wanglab/gogpt-training-data huggingface dataset:
Protein: serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (Seryl-tRNA(Ser) synthetase) (C8VIL4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Acyl carrier protein
- valine--tRNA ligase
- glycine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- arginine--tRNA ligase
- Lysine--tRNA ligase
- RNA polymerase II Elongator complex associated protein Kti12, putative
- threonine--tRNA ligase
Sequence:
MVEIFRRSYASTVRPATAPRPSPNVKHVRENAELYAQNCRDRNYPAHAEYPFKIQQLSEELRQIDKQLMPFRSRIKALERTIGRLQNPATGPEEKEQEPAIRAEAQQLKNESAALITRRELCDEQIHDLALSLPNLTSPHTPVGLEPALVEYLNFDPQSPPAWVSSPDPLRSHVSIGTDLGLIDFTSAATTTGWGWYFLTGDGALLEQALIQYSLSVARRHGWTPISPPSIVWSYLTEACGFQPRDQNNEQQIWAIEQAEKDKAKPPRSLAATAEIPLAAMHARNELDPAALPIKLVGPSRCYRAEAGSRGVDTKGLYRVHEFTKVEMFGWADSSPTSSSPTSDDLFEGLLTVQKEILTSLQLPCRILEMPTSDLGASATRKRDIEALFPSRMRGNGLEDAWGEVTSASICTDYQSRRLGTRVRGVKSVFPHTVNGTAVAVPRVLAAILENGWDAERKVVVLPEVLRPFMGGAEVIGK
Protein: Alanine racemase TOXG (EC 5.1.1.1) (TOX2 HC-toxin biosynthesis cluster protein TOXG) (Q9UW18)
Organism: Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola)
Function: Essential role in the production of the major forms of HC-toxin, all of which contain D-alanine. The absence of this enzyme reduces pathogenicity of the fungus on maize. Synthesizes D-alanine from L-alanine.
Interaction partners:
Sequence:
MSNMVLNGNIDKSDRNSILDILQSLENIAWGQPGSARCDFRSDVITRPSLRMLSAVLKTTLGDDVFREDLTTAHFEAHVAEISGREEGMFVITGTMANQLCLHALVSTRPCGILLSSESHAIHYEAGGSSMLSGAMLQPVQPSNGKYLRVEDLEEHAILTDDVHKCPTSIVSMENTAGGAVVPVHELRRIRDWAKQNNVRTHLDGARLFEAVATGAGTLKEYCSLIDLVSVDFSKNLGAPMGAMILGDKKLIQQMRRTRKGIGGGMRQGGVITAAAREALFENFGLGAEIESQTLLQVHKVAKRLGEEWTRKGGKLSKEIETNIIWLDLDAVGIKKSQFIDKGREYGVILDGCRIVCHHQIDIYAVEALIDVFHDILKADPIKNKNSDR
Protein: Protein THYLAKOID ASSEMBLY 8, chloroplastic (At-THA8) (AtTHA8) (Protein EMBRYO DEFECTIVE 3123) (Q9LVW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required during embryogenesis. Mediates group II organellar RNA introns splicing (e.g. ycf3-2 and trnA). Binds weakly to specific RNA. Promotes the biogenesis of chloroplast thylakoid membranes.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:22495966}; Peripheral membrane protein {ECO:0000269|PubMed:22495966}; Stromal side {ECO:0000269|PubMed:22495966}.
Interaction partners:
- CRM-domain containing factor CFM2, chloroplastic
- CRS2-associated factor 2, chloroplastic
- Pentatricopeptide repeat-containing protein At5g04810, chloroplastic
- Pentatricopeptide repeat-containing protein At2g15820, chloroplastic
- Protein WHAT'S THIS FACTOR 1 homolog
- Ribonuclease III domain-containing protein RNC1, chloroplastic
- Pentatricopeptide repeat-containing protein At2g41720
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- Pentatricopeptide repeat-containing protein At4g25270
- Putative pentatricopeptide repeat-containing protein At2g02150
Sequence:
MALSLSQTRPPSLSHSHTLSVIVPKRTFVSIRCGPRDNRGPLLKGRILSTEAIQSIQSLKRAHRTGVSLSLTLRPLRRLIKSDLISVLRELLRQDYCTLAVHVLSTLRTEYPPLDLVLYADIVNALTRNKEFDEIDRLIGEIDGIDQRSDDKALAKLIRAVVGAERRESVVRVYTLMRESGWGSESWEADEYVAEVLSKGLLRLGEPDLASQVSLKSSILKP
Protein: Spliceosomal protein DIB1 (Q06819)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
Subcellular location: Nucleus.
