wanglab/gogpt-training-data huggingface dataset:
Protein: Dbx (Q9W064)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSTAFLVDSLLHAQQTYTESQLKSSLSEMLLSRRSATGTDAADPADQPTESCGCSKLRGYKCDKCREIRAESVESIEEMDEDDGSSSADEIVADIGSVEGEEPHMDLDEELEEELADVDEPVSIKLPKVEPKETSMPTVGNTILKDTNSKPILKFSVSAILGDTREGVRVRNEFMQPQHIWPYLQQNFMQQHSHQYQQHHQQQQPHSHPQHQPLAVPGHQHSHPHSHHHHHHHPGAGHAHFPHPAFLTHQLPPHQHHQQQQHVQQQHPGNSCQPQTASSSSSPGSTISDSDNNHGASTANGNGSGTGNSGQDARPHELANSNPDEDSSASRRLTQDKQQQQQLLGAGGTGGGGGGGHGHGHPTPPPPPPPPVIAKPMPSRPTPFLPHTLNHPHLHSLLAHCRNPYMSVGAQVFPLPPGQGFPWAHSTRGKPRRGMMRRAVFSDSQRKGLEKRFQQQKYISKPDRKKLAERLGLKDSQVKIWFQNRRMKWRNSKERELLASGGSRDQTLPNKNNPNPDLSDAKCDRPLTPLSPSLLSPNGSATPPPPGAVAKDEPPTAAVTPKSPQSVSSRSSPSVGYGLQISSPPPLLTSLKMGDQSASATPTPLPGTTVSSAAASPPGVTASEFQAKINAEMQKQLVAADLKFKLENSIQEAKQRRFEQLQQQLHHSPHFSAMREVELAAAAAAAQLHHHHQQQQQQQQQQHAQQQHAQQQHQGGSEFMKLYYDDYDDSNSDSDEEISVT
Protein: Zinc transporter 5 (ZRT/IRT-like protein 5) (OsZIP5) (Q6L8G0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Zinc transporter that mediates zinc uptake from the rhizosphere and may be responsible for the translocation of zinc within the plant.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20419467}; Multi-pass membrane protein {ECO:0000269|PubMed:20419467}.
Interaction partners:
Sequence:
MATAAMTKVFVLLFLVAACYLPAHAAAAECDCATDTAGRDKAQALRLKVIAIFCILAGSTVGAALPSLGGRFPAIQPETDVFLSVKAFAGGVILATGLVHILPAAFEALSSPCLVGGPWKRFPFAGMVAMVSAIGTLIVDTVATGYFHRTDAKRKAAAVADEPADDLEASDEHSHGHAHGMSVMSVAPAGEEDLVRHRVISQVLELGVVVHSLIIGMSLGASDFPSTVRPLVPALTFHQFFEGIGLGGCIVQAKFRVRSVVTMALFFSLTTPAGIVVGIGISSVYDANSPTALVVQGLLEAAAAGILVYMALVDILAEDFMKTKVQRRGRLQLAMNVALLLGAGLMSMIAIWA
Protein: Phospholipase B1, membrane-associated (Phospholipase B) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A2) (EC 3.1.1.4) (Phospholipase B/lipase) (PLB/LIP) (Triacylglycerol lipase) (EC 3.1.1.3) (O54728)
Organism: Rattus norvegicus (Rat)
Function: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes.
Interaction partners:
- lysophospholipase
- Membrane bound O-acyltransferase domain containing 1
- Lysosomal phospholipase A and acyltransferase
- Phospholipase A and acyltransferase 3
- Acyl-protein thioesterase 1
- Acyl-protein thioesterase 2
- Cytochrome P450 2U1
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylcholine-sterol acyltransferase
Sequence:
MESWPGVSLVGLLLLLLLGQGPSQIHGSSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ
Protein: Protein FAM78A (Q5JUQ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGFFCDCWPSLEIRALLYAMGCIQSIGGKARVFREGITVIDVKASIDPVPTSIDESSSVVLRYRTPHFRASAQVVMPPIPKKETWVVGWIQACSHMEFYNQYGEQGMSSWELPDLQEGKIQAISDSDGVNYPWYGNTTETCTIVGPTKRDSKFIISMNDNFYPSVTWAVPVSESNVAKLTNIYRDQSFTTWLVATNTSTNDMIILQTLHWRMQLSIEVNPNRPLGQRARLREPIAQDQPKILSKNEPIPPSALVKPNANDAQVLMWRPKYGQPLVVIPPKHR
Protein: Retinol-binding protein 1 (Cellular retinol-binding protein) (CRBP) (Cellular retinol-binding protein I) (CRBP-I) (P09455)
Organism: Homo sapiens (Human)
Function: Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22665496}. Lipid droplet {ECO:0000269|PubMed:15632377}.
