wanglab/gogpt-training-data huggingface dataset:
Protein: Polyadenylate-binding protein (PABP) (Q38E63)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Eukaryotic translation initiation factor 4E, putative
- Regulator of nonsense transcripts 1, putative
- Pab1p-dependent poly
- Eukaryotic translation initiation factor 4E, putative
- Probable eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 3 subunit I
- Nuclear cap-binding protein subunit 2
- PAB1-binding protein 1
- Eukaryotic release factor 3, putative
- Probable eukaryotic initiation factor 4A
Sequence:
MTIAAQGVPSGPSATKPLQVASLYVGDLDPAINEPQLVDIFKPYGTILNVRVCRDIITQRSLGYGYVNYDDVNSASKAMEELNFKRVGEKCIRIMWQQRDPALRYSGSGNIFVKNLKEEVDSRELSLIFKKFGEILSCKVMDDESGKSRGYGFVHFKDDDAAKAAIEKMNGDKEHADADKAALYVANFIRRNARLAALVANFTNVYIKQLLPTVDKDVIEKFFSKFGGITSAAICKDKNGRAFAFCNFEKHDDAVKAIEASHDQEVEGVTQPGEKLYVQRAQPRSERLIALRQKYMQCQSLGNNLYVRNFDAEFTEKDLNELFKEYGVIRSCRVMTDANGISRGFGFVSFENADQANAALREMNGRMLNGKPLVVNIAQRRDQRLTMLKLQLQQRLQMMMHHMHPPPFGMPGHPLQRRNARSGGRGNRPHPRQQQPQPQPEPQPPLATTVPPAAAHSVMFTAPSMGFSAVPRTPQASPAIAPDTPPLPPISAEDLQQMSVDEQRAALGDRLYIKVHELAPDHAPKITGMFLEMNPKEALALLSNPKLMHEKVTEALCVLKVHASSA
Protein: Protein PEA2 (Protein PPF2) (P40091)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Localized to sites of polarized growth and is required for efficient mating and bipolar budding.
Interaction partners:
- Bud site selection protein 6
- Protein BNI1
- Protein SPA2
- GTPase-activating protein GYP3
- GTPase-activating protein MSB4
- Uncharacterized protein YMR124W
- Nuclear fusion protein FUS1
- Nuclear fusion protein FUS2
- Cell division control protein 42
- Serine/threonine-protein kinase CLA4
Sequence:
MHKFDLELSRRANPLLFSAERYEEYPLKYDELKQYLLSQNPSHPHHNSRPYTSIDYFDYLLYRSKNDESEIDLDKKLVSEFALYYVQKEHLNSDDLNPTLNELLKLQPKSADWYEMMLRILESINTTGIDQLTKENNNSFPNSKRARSSTNMGGTDKFNKGAYHTDKADDDKNEILQELTSFLMSNSIQKGIDIKPIPLDDPVKFLKNGINSILDTCVSLEKNTSSPPISPNAAAIQEEDSSKKLEELETAFSDLQLAHNFLTKQFENDRAEYVQDIEKLTRTNRELQDKLLNNHSNLSKTEKKLHELEQENKELEKANNKLNSSRHNFGMSSPASSPVTWDPSSPSSVGSPTSGSGSRSLSIMTSEFKKVLTSTQRKYEKELSDEREHRFKLERELALLKNAEANTSLALNRDDPPDML
Protein: Methyl-CpG-binding domain protein 4 (EC 3.2.2.-) (Methyl-CpG-binding endonuclease 1) (Methyl-CpG-binding protein MBD4) (Mismatch-specific DNA N-glycosylase) (O95243)
Organism: Homo sapiens (Human)
Function: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.
Subcellular location: Nucleus.