Interaction partners:
- Pre-mRNA-processing factor 31
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing factor 6
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing helicase BRR2
- Small nuclear ribonucleoprotein F
- Pre-mRNA-splicing ATP-dependent RNA helicase PRP28
- 23 kDa U4/U6.U5 small nuclear ribonucleoprotein component
Sequence:
MASVLLPQLRTGWHVDQAIVTETKRLVVIRFGRKNDRQCMIMDELLSSIAERVRNFAVIYLCDIDEVSDFDEMYELTDPMTVMFFYHNKHMMCDFGTGNNNKLNFIVDDKQEMIDILETIFRGARKNKGLVVSPYDYNHKRVS
Protein: Serine protease inhibitor Kazal-type 6 (Q8BT20)
Organism: Mus musculus (Mouse)
Function: Serine protease inhibitor selective for kallikreins. Efficiently inhibits KLK5 and human KLK2, KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14. Doesn't inhibit human KLK1 and KLK8.
Subcellular location: Secreted {ECO:0000269|PubMed:24352040}.
Interaction partners:
- Kallikrein-14
- Glandular kallikrein KLK13
- Kallikrein related-peptidase 12
- Kallikrein c
Sequence:
MKVAGVFLLLSLALLCFFSGAFSQGGQDKRGWITRSEGRFPGKGVLRHRLFQINCGEFRDPKVFCTRESDPLCGSDGQTYGNKCAFCKALEKSSGKINLKHRGKC
Protein: MRX complex DNA-binding subunit (A0A1D8PJD1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Double-strand break repair protein
- Serine/threonine-protein kinase TEL1
- DNA helicase
- Serine/threonine-protein kinase MEC1
- DNA repair and recombination protein RAD52
- DNA repair protein RAD51 homolog
- Replication protein A subunit
- DNA topoisomerase
- Flap endonuclease 1
- Midasin
Sequence:
MIHIEKLFSFILLFIALPSPASFIRMSSIYKLSIKGVRAFHPESDETIQFGFPLTLICGQNGCGKTTVIECLKYATTGTLPPNSKGGAFVHDPSLSSRTAVTGQIKLAFKNVNGKSMITTRSVQASSKSTKSATGATVTFKTLEGQLAIIEKGDKISVSSKNAELDAQIPVYLGASPAILENVIFCHQDESLWPLSEPSALKKKFDDIFEASKFTKVLDNFKSIKKDMATDIKLIEQSVNHLKIDKERAKKVQDKLHNMNESVEKYTEEITDLNIQIEKKEKQAEELFATNQEFQRTLSDYENLLTKKQALEEQIERLKTSIEILPDNDEELLNRQENFSAITTEKSNRIDDLQLQSTKLSDELKNKTKQYNELIRLDGSFKAKKAEYDSNWEKLSEIVDKNAKDFNVQISNDRVRNIAMFKTELNKRHNTLLNEQKDLLVDNKRKESERQSALQDVLNSISREEQYHEYATNVINTNNEKLSVLKRKVEVGSNNEIELEEKRNDLELTMKLLQEKKDLNEVRKLDAKIMECNTEISKLEFELDELAKKLSTSNKQSDLRSKVLFLEESAKSKKAELSKIFATIDSSYFDVLGSKLDVDVGESLLSQKISNLEIKSEEQQKKVGSLESELQINKNSIESILKTIEENNSKIDSLKSNITKVIGEDEINDYENVVNDLEDSYRNVSEDVNSAEVTRDFKNSAISFAEENKCCLLCKRLFEQGGLGSFIQDLKQSVDEHKIQEIREQSLEIKKELEDVKSINLEVINYRECLANVQNFECKLKELVDKSSQIENELEQQRKEQQTIKHSLDNALSLKKPLSDATRIHLEVSEIEFQLDELNEDLSGFGGSVVSVDELQKQQQDINLKIKKTRQDLNDYTESKYKAQRELQKLENRVKDTKLQISNLERSLAEVTGIKNNISEAEDIVRSSEEKLKQIKTSLEELQVDKQVKSNALRDTQNSNRDTEQEMQQEVEKCHQLLTSFTSLNDAVTYFETNIADKYEANALEMKELSEQCTSLETKIDDHAQEIKSLEKEVMDASRIEHNILANIDYRSQLSRLEETELQLGSMDIEDAQSRKEEYQVESKKLRDALSSLTAEHAGKIGEVKQIKDQIASLNKELETEYKNVNQSYHEEWIKLQTNLLVSNDIQIYSKALDNGIMKYHSMKMEEINRILNELWSQTYKGSDISTIAIKSDVNLQAKGNRSYNYRVVMVKESSELDMRGRCSAGQKVLASILIRLALAECFGANCGMIALDEPTTNLDAENAEALAAALNRIIEYRKSQSNFQLIVITHDEKFLTHIQGDRFTDHFYRIQRDESSKSRIYSLPIGRIQEG