Interaction partners:
- Receptor for retinol uptake STRA6
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 11
- Retinol-binding protein 4
- Retinaldehyde-binding protein 1
- Retinol-binding protein 3
- Transthyretin
- Aldehyde dehydrogenase 1A1
- Cytochrome P450 26A1
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MPVDFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ
Protein: Renalase (EC 1.6.3.5) (Monoamine oxidase-C) (MAO-C) (mMAO-C) (A7RDN6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis.
Subcellular location: Secreted {ECO:0000269|PubMed:17846919}.
Interaction partners:
Sequence:
MSRVLVVGAGLTGSLCAALLRKEITAPLYLGLWDKGGDIGGRMITASSPHNPRCTADLGAQYITCSPHYVKEHQNFYEELLAHGILKPLTSPIEGMKGKEGDCNFVAPQGFSSVIKYYLKKSGAEVSLKHCVTQIHLKDNKWEVSTDTGSAEQFDLVILTMPAPQILELQGDIVNLISERQREQLKSVSYSSRYALGLFYEVGMKIGVPWSCRYLSSHPCICFISIDNKKRNIESSECGPSVVIQTTVPFGVQHLEASEADVQKLMIQQLETILPGLPQPVATICHKWTYSQVTSSVSDRPGQMTLHLKPFLVCGGDGFTHSNFNGCISSALSVMKVLKRYI
Protein: LIM domain-binding protein 3 (Protein cypher) (Protein oracle) (Z-band alternatively spliced PDZ-motif protein) (Q9JKS4)
Organism: Mus musculus (Mouse)
Function: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10391924}. Cell projection, pseudopodium {ECO:0000269|PubMed:10391924}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10391924}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10391924}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
Interaction partners:
- Myotilin
- Alpha-actinin-2
- Myozenin-2
- Myomesin-1
- Titin
- Myopalladin
- Cysteine and glycine-rich protein 3
- Telethonin
- PDZ and LIM domain protein 3
- Beta-taxilin
Sequence:
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKDPALDTNGSLATPSPSPEARASPGALEFGDTFSSSFSQTSVCSPLMEASGPVLPLGSPVAKASSEGAQGSVSPKVLPGPSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGAGLLGGSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSSTPIEHAPVCTSQATSPLLPASAQSPAAASPIAASPTLATAAATHAAAASAAGPAASPVENPRPQASAYSPAAAASPAPSAHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASSYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYTPTPSAAYSGGPSESASRPPWVTDDSFSQKFAPGKSTTTVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHAINV
Protein: Dysferlin (F6IA09)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004483}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004483}.