Interaction partners:
- DNA mismatch repair protein Mlh1
- DNA
- DNA
- G/T mismatch-specific thymine DNA glycosylase
- DNA
- Single-strand selective monofunctional uracil DNA glycosylase
- tRNA
- DNA repair nuclease/redox regulator APEX1
- Methyl-CpG-binding domain protein 2
- E3 ubiquitin-protein ligase UHRF1
Sequence:
MGTTGLESLSLGDRGAAPTVTSSERLVPDPPNDLRKEDVAMELERVGEDEEQMMIKRSSECNPLLQEPIASAQFGATAGTECRKSVPCGWERVVKQRLFGKTAGRFDVYFISPQGLKFRSKSSLANYLHKNGETSLKPEDFDFTVLSKRGIKSRYKDCSMAALTSHLQNQSNNSNWNLRTRSKCKKDVFMPPSSSSELQESRGLSNFTSTHLLLKEDEGVDDVNFRKVRKPKGKVTILKGIPIKKTKKGCRKSCSGFVQSDSKRESVCNKADAESEPVAQKSQLDRTVCISDAGACGETLSVTSEENSLVKKKERSLSSGSNFCSEQKTSGIINKFCSAKDSEHNEKYEDTFLESEEIGTKVEVVERKEHLHTDILKRGSEMDNNCSPTRKDFTGEKIFQEDTIPRTQIERRKTSLYFSSKYNKEALSPPRRKAFKKWTPPRSPFNLVQETLFHDPWKLLIATIFLNRTSGKMAIPVLWKFLEKYPSAEVARTADWRDVSELLKPLGLYDLRAKTIVKFSDEYLTKQWKYPIELHGIGKYGNDSYRIFCVNEWKQVHPEDHKLNKYHDWLWENHEKLSLS
Protein: Homeobox protein ceh-18 (P41934)
Organism: Caenorhabditis elegans
Function: Directs gonadal sheath cell differentiation and function. Also directs gonad migration and plays a role in specifying the differentiated phenotypes of epidermal cells during postembryonic development. Plays a role in oogenesis, regulating a sheath cell signal that causes oocytes to maintain diakinesis arrest during meiosis. Negatively regulates oocyte maturation, ovulation and MAPK activation in oocytes when sperm are not available for fertilization. May be recruited by akir-1 to the promoter regions of antimicrobial peptide genes to control gene expression in response to fungal infection.
Subcellular location: Nucleus {ECO:0000269|PubMed:7958868}.
Interaction partners:
- Specificity protein transcription factor 3
- Transcription initiation factor TFIID subunit 4
- Transcription factor jun-1
- Ephrin receptor 1
Sequence:
MNTLENTFQFLAEVFEANGGCLVTERVSPSLSGASKRKSRPVKRIITEDEVIPEEEVVEEEEEEKVEQPSEEVTCPAMQVDATDAILASLRQIANNDLSEHCIREDEGNTSAEVFSNGNGEDMEQAGLAGTDLLRRVADMLQGNHNGSLNSHFLQQQFAAFKETVDPTPVSTNGNGLLTPITTQLSPLFTSTDAFNSPEKLLQAIMTPSLGFLGANGLGASNSGLLSSPLIAPSPTLLQSLMNTPTQPTASLTPKKAENRPPVVSQTLKASKRRLFDDTSRIEAASMSGDDRIDMNELEAFAQTFKKQRIKFGFTQGDVGVALGKRYGTDFSQTTISRFEALNLSFKNMCKLRPLLKEWLADVEMAIEGGATVTDLIDKKTIHNGNHHTIHHVDIHETSISNSISSVTASSLLSREQHVKRRRKRTNLDMNQRNALDTFFALNPRPDHDKMTDIANSLELDRDVVRVWFCNRRQKMRRVDEPIEGEMVTPSVSPVFPHFSSMSALEQIQEAARLASCQASNDDSDGTSGSPDAPSNDGCSDL
Protein: Structural maintenance of chromosomes protein 2 (SMC protein 2) (SMC-2) (Chromosome-associated protein E) (hCAP-E) (XCAP-E homolog) (O95347)
Organism: Homo sapiens (Human)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Condensin complex subunit 2
- Condensin complex subunit 1
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 3
- Condensin-2 complex subunit D3
- Condensin-2 complex subunit G2
- Condensin-2 complex subunit H2
- Kinesin-like protein KIF11
- DNA topoisomerase 2-alpha
- Kinetochore protein NDC80 homolog
Sequence:
MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQCQNGKISKEAKSKAKPPKGAHVEV
Protein: Visinin-like protein 1 (VILIP) (21 kDa CABP) (Neural visinin-like protein 1) (NVL-1) (NVP-1) (P62762)
Organism: Rattus norvegicus (Rat)
Function: Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner.
