wanglab/gogpt-training-data huggingface dataset:
Protein: LD05287p (Lethal (3) malignant brain tumor) (Q9VB52)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lin-52, isoform A
- Histone deacetylase HDAC1
- Transcription factor E2F2
- RE32990p
- Protein lin-54 homolog
- LD07342p
- LD06557p
- Retinoblastoma family protein
- Transcription factor Dp
- Chromatin assembly factor 1 p55 subunit
Sequence:
MLPLSMASAEAKQLQRNISLSMSPANGGVISPSTANCNGVASASGGNPNPNSLLTLAPRKEELRFLPLAPMGGNKTCNITISNVQPMKSKLKSVNIVPNSIKSAGAGATVGSADAPLFQLVPSPSNPSQPLVAILAPNRKTTLLGGGASNGQPVVIRSGTPLHKNSLTVETSNKPIQPGGSAAAAAVGGGTGGAPLTLVGKTVVPPKIQAATPVQIPSTGPGAQVSLLANPLKPRAPLILSKVAVDKLRLKFSQVKSNPNALVLGKANHVKKLLTSPNPSGEDKTRSTQKNNKQNTSASQLKPVVAPKTAMPIATEVPTADNNKMSLIKSKPVAIKAVPLPSQEAPIVPAVAPVVTSPEKVDVKPTAKPSIKTAPKPTPKPLEMSVNGPAKEKKAPAKEQKQKTMDKPPVVKEIAQHTPCGPKELPKLKRSKSFVSNHPASPVANNERRHSVAIMAKEVDVIEQPSAAIETITIEDDDESEEEQQKPEIKKTPKQNQKPEKQEAPKKKQIPMPILPAGITISTTSTAKKKAVRKNSSVTTISSSSSDSSSYSDVEVVPTKKTEKELSMLPGISIIKAESLPLSREDFERSLRCDEQVPQTPPKSSSSSSSGSHASEMSPPPKLADPKPSSPPAKNAKKANDHDANPSPSSKTNDFKKSMMQNLNMLKWRGQQPANLQNSTVRFELNEFNFLQINERCQPRQGPAAYFERPLYDRPGRRPSACVHPLLYLCQRCNFHGPAADFLAPHFCSVGCVRRSQKRRLPQSTQKESKISRTQLEQTAGTAPDLPQKRQTNYKPHKSLSAIQEQLQQRQKDKPRKPFRWSEYLKSKGKDVAAPIHLFLNPFPISPNCFEIGMKLEAIDPENCSLFCVCSIVEVRGYRLKLSFDGYSSMYDFWVNADSQDIFPPGWCDETARVLQAPKDYNSERFSWSRYLVKTGGKAAPRALFGHLNMQQQMDVRNGFAVGMHLEAEDLNDTGKICVATVTDILDERIRVHFDGWDDCYDLWVHITSPYIHPCGWHEGRQQLIVPPDYQKSAFIWDDYISEVGGMAASKELFTPRQPMEYQERMKLEVVDQRNPCLIRPATVVTRKGYRVQLHLDCWPTEYYFWLEDDSPDLHPIGWCEATSHELETPPGYLQPKSVMPCDVEGCRGFGNAKRFNLNVHALRECCPYAPENWRQWRSKTVKPPRVAPENIRRGWAKKTKRACSEAKQAIKEDSQQEIVYPKVAEVVQAKRKTSPCEEKVVKKQKQMQKEEDAEQVPDERSLAIARSFVKDYGPQFLPNYRLWQLNSAFKLDDVRTNPLHWTSWDVCEYIERALDSTDIAKVIFEQDIDGRALLMLGRKELDTYLKLKVGPAVKLYSLILNLRIAVVCKFDSKNIELESNTAGPIQREMDTPVSAIKQLPEQSQTNGYKTDHDQELSESGDDDDDEDVMLDSDDFLSVKPSCLVIDEDADGDGDCESDGDVAMVPMEVRTPLRTSS
Protein: Replication factor C subunit 4 (AtRFC4) (Activator 1 subunit 4) (Protein EMBRYO DEFECTIVE 1968) (Q93ZX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in DNA replication and thus regulate cell proliferation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 5
- Proliferating cellular nuclear antigen 1
- Proliferating cell nuclear antigen 2
- DNA primase
- DNA polymerase alpha subunit B
- Cell cycle checkpoint protein RAD17
- Chromosome transmission fidelity protein 18 homolog
- Replication factor C subunit 1
Sequence:
