wanglab/gogpt-training-data huggingface dataset:
Protein: Elongator complex protein 1 (Q9VGK7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95163}. Nucleus {ECO:0000250|UniProtKB:O95163}. Cytoplasm, cytoskeleton, spindle {ECO:0000305|PubMed:36302967}. Note=During asymmetric cell division of sensory organ precursor cells the elongator complex preferentially binds and stabilizes microtubules on the anterior side (pIIb daughter cell) of the spindle. {ECO:0000269|PubMed:36302967}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 2
- Elongator complex protein 5
- Protein KTI12 homolog
- Elongator complex protein 4
- Tetraspanin 68C, isoform A
- EG:8D8.4 protein
- Diphthamide biosynthesis protein 3
- Elongator complex protein 6
- Translin
Sequence:
MRNLKLRYCKELNAVAHPQHLLLQPELNGGASDIYFVVADNKIYAVQESGDVRLKVIADLPDIVGVEFLQLDNAICVASGAGEVILVDPQTGATSEGTFCDVGIESMAWSPNQEVVAFVTRTHNVVLMTSTFDVIAEQPLDAELDPDQQFVNVGWGKKETQFHGSEGKQAAKQKESDSTFIRDEQELNQDVSISWRGDGEFFVVSYVAAQLGRTFKVYDSEGKLNHTAEKSANLKDSVVWRPTGNWIAVPQQFPNKSTIALFEKNGLRHRELVLPFDLQEEPVVQLRWSEDSDILAIRTCAKEEQRVYLYTIGNYHWYLKQVLIFEQADPLALLHWDTRCGAEHTLHVLKESGKHLVYRWAFAVDRNNSIVGVIDGKRLLLTDFDEAIVPPPMSKIVLKFETYINAFISHGTSLWVYTCDRKIYLNEHIHTLGKELQKPIMLMPDAELSGLHLANLTHFSPHYLLATHSSAGSTRLLLLSYKDNDNKPGEWFYRVHSSVRINGLVNAVAVAPYAMNEFYVQTVNNGHTYEVSLKADKTLKVERSYVQLHEPADQIDWVIVKGCIWDGYTGALVTLRNQHLLHIDGYRIGEDVTSFCVVTNYLVYTQLNAMHFVQLDDRRQVASRNIERGAKIVTAVARKARVVLQLPRGNLEAICPRVLVLELVGDLLERGKYQKAIEMSRKQRINLNIIFDHDVKRFVSSVGAFLNDINEPQWLCLFLSELQNEDFTKGMYSSNYDASKQTYPSDYRVDQKVEYVCRLLEQQMNRFVSRFRLPLITAYVKLGCLEMALQVIWKEQQEDASLADQLLQHLLYLVDVNDLYNVALGTYDFGLVLFVAQKSQKDPKEFLPYLNDLKALPIDYRKFRIDDHLKRYTSALSHLAACGEQHYEEALEYIRKHGLYTDGLAFYREHIEFQKNIYVAYADHLRAIAKLDNASLMYERGGQLQQALLSAKHTLDWQRVLVLAKKLSEPLDQVAQSLVGPLQQQGRHMEAYELVKEHCQDRKRQFDVLLEGHLYSRAIYEAGLEDDDVSEKIAPALLAYGVQLESSLQADLQLFLDYKQRLLDIRRNQAKSGEGYIDTDVNLKEVDLLSDTTSLHSSQYSGTSRRTGKTFRSSKNRRKHERKLFSLKPGNPFEDIALIDALHNHVTKIAQQQQPVRDTCKALLQLANAADADPLAAALQREFKTLLQAVDAALDEIWTPELRGNGLMADHLTGPNVDYLALQKEQRYALLSPLKRFKPQLIMMDWQHEILQ
Protein: Large ribosomal subunit protein mL45 (39S ribosomal protein L45, mitochondrial) (L45mt) (MRP-L45) (Q9D0Q7)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BRJ2}.
