVC
- Phospholipase A2
- Lysophosphatidylcholine acyltransferase 2
Sequence:
MPIPEPKPGDLIEIFRPMYSHWAIYVGDGYVIHLAPPSEIPGAGAASIMSALTDKAIVKKELLRDVAGKDKYQVNNKHDKEYTPLPLNKIIQRAEELVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKVATVTGVGLAALGLIGVMLSRNKKQKQ
Protein: RNA-binding protein Nova-1 (Neuro-oncological ventral antigen 1) (Ventral neuron-specific protein 1) (Q9JKN6)
Organism: Mus musculus (Mouse)
Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons. Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord.
Subcellular location: Nucleus {ECO:0000269|PubMed:8558240}.
Interaction partners:
- Polypyrimidine tract-binding protein 2
- E3 ubiquitin-protein ligase UBR5
- ELAV-like protein 4
- Polypyrimidine tract-binding protein 1
- RNA binding protein fox-1 homolog 1
- RNA binding protein fox-1 homolog 2
- Serine/arginine repetitive matrix protein 4
Sequence:
MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTIEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAIMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG
Protein: Phenolphthiocerol synthesis polyketide synthase type I Pks15/1 (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41) (Q7TXK8)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).
Interaction partners:
Sequence:
MIEEQRTMSVEGADQQSEKLFHYLKKVAVELDETRARLREYEQRATEPVAVVGIGCRFPGGVDGPDGLWDVVSAGRDVVSEFPTDRGWDVEGLYDPDPDAEGKTYTRWGAFLDDATGFDAGFFGIAPSEVLAMDPQQRLMLEVSWEALEHAGIDPLSLRGSATGVYTGIFAASYGNRDTGGLQGYGLTGTSISVASGRVSYVLGLQGPAVSVDTACSSSLVAIHWAMSSLRSGECDLALAGGVTVMGLPSIFVGFSRQRGLAADGRCKAFAAAADGTGWGEGAGVVVLERLSDARRLGHSVLAVVRGSAVNQDGASNGLTAPNGLAQQRVIQAALANAGLSAADVDVVEAHGTATTLGDPIEAQALLSTYGQGRPAEQPLWVGSIKSNMGHTQAAAGVAGVIKMVQAMRHGVMPATLHVDEPSPRVDWTSGAVSVLTEAREWSVDGRPRRAAVSSFGISGTNAHLILEEAPVPAPAEAPVEASESTGGPRPSMVPWVISARSAEALTAQAGRLMAHVQANPGLDPIDVGCSLASRSVFEHRAVVVGASREQLIAGLAGLAAGEPGAGVAVGQPGSVGKTVVVFPGQGAQRIGMGRELYGELPVFAQAFDAVADELDRHLRLPLRDVIWGADADLLDSTEFAQPALFAVEVASFAVLRDWGVLPDFVMGHSVGELAAAHAAGVLTLADAAMLVVARGRLMQALPAGGAMVAVAASEDEVEPLLGEGVGIAAINAPESVVISGAQAAANAIADRFAAQGRRVHQLAVSHAFHSPLMEPMLEEFARVAARVQAREPQLGLVSNVTGELAGPDFGSAQYWVDHVRRPVRFADSARHLQTLGATHFIEAGPGSGLTGSIEQSLAPAEAMVVSMLGKDRPELASALGAAGQVFTTGVPVQWSAVFAGSGGRRVQLPTYAFQRRRFWETPGADGPADAAGLGLGATEHALLGAVVERPDSDEVVLTGRLSLADQPWLADHVVNGVVLFPGAGFVELVIRAGDEVGCALIEELVLAAPLVMHPGVGVQVQVVVGAADESGHRAVSVYSRGDQSQGWLLNAEGMLGVAAAETPMDLSVWPPEGAESVDISDGYAQLAERGYAYGPAFQGLVAIWRRGSELFAEVVAPGEAGVAVDRMGMHPAVLDAVLHALGLAVEKTQASTETRLPFCWRGVSLHAGGAGRVRARFASAGADAISVDVCDATGLPVLTVRSLVTRPITAEQLRAAVTAAGGASDQGPLEVVWSPISVVSGGANGSAPPAPVSWADFCAGSDGDASVVVWELESAGGQASSVVGSVYAATHTALEVLQSWLGADRAATLVVLTHGGVGLAGEDISDLAAAAVWGMARSAQAENPGRIVLIDTDAAVDASVLAGVGEPQLLVRGGTVHAPRLSPAPALLALPAAESAWRLAAGGGGTLEDLVIQPCPEVQAPLQAGQVRVAVAAVGVNFRDVVAALGMYPGQAPPLGAEGAGVVLETGPEVTDLAVGDAVMGFLGGAGPLAVVDQQLVTRVPQGWSFAQAAAVPVVFLTAWYGLADLAEIKAGESVLIHAGTGGVGMAAVQLARQWGVEVFVTASRGKWDTLRAMGFDDDHIGDSRTCEFEEKFLAVTEGRGVDVVLDSLAGEFVDASLRLLVRGGRFLEMGKTDIRDAQEIAANYPGVQYRAFDLSEAGPARMQEMLAEVRELFDTRELHRLPVTTWDVRCAPAAFRFMSQARHIGKVVLTMPSALADRLADGTVVITGATGAVGGVLARHLVGAYGVRHLVLASRRGDRAEGAAELAADLTEAGAKGQVVACDVADRAAVAGLFAQLSREYPPVRGVIHAAGVLDDAVITSLTPDRIDTVLRAKVDAAWNLHQATSDLDLSMFVLCSSIAATVGSPGQGNYSAANAFLDGLAAHRQAAGLAGISLAWGLWEQPGGMTAHLSSRDLARMSRSGLAPMSPAEAVELFDAALAIDHPLAVATLLDRAALDARAQAGALPALFSGLARRPRRRQIDDTGDATSSKSALAQRLHGLAADEQLELLVGLVCLQAAAVLGRPSAEDVDPDTEFGDLGFDSLTAVELRNRLKTATGLTLPPTVIFDHPTPTAVAEYVAQQMSGSRPTESGDPTSQVVEPAAAEVSVHA
Protein: Protein VASCULAR ASSOCIATED DEATH 1, chloroplastic (F4HVW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ethylene- and salicylic acid-dependent cell death control associated with cells in the vicinity of vascular bundles.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Two pore calcium channel protein 1
- non-specific serine/threonine protein kinase
- Disease resistance-like protein DSC2
- GEM-like protein 1
Sequence:
MAMLSTASVSGSVDLPRGTMKVDSSASPEVVSDLPPSSPKGSPDRHDPSTSSPSPSRGGDNQSEVISKSEEYRQLFRLPADEILVQDFNCACQESILMQGHMYLFIHYICFYSNIFGYETKKIIPFAEISCVKRAKTAGIFPNAIEILAGGKKYFFASFLSRDEAFKLIHDGWLEYGSAVKSEGEILVTEPQVSDGVVKRARSSMDLANELDIPVRDETLHLSSSSSLPVISQNGVPPSSVQRHAEPDVDVVAANTFNWKPEDTDAPKLSSDFTKVAEAKFSIPVEEFFRLFFSDGAVSFVESFHKNCGDKEFRCTSWQPHEKLGHTRNVSFQHPIKIYFGAKFGGCQESQKFRMYRNSHLVIETSQEISDVPYADYFTVEGVWDLKRDCRDSVEGCILDVYVNVAFSKRTVWKGKIVQSTLEECREAYAHWIRMAHELLKQKKLENQEGNKLIEDGEPLAAREERVSECDEEGKVEMVGEGVVKKSLKEAWVNLTSFVKRQSGTRQVIVLAFAVILLMQVTIVVLLKKGGGGQVEYHERYDEYSVNGETLGWLEKRMHFLREEMMMVEDRLQRMRQDHAALKAQFHHLERLLRRNKQ
Protein: 3-ketoacyl-CoA thiolase FadI (EC 2.3.1.16) (ACSs) (Acetyl-CoA acyltransferase) (Acyl-CoA ligase) (Beta-ketothiolase) (Fatty acid oxidation complex subunit beta) (P76503)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Acyl-coenzyme A dehydrogenase
- 3-ketoacyl-CoA thiolase FadA
- Acetyl-coenzyme A synthetase
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- Probable acetyl-CoA acetyltransferase
- Acetyl-CoA acetyltransferase
- Acetaldehyde dehydrogenase
- 3-hydroxyadipyl-CoA dehydrogenase
Sequence:
MGQVLPLVTRQGDRIAIVSGLRTPFARQATAFHGIPAVDLGKMVVGELLARSEIPAEVIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARVLVDVNKARTMSQRLKLFSRLRLRDLMPVPPAVAEYSTGLRMGDTAEQMAKTYGITREQQDALAHRSHQRAAQAWSDGKLKEEVMTAFIPPYKQPLVEDNNIRGNSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLVPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTMSDLTLIDMHEAFAAQTLANIQLLGSERFAREALGRAHATGEVDDSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAMVLEAE
Protein: Sad1 and UNC84 domain containing 1 (A0A8I6A5F2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
MWRVFVPRPGRCGRGLRRRREAAWSEPVNMDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHRLEPVFDSPRMSRRSLRLITTTAAYSSGDGQTVDTHISTSRATPAKGRETRTVKQRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAVHGPTSRVYSRDRTLRPRGASFYLDRTLWLAKYTSSSFASFIVQLFQVVLMKLNFESETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLETHTTTHSQLSQPHRAAGAMGRLCTYTGDLLVRALRRTRAAGWSVAEAMWSVLWLAVTAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGFSLWGQGNFFSLLPMLNWTAMQPAQRVDNPKDMHRPGPLSPSPPLKVDPMASQWPQESDMGQKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMVGQHLQEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGRDEEQPLLDRVQHLELELNLLKSQLSDWQHLRSSCEQADARIQETVQLMFSEDQPGGSLEWLLQKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAMSQAGISGITEAQAHIIVNNALRLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPRDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
Protein: Iron-sulfur cluster assembly protein SufB (PfSufB) (Q25799)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Iron-sulfur cluster assembly protein IscU
- Iron-sulfur cluster assembly protein SufC
- Elongation factor Tu, apicoplast
- Cysteine desulfurase SufS
- DNA-directed RNA polymerase subunit beta
Sequence:
MIKLKNFLNIYNLNYKYQYKNKINLYLIRQGLNINLIKNLSSNIFLYMFIYNFKKYSLKLLNIFKLPDWNFFDCPNINYDNIIYYSSILKDNNLIYYLKNNLNIEFLDSILIKNNSIDIIFDSMSILHTTQYFLKKLGIIFLPLFDIIFKYPLLIKKYLGTIISYKDNFFANINSIIFSEGSFCYIPKYVKCNFNLSTYFKTNSSDFAQFERTLIIVGKYSYVSYLEGCTASLYKESQLHVAIVEIIVKDYGYIKYYTLQNWYRGDYLGNGGLYNFTTKRGICLNYSKLDWIQVEVGSIITWKYPSTILKGKFSISNFYSISFISNMQIADTGSKMYHIGSYTKSYIISKSISLNNSLNIFRGLVYIKPFSYKSYNYTECSSLIFGNNSLTVTIPYIKNYNNTSYVKQEAFVSKIEIIYLFLLMQRGLSISESISLLIIGFCSDIYNKLPFEFNLEIPILFSLKIKDIFN
Protein: Ell1-associated factor 1 (A0ZWU1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Activates transcription elongation by RNA polymerase II and pyrophosphorolysis as a complex with ell1. Acts as a transcriptional transactivator of ell1 elongation activities.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96JC9}.
Interaction partners:
- RNA polymerase II elongation factor ell1
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- V-type proton ATPase subunit a
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit c
- V-type proton ATPase subunit H
Sequence:
MNSLQKGSYKVIPGSSFSKNSNGLLSIKYNFIPESVDPSRRGVLEKAQEAYRLRLPSTFDDDRPHIFEGSCQRARNVDCVLIFNAKTKTFTLEHIDEIARLNALRNPKVSKTVPSNAITQSDNSQISESKSTSQSAVTTNSTRRKEKELEASKDGKIKPSSSNTRYPAISSKGPITTDTNDEPDMEVMELDDFAKELELGFDQEFNSIDDPSTVSQTASKPISLRGLSSQERDYASSAQAEGISSASEDED