wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (P27594)
Organism: Sus scrofa (Pig)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV). Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17203407, ECO:0000269|PubMed:19109387}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon-induced, double-stranded RNA-activated protein kinase
- IRF tryptophan pentad repeat domain-containing protein.
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced GTP-binding protein Mx2
- USP domain-containing protein
- E3 ubiquitin-protein ligase TRIM21
- Antiviral innate immune response receptor RIG-I
- 2'-5'-oligoadenylate synthetase 1
- Signal transducer and activator of transcription 1
Sequence:
MVYSSCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQEQLSLAKALQKEQAFFENHAHFRDLLEEGRATIPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEYECRLFTKMRNEFCRWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDLVRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEAEEEKNRKSNQYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDKRKFLKERLMRLTQARRRLAKFPG
Protein: Phosphatidylinositol 4-phosphate 5-kinase 59B, isoform I (EC 2.7.1.68) (Q0E8Y1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASGDGDTINTIDMDSSSASQAKLAEPSNASTDHVGNSSPDLGNRPNRASSKADKERKIGHRRVGEGGEITYKKIQTSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNLDVALKEKQSEQRKPLRAPLAEDSDVDADDPLDGDAATGISRNNAAYRSVNRQRLVAHSTAMESIQAESEPIDDEEDVPPGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKIPSLDLPEIKGNHRKFRTLVTSYIALKHSPSKRKSLSKAIQRSIDSDNEVASRPVHASHSHSSGKIHQPAKPPTTEPTPAGAAGGAERGATALGPATTSGASERAPPPVKQRTPAASNLKTRVPPPVPPRGSPRRKDAQDRTTPGTTPSCSSTPPPAFDDISEDSSNKNSSSSIGRRSHHHHHHHQQSQQHQQSYYLDRKMNIGPAYRGSYKEDIVSVSEVHLDTLLAVDTSSSSQYGSRGGLAWTPPASGEGSTPTWTEGTPSFTDSSSSGDLDNFSPINSSKIDRHKPTVEEAINSLSAGMIN
Protein: Mitochondrial fission factor (Q6PCP5)
Organism: Mus musculus (Mouse)
Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:30059978}; Single-pass type IV membrane protein {ECO:0000255}. Peroxisome {ECO:0000250|UniProtKB:Q9GZY8}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4KM98}.
Interaction partners:
- Dynamin-1-like protein
- Mitochondrial fission 1 protein
- Mitochondrial dynamics protein MID49
- Mitochondrial dynamics protein MID51
- Mitofusin-2
- Mitofusin-1
- Dynamin-like GTPase OPA1, mitochondrial
- Serine/threonine-protein kinase PINK1, mitochondrial
- Splicing factor 3B subunit 4
- Mitochondrial import receptor subunit TOM20 homolog
Sequence:
MAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQEFQDGVPNASVIMQVPERIVVTGNNEDISFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPLPTPQSEESRAVGRLKRERSMSENAVRQNGQLVRNDSIVTPSPPQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNLDAAIEGASDDMTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR
Protein: Toll-like receptor 5 (Q9JLF7)
Organism: Mus musculus (Mouse)
Function: Pattern recognition receptor (PRR) located on the cell surface that participates in the activation of innate immunity and inflammatory response. Recognizes small molecular motifs named pathogen-associated molecular pattern (PAMPs) expressed by pathogens and microbe-associated molecular patterns (MAMPs) usually expressed by resident microbiota. Upon ligand binding such as bacterial flagellins, recruits intracellular adapter proteins MYD88 and TRIF leading to NF-kappa-B activation, cytokine secretion and induction of the inflammatory response. Plays thereby an important role in the relationship between the intestinal epithelium and enteric microbes and contributes to the gut microbiota composition throughout life.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 4