Interaction partners:
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL49
- Small ribosomal subunit protein mS40
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL37
- Small ribosomal subunit protein mS22
- Large ribosomal subunit protein bL12m
Sequence:
MAAPVPRGLSSLYRTLGWWSRQPILVTQSTTVVQVKTKSRFRPPTPEPKYKTEKEFLEYARKAGLVIPQERLERPIHLACTAGIFDPYVPPEGDARMSSLSKEGLTQRTERLRKNAASQLAIRKIREFDANFKTKDFPEKAKDIFIEAHLCLNNSDHDRLHTLVTEHCFPDMVWDLKYKTVRWGFVESLEPAQVVHVRCSGLVNQSNMYGQVTVRLHTRQTLAIYDRFGRLMYGQEDVPKDVLEYVVFERHLMNPYGSWRMHAKIVPAWAPPKQPILKTLMIPGPQLKPWEEYEETQGEAQKPQLA
Protein: Sulfoquinovosyl transferase SQD2 (EC 2.4.1.-) (Protein SULFOQUINOVOSYLDIACYLGLYCEROL 2) (Sulfolipid synthase SQD2) (UDP-sulfoquinovose: diacylglycerol alpha-sulfoquinovosyltransferase SQD2) (Q8S4F6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of the sulfoquinovose moiety from UDP-sulfoquinovose to diacylglycerol during sulfolipid biosynthesis. Sulfolipid contributes to maintaining a negatively charged lipid-water interface, a requirement for proper function of photosynthetic membranes. Sulfolipid may also function as a substitute of anionic phospholipids under phosphate-limited growth conditions.
Subcellular location: Plastid, chloroplast membrane {ECO:0000255, ECO:0000269|PubMed:21506606}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-sulfoquinovose synthase, chloroplastic
- Monogalactosyldiacylglycerol synthase 3, chloroplastic
- Monogalactosyldiacylglycerol synthase 2, chloroplastic
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol kinase 5
- Diacylglycerol O-acyltransferase 3
- Diacylglycerol kinase 1
- Phospholipid:diacylglycerol acyltransferase 1
- Diacylglycerol kinase 3
Sequence:
MTTLSSINLSIPPHLLPSTTNTCSSSSATSCSPPRSSSFVLHSPLSFGHRRLPISKKSKLRFCGVITKEAVSGSNDMTITQVREDDESEIDAPLLDPESLSKPRRIALFVEPSPFAYVSGYKNRFQNFIRYLREMGDEVIVVTTHEGVPEEFYGARVIGSRSFPCPYYQKVPLSLALSPRIISEIARFKPDIIHASSPGVMVFGALAIAKMLSVPIVMSYHTHVPVYIPRYTFSWLVKPMWSIIRFLHRAADLTLVPSAAIGKDLIAAGATAANQLRLWNKGVDSESFNPRFRSQEMRIRLSNGEPEKPLVIHVGRIGVEKSLELLKSVMDKLPEARIAFIGDGPYKEDLEKLFTGMPAVFTGTLQGDELSQAYASGDVFVMPSESETLGLVVLEAMSSGLPVVAARAGGIPDIIPEDQEGKTGFLFNPGDVEDCVTKLRTLLHDRETREIIGKAAREETEKYDWRAATTKIRNEQYSAAIWFWRKKKVHVLGPINWLIKRLFPVPEGNV
Protein: Replication and transcription activator (RTA) (EC 2.3.2.27) (F5HCV3)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Transcription activation.
Subcellular location: Host nucleus {ECO:0000269|PubMed:23990779, ECO:0000269|PubMed:35914008}.
Interaction partners:
Sequence:
MAQDDKGKKLRRSCVESFVGLSDELKAQLYQCVLLINDAYETIYDPSDLNRVVEDVCIRIMKECSKLGALCGLFTDINMFNLFCFFRASRMRTKGAAGYNVPCAEASQGIIRILTERILFCTEKAFLTAACSGVSLPPAICKLLHEIYTEMKAKCLGAWRRLVCNRRPIMILTSSLLKLYNTYDTAGLLSEQSRALCLLVFQPVYLPRIMAPLEIMTKGQLAPENFYSITGSAEKRRPITTGKVTGLSYPGSGLMPESLILPILEPGLLPASMVDLSDVLAKPAVILSAPALSQFVISKPHPNMPHTVSIIPFNPSGTDPAFISTWQAASQNMVYNTSTAPLKPATGSSQTVSVKAVAQGAVITATTVPQAMPARGTGGELPVMSASTPARDQVAACFVAENTGDSPDNPSSFLTSCHPCDPNTVIVAQQFQPPQCVTLLQVTCAPSSTPPPDSTVRAPVVQLPTVVPLPASAFLPALAQPEASGEELPGGHDGDQGVPCRDSTAAATAAEATTPKRKQRSKERSSKKRKALTVPEADTTPSTTTPGTSLGSITTPQDVHATDVATSEGPSEAQPPLLSLPPPLDVDQSLFALLDEAGPETWDVGSPLSPTDDALLSSILQGLYQLDTPPPLRSPSPASFGPESPADIPSPSGGEYTQLQPVRATSATPANEVQESGTLYQLHQWRNYFRD
Protein: Patatin-like phospholipase domain-containing protein atgl-1 (EC 3.1.1.3) (Adipose triglyceride lipase 1) (Q11186)
Organism: Caenorhabditis elegans
Function: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (By similarity). Component of a feedback loop involving atfs-1, atgl-1 and hlh-11. Promotes fat oxidation in response to mitochondrial stress. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. Acts coordinately with lid-1 within the lipolytic cascade to distribute stored energy to tissues. Together with lipid droplet protein cgi-58, regulates lipid reserves as well as lipid droplet size and localization during the dauer phase in response to phosphorylation by ampk. May regulate serotonin-mediated lipolysis in metabolic tissues.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:20176933, ECO:0000269|PubMed:25202121, ECO:0000269|PubMed:26083785, ECO:0000269|PubMed:26098762}. Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:26098762}. Note=Accumulates in the cytoplasm when phosphorylated and within lipid droplets when unphosphorylated during the dauer phase (PubMed:26098762). Localization on lipid droplets enhanced by interaction with cgi-58 (PubMed:26083785). {ECO:0000269|PubMed:26083785, ECO:0000269|PubMed:26098762}.