Protein: V-type proton ATPase subunit G (V-ATPase subunit G) (Vacuolar proton pump subunit G) (Q54Z13)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit C
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit H
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit d
- Vacuolar proton translocating ATPase 100 kDa subunit
Sequence:
MSSEDGIKKLLDAERTAQKIVADARQDRVQKLKKAVEEAEKEIKEFREKKDKEYKEYESKYLGASSETASQLATNANKEIDTIRNETAANKQKVVDLLIKYAITCDN
Protein: Stardust, isoform B (EC 2.7.4.8) (Stardust, isoform N) (Q9W3H6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKHKKSTNTTTTTTITALTNNDHANKMLIVAYHSSHQHEQLQQQHPSKTSTTTTTIALDVATQNLYNQKQQNKLEQIENYENCLQSERNEQHEQQFEQQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: CDet11-24 protein (O23764)
Organism: Craterostigma plantagineum (Blue gem) (Torenia plantagineum)
Interaction partners:
Sequence:
MESQLHRPTEQEVMEGQTADHGEKKSMLAKVKEKAKKLKGSINKKHGSSQDDDADNDEEINTSPAVHGAPGTSPPPPTQGGEYGGLSERDVNIPHPLASTQANLDKPADVTDASRELQVPPPVPETTPEVSDKGLTEDLGSNAGQGVKESDVDSLTQGLKGVNYGGDDSNPLSGQEHQTISDEPKSLPGQGNDLPQSHPSSEDEPKKFDANDQPQSMPQDTITGKLSSVPAVIIDRAAAAKNVVASKLGYGGSQAQESAADAGAAQQKKPLTETAAEYKNLVAEKLTPVYEKVAGAGSTVTSKVWGSGGTTAGEQTQGGEGVVDGGGAASNKGVFTKDYLSEKLKPGDEDKALSQAIMEKLQLSKKPAVEGGAGDETKASESSPGVVGTIKGAVGSLIGGGNKSSGAESAAAADEQTQALGE
Protein: Coatomer subunit alpha-1 (Alpha-coat protein 1) (Alpha-COP 1) (Q94A40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit beta-1
- Coatomer subunit gamma
- Coatomer subunit epsilon-1
- Coatomer subunit beta-2
- Coatomer subunit beta'-1
- Coatomer subunit beta'-2
- Coatomer subunit beta'-3
- Coatomer subunit epsilon-2
- Structural molecule
Sequence:
MLTKFETKSNRVKGLSFHPKRPWILASLHSGVIQLWDYRMGTLIDRFDEHEGPVRGVHFHNSQPLFVSGGDDYKIKVWNYKNHRCLFTLLGHLDYIRTVQFHHEYPWIVSASDDQTIRIWNWQSRTCVSVLTGHNHYVMCASFHPKEDLVVSASLDQTVRVWDIGALRKKTVSPADDIMRLTQMNSDLFGGVDAIVKYVLEGHDRGVNWAAFHPTLPLIVSGADDRQVKLWRMNETKAWEVDTLRGHMNNVSSVMFHAKQDIIVSNSEDKSIRVWDATKRTGLQTFRREHDRFWILAVHPEMNLLAAGHDSGMIVFKLERERPAFALSGDSLFYAKDRFLRYYEYSTQRDSQVIPIRRPGTPSLNQSPRTLSYSPTENAVLICSDLDGGSYELYIIPKDSVGRSDVVQDAKRGTGGSAVFIARNRFAVLEKSTSQVLVKNLKNEVVKKSPLPIPTDAIFYAGTGNLLCRSEDKVVIFDLQQRLVLGELQTPFVRYVVWSSDMESVALLSKHTIIIASKKLVLQCTLHETIRVKSGAWDDNGVFIYTTLNHIKYCLPNGDSGIIRTLDVPIYITKVSGNTIFCLDRDGKNKAITINATEYIFKLSLLRKRYDHVMSMIKNSQLCGQAMIAYLQQKGFPEVALHFVEDERIRFNLALESGNISVAVASATQINEKDHWYRLGVEALRQGNSGIVEFAYQQTKNFERLSFLYLITGNLDKLSKLMKIAEVKNNVMGQFHNALYLGDVKERVKILENAGHLPLAYITASVHGLNDIAERLATELGDNVPSLPEGKTPSLLMPPTPIMCGGDWPLLRVMKGIFEGGLESADRGGTVDEEDVEGDWGEELDINVDGMENRDIEDILAAAEAGEEENDEEGGWGLEDLVLPPELDTPKASANARSSVFVTPPQGMPVSQSWSQKSSLAAEQAAAGSFDTAMRLLHRQLGIKNFTPLKSMFLDLFNGSHSYLRAFSSCPVVPLAIERGWSESSSPNVRSPPALVYDFSQLDEKLKSGYKATTTGKFTEALRLFLSILHTIPLVVVETRREVDEVKELIVIVKEYVLGLQMELKRREMKDDPVRQQELAAYFTHCNLQTPHLRLALLSAMGVCYKAKNLATASNFARRLLETSPVDSQAKMARQVVQAAERNMTDETKLNYDFRNPFVVCGSTYVPIYRGQKDVSCPYCTARFVPNQEGNICTVCDLAVIGADASGLLCSPSQVR
Protein: RAD51-like protein 1 (P34348)
Organism: Caenorhabditis elegans
Function: Has a role in the homologous recombination repair (HRR) of genomic DNA during meiosis. Required for rad-51 recruitment onto ssDNA gaps generated at stalled replication fork barriers.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- RFS-1 Interacting Partner
- Helicase POLQ-like
- DNA repair protein RAD51 homolog
- Crossover junction endonuclease MUS81
- RecQ-like DNA helicase blm-1
- DNA repair and recombination protein RAD54-like
- ATP-dependent helicase wrn-1
- DNA repair endonuclease XPF
- FANCD2
- Regulator of telomere elongation helicase 1 homolog
Sequence:
MDPSENVFKYETAYDLLVRLGAERLFLRTCLSILDPVLELHPGKCYEIDGDLGVGKTQICYSFAAKFLQTKKTAKMGWIGATPLRTDHLLLHIEHFGNQTNEDILDRIVCKRVEKIAELQDSLTRFLDTINLQLVIVENIDAILHDTVYHKEMGRSMQSDVVERIRKLTKLEITVILTNHITHWRGYPAPALGAFWSSQINNRFFIEKRNDDSDIRIVSAMKGEQDDGMNRIEFKIGDRGLKAVE
Protein: Gtpbp5 protein (Q8R2K9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVSTRLVLARTCTVFEGVLKWAPSTRAVLRPSHLLLQASCRLLSVGIVDHAKHREPSGKKVLSEKKLKRHFVDHRRVLVRGGSGGSGMSCFHSEPRKEFGGPDGGDGGNGGHIILRVDQQVKSLSSVLSQYQGFSGEDGGSKNCSGRGGATLYIQWQTSQASSEVHTRTRAWASASSGTSSVVASSCLW
Protein: YTH domain-containing protein ECT2 (Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 2) (Q9LJE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (Probable). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (Probable). Binds preferentially in the 3'UTRs of target genes. May play dual roles in regulating 3'UTR processing in the nucleus and facilitating mRNA stability in the cytoplasm. Required for the correct timing of leaf formation and normal leaf morphology. Functions redundantly with ECT3. Required for proper trichome branching and morphology. Controls trichome morphology by binding transcripts related to trichome morphogenesis and affecting their stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29618631, ECO:0000269|PubMed:29643069}. Nucleus {ECO:0000269|PubMed:29716990}. Note=Localizes to cytoplasmic foci upon drought stress (PubMed:29643069). Relocates to cytoplasmic stress granules upon heat stress (PubMed:29618631). {ECO:0000269|PubMed:29618631, ECO:0000269|PubMed:29643069}.
