wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA-aminoacylation cofactor arc1 (Q9P6K7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable methionine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Probable methionine--tRNA ligase, mitochondrial
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit A
- Isoleucine--tRNA ligase, cytoplasmic
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MSFLWAKEFCVLKYPYKLFITHKFSYLLRFETVTLNNIRSPQFYAKLTFSHHQPTVSGTMSTELKFISKYLQISIPETKEGPVSSLFKAVSEQKPELLGNTDFEKAQILEWTTKAFSPIETQSIVEQLDEFLKSSTFIAQDSGISVADLAVYARIHSYICGLSAKEGYKLNNVCRWFDFIQHQESVMEAANSMSMKLANIDLNAPKIQRPSVIKKDKKEKKEGKPSQEASVKSVEKAPKGLEGAKKEKQNKKEKKDKKDKKDKKEKAPKEPPKAATPVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGDAEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCASSPDKSVVEFVLPPENAEIGDRLTFEGFDTEEPEAQLNPKRKIWEAIQPGFTSGEDLICGYKDESGLHRLFVKGKKDLGFCKAQTVVNGTLS
Protein: DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) (Q80YR6)
Organism: Mus musculus (Mouse)
Function: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (By similarity). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (By similarity). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (By similarity). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (By similarity). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (By similarity). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chromatin following DNA damage. {ECO:0000250|UniProtKB:Q99708}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-associated RING domain protein 1
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- Double-strand break repair protein MRE11
- Nibrin
- Exonuclease 1
- Protein unc-13 homolog B
- DNA repair protein RAD50
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MSISGSGCGSPNSADASNDFKELWTKLKEYHDKEVQGLQVKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLKLITELMNEKNTLQEENKKLSEQLQQKMENGQQDQVAELACEENIIPDSPVTSFSFSGINRLRKKENLHVRYVEQTHTKLERSLCTNELRKISKDSAPAPVNSEEHEILVADTCDQNHSPLSKICETSSYPTDKTSFNLDTVVAETLGLNGQEESEPQGPMSPLGSELYHCLKEDHKKHPFMESARSKEDSLRFSDSASKTPPQEFTTRASSPVFGATSTVKAHLGLNTSFSPSLLDIGKKNLLKTAPFSNIAVSRSEKVRSKSEDNALFTQHSLGSEVKVISQSFSSKQILTNKTVSDSVDEQCSADHMNTTVADKYLVPLKSLGGKASKRKRTEEESEHAVKCPQACFDKENALPFPMENQFSMNGDHVMDKPLDLSDRFAATQRQEKNHGNETSKNKLKQATIYEALKPIPKGSSSGRKALSGDCMPAKDSWETYCLQPRSLQSSSKFSPDQKTPLQIKEENPVFKTPPCSQESLETENLFGDVKGTGSLVPTKVKSRAVHGGCELASVLQLNPCRVAKTKALPSNQDTSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETVLLKMKKQEQKERSPNGDIKMNDSLEDMFDRTTHEEYESCLADSFSQVPDEEELPDTTKKTNIPADKQDGVKQKAFVGPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCLERGYIKEDLDLSPRPKRRQPYNAVFSPKGKEQRT
Protein: Sugar transporter SWEET1 (RAG1-activating protein 1) (Solute carrier family 50 member 1) (D3ZH22)
Organism: Rattus norvegicus (Rat)
Function: Mediates sugar transport across membranes. May stimulate V(D)J recombination by the activation of RAG1 (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14991772}; Multi-pass membrane protein {ECO:0000269|PubMed:14991772}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=May also localize to the endoplasmic reticulum.