Interaction partners:
- Abhydrolase domain-containing protein lid-1
- Hormone-sensitive lipase
- Abhydrolase domain-containing protein abhd-5.2
- Abhydrolase domain-containing protein abhd-5.1
- Lipase lipl-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Protein dhs-3
- Trifunctional enzyme subunit alpha, mitochondrial
Sequence:
MTMINSRPELMNLSFSGCGFLCVYHAGVAAAIKEYAPELLQNKILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEFNLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGGVSDNQPIYDEHTVTVSPFSGESDICPPDWDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALRFLTKCGLAPCIRCLTIQTIDANEPAGRVSSECFSENDDAKKVTHVAVPRMKKRASANALNSFRTRGESECETCGDSDIPLEEVNIQSFFPSIMKKPFEDAVAAERSVFQYMMSFRLVRYATTAMGISKFPFDMALAFVKKVHQYLDMVSPPRWIMLKFRGLADFILGEVEKQKSRYTNFSCLVAVAETDSFGSVLASSTMEKEEHKEIELSEDAKKEMILLRERDRRRKLLKKAGKITPNNSENQFDETSVYDVDSFEHVIDFTKSHEALYEFHYRDENQVMKTFGLFTDSQQRPYSSASQHQHHHTKSLGGTSRLVHVPEEDEDAPLSAVSAPAVIFHGGQEIVELGESDKDSGLSGIDTKRKVPDEPTTRF
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (H0YMP1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLCSIEKPSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDD
Protein: CREB homolog crh-2 (Q4JFH9)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Plays a role in regulating the developmentally arrested larval state known as dauer, when induced by long-term exposure to the Gram-negative bacterium P.aeruginosa PAO1, but dispensable for dauer formation induced by starvation. Involved in regulating expression of microRNA mir-243, during long-term exposure to P.aeruginosa PAO1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BZIP domain-containing protein.
