wanglab/gogpt-training-data huggingface dataset:
Protein: FI14001p1 (GH01416p) (RE59472p) (SNF4/AMP-activated protein kinase gamma subunit, isoform A) (SNF4/AMP-activated protein kinase gamma subunit, isoform B) (Q7JQX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSSAGGASGGSNYEDVAAARRGRFRVTSSTPQGPPETTLGRFRLMPTSNYGAISPILQRGRFAVIPEEPQAGSPALGTPPPGGRTARSPSPEWDFDIEQEQDGSLGGAGRMPGSRPSSAPAEPNAKAAKKAYKKMEKEQRRQEKEQSRREKEARKLERETARRNEREAAKLEKINRHSEKISRSTERMAMAGVGSRSGSLERRRSGEDSPVLNQSTVHGIASPNRRPTIFDVFRPRAKSDAKRQKEKHLLDPSSADSSATSSTYSVSGGTGPATSSAAGGAGGAAAAAGQGAAGGAGGLMNSMKVAMQNFSHRQHPAVTITSADGTQSTAKSKYKDGSAHPHQGSDAQYYHTVTAVRPNSSQRSPMTKVMDLFRHRSSSVVSEADKRKARAAAHQQQLAVQSAHMRRASADLEKRRASVGAAGRGLRGDGTLDPHHAAILFRDSRGLPVADPFLEKVNLSDLEEDDSQIFVKFFRFHKCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDTWRSVLHNQVMPLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGVGGSESSLRASDPVLLRKVAEVEIPATAAAATTTTPPRSPSAGSGNRSLIEDIPEEETAPARSDDADSDNNKSASEDKANNNQHDQTTTAATANGDSNNSPVEVSFADEAQEEEAADQVERSNCDDDDQPALAEIERKNASMDDDEDDGMSSAVSAASALGQSLTPAAQEMALVSE
Protein: rRNA N(6)-adenosine-methyltransferase metl-5 (EC 2.1.1.-) (Methyltransferase-like protein 5) (Q18511)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of a heterodimer with TRMT112/C04H5.1, which specifically methylates the 6th position of adenine in position 1717 of 18S rRNA.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- CTCHY-type domain-containing protein
- Cytochrome P450
- Protein aurora borealis
- Probable dimethyladenosine transferase-N
- Venom protein
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Brix domain-containing protein F44G4.1
- U6 small nuclear RNA
Sequence:
MPDKKTLWMLNELEGFEKPKIKLEQYATSSELAVSMMEMIDETIGFEGKKLIDIGCGCGMLMTTAATMYELETVLGVDIDDEALKICSRNLETAEVQDRCELLQADILDPESDLPRGTFDVAVINPPFGTKNNAGIDMQFVQIGLQMVRPGGSVFSLHKSSTRDYILKNAKKWDGVGAECCAEMRWQLPATYKFHKQKAVDIAVDLIHFKKLDS
Protein: Free fatty acid receptor 3 (G-protein coupled receptor 41) (B2GV46)
Organism: Rattus norvegicus (Rat)
Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Olfactory receptor 51E2
- Free fatty acid receptor 4
- Peptide YY
- G protein-coupled receptor 84
- Olfactory receptor
- Pro-glucagon
Sequence:
MDTSFFPGNHWLFFSVDLLVFLVGLPLNVMALVVFVNKLRRRPVAVDLLLLNLTISDLLLLLFLPFRIVEAACGMKWILPFIFCPLSGFLFFTTIYLTSLFLMTVSIERFLSVAYPLWYKTRPRLAQAGLVSGICWFLASAHCSVIYVTEYWGNATYSQGTNGTCYLEFREDQLAILLPVRLEMAVVLFMVPLCITSYCYSRLVWILSQGASRRRRKRVMGLLVATLLIFFVCFGPYNMSHVVGYVRGESPTWRSYVLLLSTLNSCIDPLVFYFSSSKFQADFHQLLSRLIRACVPWTQEVSLELKVKNGEEPSKECPS
Protein: Growth factor receptor-bound protein 7 (B47) (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein) (Q14451)
Organism: Homo sapiens (Human)
Function: Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:18853468}. Cell junction, focal adhesion {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278}. Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:18853468}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q03160}. Cell projection {ECO:0000269|PubMed:18853468}. Note=Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions. {ECO:0000250|UniProtKB:Q03160}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-2
- Epidermal growth factor receptor
- Receptor tyrosine-protein kinase erbB-3
- SHC-transforming protein 1
- Rho-related GTP-binding protein Rho6
- Mast/stem cell growth factor receptor Kit
- Lymphocyte antigen 6 complex locus protein G6f
- StAR-related lipid transfer protein 3
- Focal adhesion kinase 1
- Platelet-derived growth factor receptor beta
Sequence:
MELDLSPPHLSSSPEDLCPAPGTPPGTPRPPDTPLPEEVKRSQPLLIPTTGRKLREEERRATSLPSIPNPFPELCSPPSQSPILGGPSSARGLLPRDASRPHVVKVYSEDGACRSVEVAAGATARHVCEMLVQRAHALSDETWGLVECHPHLALERGLEDHESVVEVQAAWPVGGDSRFVFRKNFAKYELFKSSPHSLFPEKMVSSCLDAHTGISHEDLIQNFLNAGSFPEIQGFLQLRGSGRKLWKRFFCFLRRSGLYYSTKGTSKDPRHLQYVADVNESNVYVVTQGRKLYGMPTDFGFCVKPNKLRNGHKGLRIFCSEDEQSRTCWLAAFRLFKYGVQLYKNYQQAQSRHLHPSCLGSPPLRSASDNTLVAMDFSGHAGRVIENPREALSVALEEAQAWRKKTNHRLSLPMPASGTSLSAAIHRTQLWFHGRISREESQRLIGQQGLVDGLFLVRESQRNPQGFVLSLCHLQKVKHYLILPSEEEGRLYFSMDDGQTRFTDLLQLVEFHQLNRGILPCLLRHCCTRVAL
Protein: 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC 1.1.1.141) (EC 1.1.1.232) (Eicosanoid/docosanoid dehydrogenase [NAD(+)]) (Prostaglandin dehydrogenase 1) (D6RA66)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYG
Protein: Pyruvate carboxylase (EC 6.4.1.1) (A0A0R4IFJ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Malate dehydrogenase
- Citrate synthase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- L-lactate dehydrogenase B-A chain
- Pyruvate dehydrogenase E1 component subunit alpha
- L-lactate dehydrogenase A chain
- glutamate dehydrogenase [NAD
- Malic enzyme.
- Malic enzyme
- Malic enzyme
Sequence:
MLLQVGGRHSALGLLAMRRMWSLTRCAHTAPQTLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGKGLPPVAAYLHIPDIIKVAKANDVDAIHPGYGFLSERADFAQACVDAGVRFIGPTPDVVRKMGDKVQARAIAISAGVPVVPGTDAPISCLQEAQEFSNSYGFPIIFKAAYGGGGRGMRVVREYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVEIAPATQLDPHLRDRLTADSVNLARQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRSLPELGLKQDKIRINGYAIQCRVTTEDPARGFQPDTGRLEVFRSGEGMGIRLDSASAFQGAVISPHYDSLLVKVIASGKDLPAASAKMSRALAEFRVRGVKTNIPFLQNVLSNNQFLNGTVDTQFIDENSDLFNLKPVQNRAQKLLHYLGHVMVNGPTTPIPVKAKPSPIDPVIPPVPLGEPPVGFRDVLLREGPDGFAKAVRAHQGLLLMDTTFRDAHQSLLATRVRTHDLKRIAPFVAHSFNNLFSVENWGGATFDVAMRFLCECPWKRLQELRALMPNVPFQMLLRGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYLPNMLLGMEAAGTAGGVVEAAISYTGDVSDPTRQKYSLDYYLKLADELVKAGTHILCIKDMAGLLKPDSGRLLVGALRDRFPHVPIHVHTHDTAGAGVAAMLACAEAGADIVDVAVDSMAGMTSQPSMGAVVACTKGTKLNTGISLEKVFDYSEYWEVTRGLYAPFDCTATMKSGNADVYENEIPGGQYTNLHFQAHSMGLGNKFKEVKKSYTEANKLLGDLIKVTPSSKIVGDLAQFMVQNSLTRAEVEERADELSFPLSVVEFLQGHIGIPHGGFPEPFRTKVLKSLPRVEGRPGASLPAMDFQALEKQLKDAHGDEITPEDVMSAAMYPKVFQEFKDFTRTFGPVDCLDTRLFLDGPKIAEEFEVELERGKTLHIKALALGDLNKAGQREVFFELNGQLRSVLVKDTVAMKEMHFHPKALKDVRGQIGAPMPGKVVEVKVKQGQQVEKGQPLCVLSAMKMETVVNSPISGTVAKIYVTADSTLEGDDLILEITE
Protein: Cardiac-enriched FHL2-interacting protein (M0RD54)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:28717008}.