Interaction partners:
Sequence:
MEAGGVADSFLSSACVLFTLGMFSTGLSDLRHMQRTRSVDNIQFLPFLTTDVNNLGWLSYGVLKGDGTLIIVNTVGAVLQTLYILAYLHYSPQKHAVLLQTATLLAVLLLGYGYFWLLVPDLETRLQQLGLFCSVFTISMYLSPLADLAKIIQTKSTQRLSFSLTIATLLSSTSWSIYGFRLKDPYITVPNLPGILTGFIRLVLFYKYPPEQDTKYRLLQT
Protein: Serine/threonine-protein kinase BSK8 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 8) (Q9FHD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK4, BSK6 and BSK7. Involved in the regulation of sucrose-phosphate synthase 1 (SPS1) in the context of sucrose resuply after starvation. Activates BSL2, a phosphatase that may dephosphorylate SPS1, leading to the activation of SPS1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21726371}; Lipid-anchor {ECO:0000305|PubMed:12912986}.
Interaction partners:
- Serine/threonine-protein phosphatase BSU1
- Protein BRASSINOSTEROID INSENSITIVE 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Shaggy-related protein kinase eta
- Shaggy-related protein kinase iota
- Protein BRASSINAZOLE-RESISTANT 1
- Putative acyl-activating enzyme 19
Sequence:
MGCEVSKLSALCCVSESGRSNPDVTGLDEEGRGESNDLPQFREFSIETIRNATSGFAAENIVSEHGERAPNVVYKGKLENQRRIAVKRFNRKSWPDSRQFLEEAKAVGQLRNHRMANLLGCCYEDEERLLIAEFMPNETLAKHLFHWESQPMKWAMRLRVALHIAQALEYCTSKGRALYHDLNAYRVLFDDDANPRLSCFGLMKNSRDGKSYSTNLAFTPPEYLRTGRVTPESVIYSFGTLLLDLLSGKHIPPSHALDLIRDRNIQMLMDSGLEGQFSSDDGTELIRLASRCLQYEPRERPNPKSLVSAMIPLQKDLEIASHQLLGVPNSATTTALSPLGEACLRSDLTAIHEIIEKLGYKDDEGATTELSFQMWTDQMQDTLVFKKKGDSAFRHKDFAKAIECYSQFIEVGTMGSPTVHARQSLCYLMNDMPREALNNAMQAQVISPAWHIASYLQAVALSALGQENEAHTALKDGAMLESKRNPL
Protein: Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1 (EC 2.5.1.47) (EC 4.4.1.9) (Beta-substituted Ala synthase 4;1) (ARAth-Bsas4;1) (Cysteine synthase D1) (AtcysD1) (O-acetylserine (thiol)-lyase 3) (Q9S6Z7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a cysteine synthase. The cysteine synthesis reaction is more efficient than the cyanoalanine synthase activity.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10845460}.
Interaction partners:
- Assimilatory sulfite reductase
- Cystathionine beta-lyase, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Methionine gamma-lyase
- L-cysteine desulfhydrase
- Probable L-cysteine desulfhydrase, chloroplastic
- Phosphoserine aminotransferase 1, chloroplastic
- Adenosylhomocysteinase 2
- Adenosylhomocysteinase 1
Sequence:
MEEDRCSIKDDATQLIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKERIAYGMIKDAEDKGLITPGKSTLIEATSGNTGIGLAFIGAAKGYKVVLTMPSSMSLERKIILLALGAEVHLTDPSKGVQGIIDKAEEICSKNPDSIMLEQFKNPSNPQTHYRTTGPEIWRDSAGEVDILVAGVGTGGTLSGSGRFLKEKNKDFKVYGVEPTESAVISGGKPGTHLIQGIGAGLIPDNLDFNVLDEVIQVTSVEAIETAKLLALKEGLLVGISSGAAAAAAIKVAKRPENAGKLIVVIFPSGGERYLSTSLFESVRHEAENLPIQ
Protein: Beta-galactoside alpha-2,6-sialyltransferase 2 (Alpha 2,6-ST 2) (EC 2.4.3.1) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2) (ST6Gal II) (ST6GalII) (Sialyltransferase 2) (Q76K27)
Organism: Mus musculus (Mouse)
Function: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- Beta-1,4-galactosyltransferase 3
- Beta-galactoside alpha-2,6-sialyltransferase 1
Sequence:
MKPHLKQWRQRMLFGIFVWGLLFLAIFIYFTNSNPAAPMPSSFSFLERRGLLPLQGKQRVIMGALQEPSLPRSLDASKVLLDSHPENPFHPWPGDPQKWDQAPNGFDNGDEFFTSQVGRKSQSAFYPEEDSYFFVADQPELYHHRQGALELPSPGETSWRSGPVQPKQKLLHPRRGSLPEEAYDSDMLSASMSRAFLYRLWKGAVSSKMLNPRLQKAMRYYMSFNKHGVRFRRRGRREATRTGPELLCEMRRRVRVRTLDGREAPFSGLGWRPLVPGVPLSQLHPRGLSSCAVVMSAGAILNSSLGEEIDSHDAVLRFNSAPTRGYEKDVGNKTTVRIINSQILANPSHHFIDSALYKDVILVAWDPAPYSANLNLWYKKPDYNLFTPYIQHRRKYPTQPFYILHPKFIWQLWDIIQENTREKIQPNPPSSGFIGILIMMSMCKEVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLVQRLNTGTQADLHHKGKVVLPGFQTLRCPVTSPNNTHS
Protein: mRNA cap guanine-N(7) methyltransferase (EC 2.1.1.56) (mRNA (guanine-N(7))-methyltransferase) (mRNA cap methyltransferase) (P32783)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for methylating the 5'-cap structure of mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:11018011}.
Interaction partners:
- mRNA-capping enzyme subunit alpha
- mRNA-capping enzyme subunit beta
- Transcription elongation factor SPT5
- Protein NRD1
- DNA-directed RNA polymerase II subunit RPB1
- Serine/threonine-protein kinase KIN28
- Decapping and exoribonuclease protein 1
- DNA-directed RNA polymerase II subunit RPB2
- Nuclear cap-binding protein subunit 2
- Serine/threonine-protein kinase BUR1
Sequence:
MSTKPEKPIWMSQEDYDRQYGSITGDESSTVSKKDSKVTANAPGDGNGSLPVLQSSSILTSKVSDLPIEAESGFKIQKRRHERYDQEERLRKQRAQKLREEQLKRHEIEMTANRSINVDQIVREHYNERTIIANRAKRNLSPIIKLRNFNNAIKYMLIDKYTKPGDVVLELGCGKGGDLRKYGAAGISQFIGIDISNASIQEAHKRYRSMRNLDYQVVLITGDCFGESLGVAVEPFPDCRFPCDIVSTQFCLHYAFETEEKARRALLNVAKSLKIGGHFFGTIPDSEFIRYKLNKFPKEVEKPSWGNSIYKVTFENNSYQKNDYEFTSPYGQMYTYWLEDAIDNVPEYVVPFETLRSLADEYGLELVSQMPFNKFFVQEIPKWIERFSPKMREGLQRSDGRYGVEGDEKEAASYFYTMFAFRKVKQYIEPESVKPN
