wanglab/gogpt-training-data huggingface dataset:
Protein: AP2/ERF and B3 domain-containing transcription factor RAV1 (Ethylene-responsive transcription factor RAV1) (Protein RELATED TO ABI3/VP1 1) (Q9ZWM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to bipartite recognition sequences composed of two unrelated motifs, 5'-CAACA-3' and 5'-CACCTG-3'. May function as negative regulator of plant growth and development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- B3 domain-containing protein At1g16640
- Ethylene-responsive transcription factor ABI4
- Ethylene-responsive transcription factor-like protein At4g13040
- Basic leucine zipper 8
- Protein ABSCISIC ACID-INSENSITIVE 5
- Zinc finger protein ZAT12
- AP2/ERF and B3 domain-containing transcription repressor RAV2
- Zinc finger protein ZAT10
Sequence:
MESSSVDESTTSTGSICETPAITPAKKSSVGNLYRMGSGSSVVLDSENGVEAESRKLPSSKYKGVVPQPNGRWGAQIYEKHQRVWLGTFNEEDEAARAYDVAVHRFRRRDAVTNFKDVKMDEDEVDFLNSHSKSEIVDMLRKHTYNEELEQSKRRRNGNGNMTRTLLTSGLSNDGVSTTGFRSAEALFEKAVTPSDVGKLNRLVIPKHHAEKHFPLPSSNVSVKGVLLNFEDVNGKVWRFRYSYWNSSQSYVLTKGWSRFVKEKNLRAGDVVSFSRSNGQDQQLYIGWKSRSGSDLDAGRVLRLFGVNISPESSRNDVVGNKRVNDTEMLSLVCSKKQRIFHAS
Protein: Chromatin-modulating protein (A0A1D8PF47)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/threonine-protein kinase RAD53
- Serine/threonine-protein kinase MEC1
- DNA replication licensing factor MCM4
- Topoisomerase 1-associated factor 1
- Chromosome segregation in meiosis protein 3
- DNA damage checkpoint protein LCD1
- DNA replication licensing factor MCM2
- Chromatin-binding protein
- DNA replication initiation factor
- Chromatin-binding protein
Sequence:
MDLLDGIEDYSASQFKPTQVNAMATTQQDNENSDSDNTSQTQPNQSILGFDFNITTISKALNSTNDNQDKGDDDGMPNLSILDKVKNRLLGGGDASDEDENTNPDDEVSDKTQKIVHPSTGSAFQLLPQLEVDETEFSNNSSTQVIPKMKPTQKIETFYDTDKTQVIPKLNDVESWFTSKDQTQEDADNVISSKPLSKEEREAKIAKLAEQKRRERLEKERQELEQDLTKGTITDEEEELNQEANDTVVSSHNKSDGLSTKELEKAQEFLNIQKRHVDIRPEFQKKVVFTKDKLLSEFSEEEDCGTNERKTTKDKPPSSPTVEEILKSSPFTSPVKDDHNDDNVLDLFKKPSENTKNPLELYAQRLKKQLFSSPQGQTDTAKNNTKHSKKLINLDSDSDIDLASSSPTKKPPIATSTSIIGSGLKFSNRAKELDNIPELSKEQRLLIKQKFSKRKFQNSKIKTNQSKNHNVSHKQDNGFMQKLREKHINQLKLNKLNNPDHLIMEELEKDEETMTSLLEREMERVRNIRKREKLQERAKLALLEGKLGIKSNNDSEKYGDEIPESDVADSEVPDSDYNMDNDDDDDDDEDDSENESPKRAEINPRSDDSYMFGGGDNADGNGEDEGVTTTLSTQPQPVFDNTSFVDKTEGLFQNLQPRTSKEDSFISTQGEESQLQIRLPSFRDLTQVPTQTQVDQFTQVDEQATQADDVATQKILAATQKIMVPTQKIKNDTQIINKPMSQRPANSSTKRDDDDVDDDDDDDIITPANVRRGRKMIRNNNMIKIEEDDEETPSKNNNDHNPKEEEEEENDSDDPEEIQRRIKEYELKIRKRELKLRKRRKEMERKGMKNIVEGEAEESEDEWKGLGGIDEEFSDVVNSDDEKMIDNNFNIDLKNDEIRSKFMEEYQIKDQKELEKLLDDIKNHRLIKRTGINSNGLDIEISDEEDQLLEAYRKQKFMEQQQRLLQNKKLFELYKNEKSKAFFNSIQDTVEVIKIDDSDDSDIEVQTNPFNKGEKKNSGSETDKDNQGEEDEEEEDSLDKEAPIKKTIKVDEAFIRKKLSFLYSTTDEDKYERLQRISRIQHGISDGEEDIDDINVLKTKSFNNLTNNRLTPPVLESSSQPSKKRGHENDTDVDEEVDEEFMPVFKKPSIVKSFKSFQEQQGISIKDGKHHFSGVTISKQYKVVAGSKASITYMSKNNNHNKNQIKNIKEEKIQKSLHSSRRENSSFFDDSGFE
