wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotic recombination protein DMC1 (P25453)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for meiotic recombination, synaptonemal complex formation and cell cycle progression. Recruited to meiosis recombination hotspots by MEI5 and SAE3.
Subcellular location: Nucleus {ECO:0000269|PubMed:15620352}.
Interaction partners:
- Meiosis-specific protein SPO11
- Homologous-pairing protein 2
- DNA repair and recombination protein RAD54
- Synaptonemal complex protein ZIP1
- DNA repair protein RAD51
- Meiotic nuclear division protein 1
- Meiosis-specific protein HOP1
- DNA repair and recombination protein RDH54
- Pachytene checkpoint protein 2
- Pachytene arrest protein SAE3
Sequence:
MSVTGTEIDSDTAKNILSVDELQNYGINASDLQKLKSGGIYTVNTVLSTTRRHLCKIKGLSEVKVEKIKEAAGKIIQVGFIPATVQLDIRQRVYSLSTGSKQLDSILGGGIMTMSITEVFGEFRCGKTQMSHTLCVTTQLPREMGGGEGKVAYIDTEGTFRPERIKQIAEGYELDPESCLANVSYARALNSEHQMELVEQLGEELSSGDYRLIVVDSIMANFRVDYCGRGELSERQQKLNQHLFKLNRLAEEFNVAVFLTNQVQSDPGASALFASADGRKPIGGHVLAHASATRILLRKGRGDERVAKLQDSPDMPEKECVYVIGEKGITDSSD
Protein: Protein YAE1 homolog (Yae1 domain-containing protein 1) (Q9NRH1)
Organism: Homo sapiens (Human)
Function: The complex LTO1:YAE1 functions as a target specific adapter that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47118}. Nucleus {ECO:0000250|UniProtKB:P47118}.
Interaction partners:
- Protein LTO1 homolog
- ATP-binding cassette sub-family E member 1
- Formiminotransferase N-terminal subdomain-containing protein
Sequence:
MSWVQAASLIQGPGDKGDVFDEEADESLLAQREWQSNMQRRVKEGYRDGIDAGKAVTLQQGFNQGYKKGAEVILNYGRLRGTLSALLSWCHLHNNNSTLINKINNLLDAVGQCEEYVLKHLKSITPPSHVVDLLDSIEDMDLCHVVPAEKKIDEAKDERLCENNAEFNKNCSKSHSGIDCSYVECCRTQEHAHSENPSPTWILEQTASLVKQLGLSVDVLQHLKQL
Protein: Serine/threonine-protein kinase toxin HipA (Ser/Thr-protein kinase HipA) (EC 2.7.11.1) (Toxin HipA) (P23874)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system, first identified by mutations that increase production of persister cells, a fraction of cells that are phenotypic variants not killed by antibiotics, which lead to multidrug tolerance. Persistence may be ultimately due to global remodeling of the persister cell's ribosomes. Phosphorylates Glu-tRNA-ligase (AC P04805, gltX, on 'Ser-239') in vivo. Phosphorylation of GltX prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. Once the level of HipA exceeds a threshold cells become dormant, and the length of dormancy is determined by how much HipA levels exceed the threshold. The hipA7 mutation (a double G22S D291A mutation) leads to increased generation of persister cells (cells that survive antibiotic treatment) probably by entering into a dormant state, as well as cold-sensitivity. Wild-type cells produce persisters at a frequency of 10(-6) to 10(-5) whereas hipA7 cells produce about 100-fold more persisters. hipA7 decreases the affinity for antitoxin HipB, leading to increased HipA levels and persistence; depending on the protein level, can be toxic enough to reduce cell growth or even kill cells. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. Also neutralized by overexpression of gltX. With HipB acts as a corepressor for transcription of the hipBA promoter; binding of HipA-HipB to DNA induces a 70 degree bend. This brings together and dimerizes 2 HipA molecules, which distorts the promoter region, preventing sigma-factor binding; additionally HipA and HipB would physically prevent RNA core polymerase from contacting the -35 promoter box. May play a role in biofilm formation.
Interaction partners:
- Antitoxin HipB
- Endoribonuclease toxin MazF
- mRNA interferase toxin YafQ
- mRNA interferase toxin RelE
- mRNA interferase toxin MqsR
- Toxin YoeB
- Antitoxin DinJ
- Antitoxin MqsA
- Probable mRNA interferase toxin HicA
- Glutamate--tRNA ligase
Sequence:
MPKLVTWMNNQRVGELTKLANGAHTFKYAPEWLASRYARPLSLSLPLQRGNITSDAVFNFFDNLLPDSPIVRDRIVKRYHAKSRQPFDLLSEIGRDSVGAVTLIPEDETVTHPIMAWEKLTEARLEEVLTAYKADIPLGMIREENDFRISVAGAQEKTALLRIGNDWCIPKGITPTTHIIKLPIGEIRQPNATLDLSQSVDNEYYCLLLAKELGLNVPDAEIIKAGNVRALAVERFDRRWNAERTVLLRLPQEDMCQTFGLPSSVKYESDGGPGIARIMAFLMGSSEALKDRYDFMKFQVFQWLIGATDGHAKNFSVFIQAGGSYRLTPFYDIISAFPVLGGTGIHISDLKLAMGLNASKGKKTAIDKIYPRHFLATAKVLRFPEVQMHEILSDFARMIPAALDNVKTSLPTDFPENVVTAVESNVLRLHGRLSREYGSK
Protein: 2-methylisocitrate lyase (2-MIC) (MICL) (EC 4.1.3.30) ((2R,3S)-2-methylisocitrate lyase) (Q8EJW1)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Interaction partners:
- 2-methylcitrate synthase
- 2-methyl-aconitate isomerase
- Aconitate hydratase B
- Methycitrate-responsive transcriptional regulator of methylisocitrate utilization PrpR
- 2-methylcitrate dehydratase
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Malate synthase domain protein
- Acetyl-coenzyme A synthetase
- malate synthase
Sequence:
MTQSAGLRFRQALANSKPLQIVGTTNAYFALMAEQTGFQALYLSGAGVANASYGLPDLGMTSMNDVLIDAGRITSATQLPLLVDIDTGWGGAFNIARTIKEFEKIGVAAVHMEDQVSQKRCGHRPNKAVVSTEEMVDRIKAAVDARTDPNFVIMARTDAVAVEGLEAGIERAKAYIAAGADMIFAEALTELDQYRHFKAQVKAPILANMTEFGQTQLFNKEELAQAGADMVLYPLGTFRAANQAALKVMQALMNDGHQRNVLDTMQTRADLYKYLGYHAFEDKLDQLFSQDK
Protein: Uncharacterized protein C1494.09c (O60083)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- RNA polymerase II transcription factor B subunit 3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Transcription initiation factor IIE subunit alpha
- Serine/threonine-protein kinase crk1
- Transcription initiation factor IIF subunit alpha
- CTD kinase subunit alpha
- Cyclin mcs2
- General transcription and DNA repair factor IIH subunit tfb4
- General transcription and DNA repair factor IIH subunit tfb2
- General transcription and DNA repair factor IIH helicase subunit XPD
Sequence:
MALELTEHQLNKLRDFLDEILLDVSQKYQKKFHPGGYQKLEELAFDLEPYFQVVSSIPLEKHTFLVTNFTLRGIDFFVDTIVGFPASPETTFKVFSLLDSLCLRLIQSGNLSTTDTIRLKSLMENCRMVVISKLSDVQGYEMDCASIFEKSLNSIDF
Protein: Basic helix-loop-helix (BHLH) DNA-binding superfamily protein (F4IQH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLEGLVSQESLSLNSMDMSVLERLKWVQQQQQQLQQVVSHSSNNSPELLQILQFHGSNNDELLESSFSQFQMLGSGFGPNYNMGFGPPHESISRTSSCHMEPVDTMEVLLKTGEETRAVALKNKRKPEVKTREEQKTEKKIKVEAETESSMKGKSNMGNTEASSDTSKETSKGASENQKLDYIHVRARRGQATDRHSLAERARREKISKKMKYLQDIVPGCNKVTGKAGMLDEIINYVQCLQRQVEFLSMKLAVLNPELELAVEDVSVKQFQAYFTNVVASKQSIMVDVPLFPLDQQGSLDLSAINPNQTTSIEAPSGSWETQSQSLYNTSSLENSCGNYNKISKILLSTKCTHQYVPIRRVWV
Protein: Aggregation suppressing protein (Heat-shock protein) (Hsp20 family protein) (D1MC98)
Organism: Salmonella typhimurium
Interaction partners:
Sequence:
MMALRTLSALPVFADSLFSDRFNRIDRLFSQLTGDTPVAATPAYDLQKRDANNYLLTVSVPGWKEEELEIETVGGNLNITGKHTEETVEDQTHWIYRGIRKADFQLSFSLPEHAKVNNAKLEQGLLLVEIYQEIPESEKPKKIAIESKPKAIEHKS
Protein: Mitogen-activated protein kinase kinase 8 (AtMKK8) (MAP kinase kinase 8) (EC 2.7.12.2) (Q9M8J5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVMVRDNQFLNLKLSPIQAPTTIPPCRFPIIPATKVSATVSSCASNTFSVANLDRISVLGSGNGGTVFKVKDKTTSEIYALKKVKENWDSTSLREIEILRMVNSPYVAKCHDIFQNPSGEVSILMDYMDLGSLESLRGVTEKQLALMSRQVLEGKNYLHEHKIVHRDIKPANLLRSSKEEVKIADFGVSKIVVRSLNKCNSFVGTFAYMSPERLDSEADGVTEEDKSNVYAGDIWSFGLTMLEILVGYYPMLPDQAAIVCAVCFGEPPKAPEECSDDLKSFMDCCLRKKASERWTASQLLNHPFLLHQD
Protein: N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC 2.7.8.17) (GlcNAc-1-phosphotransferase subunits alpha/beta) (Stealth protein gnptab) (UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta) [Cleaved into: N-acetylglucosamine-1-phosphotransferase subunit alpha; N-acetylglucosamine-1-phosphotransferase subunit beta] (Q5RGJ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.
Subcellular location: [N-acetylglucosamine-1-phosphotransferase subunit alpha]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q3T906}.; SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit beta]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3T906}.
Interaction partners:
- N-acetylglucosamine-1-phosphate transferase subunit gamma.
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Cathepsin K
- Beta-hexosaminidase.
Sequence:
MLVVNSLLKLLQRQTYTCLSHRYGLYLCFGGLVLMIVSAFQFGEVVVEWSRDQYHVLFDSYRDNVAGKSFQTRLCLPMPIDVVYTWVNGTDINLLKDLRAVRQRLEEEQKALRERLGKNGSEITEAPKGRPECLLSHCIMGPVLVLDPALPANITVKELPTLSAAFSSAKELLQVAKPLHPSSSVTALLFHSHTEAEKAHADALKDLLTHSISRGYLTTDKEAPGLVRMHTLAYLSGFPASLKETEQLRVKLPAVVTSKTKKLQLYSEASIALLHLNTAQDFTDLTQQAKKNLTLDGKELTVSSAFLFWDLTAISQSKQDEDVSASRFEDNEELRYSLRSIEKHAPWVRHIFIVTNGQIPSWLNLDNPRVSVVTHQDIFQNQTHLPTFSSPAIETHIHRIPGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCQGSSRFGGAGGSVIGGGQPWQFAGGLGGLAGMSFCNQGCANSWLADKFCDQACNVLACGFDVGDCGQDNLNQLHRIVLRRNQTLYTLPQGELRPYFSFSGLANRVSEAHVADNQVLRHTSVANKWKTIHLLLLPGHNATQIHYNITFQSTDHHDFIMTFSVSVDTRELPKSNTSTPVRDKEEEPKPTVATPEPEVPFEAVPKEKQGPKVREQTHGDVQVPVLNETLLPDEVKIELKKLNEKLMSGDITIKGFNLTKAMLLEPYKEKDQFTLKHEKDKEEKQKLSPVAQLQNERAAARVKREKGENVDQLKPVAPSLVPVQIDDVTTKAQSRLFNIEKPHMFHLLSNLKGNLSKERDSDSEGHLRERPTGRRLQFYSDSLNRGFLPWEKRKFFQDLMEEVNRLQTELQYTADRTATGRRLQDTFADSLRYVNRLLNAQFGFTSRKVPAHMPHMIDRLIMQELQDTFPQEFDKTSSHRVRHSEDMQFAFSYFYFLMSAVQQLNISEVFDEIDTDHSGVLSDREIRTLATRIHELPLSLQDLTSLEQMLINCSKSLPSNLTHLHAVSPTQEAYYDPSMPPVTKGLVIHCKPITERIHKAFKDQNKYKFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFICLNDNIDHIHKDAGTVKAVLRDFYESMFPLPSQFELPREYRNRFLHMTELQEWRIYRDKLKFWTHCVLVTLVVFTVMSFFAEQLVMLKRWLFPRRRVSKDANPERV
Protein: Esculentin-1 (P32414)
Organism: Pelophylax lessonae (Pool frog) (Rana lessonae)
Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
Subcellular location: Secreted.
Interaction partners:
Sequence:
GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC
Protein: Blimp-1, isoform B (Blimp-1, isoform C) (M9PBR0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GATAe, isoform A
Sequence:
MHGHHNHNHLPQQQPQNPQEQQSGAIMKAANQPHHPAHSHPLNHPHPHQHAQPHPHPHPHPHHKLSARRARSRSRSRSPTPDGNQDYDVTRMREEDFERLAVYLVPDVQAERGLPNRADKTLPRSLTLKSSMVYSTPNVKTEGVWSSGVIPRGTRFGPFEGIPTSNYPNDKNKARYFWRVQGTRHITYGNIKIFKDDDYYYLDGSDRSQSNWMRYVASAYSLSVMNLVACQHQENIYFYTTRDILPNEELMVWYCKDFASRLGYDVDPETTIFGACKQAVEAEEEADEEEEEAEGEDGKPRYSMPAPEIPPDVAVSHITYVMGLHLPVGAGNGPANGSVAGSVSGATPPPPTATPCCRRSSPPAHVSTTTSTCNAHHPHIQHGRHASVIIGQDRSPMASSDKDTAGSPLSGLDHQMTPQDGSVRSVRSDEGYHSNECHEDGLTPPEDSSDSESEHNYVLDCSKKAIAPKETVIAQAQKPSSSPPAVVMANTTTNSMISHSSPTATPICETDKNEYRKFKVKMPLKYEFKNKTCVKQEPSLKEVDQEMSLPQEEEEDQVMHPEPDSICPSTTTHLGDEHMLMMERERERERERIQEREPSNQQPASSTVIVLEHNSGGQARTIVPLSKPYYEPDPPGERYMRFGQPSSSILETILTSQHRLEAAAAAANACRQANAATPPPTSPTEMAYSYKKSQRYGNAVSPDSSSNLGQNPEQLSSSAVVVGEQEMTRATMIKGECSPPPPSHHHHNVIFSPSRHAAYLGAGEAGGHSPSPGYPGYPHYGAAATSTFHSPPHSSHSPFDRQSNASSGAGSATNLHLLQTSTQMLNHPLMQPLTPLQRLSPLRISPPSSLSPDGNSCPRSGSPLSPNSLASRGYRSLPYPLKKKDGKMHYECNVCCKTFGQLSNLKVHLRTHSGERPFKCNVCTKSFTQLAHLQKHHLVHTGEKPHQCDICKKRFSSTSNLKTHLRLHSGQKPYACDLCPQKFTQFVHLKLHKRLHTNDRPYVCQGCDKKYISASGLRTHWKTTSCKPNNLEEELAMAAAATSECLDKDHPEPDSREAYEQLTQHMHPAVHPGLRHLSSGGQSPPRLIPLGNHMAPQQQSHQQQQQQHQQQGVPPPHLLMTQHSVGPAPMLLTTASQLPPPPPHHQQNSPSRLLQHGHAHPLQMQQQQQQQQQHSPKGLKSLPESGVYLHGQHVQAQESRPSVIESSNQPMIIECT
Protein: Zinc finger transcription factor Trps1 (Q925H1)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Binds specifically to GATA sequences and represses expression of GATA-regulated genes at selected sites and stages in vertebrate development. Regulates chondrocyte proliferation and differentiation. Executes multiple functions in proliferating chondrocytes, expanding the region of distal chondrocytes, activating proliferation in columnar cells and supporting the differentiation of columnar into hypertrophic chondrocytes.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MVRKKHPPLRNVASEGEGQTLEPTATESKVSGKNKELSADQMSENTDQSDVAELNSKEEHSTHGQEPSSSGKKDLQISGLSEKAGFNYESPSKGGSLVSFPHDEVTDRNMLAFSSPAAGGVCEPLKSPQRAEADDPQDMACTPSGDSLETKEEHKMSPKATEETGPVQSGQANCQGLSPVSVASKNPQVPSDGGVRLSKPKGDLLVNDNPDPAPLSPELQDFKCNICGYGYYGNDPTDLIKHFRKYHLGLHNRTRQDAELDSKILALHNMVQFSHSKDFQKVNRSVLSGVLQDISSSRPALLNGTYDVQVTSGGTFIGIGRKTPDCQGNTKYFRCKFCNFTYMGNSSTELEQHFLQTHPNKIKVSLPSSEGVKPSEKNSNKSIPALRASDSGDVGKWQDKMTVKAGDDTPVGYSVPIKPLDSSRQNGTEATSYYWCKFCSFSCESSSSLKLLEHYGKQHGAVQSGGLNPELNDKLPRGSVINQNDLAKSVEGEPLTKPEKGLSGAKKKDFPSKGAEDNMVTSYNCQFCDFRYSKSHGPDVIVVGPLLRHYQQLHNIHKCTIKHCPFCPRGLCSPEKHLGEITYPFACRKSNCSHCALLLLHLSPGVAGSSRVKHQCHQCSFSTPDVDVLLFHYETVHESQASDVKQEANHLLGSDGQQAVRDSKEHSCTKCDFITQVEEEISRHYRRAHSCYKCRQCSFTAADTQSLLEHFNTVHCQEQEITTANGEEGGHAIPTIKEEPKIDLKVYSLLNPDSKMGETVPESIVKREKLDDKEGLKDKIWTESSTDDLRGVAWRGADILRGSPSYTQASLGLLTPVSSSQEQTKTLRDSPNVEAAHLARPMYGLAVDTKGFLQGAPAGSEKSASLTQQYPASGESKTKDESQSLLRRRRGSGVFCANCLTTKTSLWRKNANGGYVCNACGLYQKLHSTPRPLNIIKQNNGEQIIRRRTRKRLNPEALQAEQLNKQQRGSGEEQVNGSPLERRSEDHLSESHPREIPLPSLSKYEAQGSLTKSHSAQQPVLVSQALDIHKRMQPLHIQIKSPQESTGDPGNSSSVSDGKGSSERGSPIEKYMRPAKHPNYSPPGSPIEKYQYPLFGVPFVHNDFQSEADWLRFWSKYKLSVPGNPHYLSHVPGLPNPCQNYVPYPTFNLPPHFSAVGSDNDIPLDLAIKHSRPGPTANGASKEKTKAPPTVKNEDPLNVVKTEKVDRSTQDELSTKCVHCGIVFLDEVMYALHMSCHGDSGPFQCSICQHLCTDKYDFTTHIQRGLHRNNAQAEKNGKPKE
Protein: Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Q9Z1P3)
Organism: Rattus norvegicus (Rat)
Function: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis.
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic, associated with mitochondria.
Interaction partners:
Sequence:
MFGLRRNAVIGLNLYCGGASLGAGGGSPAGTRLAAEEAKARREGGGEAALLPGARVVARPPPVGAEDPDVTASAERRLLKSPGLLAVPPEEMAASAAAIMSPEEELDGCEPEVLSKRPAVLPLLERVSEAAKSSGADGSLPSTPPPPEEEDDELYRQSLEIISRYLREQATGSKDAKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSFSRVMTHVFKDGVTNWGRIVTLISFGAFVAKHLKSINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGGIRNVLLAFAGVAGVGAGLAYLIR
Protein: Forkhead box O3A (Forkhead box protein O3a) (Q5I0F7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- protein acetyllysine N-acetyltransferase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Non-specific serine/threonine protein kinase.
- V-akt murine thymoma viral oncogene homolog 2,-like.
- non-specific serine/threonine protein kinase
- Serine/threonine kinase 11
- cyclin-dependent kinase
- Signal transducer and activator of transcription
- Mitogen-activated protein kinase
Sequence:
MAEELDKPLAVDVDIDPDFEPQKRPRSCTWPLPRPESNSGKAEPSDVGIIPEEEVDENGTDDACASGDITGASKPASVTEGDPSSAAALPAIETNASANDKDIYGSPGSSQHALAACSDSSINGLIPQQPRKSSARRNAWGNYSYADLITQAIESSPEKRLTLAQIYDWMVRNVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFVRVQNEGTGKSSWWMVNPDGGKGGKAPRRRAVSMDNSNKLIKSARGRAAKKKAALQASQDGSSESSSSLSKWTGSPTSRSSDELDAWTDFRSRTNSNASTLSGRLSPILANLEVDEVPDDDSPLSPMLYSSPSSMSPSTGLTELPRLADLAGTMNLNDGLSDNLMDDLLDNISLTASQSPGHDESGANLQGSPVFTFSCSGSSLAIPSGSYGTNSLFSPPSVTGLRQSPMQTIQENKQATFSCGSLFSEQSLQDLLSSESSSRSDVLLTQSDPLMSQASASVSSQNARRILLRNDPMMSNQAGPAGQAGLKKASPSGWRMNCVPSSESDYQSLMKQLQQSPFRSTSMQLNSSDSLLAGLNGSVTSAQSVSQDRFSSDLDLEAFSGSFDCDMDIITRNDLMDAEGLELSFDSHLISSQNANLTSGSFSRTKRTSSQSWVPG
Protein: Eukaryotic translation initiation factor 4 gamma 1 (C9J2Z7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPQAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEK
Protein: ZNF483 protein (Zinc finger protein 483) (Q6P088)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MQAVVPLNKMTAISPEPQTLASTEQNEVPRVVTSGEQEAILRGNAADAESFRQRFRWFCYSEVAGPRKALSQLWELCNQWLRPDIHTKEQILELLVFEQFLTILPGEIRIWVKSQHPESSEEVVTLIEDLTQMLEEKDPVSQDSTVSQEENSKEDKMVTVCPNTESCESITLKDVAVNFSRGEWKKLEPFQKELYKEVLLENLRNLEFLDFPVSKLELISQLKWVELPWLLEEVSKSSRLGSVI
Protein: Possible lysine-specific histone demethylase 1 (EC 1.-.-.-) (Q9VW97)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for heterochromatic gene silencing. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and tri-methylated 'Lys-4' of histone H3. May also demethylate 'Lys-9' of histone H3, Plays a role in the repression of neuronal genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:17434130}. Chromosome {ECO:0000269|PubMed:17434130}. Note=In early cleavage, protein displays a uniform nuclear distribution. At metaphase, protein is detected at the chromosome periphery, and between the chromosomes during anaphase. A rather uniform interphase chromatin association is detected until syncytial blastoderm. When cellular blastoderm is formed (cycle 14), protein is preferably associated with pericentric heterochromatin situated at the apical pole of blastoderm nuclei. Later in development, protein is only found over euchromatin. In the germline precursor pole cells, protein remains uniformly distributed within the nucleus.
Interaction partners:
- CoRest, isoform G
- Histone deacetylase HDAC1
- High mobility group protein 2
- Histone-lysine N-methyltransferase Su
- GEO13032p1
- G9a, isoform B
- C-terminal-binding protein
- Chromodomain-helicase-DNA-binding protein Mi-2 homolog
- Chromatin assembly factor 1 p55 subunit
- [Pyruvate dehydrogenase
Sequence:
MKPTQFGGSSSKMTEPIEYVTLISDDSDGEPTPKRNVNHPPSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYSNRPSGSGDTASNDKSGSASMGPNNQQAERRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAGTPTVLSGQEGAVFQSRLPFNKMTPNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPPFDSEPSLVRRVHSFLERHGFINFGIFKRLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHRLDFNYAGDCPVSLGDALEWIISMQEMQVMHKRGQHMQEIIATQTKIIEQRRRLKTLRDTIGKLKNEHLAMINQRKPKGTDGDLKYCYQEFNIRNTQIKMEETISTFHDLHAEEKQMLAKLHELEQNRPSDVYLSSRDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENLKTSNSQMTYKADLVVCTLTLGVLKVAVAHKESQQSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWSISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIFGNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVIPPSSKDAEGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADYYLGYPEGTPPDIGYSVAEAANLVSVGNVVKLRDLSPNLSDSSPSSKKSEENSNSNTADSTELQ
Protein: Peptidase M12B domain-containing protein (Q7Z291)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLLPLLISGLLFRNADAFLPFFNEDDLKYTFGVDTHAEVPNHEEIDPVPYYHQNGSLHKLEFMAFNKKYNLSLEPTLAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHYGEKVYAAISNCDGRIKGTVIDDGEIIVVHPFPDHHAHRSKRATENGAHVVYKRETLAGEPKDFCGLDNVVTEESLVEDESAIFEDVFVTGQRLTQQSDLIVELAVFVDENLWRHFSSKHGGMADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAGYLHNHGNAQMYLDRFCRYQRNLAVRDWDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELGHSVGMRHDEPYCQSKHIMSSSLGPGKVTWSTCSLRDYHQFLQRLDGRGKNCLRVSNMPNKLEISSNVKPGQIYDANLQCELMHGNGYQQVTPRQDSYDGICYMMWCGQSSFGRIITSHPALEGTFCGPSKWCQLGRCVPWTGTNEIQPTVQHVAPVVTTLPSRIDGSWSGWGATICSQCTCNGILGSVGLAIARRTCSAPYPANGGSDCVGSTSRAVLCSRQCGRASKSVDEYISDKCMEQKRLKNDRELTGKGSQLNRFPQRACKVFCDVQQHYGSQRNYRFFGDNLPDGTSCGYDRYCLDGECLALNCNNNALISRDQSCPTDTCPITDQSSSVYRGQWGTWSLWTSCTATCGGGYRKRNRACSITGQCEGNEDETEVCSSESCPSVLRVGNEWSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAFDCPEKNIEVRSCDNGPCNAIGVWGTWGGWSTCSTSCGPGTLVRQRTCNREPCDGSAHERRSCNVATCQNDGIWSLWNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQQFCNEQACASSSANDWGTWSGWSQCSVSCGAGVKRRTRTCRTGNCPGNYKESAICNDRDCENKNAAWGGNILS
Protein: Protein phosphatase EYA (EC 3.1.3.48) (Eyes absent homolog) (AtEYA) (O82162)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. Possesses phosphatase activity toward several phosphotyrosine-containing peptides in vitro, with low peptide substrate specificity.
Interaction partners:
- Transposase
- Uncharacterized protein
- Uncharacterized protein AT4g03830
- Uncharacterized protein F2G19.33
- Uncharacterized protein
- Putative actin-depolymerizing factor 11
- Actin-depolymerizing factor 6
- Actin-depolymerizing factor 7
- Actin-depolymerizing factor 12
- Actin-depolymerizing factor 4
Sequence:
MNNDTSKKLGTLVSDDGPVNVYVWDMDETLILLRSLLNGTYAESFNGSKDVKRGVEIGRMWEKHILKICDDFFFYEQVEECNEPFLDSLRQYDDGKDLSRYEFKQDDFSTPTDDLNKRKLAYRHRAVAERYEKGLCPFIDSESMSGLDELYNVTDEYTDRWLSSARAFLEQCSCVEESSDGTSAIEQSSQDIHILVTSGALIPSLVKCLLFRLDTFLRHENVYSSIDVGKLQCFKWIKERFNHPKFRFCAIGDGWEECAAAQALQWPFVKIDLQPDSSHRFPGLTPKTVSYYFAAVYGNSDADSSKE
Protein: Protein-lysine N-methyltransferase (EC 2.1.1.-) (Archaeal protein lysine methyltransferase) (aKMT) (F0NBH8)
Organism: Sulfolobus islandicus (strain REY15A)
Function: Catalyzes the methylation of lysine residues in target proteins, using S-adenosyl-L-methionine (SAM) as the methyl donor. Exhibits broad substrate specificity, being able to methylate the crenarchaeal chromatin protein Cren7 primarily at 'Lys-11', 'Lys-16' and 'Lys-31', as well as a number of recombinant Sulfolobus proteins in vitro. Methylates lysine residues in a rather sequence-independent manner.
Interaction partners:
- DUF2286 domain-containing protein
- Thioredoxin domain-containing protein
Sequence:
MSYVPHVPYVPTPEKVVRRMLEIAKVSQDDIVYDLGCGDGRIIITAAKDFNVKKAVGVEINDERIREALANIEKNGVTGRASIVKGNFFEVDISEATVVTMFLLTNVNEMLKPKLEKELKPGTRVVSHEFEIRGWNPKEVIKVEDGNMNHTVYLYVIGEHK