Interaction partners:
Sequence:
MGKQNSKLAPEVMEDLVKSTEFNEHELKQWYKGFLKDCPSGRLNLEEFQQLYVKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEIIEAIYKMVGTVIMMKMNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPSIVLLLQCDIQK
Protein: Reticulocalbin-2 (Calcium-binding protein ERC-55) (E6-binding protein) (E6BP) (Q14257)
Organism: Homo sapiens (Human)
Function: Not known. Binds calcium.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Neuronal pentraxin receptor
- ER lumen protein-retaining receptor 1
- Neuronal pentraxin-2
- Neuronal pentraxin-1
Sequence:
MRLGPRTAALGLLLLCAAAAGAGKAEELHYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLIDEMDLNGDKKLSEEEILENPDLFLTSEATDYGRQLHDDYFYHDEL
Protein: Protocadherin 17 (Q5HZI5)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MYLSICCCFLLWAPALTLKNLNYSVPEEQGAGTVIGNIGKDARLQPGLPPAERGSGSGRSKSGSYRVLENSAPHLLDVDADSGLLYTKQRIDRESLCRHNAKCQLSLEVFANDKEICMIKVEIQDINDNAPSFPSDQIEMDISENAAPGTRFPLTSAHDPDAGENGLRTYLLTRDDHGLFALDVKSRGDGTKFPELVIQKALDRELQNHHTLVLTALDGGEPPRSATVQINVKVIDSNDNSPVFEAPSYLVELPENAPLGTVVIDLNATDADEGPNGEVLYSFSSYVPDRVRELFSIDPKTGLIRVKGNLDYEENGMLEIDVQARDLGPNPIPAHCKVTVKLIDRNDNAPSIGFVSVRQGALSEAAPPGTVIALVRVTDRDSGKNGQLQCRVLGGGGTGGGLGGPGSVPFKLEENYDNFYTVVTDRPLDRETQDDYNVTIVARDGGSPPLNSTKSFAVKILDENDNPPRFTKGLYVLQVHENNIPGEYLGSVLAQDPDLGQNGTVSYSILPSHIGDVSIYTYVSVNPTNGAIYALRSFNYEQTKAFEFKVLAKDSGAPAHLESNATVRVTVLDVNDNAPVIVLPTLQNDTAELQVPRNAGLGYLVSTVRALDSDFGESGRLTYEIVDGNDDHLFEIDPSSGEIRTLHPFWEDVTPVVELVVKVTDHGKPTLSAVAKLIIRSVSGSLPEGVPRVNGEQHHWDMSLPLIVTLSTISIILLAAMITIAVKCKRENKEIRTYNCRIAEYSHPQLGGGKGKKKKINKNDIMLVQSEVEERNAMNVMNVVSSPSLATSPMYFDYQTRLPLSSPRSEVMYLKPASNNLTVPQGHAGCHTSFTGQGTNSSETPATRMSIIQTDNFPAEPNYMGSRQQFVQSSSTFKDPERASLRDSGHGDSDQADSDQDTNKGSCCDMSVREALKMKTTSTKSQPLEQEPEECINCTDECRVLGHSDRCWMPQFPAANQAENADYRTNLFVPTVEANVETETYETVNPTGKKTFCTFGKDKREHTILIANVKPYLKAKRALSPLLQEVPSASSSPTKACIEPCASTKGSLDGCEAKPGPLAEASSSYLPTDSQYPSPSKQPRDPSFMASDQMARVFADVHSRARRASSEMGAVLEQLEQPNRDLGRESVDAEEVVREIDKLLQDCRGNDPVAVRK
Protein: UPF0336 protein Rv0637 (P9WFJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- (3R)-hydroxyacyl-ACP dehydratase subunit HadB
- UPF0336 protein Rv0635
- Small ribosomal subunit protein bS1
- Large ribosomal subunit protein bL33B
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL6
- Adenylate kinase
- Large ribosomal subunit protein uL24
- Malonyl CoA-acyl carrier protein transacylase
Sequence:
MALKTDIRGMIWRYPDYFIVGREQCREFARAVKCDHPAFFSEEAAADLGYDALVAPLTFVTILAKYVQLDFFRHVDVGMETMQIVQVDQRFVFHKPVLAGDKLWARMDIHSVDERFGADIVVTRNLCTNDDGELVMEAYTTLMGQQGDGSARLKWDKESGQVIRTA
Protein: DNA repair protein rev1 (EC 2.7.7.-) (Reversionless protein 1) (O94623)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA polymerase zeta processivity subunit