Interaction partners:
Sequence:
MLRCLLQRATNLRNVEKGERHSDPLASITFRGTKKKTKVIKNNVNPVWNEGFEWDLKGVPLDSGAELHVVVKDHEKMGRNRFLGECRVALRDVLNSPNLAATFTVSLVDTKRNSTGATITLQVSYIPPPGMTPIFQPPPQPEAQHTPVELDTVTVFSLDTMGEDDTESMLMMEVAEEPEPVPGPQGQDIGAPTAPPKKAPPNFNQGLKKEKRQSNKSPLSDKAQDLQVRLRIIEGRQLPGVNIKPVVKVTVGGQTKRTRIKKGNNPFFDEVAFFRLVEKIFNNFEKSLLIVVFDSKSLRKDSVIGEFELDVGMVYNEHRHAILRKWLLLADPDDLSAGARGYLKVSMFVLAAGDEPPMDKKEGVEEKEDIEANLLRPAGLTLRGATFTLRVYRAEDLPQMGDALIDDVKHFLGFDTNRKNLVDPLVEVNFAGKTVSSKILEKCANPQWNQCLTLPIRFPSMCEKMRIRILDWDRASHNDVIGTAHLCMSKISAPGGDIEVDDSIGFLPTFGPCFVNMYGSPREFTAFSDPHEALNLGKGEGVAYRGRVLLELITKLSDQVDQRSEDINSDDLLVVEKFMRKRKFSLFAAFYSATLLQDVDDAVQFEVSIGNYGNKFDNTCLPLASTTQFSRAVFDGCHYYYLPWGNVKPVVVVSSEWEDIGPRIEALNMLLSIVDRLESNLEQVQLELKARSDDQEVEQRVVQLLDDVIADCSEELPELDKWPCVTPLDKALRNLRKINMQQIVQAALALKHGPETELSAVLEQAEDWTMRLRYLSEEPQNSPPDIIIWMLQGDRRVAYHRIPAHQVLFSYGYCGKHCGQLQTVFMKCPQEDGGCSKIPAQLRIKVWFGLTADVKSFNQFAEGKLSVFAETYENQTKLALVGNWGTTGLTYPKFSDVTGRVKLPKESFKPSSGWSWAGEWFISPEKTMLYDADAGHISFLEEVFENQLRLPGGQWIGMPEGYTDVNGEKAVPKDEIECPPGWVWEDIEWSEDLKRAVDDQGWEYGITLPPDRRPKSWVPSEKMYHTNRRRRWIRLRRRDMQKMEALRKQRPDESEREGWEYASLFGWKFHLKQKKTDLFRRRRWRRRMEPLEKTGPAAIFALECSLSSFTDEKNDDKSVTTTFGVSRPTISCFFDSGTLYHLRCYLYQARDLLAMDKDSFSDAYAVVSFLHQSQKTVTVRNTLNPTWDQTLIFYEVEIFGDHLVTERSPPNIVVELYDQDTYGADEFMGRCVCQPSMASSPRLAWYPIQKAGNSAGDLLAAFELIRRDKPAVHHIPGQEGDIIPPSHIMDELVLPGFLSENQQQWPEDSDLPYPPPQREPNVYMVPQGIKPVLQRTAIEILAWGLRNLKSFQLASVTSPSLQVECGGSVVQSCVIRNIKKNPNFDVNILSIDVRLPKEELYMPPLVIKVIDNRQFGRKPVVGQCSVHSLNEFYFQPESLERDSTEEEFEVIAHTPRDDVLVDIDDKEPLIPGQQDEFMDWWSKFYASMGERTKCGSYLEKGFDMLQVYDRELEKTEGFEQFADFCQTFKLYRGRTQNDSEDPSVVGEFKGSFKIYPLPDDPPMPVPTRQFRKLPPNGIEECLVRIYIIQAFGLQPKDANGKCDPYVKITLGKKSVDDHDNYIPCTLEPVFGKMFELTCCLPLEKDLKITLYDYDMVTKDEKIGETIIDLENRFLSRHGARCGLPQSYCLSGINQWRDQLKPSQLLHRLCERRNYKLPVYKQDRIYFRGHEYTVADLDEGKPLNPHLGPVMERLALLVLRRHGLVPEHVETRPLYSPLQPDIEQGRLQMWVDLFPKSLGPPGPPFNITPRKAKKFFLRCIIWNTRDVILDDVSVTGEKMSDIYVKGWMHGHEENKQKTDVHYRSLGGEGNFNWRFLFPFHYLPAEQLCTIDKKEHFWSLDKVETKLPPKLTIQIWDNDKFSFDDFLGSLEMDLNHMLSPAKSPEKCGLEMLTQSQDKLVSLLEQKTVKGWWPCVCDKEDKKILAGKVEMSLEIVCEQEQDERPAGLGRDEPNMNPHLEEPQRPETSFLWFSSPYKTFRFIVWRRFKWLILGLFILLFIILFLGVFLYAFPNYAAMKMVGPFSGLGKGTQ
Protein: Floating head (Homeobox protein) (Q90461)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQIPGRAYETYGQSARPLHQDYATSSSKPSTGKSFTIDALLARPDQAEMRERTNAYRSITNQTPVSSSALPLIYSQMPHFAYSQSIMQTQTGYPVFCYPPYNFQTTCRGAVYAQDAVLAKAAVHSHYKHKSGKSKRMRTSFTNDQLSRLEKEFARQQYMVGSERFLLASALQLTEAQVKVWFQNRRIKWRKQSLEQQQAKLAKLGLTVPPKSPGSQGREDEERDFTEESDVDIDIDDSLQD