MAPVLQSSQPWVEKYRPKQVKDVAHQEEVVRVLTNTLQTADCPHMLFYGPPGTGKTTTALAIAHQLFGPELYKSRVLELNASDDRGINVVRTKIKDFAAVAVGSNHRQSGYPCPSFKIIILDEADSMTEDAQNALRRTMETYSKVTRFFFICNYISRIIEPLASRCAKFRFKPLSEEVMSNRILHICNEEGLSLDGEALSTLSSISQGDLRRAITYLQSATRLFGSTITSTDLLNVSGVVPLEVVNKLFTACKSGDFDIANKEVDNIVAEGYPASQIINQLFDIVAEADSDITDMQKAKICKCLAETDKRLVDGADEYLQLLDVASSTICALSEMAQDF
Protein: Solute carrier family 11 member 2 (F8W1P7)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
Sequence:
MSIAYLDPGNIESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILWLMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMYLHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQVVEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTVSISKGLLTEEATRGYVK
Protein: ArfGAP with dual PH domains 1 (H0Y7Q1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSFSLSLFRKHVLGPCSVSLQSPLRDSVLATSGSLAHQPISRPPCLAPVGSLLNFMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP
Protein: C2H2 finger domain transcription factor sebA (Stress response element-binding protein A) (Q4WPF5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Transcription factor that is involved in the response to heat shock, oxidative stress, and poor nutrient conditions. Controls expression of oxidative stress response genes such as ccp1, cat1, cat2, sod2; as well as of heat shock genes such as hsf1, hsp30 and hsp90. Negatively controls the expression of the fumiquinazoline (fmq) cluster via binding to the STRE motifs at the fmqA-D promoters. Plays a role in virulence.
Subcellular location: Nucleus {ECO:0000269|PubMed:22345349}. Cytoplasm {ECO:0000269|PubMed:22345349}. Note=Accumulates in the nucleus upon exposure to oxidative stress and heat shock conditions. {ECO:0000269|PubMed:22345349}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Forkhead transcription factor
- C6 transcription factor, putative
- General transcription and DNA repair factor IIH
- C6 transcription factor, putative
Sequence:
MDATYTMAQTPVQGQPSFAYYPTESQSRQQHFTSHPFEMQYYGQVSSYPQQQAQQQHSMPEQQPVYAAQPMLNMHQMATTNAFRGALSMTPIASPQPTHLKPTIIVQQDSPALMPLDTRFVSNDFYGFPSTPPLSTSGSTISSPPSSNGSLHTPINDCFFSFEKVEGVKEGCESDVHCELLANTDWSRSDSPPLTPVFIQPQSLTASQSSDLLSAQIPCPSLSPSPSPDSATFISHPQSILSAEPSGSDFCDPRQLTVESSVGAPAELPPLPTLSCNEEEPKVVLGSATVTLPVHEGLSPSFSSSSEDPLGSLPTFDSFSDLDSEDEFANKLVDFHPIGNTYFQGDKRQRLGTYLLDEDEFLSERSLEDLDDQEAFAQSGLPSVESTDFLAVEGDATQSTEEMSSKKRVTSRRSLKKASTSESSSDSLAKKTQASATSRSGHSDTTSTVQQSTASSRQNSTANTSNSESPAAPVSVNRRGRKQSLTDDPSKTFVCSLCSRRFRRQEHLKRHYRSLHTQDKPFECHECGKKFSRSDNLAQHARTHGGGSIVMGVIDTNSSNTQPAFDEPEPRALGLALYEAANAATSKSTTSESSDGTISDTSSVGGRPAKKRRRDDHV