Protein: Centrosomal protein of 70 kDa (A8WFT5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MEQEEQREWDAVNRLLQHHGFKPVSFADPIENKNLAELVLLERKSASDVRLMLKTMLSDSERRQGLIQELIQSNSQLKEEVQQHQTRAARQSQRAAELENILDGVKVKVQDLEDSYVSKVAQQHQQFQQLQQEKRDAEKCFQSVEQKLIQEQQQASRLQKKLQYAVREEERRATRQKQTFQQILHRSARPNSTNDQQILDIIDLYESQMQQLRNELKLYKGEKDSSNSQKSRSTVDKDVTDASSTYKTLLKSYQEQLKESKAQREELRTEIQRLKEDLESRPTIKELKTCKQQLRRLDRIIQQSNIRSAQELKSQDSTEKPVTDNASIQSLDISTCRRLLTDVCKELDVQNINHLISTVNAQRNQAGSAFRLQKILYDITAVLTDHRAPLGLLRQRVPSNLEFNEEFDMIVPSLEVWSQQLTSLSDLHHALINLQKRLLPLQPESGSTALSDSVRVEDLMLIVDTLLDETQPDDKVLRSPTRHTLESIVAHFQKLFDVPSLTGIYPRMTELYSKLGEMNNAMRNLRDLLDLDDKAPASEVVSSVSSVLSQSGQEICSLLESRDIDSIILKLKEHEEFFPAFHSFMLELLQTLDVQTLDDVLPRIRSLKG
Protein: Contactin-4 (Brain-derived immunoglobulin superfamily protein 2) (BIG-2) (Q8IWV2)
Organism: Homo sapiens (Human)
Function: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Secreted {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase gamma
- Amyloid-beta precursor protein
- Neuroligin-1
- Neurexin-1
- Contactin-associated protein-like 2
- Neuroligin-4, X-linked
- Formylglycine-generating enzyme
- Astrotactin-2
- Cadherin-9
- Neuroligin-3
Sequence:
MRLPWELLVLQSFILCLADDSTLHGPIFIQEPSPVMFPLDSEEKKVKLNCEVKGNPKPHIRWKLNGTDVDTGMDFRYSVVEGSLLINNPNKTQDAGTYQCTATNSFGTIVSREAKLQFAYLDNFKTRTRSTVSVRRGQGMVLLCGPPPHSGELSYAWIFNEYPSYQDNRRFVSQETGNLYIAKVEKSDVGNYTCVVTNTVTNHKVLGPPTPLILRNDGVMGEYEPKIEVQFPETVPTAKGATVKLECFALGNPVPTIIWRRADGKPIARKARRHKSNGILEIPNFQQEDAGLYECVAENSRGKNVARGQLTFYAQPNWIQKINDIHVAMEENVFWECKANGRPKPTYKWLKNGEPLLTRDRIQIEQGTLNITIVNLSDAGMYQCLAENKHGVIFSNAELSVIAVGPDFSRTLLKRVTLVKVGGEVVIECKPKASPKPVYTWKKGRDILKENERITISEDGNLRIINVTKSDAGSYTCIATNHFGTASSTGNLVVKDPTRVMVPPSSMDVTVGESIVLPCQVTHDHSLDIVFTWSFNGHLIDFDRDGDHFERVGGQDSAGDLMIRNIQLKHAGKYVCMVQTSVDRLSAAADLIVRGPPGPPEAVTIDEITDTTAQLSWRPGPDNHSPITMYVIQARTPFSVGWQAVSTVPELIDGKTFTATVVGLNPWVEYEFRTVAANVIGIGEPSRPSEKRRTEEALPEVTPANVSGGGGSKSELVITWETVPEELQNGRGFGYVVAFRPYGKMIWMLTVLASADASRYVFRNESVHPFSPFEVKVGVFNNKGEGPFSPTTVVYSAEEEPTKPPASIFARSLSATDIEVFWASPLEKNRGRIQGYEVKYWRHEDKEENARKIRTVGNQTSTKITNLKGSVLYHLAVKAYNSAGTGPSSATVNVTTRKPPPSQPPGNIIWNSSDSKIILNWDQVKALDNESEVKGYKVLYRWNRQSSTSVIETNKTSVELSLPFDEDYIIEIKPFSDGGDGSSSEQIRIPKISNAYARGSGASTSNACTLSAISTIMISLTARSSL
Protein: Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (Heat shock 70 kDa protein 9) (A0A384P5G6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISASRAAAARLVGAAASRGPTAARHQDSWNGLSHEAFRLVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ
Protein: FHA domain-containing protein, putative (Q8IEN7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- RNA-binding protein, putative