Protein: Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) (Q96UL8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Malate synthase, glyoxysomal
- Pyruvate carboxylase
- Pyruvate kinase
- malate dehydrogenase
- Malate dehydrogenase
- malate dehydrogenase
- Enolase
- Transcription activator of gluconeogenesis acuK
- 2-methylcitrate synthase, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MAPGANIHIPPAGPPEPGPLYSDFYQQQIERQRNNNYHSTSLRNMVATSVNRTALHPGGVQPGKGHTELEEELHEHAHIDYDRVAIIANPSVAALYEDALVYETGTAITSSGALTAYSGAKTGRSPSDKRIVKEESSEKEVWWGPVNKPMTPDVWRINRERAVDYLNTRNRIYVIDGFAGWDERYRISVRVVCARAYHALFMRNMLIRPSAEELKHFHPDYVIYNAGSFPANRFTEGMTSATSVAINFAEKEMVILGTEYAGEMKKGVFTILFYEMPVKHNVLTLHSSANEGQNGDVTVFFGLSGTGKTTLSADPKRALIGDDEHCWTDRGVFNIEGGCYAKCIGLSAEKEPDIFNAIRFGSVLENVVFDPISRVVDYDDSTLTENTRCAYPIEYIENAKVPCLSDSHPSNIILLTCDARGVLPPISKLTTEQTMFHFISGYTSKMAGTEDGVTEPQATFSSCFAQPFLALHPMRYARMLADKISQHKANAWLLNTGWVGAGATTGGKRCPLKYTRAILDAIHSGELAKAEYETYDVFNLHVPKSCPGVPDELLNPKNSWTATTSFSDEVNKLAKLFNENFQKYADQATKEVIAAGPVVQ
Protein: LD17501p (Nervy, isoform A) (Q9W186)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMALDGKAIIKEEITDKDAYDAAAAAAAAVAAGAALAVASAAAVQVPPASSSSAGSASSAAAAATNNTTSAAATAAAISRRLKASSSGGDKSSTSSSSSKDSSHTSSSRSERDRERERERERERDRLCRTPPDSPPDSSRSLAPRSPHSPLQLHQHPQRNASVSPVVNGSSSGGGGVGSSGTSPTPTPGSQHAASLAAAAAAAAAAHVEQARLVSKMRKFLGALVQFSQELGQPEVCERVRALVLSLCSGSISVEEFRLALQEAINLPLRPYVVPLLKNSIALVQREILALARATNQSALQYVTNNEQAVMEFAPHGVASAEFGDIFIQLEAPTSNGSSAVFKRRSSDSMMEHGGHNGLQEWNEYMASGGAGYPPPPSKRLTLHPAHSVVAYGEYGVSSAEGLPSAAAFMQRDERDLRMSEAQARHAAPPQRAGNPQPNPNAAAPGAPGAGGEEEWKNIHTMLNCISAMVDKTKRAITILQQRGIEPQHPNSGQEVTPAAMAELRRQTEEKVAEFKRNAEDAVTQVKRQAVIEIQRAVVAAETRAAEIMTQERLRMEKFFMEMSRHSSGERDLDNKSPSMASAQNGSNLQQQCWNCGRKATETCSGCNMARYCSASCQYRDWDSHHQVCGNTRASELSAKHLHSASNLSLRNAMATRSPPTPNSAAHLQAAAAAAAAAAGAREAVSAPVGGPGAGIAVGTGAGSGGQSGGGGGGGGGGGGGAAAAAVAAATPGALVANGLGSK
Protein: GPI ethanolamine phosphate transferase 2 (EC 2.-.-.-) (Glycosylphosphatidylinositol-anchor biosynthesis protein 7) (Local anestheticum-sensitive protein 21) (P40367)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose. Although not essential, addition of ethanolamine phosphate to the second mannose plays an important role in cell separation via the GPI-based modification of daughter-specific proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10329735, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:10329735, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- Uridine permease
- Cell wall protein ECM33
- Protein TED1
- GPI-anchor transamidase
- GPI mannosyltransferase 3
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Glucosidase 2 subunit alpha