Protein: V-SNARE coiled-coil homology domain-containing protein (Q381P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRWLNPSDVTAFKTEAGDPEAATLKRAQMQCVDETVDYTSYHLCAHDPVRQVVLCVGNNVPALLVARGRRQMLLQVPNCVRWIDCSIFSGTSSVLLLSPERLVLLDYAFHGISSALSPCGKRGVLFTSLHVPQGVTWGAVGCEDGTVMYWRLQESGSTQQLVWAALTTSTMNLCRPFFSAASSEWAPRGYVLSMNSCPSNPNTFIAVVAGAAGVCKWYLDENRLSRFFSLPEPQTGCGITACRYTPGASFVVAAAFDASALYIWAENGKKDKERSVALMWSVQTGCRPCSPVGGPDDEVVSSTGMYIAHSSDPPHGARSEKKSPLHFLLHSTCDIVELVINLEEKRLIQREDILSHIKAKILPLQCEGDESSSLDLCRVIPCVGPGYWLSEWKDSDLDTLLVLSEDLGPLLVRRSRYQRNVESAVPLRNVMPEPFPWDEMLLVSPPAEVTRAIWHGASLQPDPEDPWATVLACLECEGDVEGKGLQKEILLGMVPYSATGAVCFLPLTNECLPVPATVIEQNTAANARASLPTGSAVVILEEALPKHPCRTEFILRVLADEMGVSVNAVRFSPPHVEHIMTLSKEQLIFGGASVGDDGQDGEAEIIARTAKLADCRIEQRELTPQAFQLVRGGMSILLQLRNGNLVIVDLSGGVTGEGNAPAMVHYPGGLFPAGASVTSFDTVWMGRSCSAGSTGPVCEGKNSFLALFCTLSNDRGLIIWNMSDMQMLGYHREDDGRWSYDKVMLCSSTPRFSVSAGAASLVVRAPHADVSDGKSDPSAEKNSDFRGTVSFRDVFGRVIFAVELRWCAEPPGGLWYGRVGGTDTEWTLLPSSNSKDLRLSVVVSGGEVVVSADGEYTLRGVVTPGSRIVAVEVNPGWPYDALQCDLHAEDEQEKQEEERSRLRNVLGEDSPPDTTVVLWNGRKVHLYLAERLLSGEAPSNRMQPPVVGRGRSVEHVGVCMSLRVVVVMSRDANGWRWFNVLDLESGQRLAEHTMLCLCDENDLRLHTHYIEGSGLHIYVVGVSGALGHLIVSAESNVSDQLRLTAEPLEGIRHVPAPPTFRSYLQFLPPPPAVKQEQGLLKRLTTQSWEEAATKIETNVLVKKMEGAAPQHPRPDSIVERGRDGAVLSQRRSEREGSEERRGSRYSELKAVAARENVSVTEALQMMRENEVKVHERGEKISQIESKSRELAQEATTFEALARKLNQKQKNSWF
Protein: Toxin YwqJ (P96722)
Organism: Bacillus subtilis (strain 168)
Function: Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis; no effect is seen on DNA or rRNA. Co-overexpression with cognate immunity protein YwqK does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation. Its toxic effects are probably neutralized by its cognate immunity protein YwqK, but not by immunity proteins specific to other toxins with the LXG domain (Probable). May have deaminase activity (Probable).
Subcellular location: Secreted {ECO:0000305|PubMed:34280190}. Note=Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
Interaction partners:
- Immunity protein YwqK
- Protein YwqI
- Endonuclease V
- Toxin YxiD
- Protein YwqH
- Immunity protein YobK
- Immunity protein YezG
- Protein YxiC
- Immunity protein YqcF
- Immunity protein YxxD
Sequence:
MSKVFESKSLIEEAKSRKKQYETLEEQLNTLKKAFQGVADLGDNFKGNGADNIKDFFQGQAEIVDSWLTLVSAQIAFLNGISGDIKDQELNDSYVETSFLDHELPNGDLKASEIVSAHKEEIDSILSGISDIIDLDMYTLDDYADKMGDAQKIRRDTITAVDKLDESLTTEYQNLESLDNAVLTKYSVLMQATSNGKSASPMYYDKKAFHSNEVYKSVIEVENQGTTYIDAKTQQAEARRLQEKAEEEANKPWYEKTWDGVCNFTGEVTGYYDYKRATEGVDPVTGEKLSTAERVTAGAMAAAGFIPVVGWAGRAFKGGKAIYKTGKAAIAAEHALDAYKTGKSLDILKMTEMGAYGLVASNGFSEAVTGRDMFGNKVSEEKRKQGALEAITIIGGAGLAHYFDRLYQKNAPYVNKVSNESLISNIAKTTEEKQTRLQYLRNKHGVLSKEDLHHRINLRAEVLNELSRIKSSGLTKKQRGPAVAGVLDKKTGNYYFGINNIDGKPPKVLHPLIHDRIVNMPTELKEGYIKTSGAGSHAEVNALNEALLQRPDADLKDLMVYVVSARKINKKMPEGVPMPRCPHCEYITQNTNYIPEALKYGK