- Toll-like receptor 2
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Toll/interleukin-1 receptor domain-containing adapter protein
- High mobility group protein B1
- Toll-like receptor 1
- Nucleotide-binding oligomerization domain-containing protein 2
- Toll-like receptor 6
Sequence:
MACQLDLLIGVIFMASPVLVISPCSSDGRIAFFRGCNLTQIPWILNTTTERLLLSFNYISMVVATSFPLLERLQLLELGTQYANLTIGPGAFRNLPNLRILDLGQSQIEVLNRDAFQGLPHLLELRLFSCGLSSAVLSDGYFRNLYSLARLDLSGNQIHSLRLHSSFRELNSLSDVNFAFNQIFTICEDELEPLQGKTLSFFGLKLTKLFSRVSVGWETCRNPFRGVRLETLDLSENGWTVDITRNFSNIIQGSQISSLILKHHIMGPGFGFQNIRDPDQSTFASLARSSVLQLDLSHGFIFSLNPRLFGTLKDLKMLNLAFNKINKIGENAFYGLDSLQVLNLSYNLLGELYNSNFYGLPRVAYVDLQRNHIGIIQDQTFRLLKTLQTLDLRDNALKAIGFIPSIQMVLLGGNKLVHLPHIHFTANFLELSENRLENLSDLYFLLRVPQLQFLILNQNRLSSCKAAHTPSENPSLEQLFLTENMLQLAWETGLCWDVFQGLSRLQILYLSNNYLNFLPPGIFNDLVALRMLSLSANKLTVLSPGSLPANLEILDISRNQLLCPDPALFSSLRVLDITHNEFVCNCELSTFISWLNQTNVTLFGSPADVYCMYPNSLLGGSLYNISTEDCDEEEAMRSLKFSLFILCTVTLTLFLVITLVVIKFRGICFLCYKTIQKLVFKDKVWSLEPGAYRYDAYFCFSSKDFEWAQNALLKHLDAHYSSRNRLRLCFEERDFIPGENHISNIQAAVWGSRKTVCLVSRHFLKDGWCLEAFRYAQSRSLSDLKSILIVVVVGSLSQYQLMRHETIRGFLQKQQYLRWPEDLQDVGWFLDKLSGCILKEEKGKKRSSSIQLRTIATIS
Protein: Unconventional myosin 29D short isoform (Q8T6L8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVAKNAEVHRRGILGFAPRIGLVNVDYDDLDRIDNFYLETQRYRDYYRDPHNILHKPERFRQHQGKCSIKLDTSVQNLTRPIHASSSNEAVHLQQRLKSLSTELVTLRNRLHVGHGPGQGQSQGNGAQPVAPAPNAGPKANNFDLNASSPNLNLSSSGAGLSASAVQQHTNGHHTTSKNHSFSHTLPANSGSGGGGGAGGGAVVSARNTSIPHPLPHQLAEKPGLSHQQSGSGHGQSTGTLPHMSGMGSILGQNSHSHAPVNNNSNNSNTLPMRTSNSGHLGINGGGVGHHLSHAHSQQLPFIPQSKHTNPCQSVKTLPFGFGFSESQQKMQQQQQQGNSSPKDMQDLIHLSGPLTEHAVMRTLQARFNERRYFTNVGPILLSINPYLDVGNPLTLTSTRAMPLAPQLQKIVQEAVRQQSETGYPQAIILSGTSGAGKTANAMLMLRQLFAIAGGGPETDAFKHLAAAFTVLRSLGSAKTTTNSESSRIGQFIEVQVTDGALYRTKIHCYFLDQTRVIRPLPKEKNYHIFYQLLAGLSREERQKLHLDGYSPANLRYLRGDIGQNEQEDAARFQAWKTCLGILGIPFLDVVRVLAAVLLLGNVQFIDGGGTSAASSAVSFLHDHREFENKLSPKPGHEDELSRGGTVGGAAAEEGRSGDRSGGLHRSGSPDGGAQGAELPRSLPVHDAQ
Protein: Galectin (J3KSY2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFSGCQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSCSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGTWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQPPSVRPANPAPITQTVIHTVQSASGQMFSTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRFHINLCSGSHIAFHMNPRFDENAVVRNTQINNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHVFEYYHRLRNLPTINKLEVGGDIQLTHVQT
Protein: Caspase-1 (O42284)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSRARSSGRCPRAREMCIDLVHHLVLSSQIYDIYQPRERRTRRALLICNTKFKHLRQRDGAEVDVKEMTKLLEGLGYNVECHEDKTSQEMTTVMKKFADHKDHLTSDSTFLVFMSHGMSTGICGTKSNGTTDILSFNTIYENFNNKHCRALMGKPKVVIIQCCRGDNIGSVQIRDSIDPEMPTSTSDGWRCVELQGSKTREAHLESDFATLYSSTPDTVSWRSPTEGSVFIQRLVEQFRNHAFNSDLQEMFRKVQRSFENFPRQLPTQERTTMLKKFYLFPGL
Protein: Nucleoid occlusion factor SlmA (Protein Ttk) (Synthetically lethal with a defective Min system protein A) (P0C093)
Organism: Escherichia coli (strain K12)
Function: Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.