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
Sequence:
MNLKQFTCLSCAQLLAILLFIFAFFPRKIVLTGISKQDPDQDRDLQRDRPFQKLVFVIIDALRSDFLFDSQISHFNNVHQWLNTGEAWGYTSFANPPTVTLPRLKSITTGSTPSFIDLLLNVAQDIDSNDLSEHDSWLQQFIQHNNTIRFMGDDTWLKLFPQQWFDFADPTHSFFVSDFTQVDNNVTRNLPGKLFQEWAQWDVAILHYLGLDHIGHKDGPHSKFMAAKHQEMDSILKSIYDEVLEHEDDDDTLICVLGDHGMNELGNHGGSSAGETSAGLLFLSPKLAQFARPESQVNYTLPINASPDWNFQYLETVQQIDIVPTIAALFGMPIPMNSVGIIIPDFLQLLPNKLASMKENFMHLWKLSDHHGEVALDDFTAEDIYTKMYTIQETLTKSATNYNYPLLTLAFVGFLIITIIAIYVLLRYSGPDFWQLRVSSLSVLLVSIILGVSTFASSFIEEEHQLWWWIVTAFSAVPLFVYRLNVLIIVRWFIMMACVRSIKFWNNSGQKFIYSNVMSNLLNQNPSWKWCLNMLTFLVLIMASAGFQVLHFIVTTILVGLCFTYKISWEIVNGNQAEIPLFMHDLLAKIDFAPTESNLIVLARVFFQAWAIVVISRLVLTKLKVLNKNYLIKDMKVYITILLMFQTSSQNIGQFLVFQILESQIFYFFQNIPTASLTSTSKIYFSNLVSLILQNFTFFQFGGTNSISTIDLGNAYHGVSSDYNIYVVGILMSVANFAPAIYWSMLPWSINYASIPAQVKLQTFIRSKLPAFTYHCIFGTCLMTACVVLRFHLFIWSVFSPKLCYFLGWNFVMGLLNGWLPELALLCALD
Protein: Metacaspase-1 (EC 3.4.22.-) (Q5ANA8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in cell death (apoptosis).
Interaction partners:
- Endonuclease
- AAA family ATPase
Sequence:
MFPGQGRHTYGGQQSNYSNQQQGYDQGYNQGYGQAYGQEYNQGYDRPSGPPPGQGQYNRPSGPPPGPPPGQGQYNRPSGPPPSQQGQYNRPSGPPPGQYGNNQTRGSGNEQNYGNMHGSGHYSRPPTDSQSFGVENYNYQYSNCSGRKKALLIGINYIGTKNELRGPINDVNNVEQFLLANGYSSDNIVKLTDDQRVQRAIPTRQNILDAIQWLVKDARPNDALFFHYSGHGGQTEDQPDEYGNYDEDDGYDEVIYPLDFETNGFIIDDLLHTMMVKTLPQGCRLTALFDSCHSGSVLDLPYMYSTKGVLKEPNVMKEAGAGLLQSAMAYATGDRSRMLSGLGGVVKTFMNQGKAEKANEYSKQTNTAPCDAISLSGCKDDQTSADSKENGTATGAMSYAFLTVMSQNPNQSYLSLLQNMREILSAKYSQKPQLSASHPIDTNLQFIF
Protein: Protein dom34 (Q9USL5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in protein translation. Together with hbs1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by dom34 and hbs1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of hbs1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 1 alpha-like protein
- Translation initiation factor rli1
- Uncharacterized GTP-binding protein P8A3.05
- Eukaryotic peptide chain release factor GTP-binding subunit
- Putative ATP-dependent RNA helicase C550.03c
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS7
Sequence:
MKLIQKNIEKNGSGWITMCPEEPEDMWHLYNILQVGDQLKASTVRRVVKVGATGSTSGSRVVMKLRILVENMDFDTKAAQLHIKGRTTEYHPEVKMGSYHTLDLELHRNFTLYKNEWDAFALDRVDAACNPSRNAEIGAVVLDEGLANICLITDYMTILRQRIDQVIPRKRRGDSSAYQKGLDKFYDSVFQSINSEFDFDKLKVVILASPGFVARGLYDYIFSMAVKLDLKQIVKSKNKFVILHSSTGHIHSLNEILKDPAVESKLADTKYVQEIRVLNKFYDVMNEDDRKAWYGPNHVLKAFELGAIGELLISDSLFRSSDIATRKKWVSLVEGVKEINCPVYIFSSLHESGKQLDLLSGIAAILTYPVDEEDISEDEEDEESQNFEHS
Protein: Matrix Gla protein (MGP) (Cell growth-inhibiting gene 36 protein) (P08493)
Organism: Homo sapiens (Human)
Function: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation.