- Pre-mRNA-splicing factor CWC26, putative
- Pre-mRNA-processing protein 45, putative
- Splicing factor 3B subunit 1, putative
- Pre-mRNA-splicing factor CWC22, putative
- RNA helicase
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA-processing-splicing factor 8, putative
- Pre-mRNA-splicing factor CLF1, putative
- Pre-mRNA-splicing factor RDS3, putative
Sequence:
MNTEEKINTSNDAEDDNNECVKLKKKIENEKYDINNLKDDDVYLSADSSNSYRYDNHVNKKSIKENINEISTNRSQSKKEKDSNEDMYNDKKRNNYKSSSESKEKGDKYCKKDKYDKHDKYDKNGKYDKHDKYDKYNKYDKHDKYDKHNKYDKHDKYDKHDKYDKHDKYDKHDKYDKYNKYDKHDKYDKHNKYDKHNKYDKHDKYDKHDKYDKHDKYNKHDKHDRHDKYDKQMDKIYILKKSSEHTRTSKDNSYYDSKRKYRNITSEDEEMKHHKTVDHNARKKSKSSKILVDKYSSDVENDKKGVEEKYKDKNKNSYQTLKKNDNNINEKEYDKNRSSISHYHNKDKYNKYDKYGKQNHNIRYNEQDIKRKSTKHYEKENFNNTHKGKNKNEKDEEQSEEEKEKKNVQKKETQNFNPSGLLAQEKIYKNGIEMKYTESIDAEKPDKKWRLYMFKDSNNNEPQKILHIHDKSYYLIGKEQLAVDIQLNNISISKQHAVIQFKKHESKILPFLLDLNSTNGTYINNEKIQPNKYYELRETDIIRFGSSNREFVLLHDTCQAD
Protein: Niemann-Pick type C-2h, isoform B (Q8IMH5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRLSSLLPVAFALVLSSVSAEIVNFQTCEDSVDSCSISQVRVTPCPEANANAACHIRRRHRFTMSFDFTPHFDADTLVASLGWAKSENVELPLLTMDQEACNPYTIRWALKDPVSQKRCCFTIDIKVVR
Protein: LD06146p (Q8MSY3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLHWYYFPESYDSWAVNNFDLPDHIPENPESPAERWRVSASWIVDLEQYNEWMAEEDYEVDEQGKKKTHKQRMSIDDIMSFGDEKKKPAASSGGGKQKRRRSPSPASSASTSKPGKRKRSPAVVHKKSRNDDDDEDLTRDLDDPPAEPNVQEVHKANAALQSTASPAPGGKSRGDNDMMPIKGGTMTDLDDEMTGGSAAQAMSTGDGENSQTGKTSDNSNTQEFSSSAKEDMEDNVTEQTHHIIVPSYSAWFDYNSIHVIEKRAMPEFFNSKNKSKTPEIYMAYRNFMIDTYRLNPTEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQIDADVRPTPMGPPPTSHFHILSDTPSGLQSINPQKTQQPSAAKTLLDLDKKPLGKDGGLELGDKSGLTGIKTEALENGAAGGLSSGVSQFGLKLDQYAKKPAAMRNRTAASMAREWTDQETLLLLEGLEMHKDDWNKVCEHVGSRTQDECILHFLRLPIEDPYLEDDGGFLGPLACQPIPFSKSGNPIMSTVAFLASVVDPRVAAAAAKAAMEEFAAIKDEVPATIMDNHLKNVEKASAGGKFNPNFGLANSGIAGTGNDKDDEEGKEGGASASAGGSDEEMKDLSKKDDDAKSKDNTKSDKTNTNTDSSSTSSSATGNTNNTDKKPKESSGSSPSGDKSAIKSDKSNKSSPTETAAAASGGEVDIKTEDSSGDGETKDGTEAKEGTGTGTGPLAVPKEGTFSENNMQTAAAAALASAAVKAKHLAALEERKIKSLVALLVETQMKKLEIKLRHFEELEATMEREREGLEYQRQQLITERQQFHLEQLKAAEFRARQQAHHRLQQELQGQAAAGSMILPQQQQLPQAQQPQQQQQTLPPHPHLAQQQQLPPHPHQLPPQSQPLAGPTAQHQPLPPHVVSSPNGAPFAAPPISLTGGLPPGAPTAIVTNPSDQTGPVAAGAAQSQAPTPMDTTPPSSGPVSDANAPPGSAMPPGGIPPANTAPIAGVAPSS
Protein: 39 protein (Bacteriophage SPP1 complete nucleotide sequence) (Q38151)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Interaction partners:
Sequence:
MIEKDVVQILKAVSEFYPGRFQPDDLKGTVKAWHRVLAEYELEEIMNNLTDYAKVNKFPPTVSDLLKAQSEQRDRFIPSYEETQRILKEQAEAEEAARNDPDLQAAQEENMRKIREMLGINRGGAR
Protein: EGF-like domain-containing protein (Q382Y5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMIWLQRKVFLLGLFCVLVGMIACVNGHANASCPESCDTAGRWCEIRFNRGGRVSVGECNASSFTCVCNDAVDITVTRNEESCWWSGSFDMTNNVSEESLCSADTAQCPQTCQQAGEQITRCAGSVLCTEDGDGYIFTCAISEGTILHINKSVYGCLTTIVEPELHCNPKVTCSGHGYCVNPHTLSNSCVCFSDPINGYWVGANCSECHADYGPGGGNCTQRTSTIRIILSSIGSTWAMVLPNMVVLFLFVVLGLMRRESESDRSFQSTVLRKTGLSAVQVARRNRCGLFNPKLIPPRPPQSRCFLNEGEGRAKRRGPPAY
Protein: Chaperone protein ClpD1, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpD homolog 1) (Casein lytic proteinase D1) (Q6H795)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Molecular chaperone that may function in heat stress response. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. Chaperone involved in response to abiotic stresses. Plays a positive role during dehydration and salt stress.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Os08g0432500 protein
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MEVCCCSTSSAVPGRRFAAAGAAAAAVAARWGAVGVGRAVVLAHPLRPAPRGGHAHAQQAGARRARRAVVRAVFERFTERAVKAVVLSQREAKGLGEGAVAPRHLLLGLIAEDRSAGGFLSSGINIERAREECRGIGARDLTPGAPSPSGSGLEMDIPFSGSCKRVFEVAVEFSRNMGCSFISPEHLALALFTLDDPTTNSLLRSLGADPSQLASVALTRLQAELAKDCREPAGASSFKVPKKSPAGAGRSAFSKSLNSKKEKGALDQFCLDLTTQASGGFIDPIIGREEEIERVVQIICRRTKNNPILLGEAGVGKTAIAEGLALRIANGDVPIYLVAKRIMSLDVGLLIAGAKERGELESRVTSLIREVREAGDVILFIDEVHNLIGSGTVGKGKGAGLDIGNLLKPPLARGELQCIAATTLDEHRMHFEKDKALARRFQPVLVEEPSQDDAVKILLGLREKYETYHKCKFTLEAINAAVYLSARYIPDRQLPDKAIDLIDEAGSRARMESFNRKKEGQSSILLKSPDEYWQEIRAAQNMHEVVSSNQMKYSPRQENGSAAIKAPSEDMNELTSELQVEEPIVVGTEEIARVASLWSGIPVQQLTADDRKLLVGLDGELRKRVIGQDDAVMAISRAVKRSRVGLNDPDRPIATLLFCGPTGVGKTELTKALAASYFGSESAMLRLDMSEYMERHTVSKLIGSPPGYIGYGETGTLTEAVRRKPFTVVLLDEIEKAHPDIFNILLQIFEDGHLSDSQGRRVSFKNTLIVMTSNIGSTSISKGRRSMGFMTEDTESSSYVAMKSLVMEELKAFFRPELLNRIDEMVVFRPLEKTQMLAILDIILQEVKGRLLALGIGLEVSDAMKDLICEEGYDKSYGARPLRRAVTHLIEDVISEAILFGEYKPGDTILMDIDAGGKLCMSHLNEKVVQLSDPTRTF
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate pyrophosphate decarboxylase) (Mevalonate-5-diphosphate decarboxylase) (MDDase) (O13963)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Mvd1 converts diphosphomevalonate into isopentenyl diphosphate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mevalonate kinase