Protein: Protein phosphatase 6 regulatory subunit 3 (E9PKF6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFWKFDLHSSSHIDTLLEREDVTLKELMDEEDVLQECKAQNRKLIEFLLKAECLEDLVSFIIEEPPQDMDEKIRYKYPNISCELLTSDVSQMNDRLGEDESLLMKLYSFLLNDSPLNPLLASFFSKVLSILISRKPEQIVDFLKKKHDFVDLIIKHIGTSAIMDLLLRLLTCIEPPQPRQDVLNWLNEEKIIQRLVEIVHPSQEEDRHSNASQSLCEIVRLSRDQMLQIQNSTEPDPLLATLEKQEIIEQLLSNIFHKEKNESAIVSAIQILLTLLETRRPTFEGHIEICPPGMSHSACSVNKSVLEAIRGRLGSFHELLLEPPKKSVMKTTWGVLDPPVGNTRLNVIRLISSLLQTNTSSINGDLMELNSIGVILNMFFKYTWNNFLHTQVEICIALILASPFENTENATITDQDSTGDNLLLKHLFQKCQLIERILEAWEMNEKKQAEGGRRHGYMGHLTRIANCIVHSTDKGPNSALVQQLIKDLPDEVRERWETFCTSSLGETNKRNTVDLMQQMTSNFIDQFGFNDEKFADQDDIGNVSFDRVSDINFTLNTNESGNIALFEACCKERIQQFDDGGSDEEDIWEEKHIAFTPESQRRSSSGSTDSEESTDSEEEDGAKQDLFEPSSANTEDKMEVDLSEPPNWSANFDVPMETTHGAPLDSVGSDVWSTEEPMPTKETGWASFSEFTSSLSTKDSLRSNSPVEMETSTEPMDPLTPSAAALAVQPEAAGSVAMEASSDGEEDAESTDKVTETVMNGGMKETLSLTVDAKTETAVFKSEEGKLSTSQDAACKDAEECPETAEAKCAAPRPPSSSPEQRTGQPSAPGDTSVNGPV
Protein: B-cell receptor-associated protein 29 (BCR-associated protein 29) (Bap29) (Q61334)
Organism: Mus musculus (Mouse)
Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- tRNA-dihydrouridine
- B-cell receptor-associated protein 31
Sequence:
MTIQWAAVASFLYAEIGLILLFCLPFIPPQRWQKIFSFSVWGKIASFWNKAFLTIIILLIILFLDAVREVRKYSSTNVVEKNSAIRPSAFEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAKEIANKGVLKIQAENTNKAAKKFMEENEKLKLGLRNDNAEEHLLEAENKKLIESKENLKTELKKASDALLKAQNDVMTMKIQSERLSKEYDRLLKEHSELQNRLEKEKKKGL
Protein: UPF0538 protein C2orf76 (Q3KRA6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPGEVTITVRLIRSFEHRNFKPVVYHGVNLDQTVKEFIVFLKQDIPLRTNLPPPFRNYKYDALKIIHQAHKSKTNELVLSLEDDERLLLKEDSTLKAAGIASETEIAFFCEEDYKNYKANPISSW
Protein: WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (MAPK organizer 1) (Q5BLX8)
Organism: Rattus norvegicus (Rat)
Function: Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation (By similarity). Also involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator. May also be involved in pre-mRNA splicing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16407229}. Lysosome {ECO:0000250|UniProtKB:Q9BRX9}. Nucleus {ECO:0000269|PubMed:16407229}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}.
Interaction partners:
- Splicing factor 3B subunit 4
- Pre-mRNA-processing-splicing factor 8
- Ragulator complex protein LAMTOR3
- G patch domain containing 1
- Prolyl hydroxylase EGLN3
- Late endosomal/lysosomal adaptor, MAPK and MTOR activator 2.