- DNA polymerase zeta catalytic subunit
- N-acetyltransferase eso1
- DNA polymerase kappa
- Ubiquitin-conjugating enzyme spm2
- Proliferating cell nuclear antigen
- DNA repair protein rad14
- Inheritance of peroxisomes protein 2
- DNA polymerase type-X family protein pol4
- Ubiquitin-conjugating enzyme E2 13
Sequence:
MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNYEARKFGIKNGMYVGTAKNLCPSLRVVDYDFGAYESVSREFYTILVNTLHDYIKVISIDEALLDITSSVSSFQDCFEIAESIRSQVREKTNCEVSVGIGPNVLLARLALRKAKPHNVYSLSIENVFDVLSPLSVQDLPGVGSSQAQKLFNLYGVRTIGQLQRIEKFNLQETFGVNYGLHLYNISRGIDTDIINNETPRRSISVDVNWGVRFVFQEDGIDFLKRLLHELLSRMGKCQVLLHQIQLRILKRADGAPFSPPKYLGAGEVTSFTKSSTFTSATNSFDLIWKKVTSMYKTINVDPGDVRGIGLQALKIIKDNSKIRKDYRSIQSITSRNKVSLKGASVDISSKDKEIISQKKQLSPKLIPSTPYDLPSSSQISSSALAQLPPSMQSDIQQQLRLQKRSITEYPSQLDPLFMVELPTPIRNEVNDNHEIAMNKRLSLKSHADNKIDERGKKKIRQENAFDKLLQISKKSKTINKPNVDYLTLKELPKDLQKQILKESNLQKSDLISEVKLEKPHIVTFQHVQSLEDLRGLLTKWYSKASKGPNIHDVNYFANYVCRVIREEKNLGKAQMMLKWLYQLNRKECNKPWEKAIDKIIETVQGECLQRNIPPLMIF
Protein: Squalene synthase (SQS) (SS) (EC 2.5.1.21) (E9PNM1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEFVKCLGHPEEFYNLVRFRIGGKRKDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Protein: ATP-binding cassette sub-family D member 3 (EC 3.1.2.-) (EC 7.6.2.-) (70 kDa peroxisomal membrane protein) (PMP70) (P28288)
Organism: Homo sapiens (Human)
Function: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty acyl-CoA thioesterase and ATPase activities. Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:16344115, ECO:0000269|PubMed:17761678, ECO:0000269|PubMed:24333844, ECO:0000269|PubMed:29397936}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisomal biogenesis factor 19
- ATP-binding cassette sub-family D member 1
- DNA repair protein RAD51 homolog 1
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX16
- ATP-binding cassette sub-family D member 2
- Peroxisome biogenesis factor 2
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
Sequence:
MAAFSKYLTARNSSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFFSRLIQILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILFRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKQITEDTVEFGS
Protein: Actin-binding protein Smlt3054 (Ankyrin repeat protein) (B2FKA7)
Organism: Stenotrophomonas maltophilia (strain K279a)
Function: Directly binds F-actin, which results in thickened and distorted F-actin fibers, and affects cellular F-actin localization. Thus, may be a host effector whose function is to disrupt host actin cytoskeletal structure, which may enhance invasion.
Subcellular location: Secreted {ECO:0000269|Ref.2}. Periplasm {ECO:0000269|Ref.2}.