Interaction partners:
- RNA demethylase ALKBH10B
- N
- RNA demethylase ALKBH9B
- CBL-interacting serine/threonine-protein kinase 1
- FKBP12-interacting protein of 37 kDa
- N6-adenosine-methyltransferase non-catalytic subunit MTB
- E3 ubiquitin-protein ligase HAKAI homolog
- Protein virilizer homolog
Sequence:
MATVAPPADQATDLLQKLSLDSPAKASEIPEPNKKTAVYQYGGVDVHGQVPSYDRSLTPMLPSDAADPSVCYVPNPYNPYQYYNVYGSGQEWTDYPAYTNPEGVDMNSGIYGENGTVVYPQGYGYAAYPYSPATSPAPQLGGEGQLYGAQQYQYPNYFPNSGPYASSVATPTQPDLSANKPAGVKTLPADSNNVASAAGITKGSNGSAPVKPTNQATLNTSSNLYGMGAPGGGLAAGYQDPRYAYEGYYAPVPWHDGSKYSDVQRPVSGSGVASSYSKSSTVPSSRNQNYRSNSHYTSVHQPSSVTGYGTAQGYYNRMYQNKLYGQYGSTGRSALGYGSSGYDSRTNGRGWAATDNKYRSWGRGNSYYYGNENNVDGLNELNRGPRAKGTKNQKGNLDDSLEVKEQTGESNVTEVGEADNTCVVPDREQYNKEDFPVDYANAMFFIIKSYSEDDVHKSIKYNVWASTPNGNKKLAAAYQEAQQKAGGCPIFLFFSVNASGQFVGLAEMTGPVDFNTNVEYWQQDKWTGSFPLKWHIVKDVPNSLLKHITLENNENKPVTNSRDTQEVKLEQGLKIVKIFKEHSSKTCILDDFSFYEVRQKTILEKKAKQTQKQVSEEKVTDEKKESATAESASKESPAAVQTSSDVKVAENGSVAKPVTGDVVANGC
Protein: Down-regulator of invasive growth 2 (Regulator of STE12 protein 2) (Regulator of sterile twelve 2) (Q03373)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DIG2 and DIG1 are negative regulators of the filamentation and pheromone induced mating program. DIG1 and DIG2 inhibit the transcriptional activity of STE12 by direct protein-protein interaction. DIG2 binds to the DNA binding domain (DBD) of STE12 and thus inhibits transcription when overexpressed.
Subcellular location: Nucleus.