- Phosphomevalonate kinase
- Isopentenyl-diphosphate delta-isomerase
- Farnesyl pyrophosphate synthase
- Geranylgeranyl pyrophosphate synthase
- Acetyl-CoA acetyltransferase
- Lanosterol synthase erg7
- Decaprenyl-diphosphate synthase subunit 1
- Hydroxymethylglutaryl-CoA synthase
- Squalene synthase
Sequence:
MDKKVYQCTVSAPVNIAVIKYWGKRDVALNLPTNSSISVTLSQDDLRTVTTASCSEKFENDTLWLNGNAEEIFANKRLRVCVEELRKARLDLEEENDDLDKIGALKLHVVSENNFPTAAGLASSAAGYAAFCEAIARLYDLPWTPTQLSRIARQGSGSACRSLFGGYVAWEMGELHSGADSVAVQVEPVENWPEIRVAVLVASAAKKGVSSTAGMQATVASSTLFQHRIQNIVPQRIQEMKTAIRERDFETFAKLTMTDSNQFHACCLDTFPPIFYLNDTSRAVIRVVENINATAGKTIAAYTFDAGPNAVIYFLEENSEIVLNTLYAVTKNAEGWSKQYGSSPVTVDSAAANIVSSGISRVILTRVGNGPRVLTIDESLIDASGNPKFIGSH
Protein: DnaJ protein homolog 1 (DROJ1) (Q24133)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm.
Interaction partners:
- Heat shock protein 68
- Heat shock protein 83
- Hsc70Cb, isoform G
- Myeloid leukemia factor
- Heat shock 70 kDa protein cognate 4
- Heat shock protein 26
- LD01461p
- LD43819p
- Stress-induced-phosphoprotein 1
- Nucleotide exchange factor Sil1
Sequence:
MGKDFYKILGLERKASDDEIKKAYRKLALKYHPDKNKSPQAEERFKEIAEAYEVLSDKKKRDIFDNYGEDGLKGGQPGPDGGGQPGAYTYQFHGDPRATFAQFFGSSDPFGAFFTGGDNMFSGGQGGNTNEIFWNIGGDDMFAFNAQAPSRKRQQDPPIEHDLFVSLEEVDKGCIKKMKISRMATGSNGPYKEEKVLRITVKPGWKAGTKITFPQEGDSAPNKTPADIVFIIRDKPHSLFKREGIDLKYTAQISLKQALCGALVSVPTLQGSRIQVNPNHEIIKPTTTRRINGLGLPVPKEPSRRGDLIVSFDIKFPDTLAPSLQNQLSELLPN
Protein: Peptidyl-prolyl cis-trans isomerase Fkbp12 (PPIase Fkbp12) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (Macrolide-binding protein) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (P48375)
Organism: Drosophila melanogaster (Fruit fly)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Binds to ligand-free TGF beta type I receptor, from which it is released upon a ligand-induced, type II receptor mediated phosphorylation of the type I receptor. Binding is inhibitory to the signaling pathways of the TGF beta family ligands.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8756725}.
Interaction partners:
- Calcineurin subunit B type 1
- Raptor, isoform B
- Ryanodine receptor
- Ribosomal protein S6 kinase
- Serine/threonine-protein kinase mTor
- receptor protein serine/threonine kinase
- Calmodulin
- Calmodulin-related protein 97A
- MIP05401p
- EF-hand domain-containing protein
Sequence:
MGVQVVPIAPGDGSTYPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYAYGSRGHPGVIPPNSTLTFDVELLKVE