Sequence:
MNSSSSRSSMSMPMPMDMPQMHMGMNNNCEMNQMMHPIPNFPMKWEPCTPPDEKPHPSMLFPPLSGIFNQSRHSSTGEDYHGSSSGSPSSSLSSPNEFKDEPLGLDVHFGNSLFNAPFSPSATSSHSPSSYGMMHGSHSMASHQLHQQQLSPLPSVAHFSHSHHLQHHVVQHPSQASLQMNMNQIFSGPSHQYASSSVPHTFLFKDSTIYEGMGGMGLAAAQQQLKARNKMHEMAIRQHLITDQNITANGDLVLSAEERRTLVQEGYSIPQKYPLTKSEEESLKIVRRKIKNKLSAQESRRKRKEYIDALEGRLHCFSEENKSLKKQVHQLEASNRDLQQKLHQYESKEKM
Protein: DSR-CI protein (Q24017)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSIDLDNGSINYRQRNIVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMISCSGRCGTSMSASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGIITTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: UDP-sugar transporter sqv-7 (Squashed vulva protein 7) (Q18779)
Organism: Caenorhabditis elegans
Function: Acts as a transporter of UDP-glucuronic acid (UDP-GlcA), UDP-N-acetylgalactosamine (UDP-GalNAc) and UDP-galactose (UDP-Gal) from the cytoplasm into the Golgi lumen. Involved in the biosynthesis of glycoconjugates that play a pivotal role in development. Involved in the synthesis of chondroitin sulfate and heparan sulfate proteoglycans. Required for embryonic development. Involved in vulva epithelium invagination and embryonic development. Involved in the directed migration of hermaphrodite-specific neurons.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Xylosylprotein 4-beta-galactosyltransferase
- UDP-galactose transporter
- UDP-N-acetylglucosamine/UDP-N-acetylgalactosamine transporter nstp-4
- UDP-glucuronate decarboxylase
- Lateral Signaling Target
- Chondroitin sulfate synthase sqv-5
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8
- UDP-galactose/UDP-N-acetylglucosamine transporter srf-3
- Ubiquinone biosynthesis protein coq-4, mitochondrial
- UDP-glucose 6-dehydrogenase
Sequence:
MTSTVQSPLYSRVFSAVFYGVISVLIVFVNKILLTNYKFPSFLFVGVGQMMATILILFFAKMFRIVQFPSLDSSIPRKIMPLPLLYFFNLISGLGGTQMINLPMFTVLRRFSILMTMILEFYILNVKASKAVKISVGLMIGGSFIAAIYDLSFDALGYTMIFINNICTAALGVYTKQKLDAKDLGKYGLMFYNCLFMLLPALCVVQYTGDLDRAYSFMLSDSMTSSVWTCFLLSCICGFVLNYSLVLCTHHNSALTTTCVGPIKNLFVTYVGMFSSGDYVFQWANFTGINVSVFGSILYTYVTFRSKSTTISYKPLPMTMPIDVHKPRN
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (A7ZQC5)
Organism: Escherichia coli O139:H28 (strain E24377A / ETEC)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
Interaction partners:
Sequence:
MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVLKTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKVDEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAVDAINAGQEAVVVLDQTPFYAESGGQVGDKGELKGANFSFAVEDTQKYGQAIGHIGKLAAGSLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSHNEAMKPEEIRAVEDLVNAQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGDFSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAITTVHADSDRLSEVAHLLKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSGVEPKMLRTMVDDLKNQLGSTIIVLATVAEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVGGKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ
Protein: Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) (Q8HYX6)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Ryanodine receptor 2
- Ryanodine receptor 1
- Calmodulin
- Calmodulin like 5
- Calmodulin 2
- Ryanodine receptor 3
- TGF-beta receptor type-1
- Triadin
- Serine/threonine-protein kinase mTOR
- Serine/threonine-protein kinase receptor
Sequence:
MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFGVELLNLE
Protein: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (P43123)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: UDP-N-acetylglucosamine pyrophosphorylase that utilizes N-acetylglucosamine-1-phosphate as substrate. Together with AGM1, is involved in the production of UDP-N-acetylglucosamine from N-acetylglucosamine-6-phosphate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphoacetylglucosamine mutase
- Glucosamine 6-phosphate N-acetyltransferase
- Glutamine--fructose-6-phosphate aminotransferase
- Chitin synthase 3
- Chitin synthase 2
- Chitin synthase 1
- UTP--glucose-1-phosphate uridylyltransferase
- Putative glutamine--fructose-6-phosphate aminotransferase
- Phosphoribomutase
- Bifunctional protein GAL10
Sequence:
MTDTKQLFIEAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTGKYTKPTEPNGIKLEQFIFDVFDTVPLNKFGCLEVDRCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVLVEVSSKLSYAGENLSQFKGKVFDRSGIVLEK
Protein: Actin, alpha skeletal muscle (EC 3.6.4.-) (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form] (P68139)
Organism: Gallus gallus (Chicken)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
Protein: Calmodulin-binding transcription activator 5 (AtCAMTA5) (Ethylene-induced calmodulin-binding protein f) (EICBP.f) (Signal-responsive protein 6) (AtSR6) (O23463)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator. Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767, ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986}.