Interaction partners:
- Down-regulator of invasive growth 1
- Protein STE12
- Mitogen-activated protein kinase FUS3
- Mitogen-activated protein kinase KSS1
- Ty transcription activator TEC1
- Serine/threonine-protein kinase STE11
- Nuclear fusion protein FUS1
- Protein STE5
- Serine/threonine-protein kinase STE7
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MNKEEQEDPQQEQISTVQENDPRNLQQLGMLLVSPGLDEDRLSEKMISKIKKSRDIEKNQKLLISRLSQKEEDHSGKPPTITTSPAEKTVPFKSLNHSLKRKRVPPALNFSDIQASSHLHGSKSAPPNITRFPQHKNSLRVRYMGRMAPTNQDYHPSVANSYMTATYPYPYTGLPPVPCYPYSSTPTQTHAYEGYYSPMYPGPLYNNGIIPADYHAKRKKLAGRSPHLEDLTSRKRTFVSKHHNGDPIISKTDEDIECSVTKNSLSEGASLNDDADDDNDKERIIIGEISLYDDVFKFEVRDDKNDYMKACETIWTEWHNLKK
Protein: PGL/p-HBAD biosynthesis rhamnosyltransferase (EC 2.4.1.-) (P9WN09)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of the first rhamnosyl residue on p-hydroxybenzoic acid or phenolphthiocerol derivatives to form, after O-methylation at position 2 of the sugar unit, mono-O-methyl-glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-phenolphthiocerol dimycocerosate (also called mycoside B) during p-hydroxybenzoic acid derivatives (p-HBAD) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit B
Sequence:
MRVSCVYATASRWGGPPVASEVRGDAAISTTPDAAPGLAARRRRILFVAEAVTLAHVVRPFALAQSLDPSRYEVHFACDPRYNQLLGPLPFRHHAIHTIPSERFFGNLTQGRFYAMRTLRKYVEADLRVLDEIAPDLVVGDLRISLSVSARLAGIPYIAIANAYWSPYAQRRFPLPDVIWTRLFGVRLVKLLYRLERPLLFALQCMPLNWVRRRHGLSSLGWNLCRIFTDGDHTLYADVPELMPTYDLPANHEYLGPVLWSPAGKPPTWWDSLPTDRPIVYATLGTSGGRNLLQLVLNALAELPVTVIAATAGRSDLKTVPANAFVADYLPGEAAAARSAVVVCNGGSLTTQQALVAGVPVIGVAGNLDQHLNMEAVERAGAGVLLRTERLKSQRVAGAVMQVISRSEYRQAAARLADAFGRDRVGFPQHVENALRLMPENRPRTWLAS
Protein: Matrix protein (M protein) (P0DOE7)
Organism: Human respiratory syncytial virus A (strain A2)
Function: Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it inhibits host cell transcription through direct binding to host chromatin. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
Subcellular location: Virion {ECO:0000269|PubMed:24672034}. Host cytoplasm {ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:19297465, ECO:0000269|PubMed:24672034, ECO:0000269|PubMed:29028839, ECO:0000269|PubMed:37712706}. Host nucleus {ECO:0000269|PubMed:12827470, ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:16171404, ECO:0000269|PubMed:19297465, ECO:0000269|PubMed:34685766}. Host cell membrane {ECO:0000269|PubMed:12350355}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=In the cytoplasm, associates with inclusion bodies (PubMed:23903836). During bud formation, associates at the inner side of the plasma membrane of infected cells. {ECO:0000269|PubMed:23903836, ECO:0000305}.
Interaction partners:
Sequence:
METYVNKLHEGSTYTAAVQYNVLEKDDDPASLTIWVPMFQSSMPADLLIKELANVNILVKQISTPKGPSLRVMINSRSAVLAQMPSKFTICANVSLDERSKLAYDVTTPCEIKACSLTCLKSKNMLTTVKDLTMKTLNPTHDIIALCEFENIVTSKKVIIPTYLRSISVRNKDLNTLENITTTEFKNAITNAKIIPYSGLLLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATRFAIKPMED
Protein: GH14494p (Q9VI09)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRVLLPLVGCLLAVQAGSVEEVFRSHQVVPDVIPEPPNQLLKVTYSNNLVAKDGVELTPTQVKDQPVVEWDAQPGEFYTLIMTDPDAPSRAEPKFREFKHWILANIAGNDLASGEPIAEYIGSGPPQGTGLHRYVFLLYKQSGKLEFDEERVSKRSRKDRPKFSAAKFAINHELGNPIAGTFYQAQYDDYVPKLHKQLSEN
Protein: Probable rRNA-processing protein ebp2 (O13802)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the processing of the 27S pre-rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14655046}.
Interaction partners:
- Ribosome biogenesis protein brx1
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein nsa1
- AdoMet-dependent rRNA methyltransferase spb1
- GTPase grn1
- Pescadillo homolog
- Ribosome biogenesis protein erb1
- Uncharacterized RNA-binding protein C1827.05c
- Brix domain-containing protein C4F8.04
- 60S ribosome subunit biogenesis protein nip7
Sequence:
MAGIESKQRRAQKKAAKAAMKEKKNKESNESSTSVEALNEKEMINTIKSPIIETADTADQENESEGSDEVELSDLEGIELEEDADLIRKRKLAINNTVALENIYERIKYPDDISFVENQAVTTKEPIIIENVEDDLARELAFYKQGVSSVKAAFAKLREANVLISRPHDYFAEMLKSDDHMEKVRQELIKEATAKKLSQQAKKQRELKKFGKQVQLAKQEERQREKKETLEKINLLKRKHTGGDLTTEDDFDIALSSASADTFKKGSRSTKSRPQPNPKRQKKNEKYGFGGPKHRSKSNDLDSLAATEFGRKGLKNIKSKKRPGKARREKARK
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 7.1.1.2) (G3V0I5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364066}; Matrix side {ECO:0000256|RuleBase:RU364066}.