Subcellular location: Secreted.
Interaction partners:
- Alpha-2-HS-glycoprotein
- Vitamin K-dependent gamma-carboxylase
- Bone morphogenetic protein 2
- Osteocalcin
- Osteopontin
- ATP-binding cassette sub-family C member 6
- Vitamin K-dependent protein S
- Vitamin K epoxide reductase complex subunit 1
- Elastin
- Unique cartilage matrix-associated protein
Sequence:
MKSLILLAILAALAVVTLCYESHESMESYELNPFINRRNANTFISPQQRWRAKVQERIRERSKPVHELNREACDDYRLCERYAMVYGYNAAYNRYFRKRRGTK
Protein: Polypeptide N-acetylgalactosaminyltransferase 11 (EC 2.4.1.41) (Polypeptide GalNAc transferase 11) (GalNAc-T11) (pp-GaNTase 11) (Protein-UDP acetylgalactosaminyltransferase 11) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) (Q6DJR8)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Coiled-coil domain containing 77.
- C1GALT1-specific chaperone 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MGSAALRCFCYGCLFTSVTWTLLLFIYFNFSEESQGFRHVPVKGLEPYKPLPKKIYPRFSRDSMGQHSDPRKGHNGNQLETEANADLSPELGMIFNEQDQDVRDVGYQKHAFNLLISNRLGYHRDVPDTRDSKCAKKTYPPDLPMASIVICFYNEAFSALLRTVHSVLDRTPAQLLHEIILVDDNSELDDLKKDLDGYMQENLSKKVKLVRNKQREGLIRGRMVGASHATGDVLVFLDSHCEVNEMWLQPLLAPIKENPRTVVCPVIDIISADTLIYSSSPVVRGGFNWGLHFKWDPVPLAELGGPEGFSAPFRSPTMAGGLFAMDREYFNMLGQYDSGMDIWGGENLEISFRIWMCGGSLLIVPCSRVGHIFRKRRPYGSPGGHDTMAHNSLRLAHVWMDEYKDQYFALRPELRNRDFGDIRERLALRRRLNCKSFKWYLDNIYPEMQVSGPNAKPQPPVFMNKGQKRPKILQRGRLINMQTNRCLVAQGHPSQKGGLVVAKECDYNDSEQVWSYNEEHELILSNLLCLDMSETRSSDPPRLMKCHGSGGSQQWVFGKSNRLYQVSVGQCLKLVDPMSRKGYVSMAICDGSPSQQWHLEN
Protein: Prolactin (Q569P7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAQGSRQYFAVAILMCAFVSINGVGLNDLLDRASQLSDKLHYLSTSLTNDLDSHFPPIGRGMMPRPSLCHTSSLQIPNDKDQAMKVPEDELLSLARSLLLAWSDPLALLSSEASSLAHPERNTINSKTKELQDNINSLGAGLEHVVHKMGSSSDNLSTLPFNGNNLGQDKTSRLVNFHFLLSCFRRDSHKIDSFLKVLRCRAAKKRPDMC
Protein: ATP-dependent permease AUS1 (Q08409)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transporter involved in the uptake of sterol.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cell wall protein DAN1
- Sterol uptake control protein 2
- Oligomycin resistance ATP-dependent permease YOR1
- Phosphatidylglycerol/phosphatidylinositol transfer protein
Sequence:
MSISKYFTPVADGSLTFNGANIQFGADAQGESKKSYDAEDSMPNPANQLNDITFQAEAGEMVLVLGYPTSTLFKTLFHGKTSLSYSPPGSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFLTVEQTIDFALSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATRSVNLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLTYFRDTLGIEKDPNDCIIEYLTSILNFQFKNKNLGNLSNSSSASVLKTATGEVTKYTYNSDFDLYDQWKHSSYYRNIKQQIQGSSIDDSIKEVDPSDVSPIFNIPLKKQLLFCTKRAFQRSLGDKAYMTAQFISVVIQSLVIGSLFYEIPLTTIGSYSRGSLTFFSILFFTFLSLADMPIAFQRQPVVKKQSQLHFYTNWVETLSTTVFDYCFKLCLVIVFSIILYFLAHLQYKAARFFIFLLFLSFYNFCMVSLFALTTLVAPTISVANLFAGILLLAIAMYASYVIYLKNMHPWFVWIAYLNPAMYAMEAILSNELYNLKLDCSETIVPRGPTYNDVPFSHKACAWQGATLGNDYVRGRDYLKQGLSYTYHHVWRNFGIIIGFLVFFIACTLFASQYIKPYFNKDEIERNNSRLTRWLPFLNKKRGTRSSARNDSKYVGIPKSHSVSSSSSSLSAVPYQISPSNKEMALNDYNEQPITETVETQKHIISWKNINYTVGTKKLINNASGFISSGLTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLFLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRGGECVFFGPMDDACGYFMSHDNTLVYDKEHDNPADFVIDAVGNSNSSAGKDTAEEALTLNKEAIDWSALWESSVEKKLVKKETARLEDDARASGVDYTTSLWKQPSYLQQLALITRRQYICTKRDMTYVMAKYCLNGGAGLFIGFSFWHIKHNIIGLQDSIFFCFMALCVSSPLINQIQDKALKTKEVYVAREARSNTYHWTVLLLSQSIIELPLALTSSTLFFVCAFFSCGFNNAGWSAGVFFLNYMLFAAYYSTLGLWLIYTAPNLQTAAVFVAFIYSFTASFCGVMQPYSLFPTFWKFMYRVSPYTYFVETFVSILLHNWEIKCDMSEMVPGQPLTGQSCGQFMEAFIEEYGGYLHNKNTFTVCAYCTYTVGDDFLKNENMSYDHVWRNFGIEWAFVGFNFFAMFAGYYLTYVARIWPKVFKIITKVIPHRGKKPVQN
Protein: Nuclear pore protein (Q55GW5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}. Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU364035}.
Interaction partners:
- Nucleoporin 155
- Nuclear pore complex protein nup54
- Nuclear pore protein
- Uncharacterized protein
- Nuclear pore complex protein
- Nuclear pore complex protein nup85
- Uncharacterized protein
- Nucleoporin 133
- Protein SEC13 homolog
- Nuclear pore complex protein nup43
Sequence:
MNVKEMDFNDLSNKSNQIINRISSFSSPIGLSSFNIERNLQEIGDTSKQLNDLTSSKTPFSNPLEPNVFQDSKINRKYGLDPKVLAKNLSNINTSSFTDVQSVPTDIDGYLKVQFENIILNTICDIQKKTSKEFQSHYEQTSIHDWNRDKKYLEEILGQKHIKVLPSVGGASASNQSSSSSSLFQQSVRGGLSSSIMGQSVRPTYGQQSQFGGSSTISIGGNISRVGGGSGGGIYSQRQTGQNEDRTKLSDKMKKYASIIEEYDIHMADQSKSYGFPLVHRLMDACLSTDINIGGGINTNTATTIVTHVWNLLLTLTSEIDTTNYIQQLKEQQQQQQQQTPQLKEQQQKQQQLTELQKHTKYHTKPTMAQLLKRSISFLETQFSQVIESRLPKHSNVSLPLNIIVAYIKSLNQSPLTDSSDEIYEGCSIWCIIYYLLRSGYTLEAYQFALEKCGSRYFDILSPIFKEKQQQQQQQQQQQQQQQQQQQQKSSLPTTTNNTSINKDQRDRMTREFNTAKTESKDVFKISVFNLLSCNDPNSTKQQVITSIQDYIWWRLNFIRERITIEPTNDSAISLLESLQNDIKNSIEKNRNNYETLEIFQLLLVSLQFEDAIVSLYQFCPDDSLHLAIALDYYKLLRTSNSGINNKHVDEINKFNKSTTNTNTMTYQQNQQQQQQQQQQQQQEQQKEIYDQTSKSIHLVEMIKQYTKIFSFEENREAFFYYLLIADNDIKIQEISELVVSSPNGFKFAHELSLFSEFINKQQWRTIIEQSALELENKNEYQSAIEFWIMIEEYPRVLEIYNSRISVLLTSISSERDQLYQFGKQLFNDYQGRLKTTSTARTSYLAFEQLLKLCDFFDLYNKEKYQEAIQKIENLEILPISESEIDSKVQDYRFLSPHITRNFSSIIQAYVDIIVKQYHLLNNFDEFTNRSALFAGRKQTIQDLQSRTQCIALFAGKIDFPMSGNILPRLMNLFISMSN