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MAFPEPKPRAPELPRKQLKTLDCGQGAVRAVRFNVDGNYCLTCGSDKTLKLWNPLRGTLLRTYSGHGYEVLDAAGSFDNSHLCSGGGDKTVVLWDVATGQVVRKFRGHAGKVNTVQFNEEATVILSGSIDSSVRCWDCRSRKPEPVQTLDEARDGISSVKVSDHEILAGSVDGRVRRYDLRMGQVTSDYVGSPITCTCFSRDGQCTLISSLDSTLRLLDKDTGELLGEYVGHKNQKYKLDCCLSERDTHVVSCSEDGKVFFWDLVEGSLALALPVGSNVVQSLAYHPADPCLLTAMGGSIQYWREETYEAEGGAG
Protein: Heat stress transcription factor A-4c (AtHsfA4c) (AtHsf-20) (Protein ROOT HANDEDNESS 1) (Q9FK72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). May be involved in general response to auxin.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 8
- Chaperone protein ClpB4, mitochondrial
- Heat shock protein 90-5, chloroplastic
Sequence:
MDENNGGSSSLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDPEKWEFLNDDFVRGRPYLMKNIHRRKPVHSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEFELQVTTLKDRLQHMEQHQKSIVAYVSQVLGKPGLSLNLENHERRKRRFQENSLPPSSSHIEQVEKLESSLTFWENLVSESCEKSGLQSSSMDHDAAESSLSIGDTRPKSSKIDMNSEPPVTVTAPAPKTGVNDDFWEQCLTENPGSTEQQEVQSERRDVGNDNNGNKIGNQRTYWWNSGNVNNITEKAS
Protein: Probable quinone oxidoreductase (EC 1.6.5.5) (NADPH:quinone reductase) (O74489)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mitochondrial FAD-linked sulfhydryl oxidase erv1
- Ceramide very long chain fatty acid hydroxylase scs7
Sequence:
MSNLLVQVSKTGPSSVLQVITKEIPKPAPNGLVIKNAYAGLNYIDTYLRTGLYTAPLPYIPGKEAAGVVAAVGDKVEADFKVGDRVVYLTPFGAYAQYTNVPTTLVSKVSEKIPLKIASAALLQGLTAYTLIEEAYPVKTGDTVVVHAAAGGVGLLLCQMLRARNVHVIATASTAAKRRIAIKNGAEIACSYEDLTKVVADYTNGKGVDAAYDSVGIDTLSSSLDALRNGGTMVSFGNASGAIDAIPLKFLSARCLKFVRPSLFGYITGHAVFEGYVSRLWKEILDNNLNIAIHHIFKLSEAKEAHDAIESRATTGKLLLLCNEDLADA
Protein: Elongation factor 1-beta (EF-1-beta) (O74173)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
Interaction partners:
- Elongation factor 1-gamma
- Putative glutathione S-transferase C1183.02
- Elongation factor 1-alpha-A
- Elongation factor 2
- Elongation factor 1-alpha-B
- Putative glutathione S-transferase C460.02c
- Translationally-controlled tumor protein homolog
- Elongation factor 1-alpha-B/C
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS3
Sequence:
MGFSDLTSDAGLKQLNDFLLDKSFIEGYEPSQADAVVFKAVGVAPDTAKYPNGARWYKQIATYDLATLPGTAKEVSAYGPEGAAAAEEDEIDLFGSDEEEDPEAERIKAERVAEYNKKKAAKPKAVHKSLVTLDVKPWDDETPMDELEKAVRSIQMDGLVWGLSKLVPVGFGVNKFQINLVVEDDKVSLEALQEELEGFEDYVQSTDIAAMSKL