Interaction partners:
- Mitochondrial disaggregase
- Obscurin-like protein 1
Sequence:
MQGNKKCADGFSDTSSIGSVLDEADREVSNLTDRAFRSLCISEDTSFHDSDLALSPEITSQVSGTFHQETVSHANRKSGIWSQLPSQGTEHSGWAATFQQQPKYVQGEEKYPKNSPLPTPVQRRLEVPISGLRSSSKPISKVSSLIRSFDRTEAQPCDSRPPPSKPPALKNTPKFAHPPESGVNFCFDSAFLTVRRVPAGVSSTHQSSHQPCRAPGEPEPPTNPEIACHSSDSLLRAPDRVAGSCEPRFPSPSLKPPKAETGRGKEWISRGTFLHSENSAFESWDAHQPKLRERKDITETTPESKAPKHYEDMPLLKEPYPAESKLSPCQGRANCAQEENRSPSGIQSTSGAWGARDSGSQVFPVEGNASQIDPQVKRNQAPWRKPKTGKGGTDGPHDASEDKKQPNRKGLPLYSKLNPQGQLPENGVLDLPEESSDHYSSPFNISKLLTPIISTKHVLETSDTQPVETSPSPPGQLNGYQEKESSEAQSRDSYKSKAPSLLFNLKDVRKRVKSTYSPLPLLKGFDEKTRGKLDGKQEPLSNGVTLPNGLEENPPTAELVKETLDDAPSVLHSSTQKDPAMDSRESFADSHPTFSSPSASSKTHFSINGEAAERNSHEKEEANGESEQGLSEGGWHPDSRENLPRKHLSLKLCNRDSETGQATEKMKPRQLEKRLSRSISQETEPEREMGFQNLPVSQKFSPGPLSPEEEDVFYSDSQSDFTPCVQTKAKFSTSSSDQSFASFEDQQKMWFTEGPREDGKSHVSLGDNQKDEKETEVEKEEPQQCALHNGVEEHRQKETQRKAQGVLGGRPRKASAEEVSVRGSWTGADKDTALSHAKDPTPLPASTNKHRLFPIKDNTLRATPVIKPIILPLLRTVSSEDSLSGGHKENELPRQPWGEDAGGLGASESQEMRNTPLSNSTPSTEQKCVVYEGVEEDPVHTAAQDETSQQTRKGSFSFLPLVEEGGKTKPPPDTADERLAHEKSRSADSGKLEAPQHIPTIALHSDDLEDSPPSLPQHTCWEEQGFKSHFLSAPRAGPSGRRPVPSEAATSPNPSSLGGSSTCSPAASSIWEDASQAAGEHWQRQEPPGPGPWASPGPSGPTGLTRREDMTRGLTWEAEGSDPHLERLADFRTLSPRGIFLTGAAEKPEPSSLLEKAAGKPPAVPPKTEKALRRAKKLASKRRKSDQMSEKHTEAWEGKSFTEDAQGTEQRPVSPGKGPRPRFPEVRSLPPPTHRHSVSCGWEPAGRRPWGSQSLIPLPPYPATQKVLQDPQSGQYFVFDMPLQVKIKTFYDPETGKYVKVSVPSSEEDPSEPPLQDALTAPYLLYPGFQPVPVTSLMPLRCSSQLAAPTFLRQGSSHRPQSSQGARLQPPPERLGESAQHVSSAQRPRGPPLSPEEEGAEAPSLSIISTDDLEDFATEGVS
Protein: Keratin 76 (Type II keratin Kb9) (Q6IFZ5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSRQACKKSFSCGSQGFSGRSAVVSGSSRSSCVARSGAASGGACGFRGGAGTFGSHSLYNLGGSKSISISVAGGFSGGRSSCGSGFGSGYGGSFGSSRGMGGGFGGASGFGGAGGFGRPGGFGPGGCPGGIQEVTINQSLLQPLNVEIDPQIGQVKAQEREQIKILNNKFASFIDKVRFLEQQNKVLETKWELLQQQTTRSGSGPLNLESFFESYISCLRKQLDSLLGAKGSLQGELKSMQDLVEDFKRKYEEEINRRTTAENEFVALKKDVDGAYMSKVELQAKVDSLTDEINFLRTLYDMELSQMQSHISDTSVVLSMDNNRCLDLDSIIAEVKAQYEDIAQRSKAEAEALYQTKLGELQTTAGRHGDDLRSTKSEIMELNRTIQRLRAEIENVKKQNTNLQASIAEAEQRGERALKDADAKFQDLQAALQKAKEDLARLLREYQELMNVKLALDVEIATYRKLLEGEECRLSGEFQNAVSISVVSNVTSTSSSGGYRGAGGSNYGGDSSGRSSSSIGSRGSSGSRLGSGGSISVSQQRTSFNSGGSQTSVGSCYKSGRGGTSSVHFSQTTSSSQQRSK
Protein: Phosphoenolpyruvate carboxykinase (ATP) (PCK) (PEP carboxykinase) (PEPCK) (EC 4.1.1.49) (P22259)
Organism: Escherichia coli (strain K12)
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphoenolpyruvate synthase
- Phosphoenolpyruvate carboxylase
- Pyruvate kinase I
- Pyruvate kinase II
- Citrate synthase
- Malate dehydrogenase
- Enolase
- Malate synthase A
- Acetyl-coenzyme A synthetase
- NADP-dependent malic enzyme
Sequence:
MRVNNGLTPQELEAYGISDVHDIVYNPSYDLLYQEELDPSLTGYERGVLTNLGAVAVDTGIFTGRSPKDKYIVRDDTTRDTFWWADKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFVVDAFCGANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGFKPDFIVMNGAKCTNPQWKEQGLNSENFVAFNLTERMQLIGGTWYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEKGDVAVFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGCYAKTIKLSKEAEPEIYNAIRRDALLENVTVREDGTIDFDDGSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFLTADAFGVLPPVSRLTADQTQYHFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTQYAEVLVKRMQAAGAQAYLVNTGWNGTGKRISIKDTRAIIDAILNGSLDNAETFTLPMFNLAIPTELPGVDTKILDPRNTYASPEQWQEKAETLAKLFIDNFDKYTDTPAGAALVAAGPKL
Protein: Kexin (EC 3.4.21.61) (Protease KEX2) (Proteinase YSCF) (P13134)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Processing of precursors of alpha-factors and killer toxin.
Subcellular location: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein.
Interaction partners:
- Dipeptidyl aminopeptidase A
- Aspartic proteinase 3
- Intermediate cleaving peptidase 55
- Pheromone-processing carboxypeptidase KEX1
- Vacuolar protein sorting/targeting protein VPS10
- Alcohol-sensitive RING finger protein 1
- Uncharacterized RING finger protein YBR062C
- Carboxypeptidase Y
- Aspartic proteinase MKC7
- Mating factor alpha-1
Sequence:
MKVRKYITLCFWWAFSTSALVSSQQIPLKDHTSRQYFAVESNETLSRLEEMHPNWKYEHDVRGLPNHYVFSKELLKLGKRSSLEELQGDNNDHILSVHDLFPRNDLFKRLPVPAPPMDSSLLPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVVAAIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGEIAAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYSCSWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGDNCNYDGYTNSIYSITIGAIDHKDLHPPYSEGCSAVMAVTYSSGSGEYIHSSDINGRCSNSHGGTSAAAPLAAGVYTLLLEANPNLTWRDVQYLSILSAVGLEKNADGDWRDSAMGKKYSHRYGFGKIDAHKLIEMSKTWENVNAQTWFYLPTLYVSQSTNSTEETLESVITISEKSLQDANFKRIEHVTVTVDIDTEIRGTTTVDLISPAGIISNLGVVRPRDVSSEGFKDWTFMSVAHWGENGVGDWKIKVKTTENGHRIDFHSWRLKLFGESIDSSKTETFVFGNDKEEVEPAATESTVSQYSASSTSISISATSTSSISIGVETSAIPQTTTASTDPDSDPNTPKKLSSPRQAMHYFLTIFLIGATFLVLYFMFFMKSRRRIRRSRAETYEFDIIDTDSEYDSTLDNGTSGITEPEEVEDFDFDLSDEDHLASLSSSENGDAEHTIDSVLTNENPFSDPIKQKFPNDANAESASNKLQELQPDVPPSSGRS
Protein: Spinophilin, isoform T (X2JC06)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEKPMHHAPAPVGKVSQIANIFQRKPIEIQPVEQLSAVAAAHAAAAAAAAAAHHAHVQGAPAVRTESHSARFNNARALFEKLGVESNSNVSSRLLRSGSREDNLCDGSDRSSSRSSDRSQSPPKRRTPFPSGVSLVHNNNNAAIVAQNGVPPEQRLSNSKFIVEPAAQVVPTSVVKYPQHNISRLKSEEPSPVPPPASGSVSALFASSGGDKPEKPERKFNSRELIEKQKKWTSHFTKTKTTRTHSDLNRCDIIRTVPGTGLIMDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSSILENKIRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLVKQVVPQSLSPPGTVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Oligoendopeptidase F homolog (EC 3.4.24.-) (O51264)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- Inner membrane protein BB_0250