Interaction partners:
- NEFA-interacting nuclear protein
- Zinc finger CCCH domain-containing protein 16
- At2g43110
- Alpha/beta-Hydrolases superfamily protein
- Peptidyl-prolyl cis-trans isomerase CYP59
- BTB/POZ domain-containing protein At3g19850
Sequence:
MAGVDSGKLIGSEIHGFHTLQDLDIQTMLDEAYSRWLRPNEIHALLCNHKFFTINVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGEDTPTFVRRCYWLLDKSQEHIVLVHYRETHEVHAAPATPGNSYSSSITDHLSPKIVAEDTSSGVHNTCNTGFEVRSNSLGSRNHEIRLHEINTLDWDELLVPADISNQSHPTEEDMLYFTEQLQTAPRGSVKQGNHLAGYNGSVDIPSFPGLEDPVYQNNNSCGAGEFSSQHSHCGVDPNLQRRDFSATVTDQPGDALLNNGYGSQDSFGRWVNNFISDSPGSVDDPSLEAVYTPGQDSSTPPTVFHSHSDIPEQVFNITDVSPAWAYSTEKTKILVTGFFHDSFQHLGRSNLICICGELRVPAEFLQMGVYRCFLPPQSPGVVNLYLSVDGNKPISQLFSFEHRSVQFIEKAIPQDDQLYKWEEFEFQVRLAHLLFTSSNKISVLTSKISPENLLEAKKLASRTSHLLNSWAYLMKSIQANEVPFDQARDHLFELTLKNRLKEWLLEKVIENRNTKEYDSKGLGVIHLCAVLGYTWSILLFSWANISLDFRDKQGWTALHWAAYYGREKMVAALLSAGARPNLVTDPTKEFLGGCTAADLAQQKGYDGLAAFLAEKCLVAQFKDMQTAGNISGNLETIKAEKSSNPGNANEEEQSLKDTLAAYRTAAEAAARIQGAFREHELKVRSSAVRFASKEEEAKNIIAAMKIQHAFRNFEVRRKIAAAARIQYRFQTWKMRREFLNMRKKAIRIQAAFRGFQVRRQYQKITWSVGVLEKAILRWRLKRKGFRGLQVSQPDEKEGSEAVEDFYKTSQKQAEERLERSVVKVQAMFRSKKAQQDYRRMKLAHEEAQLEYDGMQELDQMATEES
Protein: Transcription factor egl-13 (Protein egg laying defective 13) (Q23045)
Organism: Caenorhabditis elegans
Function: Probable transcription factor that is required for uterine and neuronal cell fate decisions. Controls genes required for the specification and differentiation of O(2) and CO(2)-sensing neurons and for maintaining URX sensory neuronal cell fate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:9834196}. Note=Localized to nucleus during interphase. {ECO:0000269|PubMed:23946438}.
Interaction partners:
Sequence:
MSRRRKANPTKLSENAKKLAKEVENSQEENDCDMLAKPQTPTIIIPGHMDDTPNPAGSPHDASIKSSSSTISDHTSTSATTGISDFPDILAQTEHGCSVLIDGNHLREIINSVDTQDGKQDLLSDVIRQLTSIKERLTNDESPVKDDLKEDPDDMSPMLHAGNFDSEMLLRQHELMQHQQQQMIIANMLKATQSLPLLFNGGLNYEAILNNPVLNATIAGHLPNPLASNISLLQKSISAKLAAAGNMQTVEKVETPLNLSKDTPSPTAIPQSPLSGFRLPYSLGTNYGSDGQLFNNCSPNSSGKSTPGNTSVTSEVATPRPQAKSPNHIKRPMNAFMVWARDERRKILKAYPDMHNSNISKILGSRWKGMSNSEKQPYYEEQSRLSKLHMEQHPDYRYRPRPKRTCVIDGKKVRVNEYKTIMKTKKDLMWGDEPGFSQPSDLQMDLASHVNLLNDLTQHHHQSHLLQTAE
Protein: Imaginal disk growth factor 6 (Q23997)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably required to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:18342251, ECO:0000269|PubMed:7875581}. Note=It is transported to target tissues via hemolymph.