Protein: cDNA FLJ16308 fis, clone PUAEN2006335 (Q6ZN96)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSEVVAGNSVGPTMGAASSGPLPPPPPPLPPSSDTPETVQNGPVTPPMPPPPPLPGPAAETVPAPPLAPPLPSAPPLPGTSSPTVVFNSGLAAVKIKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKIPQKGSNKVTLLEANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERKPLENLSDEDRFMMQFSKIERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHKSKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITALKKNNITKFPNVHSRVRISSSTPVVEDTQS
Protein: Trehalose 6-phosphate phosphatase (EC 3.1.3.12) (Q9VM19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPEKQVAPVISNLEDFANNLPGYLISESPVAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHDYELPTEIQKNYTQMVRELKEKVEKNGAWVEDKKVSLTYHYRDTPAALKDQQKQLASEICTKFGFRANQAHEAIEAKPPVNWNKGEAAVYILKQKFGDNWSQKVSVVFAGDDTTDEDAMRVLRGLGRSFRISADAQIQTYADFRLPKQAVMTDLLKWIANVYVS
Protein: 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (A0A1D8PQK5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 3-isopropylmalate dehydratase
- Acetolactate synthase
- Acetolactate synthase regulatory subunit
- Homoaconitase, mitochondrial
- Orotidine 5'-phosphate decarboxylase
- Phosphoribosylaminoimidazole carboxylase
- Imidazoleglycerol-phosphate dehydratase
- Threonine dehydratase
- N-
- Alpha-aminoadipate reductase
Sequence:
MSVKTKTITVLPGDHVGTEIVNEAIKVLKAIEAATPYQKIQFDFKHHLIGGAAIDATGVPLPDDALESAKSSDAVLLGAVGGPKWGTGTVRPEQGLLKIRKELNLYANIRPCNFASDSLLELSPLKAEVVKGTNLIIVRELVGGIYFGERQEQEESEDKKTAWDTEKYTVDEVTRITRMAAFMALQHNPPLPIWSLDKANVLASSRLWRKTVDKVISEEFPALSVQHQLIDSAAMILIQNPTKLNGIIITSNMFGDIISDEASVIPGSLGLLPSASLASLPDTNTAFGLYEPCHGSAPDLPANKVNPIATILSAASMLRLSLDCVKEAEALEEAVKQVLDSGIRTADLRGTSSTTEVGDAIAETVTKILKQNT
Protein: Target of Nesh-SH3 (Tarsh) (ABI gene family member 3-binding protein) (Nesh-binding protein) (NeshBP) (Q7Z7G0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- ABI gene family member 3
Sequence:
MLSSLGCLLLCGSITLALGNAQKLPKGKRPNLKVHINTTSDSILLKFLRPSPNVKLEGLLLGYGSNVSPNQYFPLPAEGKFTEAIVDAEPKYLIVVRPAPPPSQKKSCSGKTRSRKPLQLVVGTLTPSSVFLSWGFLINPHHDWTLPSHCPNDRFYTIRYREKDKEKKWIFQICPATETIVENLKPNTVYEFGVKDNVEGGIWSKIFNHKTVVGSKKVNGKIQSTYDQDHTVPAYVPRKLIPITIIKQVIQNVTHKDSAKSPEKAPLGGVILVHLIIPGLNETTVKLPASLMFEISDALKTQLAKNETLALPAESKTPEVEKISARPTTVTPETVPRSTKPTTSSALDVSETTLASSEKPWIVPTAKISEDSKVLQPQTATYDVFSSPTTSDEPEISDSYTATSDRILDSIPPKTSRTLEQPRATLAPSETPFVPQKLEIFTSPEMQPTTPAPQQTTSIPSTPKRRPRPKPPRTKPERTTSAGTITPKISKSPEPTWTTPAPGKTQFISLKPKIPLSPEVTHTKPAPKQTPRAPPKPKTSPRPRIPQTQPVPKVPQRVTAKPKTSPSPEVSYTTPAPKDVLLPHKPYPEVSQSEPAPLETRGIPFIPMISPSPSQEELQTTLEETDQSTQEPFTTKIPRTTELAKTTQAPHRFYTTVRPRTSDKPHIRPGVKQAPRPSGADRNVSVDSTHPTKKPGTRRPPLPPRPTHPRRKPLPPNNVTGKPGSAGIISSGPITTPPLRSTPRPTGTPLERIETDIKQPTVPASGEELENITDFSSSPTRETDPLGKPRFKGPHVRYIQKPDNSPCSITDSVKRFPKEEATEGNATSPPQNPPTNLTVVTVEGCPSFVILDWEKPLNDTVTEYEVISRENGSFSGKNKSIQMTNQTFSTVENLKPNTSYEFQVKPKNPLGEGPVSNTVAFSTESADPRVSEPVSAGRDAIWTERPFNSDSYSECKGKQYVKRTWYKKFVGVQLCNSLRYKIYLSDSLTGKFYNIGDQRGHGEDHCQFVDSFLDGRTGQQLTSDQLPIKEGYFRAVRQEPVQFGEIGGHTQINYVQWYECGTTIPGKW
Protein: ETS domain-containing protein ets-7 (ETS class transcription factor ets-7) (O01519)
Organism: Caenorhabditis elegans
Function: Probable transcription factor (By similarity). Involved in responses to oxidative stress.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
Interaction partners:
- Runt-related transcription factor rnt-1
- ETS domain-containing protein
- Serine carboxypeptidase ctsa-1.2
Sequence:
MSSKRTSPNGKQRLLNFLRGLLEDDSHSDLITWSNKDTLEFQMLKPHKVAELWGAATGNPGMNYDKMSRGLRYFYTNNTLKKVKGKDSRYCFLDTPLLAPFPDFFPKANEPMRRVPLFSIENLLASSEETTSNFSLQSSPSSSSNSSSARTMSATSSPTSSLEDVINPPVLIDPFQMQMAHITQTFLATQLPALQAFPMQLQLQFLKTLLPTLFPNNN
Protein: Threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P9WFT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
Interaction partners:
- Valine--tRNA ligase
- Histidine--tRNA ligase
- Translation initiation factor IF-2
- Phenylalanine--tRNA ligase beta subunit
- AP-4-A phosphorylase
- Leucine--tRNA ligase
- Large ribosomal subunit protein uL15
- Isoleucine--tRNA ligase
- Methionine--tRNA ligase
- Small ribosomal subunit protein uS15
Sequence:
MSAPAQPAPGVDGGDPSQARIRVPAGTTAATAVGEAGLPRRGTPDAIVVVRDADGNLRDLSWVPDVDTDITPVAANTDDGRSVIRHSTAHVLAQAVQELFPQAKLGIGPPITDGFYYDFDVPEPFTPEDLAALEKRMRQIVKEGQLFDRRVYESTEQARAELANEPYKLELVDDKSGDAEIMEVGGDELTAYDNLNPRTRERVWGDLCRGPHIPTTKHIPAFKLTRSSAAYWRGDQKNASLQRIYGTAWESQEALDRHLEFIEEAQRRDHRKLGVELDLFSFPDEIGSGLAVFHPKGGIVRRELEDYSRRKHTEAGYQFVNSPHITKAQLFHTSGHLDWYADGMFPPMHIDAEYNADGSLRKPGQDYYLKPMNCPMHCLIFRARGRSYRELPLRLFEFGTVYRYEKSGVVHGLTRVRGLTMDDAHIFCTRDQMRDELRSLLRFVLDLLADYGLTDFYLELSTKDPEKFVGAEEVWEEATTVLAEVGAESGLELVPDPGGAAFYGPKISVQVKDALGRTWQMSTIQLDFNFPERFGLEYTAADGTRHRPVMIHRALFGSIERFFGILTEHYAGAFPAWLAPVQVVGIPVADEHVAYLEEVATQLKSHGVRAEVDASDDRMAKKIVHHTNHKVPFMVLAGDRDVAAGAVSFRFGDRTQINGVARDDAVAAIVAWIADRENAVPTAELVKVAGRE