Interaction partners:
Sequence:
MLATRRLLGWSLPARVSTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRGDWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS
Protein: ShKT domain-containing protein (Q9GYJ2)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin-like domain-containing protein
- Intrinsically Disordered Protein, class B
- Uncharacterized protein
- Glycoside hydrolase family 19 catalytic domain-containing protein
- Activated in Blocked Unfolded protein response
- Sulfate permease family protein 3
Sequence:
MNKSIFLVGAFLAVAFGQTCSPDRITAPCDVGLPCETGSTCDLTLLSCCLNADLITTVVPSNVVTDASGSTVTVATTIRSGSTVTSRTSSGTGCVDRVNSATGTSDCANRRALCNDANYFDVMTQQCPKTCGRCSSFSSTPTTGTCTDLKNPKTGTSDCASLRSFCNDSNYIDLMRTQCPRTCGFCGSSGSSSTTRSSATVSSGTCVDRVNPATGRSDCASNIGLCNNSAYQSVMRAQCPRTCGFCTSG
Protein: Photosystem I reaction center subunit III, chloroplastic (Light-harvesting complex I 17 kDa protein) (PSI-F) (P12355)
Organism: Spinacia oleracea (Spinach)
Function: Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
Subcellular location: Plastid, chloroplast thylakoid lumen.
Interaction partners:
Sequence:
MSFTIPTNLYKPLATKPKHLSSSSFAPRSKIVCQQENDQQQPKKLELAKVGANAAAALALSSVLLSSWSVAPDAAMADIAGLTPCKESKQFAKREKQALKKLQASLKLYADDSAPALAIKATMEKTKKRFDNYGKYGLLCGSDGLPHLIVSGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAIRDEKKPTQKEIIIDVPLASSLLFRGFSWPVAAYRELLNGELVDNNF
Protein: Glutathione reductase (GR) (GRase) (EC 1.8.1.7) (P41921)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Maintains high levels of reduced glutathione in the cytosol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23613772}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23613772}. Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}. Peroxisome {ECO:0000269|PubMed:36164978}.
Interaction partners:
- Glutathione synthetase GSH2
- Thioredoxin reductase 1
- Thioredoxin reductase 2, mitochondrial
- Peroxiredoxin PRX1, mitochondrial
- Glutathione peroxidase-like peroxiredoxin 1
- Glutathione peroxidase-like peroxiredoxin 2
- AP-1-like transcription factor YAP1
- Glutamate--cysteine ligase
- Transcriptional regulator URE2
- Glutathione S-transferase 1
Sequence:
MLSATKQTFRSLQIRTMSTNTKHYDYLVIGGGSGGVASARRAASYGAKTLLVEAKALGGTCVNVGCVPKKVMWYASDLATRVSHANEYGLYQNLPLDKEHLTFNWPEFKQKRDAYVHRLNGIYQKNLEKEKVDVVFGWARFNKDGNVEVQKRDNTTEVYSANHILVATGGKAIFPENIPGFELGTDSDGFFRLEEQPKKVVVVGAGYIGIELAGVFHGLGSETHLVIRGETVLRKFDECIQNTITDHYVKEGINVHKLSKIVKVEKNVETDKLKIHMNDSKSIDDVDELIWTIGRKSHLGMGSENVGIKLNSHDQIIADEYQNTNVPNIYSLGDVVGKVELTPVAIAAGRKLSNRLFGPEKFRNDKLDYENVPSVIFSHPEAGSIGISEKEAIEKYGKENIKVYNSKFTAMYYAMLSEKSPTRYKIVCAGPNEKVVGLHIVGDSSAEILQGFGVAIKMGATKADFDNCVAIHPTSAEELVTMR