Subcellular location: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_01839, ECO:0000269|PubMed:15916962}.
Interaction partners:
- Cell division protein FtsZ
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Cell division protein ZipA
- Macrodomain Ter protein
- Septum site-determining protein MinC
- Cell division protein ZapB
- Cell division protein ZapA
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Cell division protein FtsA
- Negative modulator of initiation of replication
Sequence:
MAEKQTAKRNRREEILQSLALMLESSDGSQRITTAKLAASVGVSEAALYRHFPSKTRMFDSLIEFIEDSLITRINLILKDEKDTTARLRLIVLLLLGFGERNPGLTRILTGHALMFEQDRLQGRINQLFERIEAQLRQVLREKRMREGEGYTTDETLLASQILAFCEGMLSRFVRSEFKYRPTDDFDARWPLIAAQLQ
Protein: Mediator of RNA polymerase II transcription subunit 19a (Q9FMP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 8
- rRNA 2'-O-methyltransferase fibrillarin 2
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 32
- Mediator of RNA polymerase II transcription subunit 15a
- Mediator of RNA polymerase II transcription subunit 22b
Sequence:
MEPERLKFGGPRELCGAADLISQFKLVQHHEFFCKKSLPVSLSDSHYLHNVVGDTEIRKGEGMQLDQLIESISQSRETNIRIQPFDIDELQESFQLNDMTPVELPPAEKGAPTIPSKSKSESKDRDRKHKKHKDRDKDKDREHKKHKHKHKDRSKDKDKDKDRDRKKDKNGHHDSGDHSKKHHDKKRKHDGDEDLNDVQRHKKNKHKSSKLDEVGAIRVAG
Protein: Putative neural-cadherin 2 (Cadherin-N2) (dN2-cadherin) (Q9VJB6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Armadillo segment polarity protein
Sequence:
MVDPLKIFWVLTNSTYLVTKFVRIGIADKNDSPPYFDRFLYETEIDENADLQSTVLTVNAKDHNESTNIRYQITGGNIGNAFAVQNTTGVIYVASPLDYETRPRYELRLEATRNRKNNYTTVVINVRDVNDNPPVFDRQTYRTQITEEDDRNLPKRILQVTATDGDVDRPINIVYFLTGQGIDPDNPANSKFDINRTTGDIFVLKPLDRDQPNGRPQWRFTVFAQDEGGEGLVGYADIQVNLKDINDNAPQFPQGIYFGNVTENGTAGSSVMTMSAVDYDDPNESTNAKLIYSIEKNVIEEETGAPIFEIEPETGLIKTAVCCLDRERTPDYSIQVVAMDGGGLKGTGTASIRVKDLNDMPPQFTKDEWVTEVDETNGTYIPETPILTVTVQDEDETNTFQYKVVPNSGFGADKFAMVRNGDGTGSLKIIQPLDYEDPLQSSGFRFRIQVNDKGDDGPGGSDKYHVAYSWVVVKLRDINDNVPKFDREHIEVSIYEDTKVGTILEQFKATDADQGGHSKVAYKIVRSTNRKRQFAISDRGAVSIQRPLDRETQDRHHIQILAIDDGSPARTATATLTVIVKDVNDNAPTFAQDYKPTLPENVSGKKILEVAAKDPDDRLRGNGGPFTFRLDPLASDEIKAGFKVEYDRRGDNENGVAIISSLRPFDREAQKSYAIPIEIKDNGAPAMTGTSTLTVTIGDVNDNKMQPGSKSVLVYNYQGQSQDTPIGRVYVNDPDDWDVPDKKYYWEVQEHQRFKLDTDTGILTMRAGTRRGRYQLRFKVYDREHGQEDIPANLSVTVRDITAEAVQQAGSMRLSHITDEDFVRTWNPVKNQVEPSKLERFRNKLAELLYTDRDNVDVFSVQLKEGSPYPLTDVHFAARSATQQPYFKAVRLNGVVQMHREEIEKDVGLNITMVNINECLHEGKGKCGSNSCTSKVELGKKPYTVSVNRTALVGVRLDISAQCVCRARNFTHQDHNCRTHLCYNGGRCVETRNGPKCVACPVGYNGPRCQQSTRSFRGNGWAWYPPLQLCQESHLSLEFITRVADGLILYNGPIVPPKPEETVISDFIALELEQGYPRLLIDFGSGTLELRVKTKKTLDDGVWHRLDIFWDTENVRMVVDFCRTALVSEMEDGTPPEFDDNACQARGQIPPFAESLNLNQPLQLGGLYRQHFDQTLYNWQYAFSSKGFDGCIRNVIHNSEHYDLAFPALARNSFPACPQTDEVCLKTEHTARCWEHGNCVASLVQAKCHCQPGWMGPGCNVPTIPTTFKAQSYVKFALSFEPDRFSTQLQLRFRTREQGGELFRVSDQHHREYAILELRRGHLQFRYNLNSMRNEEQLLTLTAIAVNDGQWHVIRISRYGSAALMELDGGESRRYNESFHFTGHQWLTIDKQEGVYAGGKAEYTGIKTFEVQSDFQRSCLDDIRLDGKHLPLPPAMNGTQWGQATMARNLERNCPSNRPCSNVICPDPFDCVDLWNEYECTCSEGRIMSSDTKGCVDRNECLDLPCLNGATCINLEPRLRYRCICPEGYWGENCELVQEGQRLKLSMGALGAIFVCLIIILILALIFVLYSRKRKTTKKKKRSGPEKDVRETVISYEDEGGGEDDMTAFDITPLQIPISAQGGPPDIAACKMPIIYPVMTLLPPGQELNVAYLMEERKQRIDKDNNAPPFDDLRNFTFEGSGSIAESLSSLASGTDDENQDFNYLQNWGPRFNALAAMYVHDKAKASSQLPSDGGGGSGDGPGPGASSSSPLGGGGTGGGSGIPGNVLAVVATGSGAGPGGGGGSSGLMPLPEVDKVVL
Protein: NAD(+) hydrolase SARM1 (NADase SARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and TIR motif-containing protein 1) (F1QWA8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (By similarity). Wallerian degeneration is triggerred by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (By similarity). Can activate neuronal cell death in response to stress (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6SZW1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion {ECO:0000250|UniProtKB:Q6SZW1}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q6PDS3}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Myeloid differentiation primary response protein MyD88
- Nicotinamide-nucleotide adenylyltransferase
- MORN repeat-containing protein 4
- Toll-interleukin 1 receptor
- Nicotinamide-nucleotide adenylyltransferase
- TNF receptor-associated factor 6
Sequence:
MFLSLVVYLSKICRYLSMFSSDRLTVPEYVSSRLHNRRTAPDPRAVSPGISTDVQAVLDGSLPALRSAIRTLRSSKDTGDLEETRRAIAETFQLVEEAWVLPTVGRRVAEEICNRIRLDGGLELLLQLMQTPAVEITYESAKLLEQILVSENRDYVARMGLGVILNLTREQEDAQLARSVSGILEHMFKHTEETSAQLITNGALDTILYWCRGTDPTVLRHCAVALSNCAMYGGHRCQRLMIEKQAAEWLFPLAFSKEDELIRFHACLAVAVLAANREMEKEVVKSGTLELVEPFIASLDPDEFARNMLDSADSMQGRTAADLQHLLPLLDGTRLEGKCIAAFYLCVETSIKSRQRNTKIFQEIGAVQSLKRIVMYSSNATVCSLAKRALKMMSEEVPRRILSSVPNWKSGEVQTWLQQIGFSAFSERFQELQVDGDLLLNITEQDLIQDLGMTSGLTRKRFLRDLRVLKTYANYSTCDPNNLADWLADADPRFRQYTYGLVQSGVDRNNIVHITDQQLLTDCHVENGIHRAKILSAARRPSKPCLTDSQPKGPDVFISYRRTTGSQLASLLKVHLQLRGFSVFIDVEKLEAGRFEEKLITSVQRARNFILVLSANALDKCMGDVAMKDWVHKEIVTALNGKKNIVPVTDNFVWPDPTSLPEDMSTILKFNGIKWSHEYQEATIEKILRFLEGCPSQEKPDGAKTDKKEPQKK
Protein: Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase); Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART)] (Q9I9E6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSERVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMVDDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSDELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDSASVQWLQDCAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTALKEGGGVITSGGRVLTVTAVRPTLESALQSANEGVGAISFPDAVYRRDIGHRAITYLTHTRGLTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVERSALLPRLKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPFGRPGQTIGDVLLTPTKIYSRVLQPVLRSGAVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRLLQAHEESWIIGSLTHRHPGAESVVVRNLERSLRAGPDCSPDTGVLRNGSAAADQNSRRRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREAEHRAFPAALELVSSGAVKLRDDGHIVWSTRETH