Protein: Paternally expressed 10 (A0A087WXK2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTERRRDELSEEINNLREKVMKQSEENNNLQSQVQKLTEENTTLREQVEPTPEDEDDDIELRGAAAAAAPPPPIEEECPEDLPEKFDGNPDMLAPFMAQCQIFMEKSTRDFSVDRVRVCFVTSMMTGRAARWASAKLERSHYLMHNYPAFMMEMKHVFEDPQRREVAKRKIRRLRQGMGSVIDYSNAFQMIAQDLDWNEPALIDQYHEGLSDHIQEELSHLEVAKSLSALIGQCIHIERRLARAAAARKPRSPPRALVLPHIASHHQVDPTEPVGGARMRLTQEEKERRRKLNLCLYCGTGGHYADNCPAKASKSSPGKLPGPAVEGPSATGPEIIRSPQDDASSPHLQVMLQIHLPGRHTLFVRAMIDSGASGNFIDHEYVAQNGIPLRIKDWPILVEAIDGRPIASGPVVHETHDLIVDLGDHREVLSFDVTQSPFFPVVLGVRWLSTHDPNITWSTRSIVFDSEYCRYHCRMYSPIPPSLPPPAPQPPLYYPVDGYRVYQPVRYYYVQNVYTPVDEHVYPDHRLVDPHIEMIPGAHSIPSGHVYSLSEPEMAALRDFVARNVKDGLITPTIAPNGAQVLQVKRGWKLQVSYDCRAPNNFTIQNQYPRLSIPNLEDQAHLATYTEFVPQIPGYQTYPTYAAYPTYPVGFAWYPVGRDGQGRSLYVPVMITWNPHWYRQPPVPQYPPPQPPPPPPPPPPPPSYSTL
Protein: ELAV-type RNA binding protein variant E (RRM domain-containing protein) (A7KQE9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSGAVLPAVLVVPKMESVVVPIAESTVINAKDTTPSTAADNDVSPSPSEPDTDAIKMFVGQIPRQWNETDCRRLFEKYGSVFSCNILRDKSTQASKGCCFVTFYHRKDAIEAQGALHNIKVIEGMHHPVQMKPADTENRNERKLFIGQLSKKHNEENLREIFAKFGHIEDCSVLRDQDGKSRGCAFVTFTNRSCAVVATKEMHHSQTMEGCSAPLVVKFADTQKDKDVKTKSMITGSGAGSPKGGAASLLQNLNPALLQQLGGGQNYQAVASLLSLINGQQGQQQQHQQQQNVLGILGTGNPLLGNPAMAAQNQFDAITMAQIAHQQQMLALQGFAVQQGAPSQQQQGLAGGMAGAKTTSPVAASLANHQQIALTPFAGGAAALDHFQAMQQYALLANLQATGGVGVQATTSAAQMVGNGDVKGPDGANLFIYHLPQDFGDSDLINTFAPFGGILSAKVFIDKVTNLSKCFGFVSYENAQSATNAISAMNGFQIGSKRLKVQLKVDRGNPYNR
Protein: Linalool synthase Tps-5031L19, chloroplastic (PsTps-5031L) (EC 4.2.3.-) (C0KWV3)
Organism: Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSMRTYVAIMKKPSVEHVDNVDKKASKPSWRVSLSAGLRSSCSLQLEVKPADQILTARRSGNYQPSLWDFNYLQSLNTTHYKEVRHLKREAELIEQVKMLLEEEMEAVQQLELVDDLKNLGLSYFFEDQIKQILTFIYNEHKCFHSNSIIEAEEIRDLYFTALGFRLLRQHGFQISQEVFDCFKNEEGSDFKARLGDDTKGLLQLYEASFLLREGEDTLELARQYATKFLQKKVDHELIDDNNLLSWILHSLEIPLHWRIQRLEARWFLDAYASRRDMNQIILELAKLDFNIIQATQQEELKDLSRWWKSSCLAEKLPFVRDRLVESYFWAIALFEPHQYGYHRKIAAKIITLITSLDDVYDIYGTLDELQLFTDAIQRWDTESISRLPYYMQLFYMVLYNFVPRLAYDGLKEKGFITIPYLQRSWADLVEAYLKEAKWYYNGYTPSMEEYLNNAYISIGATPVISQVFFTLATSIDKPVIDSLYEYHRILRLSGILVRLPDDLGTSPFEMKRGDVPKAIQLYMKERNATEIEAQEHVRFLIREAWKEMNTATAAVDCPFTDDLVTAAANLGRAAQFMYLDGDGNHSQLHQRIACLLFEPYA
Protein: Copine 1 (F2Z2V0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGKPAGRGTITVSAQELKDNRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAEFECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLMALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAHQGTASYFMLLLLTDGAVTDVEATREAVVRASNLPMSVIIVGVGGADFEAMEQLDADGGPLHTRSGQAAARDIVQFVPYRRFQNAPREALAQTVLAEVPTQLVSYFRAQGWAPLKPLPPSAKDPAQA