Interaction partners:
Sequence:
MIIKALAIVSLCLASIQASKVGAPQLPKKHLVCYYDSASFVKEGLGKLVIDELEPALQFCDYLVYGYAGIERDSHKAVSLNQQLDLDLGKGLYRTVTRLKRKYPNVKILLSVGGDKDIELDKDAKELPNKYLELLESPTGRTRFVNTVYSLVKTYGFDGLDVAWQFPKNKPKKVHSGIGSLWKGFKKVFSGDSIVDEKSEEHKEQFTALLRDVKNAFRPDNLLLSTTVLPNVNSSLFYDIPAVVNYLDFVNLGTFDFFTPQRNPEVADYAAPIYELSERNPEFNVAAQVKYWLRNNCPASKINVGVATYGRPWKLTDDSGDTGVPPVKDVKDEAPVGGNTQVPGIYSWPEVCALLPNQNNAYLKGANAPLIKVQDPAKRFGSYAYRAADKKGDNGIWVSFEDPDTAADKAGYVRTENLGGVALFDLSYDDFRGLCTNEKYPILRAIKYRLTN
Protein: Lysophospholipase, putative (D6XM23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acyltransferase, putative
Sequence:
MFGTPVENLTANQIKEELRTLYGVSDFSGCIEQKDLQEKLEKTRETELITHGLKYGPLLQIGNRQSPSGIVTLTHGLGDSANGWESVAVELSRRLPHLLFLLPTASMQPVGINGGAVMNSWYDIRNVSSGNGVTEDAEAIIMSANYLKSLAYTASRRYQVPAGRVVYAGFSQGAVISLAAGLTARIAPAGVAALSGYFAAAEKILPQLCNKSLPVLLCHGTMDNIIPFSAAEKTKETLESLGVGPVTLYSYPMEHSSHPKEINDLEKFLQQVLPGPSSKS
Protein: Transcription factor tau 138 kDa subunit (TFIIIC 138 kDa subunit) (Transcription factor C subunit 3) (P34111)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. TFC3 is essential for cell viability. Cooperates with TFC6 in DNA binding.
Subcellular location: Nucleus. Mitochondrion.
Interaction partners:
- Transcription factor tau 95 kDa subunit
- Transcription factor tau 91 kDa subunit
- Transcription factor tau 55 kDa subunit
- Transcription factor tau 60 kDa subunit
- Transcription factor tau 131 kDa subunit
- Transcription factor TFIIIB component B''
- Transcription factor IIIB 70 kDa subunit
- TATA-box-binding protein
- Transcription factor IIIA
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MVLTIYPDELVQIVSDKIASNKGKITLNQLWDISGKYFDLSDKKVKQFVLSCVILKKDIEVYCDGAITTKNVTDIIGDANHSYSVGITEDSLWTLLTGYTKKESTIGNSAFELLLEVAKSGEKGINTMDLAQVTGQDPRSVTGRIKKINHLLTSSQLIYKGHVVKQLKLKKFSHDGVDSNPYINIRDHLATIVEVVKRSKNGIRQIIDLKRELKFDKEKRLSKAFIAAIAWLDEKEYLKKVLVVSPKNPAIKIRCVKYVKDIPDSKGSPSFEYDSNSADEDSVSDSKAAFEDEDLVEGLDNFNATDLLQNQGLVMEEKEDAVKNEVLLNRFYPLQNQTYDIADKSGLKGISTMDVVNRITGKEFQRAFTKSSEYYLESVDKQKENTGGYRLFRIYDFEGKKKFFRLFTAQNFQKLTNAEDEISVPKGFDELGKSRTDLKTLNEDNFVALNNTVRFTTDSDGQDIFFWHGELKIPPNSKKTPNKNKRKRQVKNSTNASVAGNISNPKRIKLEQHVSTAQEPKSAEDSPSSNGGTVVKGKVVNFGGFSARSLRSLQRQRAILKVMNTIGGVAYLREQFYESVSKYMGSTTTLDKKTVRGDVDLMVESEKLGARTEPVSGRKIIFLPTVGEDAIQRYILKEKDSKKATFTDVIHDTEIYFFDQTEKNRFHRGKKSVERIRKFQNRQKNAKIKASDDAISKKSTSVNVSDGKIKRRDKKVSAGRTTVVVENTKEDKTVYHAGTKDGVQALIRAVVVTKSIKNEIMWDKITKLFPNNSLDNLKKKWTARRVRMGHSGWRAYVDKWKKMLVLAIKSEKISLRDVEELDLIKLLDIWTSFDEKEIKRPLFLYKNYEENRKKFTLVRDDTLTHSGNDLAMSSMIQREISSLKKTYTRKISASTKDLSKSQSDDYIRTVIRSILIESPSTTRNEIEALKNVGNESIDNVIMDMAKEKQIYLHGSKLECTDTLPDILENRGNYKDFGVAFQYRCKVNELLEAGNAIVINQEPSDISSWVLIDLISGELLNMDVIPMVRNVRPLTYTSRRFEIRTLTPPLIIYANSQTKLNTARKSAVKVPLGKPFSRLWVNGSGSIRPNIWKQVVTMVVNEIIFHPGITLSRLQSRCREVLSLHEISEICKWLLERQVLITTDFDGYWVNHNWYSIYEST