Protein: At1g22630/F12K8_2 (F12K8.2 protein) (SSUH2-like protein) (Q9SKA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLKFPLCCSELSLEPKILAFESQLVSGRRDTIKVSAGKIGNFSLGSIFKSCETCGAKGAIECPGCKGTGKNKKNGNMFERWKCFDCQGFGMKSCPKCGKGGLTPEQRGER
Protein: Uncharacterized protein (Q382U8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVRCQSSHPKAILVQLHVVAPSLQYDYQKGPPPPEEACELDVELLCNDISNKMRLLGGMAIGLPKEGLVVEGSHREESGNGGLYNIVVRLQHASNLSVSALRAACAAVMEGAVTIAGDDRGKQRLAHKQPALKVVPVAVRVVKLDKLQ
Protein: Fibrillin 1 (A0A8I6G7Y9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MRRGGLLEVALAFTLLLESYTSHGADANLEAGSLKETRANRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQISPSCGSRSRIIHIVLAALSGGGVQVQHHETLSPYLAAVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVVSNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKFNEVSQKCEDIDECSTIPGVCDGGECTNTVSSYFCKCPPGFYTSPDGTRCVDVRPGYCYTTLTNGRCSNQLPQSITKMQCCCDVGRCWSPGVTVAPEMCPIRSTEDFNKLCSVPLVIPGRPDYPPPPLGPLPPVQPVPGFPSGPVIPVPRPPPEYPYPSPSREPPKVLPFNVTDYCQLVRYLCQNGRCIPTPGSYRCECNKGFQLDIRGECIDVDECEKNPCTGGECINNQGSYTCHCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYRRGQCVKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGSDINECALDPDICPNGICENLRGTYKCICNSGYEVDITGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFVYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSPESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSECCSSLGAAWGSPCTICQVDPICGKGYSRIKGTQCEDINECEVFPGVCKNGLCVNSRGSFKCECPSGMTLDATGRICLDIRLETCFLKYDDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPLRNSREYEELCPRGPGFATKDITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTGYESGFMMMKNCMVQSSVQRGQSVPGFPATGVGKGNNIDECQRDPLLCRGGICHNTEGSYRCECPSGHQLSPNISACIDINECELSANLCPSGRCVNLIGKYQCACNPGYHPTHDRLFCVDIDECSIMNGGCETFCTNSDGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGRHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKDGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDINECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYTCDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCELCPPVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYHADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRLTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNADQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECATGNGNLCRNGQCVNTVGSFQCRCNEGYEVAPDGRTCVDINECVLDPGKCAPGTCQNLDGSYRCICPPGYSLQNDKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSTGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPFGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILEGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECAEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCIDENECQTKPGICENGRCLNTLGSYTCECNDGFTASPTQDECLDNREGYCFSEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFEGTVAYKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTACVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTACIDNNECTSEINLCGSKGVCQNTPGSFTCECQRGFSLDQSGASCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHVCGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDINECGSSQAPCSYGCSNTEGGYLCGCPPGYLRIGQGHCVSGMGMGRGGPEPPASGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASDIQDGSEMEANVSLASWDVEKPASFAFNISHINNKVRILELLPALTTLMNHNKYLIESGNEDGFFKINQKEGVSYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDRYDKDYLSGELGDNLKMKIQILLH
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (Suppressor of upstream AUG protein 5) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein SUA5) (tRNA threonylcarbamoyladenosine biosynthesis protein SUA5) (P32579)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Required for normal translation, by ensuring translation fidelity at the level of codon recognition, appropriate translation initiation selection and maintenance of reading frame. Also involved in telomere replication. Binds to single-stranded telomeric (ssTG) DNA and positively regulates telomere length.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- tRNA N6-adenosine threonylcarbamoyltransferase
- EKC/KEOPS complex subunit CGI121
- EKC/KEOPS complex subunit BUD32
- EKC/KEOPS complex subunit PCC1
- Ribosome quality control complex subunit 2
- Dephospho-CoA kinase CAB5
- tRNA dimethylallyltransferase
- EKC/KEOPS complex subunit GON7
Sequence:
MYLGRHFLAMTSKALFDTKILKVNPLSIIFSPDAHIDGSLPTITDPETEAALVEAARIIRDTDETVAFPTETVYGLGGSALNDNSVLSIYRAKNRPSDNPLITHVSSIDQLNRKVFNQPHLSGTSLFDNIPSIYRPLISSLWPGPLTILLPVPSSEHSALSKLTTADQPTFAVRIPANPVARALIALSDTPIAAPSANASTRPSPTLASHVYHDLKDKIPIILDGGACKVGVESTVVDGLCNPPTLLRPGGFTYEEIVKLGGEAWSLCKVENKKTVEKGEKVRTPGMKYRHYSPSAKVVLLVPHCEGDGILKGVDRMERLKRLIETELKANSNIKKIAILTSLKLRDSDLQSKIFNEPDFSSKTFIIERLGQSGEEIQTNLFAALRKVDENDKVDLIFVEGINEEGEGLAVMNRLRKAAANNCIQF
Protein: Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) (F4IA25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364099}.
Interaction partners:
- AMP deaminase
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Guanylate kinase 2
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 1
- Adenylosuccinate synthetase, chloroplastic
- At1g72880
- GMP synthase
- AICARFT/IMPCHase bienzyme family protein
Sequence:
MALEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGDSEETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSGVPRVSFDLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFYSGFELNHGKQKYLLCPDEFVVGYGMDFAEQYRNLSYIGVLKPEYYM