Protein: UL25 protein (O39492)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Interaction partners:
Sequence:
MALGRLEFACLGVDIHAVADRVFVPDERNFIAPAFPLRFWDEPVFARIGDADAPARELAAARARNQAAAAAADNLLAKQRAAGAEVDARIRPIEARVAEVAAVLADLEEAARRAEEADAAAESARAGRAAADAEEGGGGAGALEAVRARRVQIAKNDPPLEYDTTLAADLLAMVYTARAGGGSAGIVFGTWYRTLQDRLIAERPLATRGMDYRDGRMSRTFMAAAVAALQSSGRMYVGNRAYSAFECAVLCLHLAHRAVAGGSQSPVTFVGLVEQIPAYLDALARAIDEGAARRVQYAFDLERLPRGQFQAPGGGAGRYERGALEAHAVVAALQRLRVLPAIPGALGGGAAPARAADADGVAYVDDVHRAAGAYLARAQNLFLAEDQSLLRATVDTITALLLVRRLLWNGNVYADKLRNNFQIGTLVPGAAAPGDVTRGADGGLDGAVGARSGDANLTFLCARYVARVYEACPEVEVTQLFPGAAALALDALAPRSAAGAPRAISVSGGRHQGGLLRLVALELENRHRAAPAPVVEVVAAHDAVALQYERGLGVLMQQPRLRRALDETRRLSQFNVASDYDLLYFLCLGFVPLFTSAV
Protein: Collagen alpha-1(XV) chain [Cleaved into: Restin (Endostatin-XV) (Related to endostatin) (Restin-I); Restin-2 (Restin-II); Restin-3 (Restin-III); Restin-4 (Restin-IV)] (P39059)
Organism: Homo sapiens (Human)
Function: Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
Interaction partners:
- Collagen alpha-3
- Collagen alpha-4
- Collagen alpha-1
- Glypican-4
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-2
Sequence:
MAPRRNNGQCWCLLMLLSVSTPLPAVTQTRGATETASQGHLDLTQLIGVPLPSSVSFVTGYGGFPAYSFGPGANVGRPARTLIPSTFFRDFAISVVVKPSSTRGGVLFAITDAFQKVIYLGLRLSGVEDGHQRIILYYTEPGSHVSQEAAAFSVPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQALAFESSAGIFMGNAGATGLERFTGSLQQLTVHPDPRTPEELCDPEESSASGETSGLQEADGVAEILEAVTYTQASPKEAKVEPINTPPTPSSPFEDMELSGEPVPEGTLETTNMSIIQHSSPKQGSGEILNDTLEGVHSVDGDPITDSGSGAGAFLDIAEEKNLAATAAGLAEVPISTAGEAEASSVPTGGPTLSMSTENPEEGVTPGPDNEERLAATAAGEAEALASMPGEVEASGVAPGELDLSMSAQSLGEEATVGPSSEDSLTTAAAATEVSLSTFEDEEASGVPTDGLAPLTATMAPERAVTSGPGDEEDLAAATTEEPLITAGGEESGSPPPDGPPLPLPTVAPERWITPAQREHVGMKGQAGPKGEKGDAGEELPGPPEPSGPVGPTAGAEAEGSGLGWGSDVGSGSGDLVGSEQLLRGPPGPPGPPGLPGIPGKPGTDVFMGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPGPPGKKGQAGPPGVMGPPGPPGPPGPPGPGCTMGLGFEDTEGSGSTQLLNEPKLSRPTAAIGLKGEKGDRGPKGERGMDGASIVGPPGPRGPPGHIKVLSNSLINITHGFMNFSDIPELVGPPGPDGLPGLPGFPGPRGPKGDTGLPGFPGLKGEQGEKGEPGAILTEDIPLERLMGKKGEPGMHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGTKGDPGVIMQGPPGLPGPPGPPGPPGAVINIKGAIFPIPVRPHCKMPVDTAHPGSPELITFHGVKGEKGSWGLPGSKGEKGDQGAQGPPGPPLDLAYLRHFLNNLKGENGDKGFKGEKGEKGDINGSFLMSGPPGLPGNPGPAGQKGETVVGPQGPPGAPGLPGPPGFGRPGDPGPPGPPGPPGPPAILGAAVALPGPPGPPGQPGLPGSRNLVTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGELIPIPADSPPPPALSSNPHQLLPPPNPISSANYEKPALHLAALNMPFSGDIRADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSIFSGHGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCANRLIVLCIENSFMTDARK
Protein: BTB domain-containing protein (Q9U1W5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGLAQSHSRTPSRDPLPNDHQVMDVYEESGPRRGRKRKAAKGSEIEMKKVAKLNTCAYVYQKLFLQGENSDIVLAACGREWRVHKLYLKQTKFFESMFDGLWTESNSGRVQMEITDPNIDADGLNSVLGSLYHNEIEIDLDKIEGTVAAASYIVLDSVTDRCSEMMIEALSTKNAVRFYDVSTKYGLEKVREKSMEVLLHQFWKIMTDREKLNEVDRQLFVTLLNSPNLLIIEGEFDLYKVVKSWIYMREVPDCCKDDSPETFTQNASKFFKESKTSMFIKYADIFASLRIEQFLTCSETIKTVKSDALIPLSIVDEMTSALWSSLLENEESPKTLEMDDDEFFKRCIRLGRSLDSFPKCWRWIGFNFGVDLLLHVNDYSVCIKRNCLNQKAPYSVNLKSKHVLHYRLVICDSNGQILYDSGKTTWEMKPDEARTIYRMSEDLATQISVHFQYLIHQPICSTGHYVNKYLDDQNSTDDEDDEEEEDDDGDDEEDSS
Protein: Ciliary neurotrophic factor (CNTF) (P20294)
Organism: Rattus norvegicus (Rat)
Function: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Subcellular location: Cytoplasm.
Interaction partners:
- Leukemia inhibitory factor receptor
- Ciliary neurotrophic factor receptor subunit alpha
- Interleukin-6 receptor subunit beta
- Leptin
- Erythropoietin
- Granulocyte colony-stimulating factor
- Glial cell line-derived neurotrophic factor
- Neurotrophic factor BDNF precursor form
- Prolactin
- Prolactin-6A1
Sequence:
MAFAEQTPLTLHRRDLCSRSIWLARKIRSDLTALMESYVKHQGLNKNINLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRVHFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPATVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESHYGAKDKQM
Protein: Transaldolase (Q5BBY2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MGITTRRPLLPAPTESIVDSFGSSVTGTDLGTDISRRTDKTSYSIPDDGSPVTIPTRRKHRSRGEDSTKLSRSAHHSQTSLLIEYFEGGKGSGGSGGAIVSRPSVRVRVTPSSRKKSKEPSVHITDSSGNRRPSYSRRISLGSPSKSKSGREILGDDLSYSSSADENQSPGPVEIELLNRDQGSELSTLSRDRRYLPTSDISSMPADSMLEAPSSGAQQQRTESPELEEPESKDYLKTPSRQRSRSLSTERIAQRAAEKVSNYSRDASSKRRAGKNRGIATDYQEVEAKSPRHRGYTKDDDMASPESSMLSASAVSSHRRSGDQYSFRSNTSKSSLNNPKLLETVEDAIRRLILPELKELKKDQKVMTNTSKFERDISSSHSPASSESRDGLVRRLSKHASAPNVRKPKVVLNKDSRDEGIVLADGSISSQKERRASRDSEMTAESGYVRGSRPELSEQDMVRRQKSKGLRDAERAGIVASRLTANNLKHHDSNSSLCKSESRRGSEPKNINETELVFQKHNVAPMPFRSALESEMTRASLLSEQTAEPEPRDSRHDLGLKHSNISSHNLSVHSASDNGREWSHSPSVEAAAGAIAAAAAANLLDTHSDSNELVHGGSRRALSPIQSVASNQSESHVRQGSTQHVPQEYSGDEREMEPKLSIDSLSSAPSTNLARSKREGITAESQDEISRYQKEAGPDLGYEGSSVLSNQTLRDKTWQEESDDGAYRHSLAETASIDPKHMANYADGSESDFIEKANQGRPVAEGVGVNPRFVHPAAVESAVASVLDPSILDTKSNQSAGSHSQSNTFVQGETGSTRSLGQLNQHSPTSRRGSPLKQQHNVSSSPDATSFPRRMGVTSPPQSVTQSIDDLTEPVELLPDEHGESPPPQDRELSPEDESEINTNPSIIQGPAAGVGPDSTWQYNSSSGKGGHSPLFDNAATAAAAGAGLGLASSRQEYGHDYYPGDDYADAYQDQQYANGPIFSTPPGAKDEGYVSAANPISPSPQPGIKGFSGIDTNGLGLFDSPGDDAFEPSHQRHFSGYSHGVGSPLYDSATGRGIERIQSKDIVALMDHLTVRDAQRNARDTEILVTLVRSAAEMRNSFEEMKKFIAQQDGMILDSNERTYKAINGPRPLPASGSRTRQASVEDGEDSPAKRKNLFKRALKGLSLKSGNDLSRIEDMLEQLLDDMEALRSSQNDMMRSRGPASVDPDGYEPEGHAGTSSPGDHSGFLSNSSRAAPEPRGTGLLRDAENRISTVPEADEDVLDERGEFLSPQLPLQENGEPRRERAGSAPVSTPPREAVASGALSNSNETTPKASDKARKHKSSSSSFFPKISRWSRTTASSMGDNIRNSMQPGKKERVSFDASRSGSDLAHGPYKAPDYYDPQGDDRLRSNYTLDEGSPQQENRPPSPLVPSQISEAPKYRAHRDSLDMQHPQPRQGPTGRYQSQLESQAQIYGASGNHSDQWGSNPSFSAINGNRRLSGASRLSPISDAGYSETSMRSSRQGPPRPPKIKDDGPLFPERPAKIKEGEERSYADRVVSRSSAMQSPGRSTPPARKPTGPRPLNSNSQYNSPNRRRRNYRDSPEHVDEEHDY
Protein: Putative transport protein YidE (P60872)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01016}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01016}.
Interaction partners:
- Putative electron transfer flavoprotein subunit YgcQ
Sequence:
MSDIALTVSILALVAVVGLFIGNVKFRGIGLGIGGVLFGGIIVGHFVSQAGMTLSSDMLHVIQEFGLILFVYTIGIQVGPGFFASLRVSGLRLNLFAVLIVIIGGLVTAILHKLFDIPLPVVLGIFSGAVTNTPALGAGQQILRDLGTPMEMVDQMGMSYAMAYPFGICGILFTMWMLRVIFRVNVETEAQQHESSRTNGGALIKTINIRVENPNLHDLAIKDVPILNGDKIICSRLKREETLKVPSPDTIIQLGDLLHLVGQPADLHNAQLVIGQEVDTSLSTKGTDLRVERVVVTNENVLGKRIRDLHFKERYDVVISRLNRAGVELVASGDISLQFGDILNLVGRPSAIDAVANVLGNAQQKLQQVQMLPVFIGIGLGVLLGSIPVFVPGFPAALKLGLAGGPLIMALILGRIGSIGKLYWFMPPSANLALRELGIVLFLSVVGLKSGGDFVNTLVNGEGLSWIGYGALITAVPLITVGILARMLAKMNYLTMCGMLAGSMTDPPALAFANNLHPTSGAAALSYATVYPLVMFLRIITPQLLAVLFWSIG
Protein: Chemerin-like receptor 1 (Chemokine-like receptor 1) (Formyl peptide receptor 1) (E7FF45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMDPFNFTESPPNHNSSEYDDDYVDYQNSELGKSLNIMSLIVYSLAFVLGVVGNGIVIWVTGFKMKRTVNTVWFLNLAVADFLFTAFLPLSVAYTAMGFHWPFGQFMCKFNSTLGFLNMFASVYILVVISVDRCVSVVRPIWAQNHRNVGRASAVSFGVWLFALLLSSPYFVFKDTAQDNRDPKIINCFNNFAFSDADTQEVEDLRMLRHRAMIITRFIIGFVVPFVIIVSCYAVIIHRLQRNRSMSGKTGRPFRIIAAVITAFFLCWAPYHILVLIEMVNHMSTEYSPTLQHVITVGIPIVTSLAFLNSCLNPLLYVFMGQDFKDKVRKSILKVLETAFTEEVSRTNTWTNSMTTIRNKENGSKSFSDAEV
Protein: Putative NAC domain-containing protein 94 (ANAC094) (Q9FIW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Metacaspase-5
- Remorin family protein
- D111/G-patch domain-containing protein
- AAA-ATPase ASD, mitochondrial
- Aspartic proteinase 39
- Remorin family protein
- bZIP transcription factor 28