Interaction partners:
Sequence:
MEMDIQESLLRLLRPLGLQRAEALAGALAREAGASKGLHDSQVLARAHALSVAPVEGRLGDLVWQVRQREHDGAPQVDLRWGLHRLGLDAPSRASTRDLVRAYERRLADRNEPMVYSTLAERVAGSMAEHTSLFQGMAMAVEEARARRSDANRLRENAPWQGWLVGASRAGHEAALLACIGMGADARLPDASGNTPLHHAARFGHFSLVTPLVEAGADVAALNAHGWAPLHLAALHKHARACLHLMAHGANPEQPGWRGRTPTRMHRHEQTQAL
Protein: Caffeine-induced protein 16 (O13798)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- DIS3-like exonuclease 2
- Poly
- Poly
Sequence:
MLFAKLLLKPVQILFAYAKAKSKEISIKEANLLIFQDETDNLRKISTPNKLAVSLAGGLKALLSSNQLCHAFHYHNKKIRLVDTSLNNLPVPILLPKLINYLLARKSQKSAAEWEEIERALLSCCKRSKDPSILFPTDVPCSLDDDVSFLTFKGHKNHLENRSFFHDSESDNFKVVLSNCAINSKEDNNLVTEDRVNLGAKLLLVPVQNLIKLLKVSKISVDLAVIDHSFQDQKLTLEVGNGGLEVVKLFGGWIRILESECLGHVFSFKKTMKRKEVALVNRKADIDTTDLFIALRQLVDSKFKSYGIKAQKHAINRISKLGKMITSNHAEEKLTTIPITEAKKESVSNTALIARKNIIRERKYLSRMFDIFEHIDSYFNHEINMLLVDLLLEPLQVAFVYKNLARRWISLEEIENLWLKVFDSSHPLGKSITSTLQAIGTRKILTQLSINMIPRYNQDNCSAGDIYILCFSENCWLYSVLQKTIDHWVNENVELFYKKFEILKSLLIEDIANSTFSKEVSLNSSLRWYCVAILVTPLQLIINHLKDKTEMLSLDAVMTLILGKNTREVNSSIEELKITDCLSFLLEHNIFNTFLVYNEGIVKLNKDFDDFTPLNLLKCVNYSLMEFQKNSTFDMLEKLYEIGREIDMSKFSTLKYNLQLPNVDLLKESEAVSETKNTKNNTFILKSDLKEEERLTNFTIEEINKHKAIGVALRKLLEEADTSSNFSSSNNHVLDSSKHTVSSASTSSRKFIENYKSLESIGLTSFVKDNKLKASKELQKLIEENVFPKNLILFIFRKCVIGIKSFEKLQSYVFTYYCERYPKLILKRVLRFLEEIGFITSQYPRKLTDTGALFLKHPSEWGVLQHTFISSNFFENVPCYISLEQSLQNFQNDIRPDTVRTTAMKAIIKKLLKSLRKLEGPVKIACFGSYRTGLMTKNSDLDLVIYSSKEALLPYYDRVKSIIKNEFSNVMPIRGARIPIIKFTGQYNIHCDLSFDNLLPIHNSDLILNYSLIDERVKTLLMLVKYWASNRLIDKTHHAFPSSYTWCIMVIFYLQQIPEPILPNLQKLSTQYSKIVRDNDYGNVNCWFNRDTECYRGSMQKGRKNIALLLRGFFCYYGLTTQYSFDWEAYMIDISSSQLKRKSTEFKDCPFVVLDPFLKKKNLTKALTQKSVKVVRYELERACRILSDPKCNLDHLLDPLIQ
Protein: Large ribosomal subunit protein mL57 (54S ribosomal protein L15, mitochondrial) (YmL15) (P36523)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL60
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein mL58
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL67
- Small ribosomal subunit protein mS42
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL46
Sequence:
MENSMMFISRSLRRPVTALNCNLQSVRTVIYLHKGPRINGLRRDPESYLRNPSGVLFTEVNAKECQDKVRSILQLPKYGINLSNELILQCLTHKSFAHGSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAESCENGQLSLQFSNLGTKFAKELTSKNTACTFVKLHNLDPFIFWKMRDPIKDGHINGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLLDKEDLHSLVNIANENVASAKAKISDKENKAFL
Protein: Meiosis-specific nuclear structural protein 1 (Q587B8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAGDARVERLRRVNRYKAVQAELAREREEAEFQAMRERKISAAARDEALAKELAERQRLELKDAKMLQFVRDLPELRNLEAQLKHARMKVDRSDQVDECCKRREERLQEEREYNAYLAEKEAKEKAEEEEKRRKAIQAFNEHQAAQLKLIEERRAQAERDAEQSRQERFAVDAVAARLQEKEFLEALERREKQRQLQAEQDEFYRLRKEIKENERLRQQREDEAIEAYLAEKGRRRETDEKLLREKEAVKARILEEQSKKIMEERLKREELESLLSDYYEAERISRERQALADAKERSEKLADAVKQENWNLIQDRIKARDLERQEEAMMRQKAVEDLAQQAKAKRLERERQIEIKKQKILETERRLEKFQELKREEQRLAAEVEERERKRAEELQEYIRRARAQLLEEYVPTLGQHVPARLLTVDEKKKFGITK
Protein: GH07444p (Q9VZF1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFLNYVFGPNLYMEYRGVPEPQRKMYEAGAVEKFGEQILSTLSVMWSVGYYTSPLLVTFLYRRGYLVTDSIPTLAKITTSVGLIVILSLVMRGLGRKQSRSYSNMIKALVRAKSSKAPGDANSELRRFDIEFNAWPVDFDVKALTGDTKKPVVTARRREPIQLATLPCEAIAYLAINTFGLSMIYPGSVKLLQKLMRPMLISGRAKLIEDDNGIRYKVKTIDSNEIDTLFIDNRPNNVGNGKTLVICSEGNAGFYEVGIMATPVALKYSVLGWNHPGFAGSTGTPHPHQDKNAIDAVVQFAINNLRFPVEDIILYGWSIGGFSTLYAASVYPDVKGVVLDATFDDVLYLAVPRMPAALAGIVKVAIRNYCNLNNAELANEFNGPISFIRRTEDEIIAEDNHIDTNRGNFLVLSVLKHRYPNIFGASQLNKAKGLLSKPLEPYSIPVADEKLCMSRLITYASDEGKSFPMNIGADYSEEVRNLMAVFLLRKHLRDYNSTHCTQLPGEFFTMPWDIPTEQGFVFT
Protein: LD29992p (Q95T04)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKHDVHVELPPSELKSDVIKVCGTPARVAEAREALVKMIEDYEADRADRELRSFVLQVDVDTEFHSKLIGRHGAVINKLRADHDVIISLPKRDEPNDRIISITGYQANAEAARDAILEIVGDPETLHREVIEIDKRIHPHLIGQRRRTIRKIIEDNKVNIKFSADDDNPNSIFISGKIEDVENVKELLFGMAEDYERDYLDNVAIAPPTIGAFLTGQGSGSDAAGASENGFVIKDAPWEKQKQAKNLTAPNTQSQEDFPHFAAGGAPVASTPITSVWGPKN
Protein: Acid-sensing ion channel 2 (ASIC2) (Amiloride-sensitive cation channel 1, neuronal) (Brain sodium channel 1) (BNC1) (BNaC1) (Q925H0)
Organism: Mus musculus (Mouse)
Function: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11306621, ECO:0000269|PubMed:15537887, ECO:0000269|PubMed:15708491}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16515}. Note=Localized at the plasma membrane, in the soma and punctated peripheral processes of neurons. {ECO:0000269|PubMed:11306621}.
Interaction partners:
- Acid-sensing ion channel 1
Sequence:
MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPTVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEEEGSHDENMSTCDTMPNHSETISHTVNVPLQTALGTLEEIAC
Protein: Alkaline/neutral invertase A, mitochondrial (A/N-INVA) (EC 3.2.1.26) (Q9FXA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development and floral transition. May generate glucose as a substrate for mitochondria-associated hexokinase, contributing to mitochondrial reactive oxygen species homeostasis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21441406}.
Interaction partners:
- AT1G06500 protein
- At5g49410
Sequence:
MSAIYLLRKISTKTPSRFHRSLFFSTFSKDSPPDLSRTTSIRHLSSSQRFVSSSIYCFPQSKILPNRFSEKTTGISVRQFSTSVETNLSDKSFERIHVQSDAILERIHKNEEEVETVSIGSEKVVREESEAEKEAWRILENAVVRYCGSPVGTVAANDPGDKMPLNYDQVFIRDFVPSALAFLLKGEGDIVRNFLLHTLQLQSWEKTVDCYSPGQGLMPASFKVRTVALDENTTEEVLDPDFGESAIGRVAPVDSGLWWIILLRAYGKITGDFSLQERIDVQTGIKLIMNLCLADGFDMFPTLLVTDGSCMIDRRMGIHGHPLEIQSLFYSALRCSREMLSVNDSSKDLVRAINNRLSALSFHIREYYWVDIKKINEIYRYKTEEYSTDATNKFNIYPEQIPPWLMDWIPEQGGYLLGNLQPAHMDFRFFTLGNFWSIVSSLATPKQNEAILNLIEAKWDDIIGNMPLKICYPALEYDDWRIITGSDPKNTPWSYHNSGSWPTLLWQFTLACMKMGRPELAEKALAVAEKRLLADRWPEYYDTRSGKFIGKQSRLYQTWTVAGFLTSKLLLANPEMASLLFWEEDYELLDICACGLRKSDRKKCSRVAAKTQILVR