- dITP/XTP pyrophosphatase
- Phosphatidylcholine synthase
Sequence:
MINRNEINENDKWDLSFLFANEEEYVKTINAIEIKTKEFKKYEKLELNFDLFKETLNKYYEIMEDLEKVSYYAMLQLETDVTNKDSNKIYSICVNLATKVSNTTSYFMPKILKTDEKKIQAWINDPELKDKKIAIEKILREKKHILSEQEEKILANYTPLYTSYQSIFSALTNADMEFGEINKHPLTNSTYTLFLQNEDQKIRKEAFLRFYQKYKNNENTLANLIISDFKKNHFIAKTRRFQNTFSMQLFSNNIDKKVYTNLIETVNENLPVLNDYYEFRKKVLNQEYLYHYDVYVPLTKGIIFKNSFEDACEKILKSLEVLGNEYTKILRNGLLKERWVDKYENTGKRSGAFSAGSYNGKPYILLNYKDESIRDMFTLAHEAGHSMHSYFSIKNNPFPHYNYSIFEAEIASIINEQILAEYLLKNETDTNKIKYIKLTQIDDMISTFFRQTMFAEFEYIIHEMISKEEPVVKETLTETYMNLLKKYFGPSLKFDELSPLECLRIPHFYSPFYVYQYATGIAAALSIYKGIKENKKDAVENYIKFLKTGGSKYPLDSLNITGVDLTKKATIENTINIFKCRLEEIKKIFQ
Protein: SUMO-activating enzyme subunit 1A (SUMO-activating enzyme subunit 1-1) (Ubiquitin-like 1-activating enzyme E1A) (Q8VY78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2. Functionally redundant with its paralog SAE1B.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SUMO-activating enzyme subunit 2
- SUMO-conjugating enzyme SCE1
- Small ubiquitin-related modifier 5
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 3
- SUMO-activating enzyme subunit 1B-1
- E3 SUMO-protein ligase MMS21
- E4 SUMO-protein ligase PIAL1
- E4 SUMO-protein ligase PIAL2
Sequence:
MDGEELTEQETALYDRQIRVWGANAQRRLTKAHILVSGIKGTVAEFCKNIVLAGVGSVTLMDDRLANMEALNANFLIPPDENVYSGKTVAEICSDSLKDFNPMVRVSVEKGDLSMLGTDFFEQFDVVVIGYGSRATKKYVNEKCRKLKKRVAFYTVDCRDSCGEIFVDLQDYKYTKKKLEEMVECELNFPSFQEAISVPWKPIPRRTAKLYFAMRVIEVFEESEGRKHGECSLLDLARVLEIKKQLCEANSVSESHIPDILLERLITGTTEFPPVCAIVGGILAQEVIKAVSGKGDPLKNFFYYDGEDGKGVMEDISDSFTS
Protein: dTDP-4-dehydrorhamnose 3-epimerase (EC 5.1.3.-) (Novobiocin biosynthesis protein W) (dTDP-6-deoxy-D-xylo-4-hexulose 3-epimerase) (Q9L9E5)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: dTDP-6-deoxy-D-xylo-4-hexulose 3-epimerase that acts together with NovU to catalyze the formation of dTDP-4-keto-6-deoxy-5-C-methyl-L-lyxo-hexose from dTDP-4-keto-6-deoxy-D-glucose in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Interaction partners:
Sequence:
MRLRPLGIEGVWEITPEQRADPRGVFLDWYHVDRFAEAIGRPLRLAQANLSVSVRGVVRGIHFVDVPPGQAKYVTCVRGAVFDVVVDLRVGSPTYGCWEGTRLDDVSRRAVYLSEGIGHGFCAISDEATLCYLSSGTYDPATEHGVHPLDPELAIDWPTGTPLLSPRDQDALLLAEARDAGLLPTYATCQAVTVPSPAPGSVGDPGP
Protein: Keratin, type II cytoskeletal 5 (Cytokeratin-5) (CK-5) (Keratin-5) (K5) (Type-II keratin Kb5) (Q6P6Q2)
Organism: Rattus norvegicus (Rat)
Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q922U2}.
Interaction partners:
- Keratin, type I cytoskeletal 14
- Tumor protein 63
- Type I hair keratin KA29
- Galectin-7
- Uteroglobin
- Collagen alpha-1
- Aquaporin-5
- Keratin, type I cytoskeletal 15
Sequence:
MSRQSSVSFRSGGSRSFSAASAITPSVSRTTFSSVSRSGGGGGRVSLGGAYGAGGYGSRSLYNVGGSKRISFSSGGGSFRNQFGAGAGGGYGFGGGAGSGFGFGGGAGSGFGFGGGAGFGGGYGGAGFPVCPPGGIQEVTVNQNLLTPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTIKQNLDPLFEQYINNLRRQLDGVMGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTNSLSSGYGGRSNIGYGSGLGSGIGGFASDIGPLLNRRGLGSGLSVGGSGFSASSGQGGGFSSGGGSSSSVKFVSTTSSSRRSFKS
Protein: Calsequestrin-2 (Calsequestrin, cardiac muscle isoform) (P31235)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000250|UniProtKB:O09161}.
Interaction partners:
- Triadin
- Ryanodine receptor 2
- Ryanodine receptor 3
- Aspartyl beta-hydroxylase/Triadin domain-containing protein
- Calsequestrin-1
- Inward rectifier potassium channel 2
- Calmodulin
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Calmodulin 2
- Calmodulin like 5
Sequence:
MKRAHLFVVGVYLLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQILKKYDLLCLYYHAPVSADKVAQKQFQLKEIVLELVAQVLEHKEIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIINSKLEVQAFERIEDHIKLIGFFKSADSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPTPIPNKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVPFAEKSDPDGYEFLEILKQVARDNTDNPDLSIVWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEDEDDDDDNDDDDDDNGNSDEEDNDDSDEDDE
Protein: T-box transcription factor T (Brachyury protein) (xBRA) (Protein T) (P24781)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence. Causes dorsal mesodermal differentiation of animal cap ectoderm when co-expressed with wnt8 and noggin. None of these molecules causes dorsal mesoderm formation when expressed alone. Establishes the left/right axis at early gastrula stage by directly up-regulating mesodermal expression of zic3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15178}.
Interaction partners:
Sequence:
MSATESCAKNVQYRVDHLLSAVENELQAGSEKGDPTEKELKVSLEERDLWTRFKELTNEMIVTKNGRRMFPVLKVSMSGLDPNAMYTVLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKDPVSFSKVKLTNKMNGGGQIMLNSLHKYEPRIHIVRVGGTQRMITSHSFPETQFIAVTAYQNEEITALKIKHNPFAKAFLDAKERNDYKDILDEGIDSQHSNFSQLGTWLIPNGGSLCSPNPHTQFGAPLSLSSPHGCERYSSLRNHRSAPYPSPYTHRNNSPNNLADNSSACLSMLQSHDNWSTLQMPAHTGMLPMSHSTGTPPPSSQYPSLWSVSNSAITPVSQSGGITNGISSQYLLGSTPHYSSLSHAVPSPSTGSPLYEHGAQTEIAENQYDVTAHSRLSSTWTPVAPPSV