- bZIP transcription factor 60
- Receptor-like protein 11
- Protein LIFEGUARD 3
Sequence:
MVLVMDDEESNNVERYDDVVLPGFRFHPTDEELVSFYLKRKVLHKSLPFDLIKKVDIYKYDPWDLPKLAAMGEKEWYFYCPRDRKYRNSTRPNRVTGGGFWKATGTDRPIYSLDSTRCIGLKKSLVFYRGRAAKGVKTDWMMHEFRLPSLSDSHHSSYPNYNNKKQHLNNNNNSKELPSNDAWAICRIFKKTNAVSSQRSIPQSWVYPTIPDNNQQSHNNTATLLASSDVLSHISTRQNFIPSPVNEPASFTESAASYFASQMLGVTYNTARNNGTGDALFLRNNGTGDALVLSNNENNYFNNLTGGLTHEVPNVRSMVMEETTGSEMSATSYSTNN
Protein: Rod shape-determining protein MreD (Q01467)
Organism: Bacillus subtilis (strain 168)
Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Peptidoglycan glycosyltransferase RodA
- Cell shape-determining protein MreB
- Cell shape-determining protein MreC
- Septum site-determining protein MinC
- Cell shape-determining protein Mbl
- Probable peptidoglycan glycosyltransferase FtsW
- Septum site-determining protein MinD
- Penicillin-binding protein H
- Cell shape-determining protein MreBH
- UDP-N-acetylglucosamine--N-acetylmuramyl-
Sequence:
MKRFLLPFVMMLVFSAESIFTDLVHFPFVTDDQVLAPRFLMLVLIFMSAFINQKHAMIYGFIFGFLYDMNYTSLLGVYMFGFAGLCYLASKAFKVLHTNAFVVILIAVLAVCLLEFYVFGIQSLIHKDIMTFNGFVLDRFIPTILLNIAAALILVLPFRLFFMSLKKELRDE
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 (Complex I-B9) (CI-B9) (NADH-ubiquinone oxidoreductase B9 subunit) (Q9CQ91)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase flavoprotein 3, mitochondrial
Sequence:
MAGRISAFLKNAWAKEPVLVVSFSVWGLAIIMPMISPYTKYASMINKATPYNYPVPVRDDGNMPDVPSHPQDPLGPSLDWLKNL
Protein: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (EC 5.2.1.8) (Parvulin-14) (Par14) (hPar14) (Parvulin-17) (Par17) (hPar17) (Peptidyl-prolyl cis-trans isomerase Pin4) (PPIase Pin4) (Peptidyl-prolyl cis/trans isomerase EPVH) (hEPVH) (Rotamase Pin4) (Q9Y237)
Organism: Homo sapiens (Human)
Function: Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.
Subcellular location: [Isoform 1]: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion. Mitochondrion matrix. Note=Imported in a time- and membrane potential-dependent manner to the mitochondrial matrix, but without concomitant processing of the protein. Directed to mitochondria by a novel N-terminal domain that functions as a non-cleavable mitochondrial targeting peptide.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP1A
- WD repeat-containing protein 48
- Bifunctional glutamate/proline--tRNA ligase
Sequence:
MPPKGKSGSGKAGKGGAASGSDSADKKAQGPKGGGNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK