wanglab/gogpt-training-data huggingface dataset:
Protein: Calnexin (CeCNX-1) (P34652)
Organism: Caenorhabditis elegans
Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16256074}. Cytoplasmic vesicle {ECO:0000269|PubMed:16256074}. Note=Perinuclear localization in excretory and germ cells. In intestinal cells, clustered signals around vacuoles with vesicles are detected.
Interaction partners:
- Endoplasmin homolog
- Calreticulin
- Heat shock 70 kDa protein C
- Endoplasmic reticulum chaperone BiP homolog
- BZIP domain-containing protein.
- Tumor susceptibility gene 101 protein
- Translocon Sec61/SecY plug domain-containing protein
- Heat shock protein 70
- UDP-Glucose Glycoprotein glucosylTransferase
- Protein disulfide-isomerase
Sequence:
MVNRKWMYIFIQFLLVSSIRSDDDVFEDDEEEVTKGSDDKEEFVPSLFVAPKLSDKSTPNFFDYFPVGSKIGLTWIKSLAKKDDVDSDIAKYNGEWSIGAPTKVSIEGDLGLIVKTKARHHAIAAKLNTPFAFDANTFVVQYDIKFEEGQECGGGYLKLLSEGAEKDLANFQDKTAYTIMFGPDKCGATGKVHLIFRYKNPINGTISEYHANQPTTIGSTYWDDHNTHLFTLVVKPTGEYSVSVDGKSLYYGNMMSDVTPALTPPKQIFDETDLKPVDWDERENIEDESAVKPDDWDENEPQSVVDEAATKPYDWNEEENELIADPEAKKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKAPTIKNPKYKGKWIRPKISNPAFKGKWTARLIDNPNYFEPKPFAGLAPITAVGIEMWTMSENILFDNILITSSEEDSSDVAKQTFYVKQKEEYRLAAATGNGNGFFQQIIDATNEKPWLWAVYILCVLLPLVAIGVFCFGKQSKPTPNFAKKSDAYSADDDRVPNLVDDDEEEIIGDEEDDVNQPGPSGSQSNPEPQDEEENAEQQSANSSQSSAAEEEDDEHVVPENEPVKPTEEFAKKSPKNTGGAKRRTARRGD
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (Q9K0N4)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: Acts as a chaperone.
Interaction partners:
- Chaperone protein DnaJ
- Protein GrpE
- Chaperonin GroEL
- Co-chaperonin GroES
- DnaJ protein, truncation
- Chaperone protein ClpB
- Co-chaperone protein HscB homolog
Sequence:
MAKVIGIDLGTTNSCLAISENGQTKVIENAEGARTTPSVIAYLDGGEILVGAPAKRQAVTNAKNTIYAAKRLIGHKFEDKEVQRDIESMPFEIIKANNGDAWVKAQGKELSPPQISAEVLRKMKEAAEAYLGEKVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAFGMDKGDNKDRKVAVYDLGGGTFDISIIEIANLDGDKQFEVLATNGDTFLGGEDFDQRLIDHIIAEFKKEQGIDLKQDVMALQRLKEAAEKAKIELSSGQQTEINLPYITMDATGPKHLAMKITRAKFESLVEDLITRSIEPCKIALKDAGLSTGDIDDVILVGGQSRMPKVQEAVKAFFGKEPRKDVNPDEAVAVGAAIQGEVLSGGRSDVLLLDVTPLSLGIETMGGVMTKLIQKNTTIPTKASQVFSTAEDNQSAVTIHVLQGERERASANKSLGQFNLGDIAPAPRGMPQIEVTFDIDANGILHVSAKDKGTGKAANITIQGSSGLSEEEIERMVKDAEANAEEDKKLTELVASRNQAEALIHSVKKSLADYGDKLDAAEKEKIEAALKEAEEAVKGDDKAAIDAKTEALGAASQKLGEMVYAQAQAEAQAGESEQANASAKKDDDVVDADFEEVKDDKK
Protein: Pinin (Q8IFW3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVNDSGLSTVDDLEQKLNSAKQSLVILNENIRRIAGRVPRESLQRSEKFKYTQDGKKNEHNGDRPFPRNATPGGVFKDKRRMYESKNPISRFPIEENEGRPPRINSRVIREMPTKKEIVEAQGTDSESRARNRRMFGSLLGTLQKFCQEESRLKSKEDKKAEIDRKVEKQELQERAMLRKQRETLFLDRKKKQFEIRKLEYKMARIKDFKVWEATMLNAKNNIRTKTKPHLFFRPKVHSPRTEKLLSKSKSEADVFIEFRREELEVELKNLENMNFGKMEDDTAIDESFYEEPDDEEQLDKCK
Protein: Small ribosomal subunit protein bS18m (28S ribosomal protein S18-1, mitochondrial) (MRP-S18-1) (28S ribosomal protein S18c, mitochondrial) (MRP-S18-c) (Mrps18-c) (S18mt-c) (Q8R2L5)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82917}.
