wanglab/gogpt-training-data huggingface dataset:
Protein: Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (SCOT) (EC 2.8.3.5) (3-oxoacid CoA-transferase 1) (Somatic-type succinyl-CoA:3-oxoacid CoA-transferase) (SCOT-s) (Succinyl-CoA:3-oxoacid CoA transferase) (P55809)
Organism: Homo sapiens (Human)
Function: Key enzyme for ketone body catabolism. Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl-CoA thiolase into two acetyl-CoA molecules which enter the citric acid cycle for energy production. Forms a dimeric enzyme where both of the subunits are able to form enzyme-CoA thiolester intermediates, but only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl-CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:B2GV06}.
Interaction partners:
- Acetyl-CoA acetyltransferase, mitochondrial
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Dehydrogenase/reductase SDR family member 6
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetoacetyl-CoA synthetase
Sequence:
MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN
Protein: Proteasome subunit alpha type-6 (20S proteasome alpha subunit A) (20S proteasome subunit alpha-1) (Q9LSU3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-2
- Proteasome subunit beta type-3
- Proteasome subunit beta
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-7-B
- Proteasome subunit alpha type-7-A
Sequence:
MSRGTGAGYDRHITIFSPEGRLYQVEYAFKAVKSAGVTSIGVRGKDSVCVVTQKKVPDKLLDHTSVTHLFPITKYIGLLATGLTADARSLVYQARNEAAEFRFKWGYEMPVDVLAKWIADKAQVYTQHAYMRPLGVVAMVLGYDEEKNAQLFKCDPAGHFFGHKATSAGLKEQEAINFLEKKMKDDPQFSYEETVQIAISALQSVLQEDFKATEIEVGVVRKDDRVFRALTTEEIDQHLTAISERD
Protein: RNA-binding protein Musashi homolog 1 (Musashi-1) (G5EFS2)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11122376}. Perikaryon {ECO:0000269|PubMed:11122376}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 14
- Importin N-terminal domain-containing protein
- Actin-related protein 2/3 complex subunit
- Suppressor of forked domain-containing protein
- Numb-related protein 1
Sequence:
MTTTVSTGATAVATLRETSPPVDGHEEARLNADSDDGSHGSQDPGKMFIGGLSWQTTAENLRDYFGRFGEVNECMVMRDPATKRARGFGFITFVDPSSVDKVLNNREHELDGKKIDPKVAFPKRTQAKLVTKTKKVFIGGLSATSTLEDMKQYFETYGKVEDAMLMFDKATQRHRGFGFVTFDSDEVADKVCEIHFHEINGKMVECKKAQPKEVMLPVQLNKSRAAAARNLYGMPPETLLAYAQYLPRFGGNLMYPNFTNVFNNMPGGYSGLSTPGGSSNRPPHQFDTASLYSLNNGGQLLDSQAQMFMNQQSYHSHSKY
Protein: Phosphatidate phosphatase LPIN3 (EC 3.1.3.4) (Lipin-3) (Q99PI4)
Organism: Mus musculus (Mouse)
Function: Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis therefore regulates fatty acid metabolism.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Diacylglycerol O-acyltransferase 1
- Phosphatidate phosphatase LPIN1
- Diacylglycerol O-acyltransferase 2
- Phosphatidate phosphatase LPIN2
- Phosphatidate cytidylyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
Sequence:
MNYVGQLAETVFGTVKELYRGLNPATLSGGIDVLVVRQRDGSFRCSPFHVRFGKLGVLRSREKVVDIEINGEPVDLHMKLGDSGEAFFVQELDSDEEDVPPRLCTSPIPWGGLSGFPSDSQIGTASEPEGLVITGRRKRRRRRKPRRREEDAVDSSSEELEAGAESELTLLEKPTPESPSAQEAEEPSSQPKDIHPYSDGECTPQANLSSGDLMSPKSDSELELRSLEPSPLRAESHMQWVWGRLPKVAKAERPEFSLILESMAEAICALPEEPSPSSSPSEAGVDTLSPPVLHPGVRADTFHPAVEAHCEETAVDSPLAAPESKETKTQNSRGAGHPPATKSWSWTTPESHTPSGHPQVSRGKGSLKRNQHLGPSDIYLDDLPSLDSENVALYFPKSEYGMGARRWSEPSNQKLLESPNPEHIAECTLDSVDKIELSLCGGLADNRDISLEKFTQHMVSYEDLTKNPGLLDDPNLVVKINEKHYNWAVAAPMILSLQAFQKNLPESTVDKLEKEKMPRKGGRWWFSWRRRDFPAEEHSSQREKAATRKQQGEKTEVLSSDDDVPDSPVILEVPPLPSSTPGYVPTYKKSLRLSSDQIRCLNLNEGANDVVFSVTTQYQGTCRCKATIYLWNWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIHLNGYKFLYCSARAIGMADLTKGYLQWVSEHGCGLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPQRQPFHAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKSHKSTYQRLGEVVELLFPPVVRGPSTDLASPEYSNLSYWRKPLPYVDFEALA
Protein: BCL2-antagonist/killer 1 (F7EQF3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MASGQGPGPPKGDCDEALSASEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLSLEPNSVLGQVGRQLALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYRLALYVYQRGLTGFLGQVTCFLADIILHHYIARWIAQRGGWVTLSLRRDPILSVVVIFGVVLLGQFVVHRFFRS
Protein: Proto-oncogene Wnt-3 (Proto-oncogene Int-4) (P17553)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis. Required for normal formation of the apical ectodermal ridge and for normal embryonic limb development.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56703}. Secreted {ECO:0000250|UniProtKB:P56703}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-8
- Wnt inhibitory factor 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Cerberus
- Low-density lipoprotein receptor-related protein 6
- Frizzled-7
- Frizzled-1
- Glypican-3
Sequence:
MEPHLLGLLLGLLLSGTRVLAGYPIWWSLALGQQYTSLASQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYALFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCVFHWCCYVSCQECIRIYDVHTCK
Protein: ATP-dependent 6-phosphofructokinase, platelet type (ATP-PFK) (PFK-P) (EC 2.7.1.11) (6-phosphofructokinase type C) (Phosphofructo-1-kinase isozyme C) (PFK-C) (Phosphohexokinase) (Q01813)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Hexokinase-1
- ATP-dependent 6-phosphofructokinase, muscle type
- ATP-dependent 6-phosphofructokinase, liver type
- Fructose-bisphosphate aldolase A
- Transaldolase
- Fructose-bisphosphate aldolase B
- Fructose-1,6-bisphosphatase 1
- Fructose-bisphosphate aldolase C
- Fructose-1,6-bisphosphatase isozyme 2
Sequence:
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQPWSV
Protein: ABC transporter, putative (Q387E3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ABC transporter, putative
- Peroxin 19
- DNA repair protein RAD51 homolog
- Peroxisomal membrane protein PEX14
Sequence:
MTTHWVRDYGAIVTSAATFFLCASYQRVLLRHGDALIPSEKKEKGGATSSFFREFMQVARIALPTVWCKEALGTFVFVLLFFVLAVIRALTSEANGRVLKSMTEGTGGTRLRNFTHTLLLRTALHLLSSVCSSCVEHLRTWLIGCYRVRLSKHFQERYYSQLVFYRAAVIDKRLEAVDSVVTTYCAEFAEHFTELPYYFVLPALGSATSMVALIRRVGAGASAAACGLVLASVLLMKKFSPPFGKIYASLLSKEDAYRRMLSNSLSNVENIALHRGGEHTRKKLDTQLGVLKGYLDHFALSRGHFNLLELSFATTLRNIASIIVFGDALRKENKSTSDIYVELLYLRDLSKSVTDVVSNFREISHLSTYTLKLAEFDRTLKDIEGDTCDTFPCVASIPDVGTVVPTVVSPSVPIAGALSFPLFTFTNVKLKTPTGHVLFENLNLTIQNDQDWVITGNNGSGKTSLLRLISGLWRACEGDITMSSCVKLLFAPQESYVVPHCTLVEQILYPKIITSLNEGDIACIKEAISLAGAESVVEVLGGFESPAVGCDLSNVDETYDWSSLSGGQKQRVNMARVFYQVLQADRSREIPVVLLDEATSMMDDTEEKVMLNLRKLNARMISVTHREQVVKHHTHVLRALPGGRWMTTKVTQYVGSDDVVTQGISSVGGSSNAEGVGVDLHRGF
Protein: Small ribosomal subunit protein eS24z (40S ribosomal protein S24-1) (Q9SS17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein uS10z/uS10x
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS25w
- Small ribosomal subunit protein uS15y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS1z
Sequence:
MAEKAVTIRTRKFMTNRLLSRKQFVIDVLHPGRANVSKAELKEKLARMYEVKDPNAIFVFKFRTHFGGGKSSGFGLIYDTVESAKKFEPKYRLIRNGLDTKIEKSRKQIKERKNRAKKIRGVKKTKAGDAKKK
Protein: Glycoprotein 130 (Q95US4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Beta-lactamase-type transpeptidase fold containing protein
- NLP/P60 domain-containing protein
- Glucosamine-6-phosphate isomerase
- Uncharacterized protein
- Signal peptidase complex subunit 3
Sequence:
MKKNYLFLLIIFFTFILKCNSQTKPLPSDQMEMAKDLYYQIYQKNTTDPCLDNNMFTCKLINDGVNTGIYTITQLGLKKNNDTLSIITNANFSVFKNATYILIGDGIILDSSLFNTLPNFYNKASIYIYNESIPIPNDIIIPINLNQVTFTFINVPIPSNIFSGSIEVFNILGIGYGFSLPSLLPENVALKRFSTFLGYYSPFPSNAGSALKSLTSLRLSFNNDITEIGYKNYSFPTFQPFNKLQTLYITFINFGDDSNSQLWNFEQSITNLTTLNDFHITGKGFILNPSFKYTDFSNLPETFFIYFSNGCDLISNCISKPCLKLPKKSGISVIGCDFNIKNIDFTNVTYMKMQNNDFEQELPTNEGGDSSNINYSTTRLDFQDNVLIGSIPEGYCQFYKSKYPTLSYNELTGEIPTCFSCMGANYTITKNLLPNQFTDFNEKSLPTNCETFNFSLDYNKIVKTDGSTIITIKGKDFGWDFSLPSGNNDNVTLLITIPNNEITLSIPKGEGSNKTFIANFGYQFKFSQTFTYSYEIPVITSYSFGNDSKFYLNGNGFSFINNNSITLNGVSYKFTIATADEQPSGNGYSSSISFIDDGGEINNPIDSMLIGDEFNVSINVGNQVSNIVTFYLYKSISISSLSNNKLNISGSSSLVTVTFDGEFGTTNSKIVFVSINGIQCIVKSVTPQSLTISSYPSVPSVGKYQISINVGGLIFTDQIEYIKTPTTTNTTSSEENGHDGSFGSLSSQPISLLSLIILSIISLITLPK
Protein: Cytochrome c-type protein TorY (P52005)
Organism: Escherichia coli (strain K12)
Function: Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorZ. Required for electron transfer to the TorZ terminal enzyme.
Subcellular location: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Trimethylamine-N-oxide reductase 2
- Trimethylamine-N-oxide reductase 1
- Chaperone protein TorD
- Periplasmic nitrate reductase, electron transfer subunit
- Cytochrome c-type protein TorC
- Biotin sulfoxide reductase
- Ferredoxin-type protein NapF
- Periplasmic nitrate reductase
- Ferredoxin-type protein NapH
- Ferredoxin-type protein NapG
Sequence:
MRGKKRIGLLFLLIAVVVGGGGLLLAQKVLHKTSDTAFCLSCHSMSKPFEEYQGTVHFSNQKGIRAECADCHIPKSGMDYLFAKLKASKDIYHEFVSGKIDSDDKFEAHRQEMAETVWKELKATDSATCRSCHSFDAMDIASQSESAQKMHNKAQKDSETCIDCHKGIAHFPPEIKMDDNAAHELESQAATSVTNGAHIYPFKTSHIGELATVNPGTDLTVVDASGKQPIVLLQGYQMQGSENTLYLAAGQRLALATLSEEGIKALTVNGEWQADEYGNQWRQASLQGALTDPALADRKPLWQYAEKLDDTYCAGCHAPIAADHYTVNAWPSIAKGMGARTSMSENELDILTRYFQYNAKDITEKQ
Protein: Spatacsin isoform 2 (Spatacsin variant 2) (D4HMK9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLEALSRSDAGAQAVLEVDLLADGELCVGLKDWRRVKLSAGPSLLCCVNAQGETSLRNISDSRRAEHTLQHTCVDFLWEDVSVSSGARVKPKLLLLDSEFSLHMYDVDQDDQPTLVCETSSNTLLQIIKHTHADMCAVASVRLLCFSEGRCMLLVNTCVLLQLRLTEDTLEPISCCRLGVECVEECVDCRLCRGALFILLNSGLSYVFDSTDGQLLAKVDFPSYCCNAGVSPSTSSFCLLQISADLSTAVSVTRQNQAYAVHLDHYFSVYTDHLYCRAAPIRPFLRPVESWDQDSLSSSTHSLSALNKPLQADRSWESRLSALYNQTKAPVRPVHISPWYKDFPHIECRRAAATAKLCHSSVKTGGAVMSFNVPDGATPAGLNVSEFSALITFVSPANANTVLAYWGLENESVTYHRADANAIPVQRSAEENLCLLLKTSGLSVVLFCVSQDELLNRLMVFGSAGTVDSLCHLNAWGRCSIPIHALQAGLKNHQLDTVDFFLKSKENILSSSSGFSPGDPPPSSSNTHTHLRSIEALCPALDLLRSAIRDTHTEAQSQQFCEQLLSITMSFLNTQTRVLLSGAHDLDDNLQQCVCVLDGFISDLRVFLKRFPWGVGGDARTHTDAHTHTAASGREEEHQWISLSDEEVVHRAVLSRRISHAQAFLRRRGSAEHTLQDIRRTGLKHTHTCLTLRDLQQATTLLTHMGFNVKEQLHNICVYTADRDLRAFMVEELQKQHHLSADELKQVNFIHTIESLCSKPANRSSRRLDANRVLQVSRCDPQSRRLLEKLLQDSDSSSTSLLDPLRLHWVKHWDRDAQTHILLSRTHTHTQCSGDAAVLWAYLTSLHDSVRCSAWLSSSSVCDRESSAAPCWPQLTAHVLDTCTRCGEHLHNIILDQLARQGQFVPAEMQDSIGSVPLSDLSCIVELLILAHDCFSVTCNLEGIVRVLQACRHLSHTHLAHGDAHGLLVRLLTGIGRYNDMTYVFDLLHQNHRFEMLLRKKVESNVRLKTALLDYIKRCLPGDSEKHNMVALCFSMCREIGENHEAAARTQLKLIESQPWVITAELKKALVKVQTLLKDAAESYSKDSCVRQAVRCVKLAKLVTLQLHFLNQGLELRIINLQHTDLQNTSNTLPHCYQVFVLAEAYDFSPDWAEVLYQKVIMRGDFSYLEEFKRHRPLAASLFQDISNKVCHQKPPASCSQHLKKLLSHCEDVYTHYKLAYEHQFLDVANMLLQDSKTNSFLKDRLRT
Protein: Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Type I protein arginine N-methyltransferase) (Type I PRMT) (Q9URX7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in target proteins (By similarity). Asymmetrically dimethylates the polyadenylate-binding protein pab2, modulating pab2 oligomerization.
Subcellular location: Nucleus {ECO:0000269|PubMed:15175657}.
Interaction partners:
- Protein arginine N-methyltransferase 2
- Histone H4
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL30C
- Protein gar2
- H/ACA ribonucleoprotein complex subunit gar1
- Pre-mRNA-splicing factor srp2
- Histone H2A-beta
- Histone H2A-alpha
- Ribosomal lysine N-methyltransferase 4
Sequence:
MPGNTKKSADSGLTAKDYYFDSYSHWGIHEEMLKDDVRTLSYRDAIMQNPHLFRDKIVLDVGCGTGILSMFCARAGAKHVYGVDMSEIIHKAVQIVEVNKLSDRITLIQGKMEEIQLPVEKVDIIVSEWMGYFLLYESMLDTVLVARDRYLAPDGLLFPDRAQIQLAAIEDADYKSEKIGFWDDVYGFDFSPIKKDVWKEPLVDTVDRIAVNTNSCVILDLDLKTVKKEDLAFSSPFEITATRNDFVHAFLAWFDIEFSACHKPIKFSTGPFSRYTHWKQTVFYTHKDLTVKAGEYIRGTITCKPAEGNHRELDIDISYTFNPREPNREPVSEDLSYRMC
Protein: Cytochrome c oxidase subunit 7e (EC 7.1.1.9) (Cytochrome c oxidase polypeptide VIIe) (P20609)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Subcellular location: Mitochondrion inner membrane.
Interaction partners:
- Cytochrome c oxidase polypeptide 6, mitochondrial
- NADH-ubiquinone oxidoreductase 23 kDa subunit
- Cytochrome c oxidase subunit 4, mitochondrial
- Glutathione reductase
Sequence:
MSHALPALIKMHITKDIGYGLLLGIIPGVWFKYQIGQSIQKREDFYAAYDKRN
Protein: Fluoride-specific ion channel FluC (Fluoride exporter) (P37002)
Organism: Escherichia coli (strain K12)
Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00454, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16429150}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00454, ECO:0000269|PubMed:16429150}. Note=Could be a dual-topology protein, which inserts into the membrane in two opposite orientations (PubMed:16429150). May form an antiparallel homodimer in the inner membrane (PubMed:16429150). {ECO:0000269|PubMed:16429150}.
Interaction partners:
- Ribosomal large subunit pseudouridine synthase C synthase)
- H
- Beta-galactosidase
- Maltose/maltodextrin-binding periplasmic protein
Sequence:
MLQLLLAVFIGGGTGSVARWLLSMRFNPLHQAIPLGTLTANLIGAFIIGIGFAWFSRMTNIDPVWKVLITTGFCGGLTTFSTFSAEVVFLLQEGRFGWALLNVFVNLLGSFAMTALAFWLFSASTAH
Protein: Tubulin alpha chain (C9J2C0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MLWGCRAKACWGPRLSDLVASLSPQRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFDAQASKINDDDSFTTFFSETGNGKHVPRAVMIDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEE
Protein: Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2) (Membrane-associated guanylate kinase-interacting protein) (Maguin) (Q9Z1T4)
Organism: Rattus norvegicus (Rat)
Function: May function as an adapter protein or regulator of Ras signaling pathways, in synaptic junctions.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat-containing protein 7
Sequence:
MALIMEPVSKWSPSQVVDWMKGLDDCLQQYIKNFEREKISGDQLLRITHQELEDLGVSRIGHQELILEAVDLLCALNYGLETENLKTLSHKLNASAKNLQNFITGRRRSGHYDGRTSRKLPNDFLTSVVDLIGAAKSLLAWLDRSPFAAVTDYSVTRNNVIQLCLELTTIVQQDCTVYETENKILHVCKTLSGVCDHIISLSSDPLVSQSAHLEVIQLANIKPSEGLGMYIKSTYDGLHVITGTTENSPADRCKKIHAGDEVIQVNHQTVVGWQLKNLVNALREDPSGVILTLKKRPQSMLTSAPALLKNMRWKPLALQPLIPRSPTSSVATPSSTISTPTKRDSSALQDLYIPPPPAEPYIPRDEKGNLPCEDLRGHMVGKPVHKGSESPNSFLDQEYRKRFNIVEEDTVLYCYEYEKGRSSSQGRRESTPTYGKLRPISMPVEYNWVGDYEDPNKMKRDSRRENSLLRYMSNEKIAQEEYMFQRNSKKDTGKKSKKKGDKSTSPTHYSLLPSLQMDALRQDIMGTPVPETTLYHTFQQSSLQHKSKKKNKGAIAGKSKRRISCKDLGRGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTAGYAERERIKQEQDYWSESDKEEADTPSTPKQDSPPPPYDTYPRPPSMSCASPYVEAKHSRLSSTETSQSQSSHEEFRQEVTGSSAVSPIRKTASQRRSWQDLIETPLTSSGLHYLQTLPLEDSVFSDSAAISPEHRRQSTLPTQKCHLQDHYGPYPLAESERMQVLNGNGGKPRSFTLPRDSGFNHCCLNAPVSACDPQDDIQPPEVEEEEEEEEEEAAGENIGEKNENREEKLGDSLQDLYRALEEASLSPLGEHRISTKIEYKLSFIKRCNDPVMNEKLHRLRILKSTLKAREGEVAIIDKVLDNPDLTSKEFQQWKQMYLDLFLDICQNTTSNDPLSISSEVDVITSSLTHTHSYIETHV
Protein: Meiosis initiator protein (A0A5K7RLP0)
Organism: Mus musculus (Mouse)
Function: Gatekeeper of meiotic initiation in both male and female germ cells. In complex with STRA8, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis. Temporal expression of MEIOSIN is required for meiotic entry decision.
Subcellular location: Nucleus {ECO:0000269|PubMed:32032549}.
Interaction partners:
Sequence:
MLGSDKFSCFSDQHRARSPSPTDRKDKKNHTNKLRELALLIPVTMKTRDKKYTKKEILLRVLHYIQYLQRNIDMTKALLKLHSSNGKGRFVGPGLNPSAGQTQQQHSTPSSSQKPSLWSTSSKPRKKKFTRVSEHPSWPYNPRRSLALDQAENPNTIHPGLKEENEECATYPGVLSPSTYPTTEPSVSEGDGQGAQLVFLDMAQNIFAYDILSDHAVEVQGGEPNADIKVQRSFFLTRAQPCVSSCRQKLFLCTSSEADKEAPDSDPWLPVWTSEDSPNGSPLALGSSQINTWHVADYLNEILGVSSSLFSSPSKILPDHVLEDGTYFLTEGLLESSPATCEVESPQEKEVSSEGPTGPPNFQSSVSLDHCYLSLSENVKVLSNCGSSSESTDTESLWGQEEVRGVATYPRRTGVFSLAQPSVLQQANPEGLQTSSDEDRDYTWTPTGQSSGLPVASKKIKKVQASQGPVKPKDSRKACPGQVKKKCVNGFIMFCRMNRKQYIRACPGTASTAATKDLAQLWRGMTLEEKKPYCTKARRFSRQNNRIVKQENSSSEDDDGETPKPFYQLLAEKAQVSLGLTSLPTPNCQ
Protein: CPN10-like protein (Heat shock protein 1 (chaperonin 10), related sequence 1) (Q9JI95)
Organism: Mus musculus (Mouse)
Interaction partners:
- 60 kDa heat shock protein, mitochondrial
- GrpE protein homolog 1, mitochondrial
- GrpE protein homolog 2, mitochondrial
- Mitochondrial disaggregase
- Stress-70 protein, mitochondrial
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- T-complex protein 1 subunit alpha
Sequence:
MAGQAFRKFLLLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVN
Protein: At4g01410 (Late embryogenesis abundant (LEA) hydroxyproline-rich glycoprotein family) (Putative hypoersensitive response protein) (Q9M132)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- AT4G01090 protein
- Protein ENHANCED DISEASE RESISTANCE 4
- MATH domain and coiled-coil domain-containing protein At3g58220
- Protein PAL OF QUIRKY
- Protein kinase superfamily protein
- PRA1 family protein F1
- F19P19.6 protein
- PRA1 family protein B1
- Late embryogenesis abundant
- Clathrin heavy chain 2
Sequence:
MGEGEAKAEHAAKADHKNAPSASSTPESYSKEGGGGGGDARRAICGAIFTILVILGIIALILWLVYRPHKPRLTVVGAAIYDLNFTAPPLISTSVQFSVLARNPNRRVSIHYDKLSMYVTYKDQIITPPLPLPPLRLGHKSTVVIAPVMGGNGIPVSPEVANGLKNDEAYGVVLMRVVIFGRLRWKAGAIKTGRYGFYARCDVWLRFNPSSNGQVPLLAPSTCKVDV
Protein: Nuclear transcription factor Y subunit A-1 (AtNF-YA-1) (Protein EMBRYO DEFECTIVE 2220) (Transcriptional activator HAP2A) (Q9LXV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit B-1
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit B-8
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit B-6
- Nuclear transcription factor Y subunit B-7
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-9
Sequence:
MQSKPGRENEEEVNNHHAVQQPMMYAEPWWKNNSFGVVPQARPSGIPSNSSSLDCPNGSESNDVHSASEDGALNGENDGTWKDSQAATSSRSVDNHGMEGNDPALSIRNMHDQPLVQPPELVGHYIACVPNPYQDPYYGGLMGAYGHQQLGFRPYLGMPRERTALPLDMAQEPVYVNAKQYEGILRRRKARAKAELERKVIRDRKPYLHESRHKHAMRRARASGGRFAKKSEVEAGEDAGGRDRERGSATNSSGSEQVETDSNETLNSSGAP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q57W24)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein LTV1 homolog
- Glycogen synthase kinase 3
Sequence:
MGGDGRISRNTLIGGKYHVVKQIGSGSFGDVFQGTNIQTGEHIVVKLEPARGQQRLRSEVWMYHHLRRAGGDHLVGIPNILHYGVQGDFNVMVMDLLGPSLEDLFSFCGRRLSLKTTLMLAEQMIARIEFVHSNNIIHRDIKPDNFLMGTGKKGHHVYIIDFGLAKKYRDARTHQHIPYKEGKSLTGTARYCSINTHIGIEQSRRDDLEGIGYILMYFLRGSLPWQGLKAPTKRERYMRLAKLKMSTPLETLCRGFPAEFAAYLNYTRSLHFEDKPDYSYLKRLFRELFVREGYHMDYVFDWTLKRIHDTLHPSSDAALEDGDEESDDTE