Protein: fur leader peptide (A8DYP9)
Organism: Escherichia coli (strain K12)
Function: Cotranscribed with fur, it is essential for fur translation. The fur ribosomal binding site (RBS) is occluded by the 5'-mRNA secondary structure, which is opened by uof translation.
Interaction partners:
- mgtA leader peptide
- Ferric uptake regulation protein
Sequence:
MIRIISRANSVTSSNEVNRLVTGQIPHD
Protein: Rifin (Q8I2E5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYTNILLFPLKLNILVNTHKKPSITARHIQTTRLLCECELFSPQNYDNDPEMKRVMQQFHDRTTQRFHEYDERMKTTRQECKEQCDKEIQKIILKDKMEKQMAEKLSTLETKINTDDIPTCVCEKSMADKTEKFCLNCGKNMAAIAPWWGLVCGSGYAGWLHSAMAAAIDKAIAEGAAAGIKAGHLAGTNAVIEQLRTLGIYFVGNKQLETIIDVTNYMNVSFIYDKVYSHYITLCTPRPVNGHLVSNFNFSDRFCKLFHQKDLVSLDIKSVKAIIKKNVEEAVAGAEQAAKAEVSNVTATKTTEFTTKNIAEVEAATTSYYTPIIASIVAIVIIVLIMVIIYKILRYRRKKKMKKKLQYIKLLEE
Protein: TPX2 C-terminal domain-containing protein (Q57V56)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATLNNLTVGSDSDSSTEAPLAVRPDAAAAAEGAAMEGNSAPGEAAAPAGVSAGEEAAPKEGEAAADGSGTSPGGKEGEGEKTFKKISSESTTLTHAASKTDESAREATEGGDANANAAAGSSKVSKELTPREGASKSEQEQGAAAEKSAPNPGVAPPLDPAAVRSKRSSVKPSPAAVSPASREVDPNGKSTSQAGDGAEAKPSKTREKRHGTQKKSRSKRTDLEEEISLMKKAEKCGIGAGSLHDIVSVSGGDGLSPQPGSSPAKLSRSPRKMASRHGEGSKGNKNGENVSEGADGQQMPVVVDIPVPSVHKVFHTNRGDGRVVVGDISGIYTKRKRKLVNEYRTEADDKENSPQISPLTLQNVGRHIRESGGVHKGYTARRCYSSESSLFKSCVSLNTDPKTASRRKRSVRRGGGRQIERTGRALQRLNIPAYHRRLIIDMHQKGISERQAEEGSNSDDWLHTAGMGRRYSVSPERSARLGGHDRLPQRRYHSTIDGNRYGYSPRGASNDRLPERRRSKRGEDYRKEHTYKPTISKFAQALPRSDVPCHERLYSARPSVQRNKNADGEDYEAPALSPRLQEFVNNSSFELFRPHISKRARALEVEAPFYDRLHPSKEELARKRPEEPKPVPTPRVSTSRPISISPRLLARREPPPPESLPSFRPMITPRAKGVECSKPFYDRLHPSKEQRARKQKEEEPKSAPPRTSPRRAVSVSQRLLEPHQPPPYEKYDPSFRPEISPRARALERDGPFHKRLYLTPYELEEAHALHRRRQFESSCNFQPEIVELMRQNYDAKKVKRGTSKPVKAHRQRS
Protein: Cobalt-containing nitrile hydratase subunit alpha (L-NHase) (L-nitrilase) (EC 4.2.1.84) (Q7SID2)
Organism: Pseudonocardia thermophila
Function: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
Interaction partners:
- Cobalt-containing nitrile hydratase subunit beta
- nitrile hydratase
- Amidase
- Nitrile hydratase
- Amidase
- Amidase
- Aspartyl-tRNA
- Nitrile hydratase accessory protein
- Aspartyl-tRNA
- Aspartyl-tRNA
Sequence:
MTENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVGPHLGAKVVVKAWTDPEFKKRLLADGTEACKELGIGGLQGEDMMWVENTDEVHHVVVCTLCSCYPWPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEVPPSKEIKVWDSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPAKAV
Protein: PHD finger protein 10 (PHF10 isoform Sl) (S5FZ81)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAAGPGAALSPRPCDSDPATPGAQSPKDDNEDNSNDGTQPSKRRRMGSGDSSRSCETSSQDLGFSYYPAENLIEYKWPPDETGEYYMLQEQVSEYLGVTSFKRKYPDLERRDLSHKEKLYLRELNVITETQCTLGLTALRSDEVIDLMIKEYPAKHAEYSVILQEKERQRITDHYKEYSQMQQQNTQKVEASKVPEYIKKAAKKAAEFNSNLNRERMEERRAYFDLQTHVIQVPQGKYKVLPTERTKVSSYPVALIPGQFQEYYKRYSPDELRYLPLNTALYEPPLDPELPALDSDGDSDDGEDGRGDEKRKNKGTSDSSSGNVSEGESPPDSQEDSFQGRQKSKDKAATPRKDGPKRSVLSKSVPGYKVEEKSP
Protein: 2-methylcitrate dehydratase 1 (2-MC dehydratase) (EC 4.2.1.79) (Q8NSH9)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer 2-methyl-aconitate.
Interaction partners:
- 2-methylcitrate synthase 1
- 2-methylcitrate synthase 2
- Probable 2-methylisocitrate lyase 1
- Uncharacterized protein involved in propionate catabolism
- Probable 2-methylisocitrate lyase 2
Sequence:
MRIHDVYTHLSADNFPKAEHLAWKFSELATDPVEVTPDVSEMIINRIIDNAAVSAASVLRRPVTVARQQAQSHPREKGGKVFGISGSYSPEWAAFANGVAVRELDFHDTFLAAEYSHPGDNIPPLLAVAQAQRSSGRDLIRGIATAYEVQVELVRGICLHEHKIDHVAHLGPSAAAGLGTLLHVDEETIYQAIGQALHTTTATRQSRKGEISSWKAFAPAFAGKMAIEAMDRAMRGEGSPAPIWEGEDGVIAWLLSGKDHVYHVPLPEHGEPKLGILETYTKEHSAEYQSQAPIDLARRMKPLVDAAGGTEHIAEIVLRTSHHTHYVIGTGANDPQKMDPQASRETLDHSIMYIFAVALQDGVWHHEFSYTRKRSTRPETVELWHKIRTVEDPEWTRRYHSDDPAKKAFGAKAVITMADGTVIEDELAVADAHPLGARPFARENYIEKFRTLAQGIVIDSEQERFLHAVQSLPDLDDLDQLNIEVDISNQAATKAGLL
Protein: Arachidonate 12-lipoxygenase, 12R type (A0A3B3IRK2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELELSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLLETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLYLPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTVPELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPDDRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI
Protein: CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (Leukocyte mono-Ig-like receptor 1) (Mast cell-derived paired immunoglobulin-like receptor 1) (Myeloid-associated immunoglobulin-like receptor 1) (MAIR-1) (MAIR-I) (CD antigen CD300a) (Q6SJQ0)
Organism: Mus musculus (Mouse)
Function: Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}; Single-pass type I membrane protein {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}.
Interaction partners:
Sequence:
MTQLASAVWLPTLLLLLLLFWLPGCVPLHGPSTMSGSVGESLSVSCRYEEKFKTKDKYWCRVSLKILCKDIVKTSSSEEARSGRVTIRDHPDNLTFTVTYESLTLEDADTYMCAVDISLFDGSLGFDKYFKIELSVVPSEDPVSSPGPTLETPVVSTSLPTKGPALGSNTEGHREHDYSQGLRLPALLSVLALLLFLLVGTSLLAWRMFQKRLVKADRHPELSQNLRQASEQNECQYVNLQLHTWSLREEPVLPSQVEVVEYSTLALPQEELHYSSVAFNSQRQDSHANGDSLHQPQDQKAEYSEIQKPRKGLSDLYL
Protein: Immune-associated nucleotide-binding protein 4 (AtIAN4) (AIG1-like protein) (Q9C8U7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Plant intracellular Ras-group-related LRR protein 7
- F-box protein At3g17710
- Plant intracellular Ras-group-related LRR protein 8
- Plant intracellular Ras-group-related LRR protein 6
- Plant intracellular Ras-group-related LRR protein 4
- Plant intracellular Ras-group-related LRR protein 5
- Plant intracellular Ras-group-related LRR protein 3
- Plant intracellular Ras-group-related LRR protein 2
- Zinc finger CCCH domain-containing protein 26
- Serine/threonine-protein phosphatase PP1 isozyme 8
Sequence:
MAGLEDTTDLRLPSASEPIKNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAVTPCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVLAEDGLHAVVLVLSVRTRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANNMTLDDYLSKGCPEFLKTVLRLCGGRRILFDNRTTDEGKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQKEAETLREQQKEVESKDLAAAEIEKWKKHYQTEHDKNMNMMAEMLGNRLREDSERQEKMLLALRDNLEISQRQNKLNELTDNEPDLIHCGVSLRRMPCNML
Protein: Surfeit locus protein 6 homolog (Q9VDS6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in a nucleolar function.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Protein Peter pan
- Probable rRNA-processing protein EBP2 homolog
- Ribosomal RNA processing protein 1 homolog
- Protein MAK16 homolog
- Nucleolar GTP-binding protein 1
- RRM domain-containing protein
- Probable ribosome production factor 1
- RRP15-like protein
- Ribosome biogenesis protein BRX1 homolog
- Pescadillo homolog
Sequence:
MTQAEIVKCLREEYEIEHNKDQKPEKEDLPAITKKFYQRVLELLTIHKVPYSKQEDEETYEEYLLSDTEESGNKKKKQQGKLKNQDSDDEDVEARIASIKNKLRQKKGPTTERQQKRRESKKLKRSKGVQKLLLSSAKNLKNENVKHQKLKNGVVKSEQETEDSKEQIQPVKVQPVYNQEAKIVYSKVDFAANPGGKAKKSHQNPKEILKKLRDTKKHLTELREQGETDKAAEIQTDIAWRNAFDKVEGKKVKDDTKLLQKAIKKRRVEKKKSKTKWTERKQKVEHDKEKRQKKRQENLEKRSKDKKNRKLKTASKRGRIIPGY
Protein: C-C motif chemokine 26 (CC chemokine IMAC) (Eotaxin-3) (Macrophage inflammatory protein 4-alpha) (MIP-4-alpha) (Small-inducible cytokine A26) (Thymic stroma chemokine-1) (TSC-1) (Q9Y258)
Organism: Homo sapiens (Human)
Function: Chemoattractant for eosinophils and basophils. Acts as a ligand for C-C chemokine receptor CCR3 which triggers Ca(2+) mobilization in eosinophils. Also acts as a ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis.
Subcellular location: Secreted {ECO:0000269|PubMed:10488147}.
Interaction partners:
- C-C chemokine receptor type 3
- C-C motif chemokine 2
- C-X-C motif chemokine 10
- Eotaxin
- C-C motif chemokine 17
- C-C motif chemokine 21
- C-X-C motif chemokine 11
- C-X-C motif chemokine 9
- Stromal cell-derived factor 1
- C-X-C motif chemokine 14
Sequence:
MMGLSLASAVLLASLLSLHLGTATRGSDISKTCCFQYSHKPLPWTWVRSYEFTSNSCSQRAVIFTTKRGKKVCTHPRKKWVQKYISLLKTPKQL