Interaction partners:
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS2m
- Large ribosomal subunit protein mL66
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein uS15m
Sequence:
MAALVALCSGIGRKNLTTAAGCFTDRGTQAVSVIWRRCFSQFEQVTSNEDLPVPMENPYKEPLKKCVLCEKRVDYKNVQLLSQFISPFTGCIYGRHITGLCGKKQREITKAIKRAQKMGFMPVTYKDPAYLKDPRVCNIRYRE
Protein: Allantoicase (EC 3.5.3.4) (Allantoate amidinohydrolase) (P25335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Interaction partners:
- Ureidoglycolate lyase
- Allantoinase
- Urea amidolyase
- Protein DAL82
- Allantoin permease
- Malate synthase 2
- Protein DCG1
- Nitrogen regulatory protein DAL80
- Transcriptional activator protein DAL81
- Urea active transporter
Sequence:
MKFFSLADEAEFKSIIISKNKAVDVIGSKLGGQVVSFSDEWFASAENLIQPTAPIRDPTRFVHSGAWYDGWETRRHNEMEYDWVIIKMGVAAAHIIGGEIDTAFFNGNHAPFVSIEALYDEGEEGNIVEDDSRWVEIVEKFECGPSQRHLFVRGNGLTKERFTHIKLKMYPDGGIARFRLYGRVVPPELKTKDHIIDLAYVCNGAVALKYSDQHFGSVDNLLLPGRGHDMSDGWETKRSRQPGHTDWAVIQLGRESSFIEKIIVDTAHFRGNFPQFITVEGCLKESESSENTGEGTWVELVGKSKTGPDKEHVYEIRKSIRVSHVKLTIIPDGGVKRIRVWGY
Protein: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P86780)
Organism: Bunodosoma caissarum (Sea anemone)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Induces insulin secretion in isolated rat islets under high glucose concentration conditions, but not under low glucose concentration conditions. Increases perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate, and potassium, sodium, and chloride excretion levels in rat kidney. Does not increase perfusion pressure in the rat mesenteric vascular bed.
Subcellular location: Secreted {ECO:0000269|PubMed:19463845, ECO:0000305}. Nematocyst {ECO:0000269|PubMed:19463845, ECO:0000305}.
Interaction partners:
Sequence:
GATIMPGTLWCGKGNSAADYLQLGVWKDTAHCCRDHDGC
Protein: Microtubule-associated protein 6 (MAP-6) (Stable tubule-only polypeptide) (STOP) (Q96JE9)
Organism: Homo sapiens (Human)
Function: Involved in microtubule stabilization in many cell types, including neuronal cells (By similarity). Specifically has microtubule cold stabilizing activity (By similarity). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B. Regulates KIF5A-mediated axonal cargo transport (By similarity). Regulates axonal growth during neuron polarization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14692697}. Golgi apparatus {ECO:0000250|UniProtKB:Q63560}. Cell projection, axon {ECO:0000250|UniProtKB:Q63560}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63560}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q63560}; Lipid-anchor {ECO:0000250|UniProtKB:Q63560}; Cytoplasmic side {ECO:0000250|UniProtKB:Q63560}. Note=Localizes predominantly in the proximal part of the axon (By similarity). Preferentially is concentrated on a portion of the microtubule polymer in which tubulin is modified by detyrosination and acetylation and is also resistant to depolymerization induced by both nocodazole and cold (By similarity). In unpolarized neurons, localizes to the Golgi and to secretory vesicles accumulating transiently at the tips of a subset of neurites (By similarity). Following neuronal polarization and during axon outgrowth, accumulates in the axonal growth cone and subsequently localizes throughout the axon (By similarity). Partially localizes to dendrites in mature neurons (By similarity). Colocalizes with neurofilament (NF)-rich inclusions in spinal cord and brain neurons of patients with amyotrophic lateral sclerosis (ALS) (PubMed:14692697). {ECO:0000250|UniProtKB:Q63560, ECO:0000269|PubMed:14692697}.
Interaction partners:
- Transmembrane protein 106B
- Calmodulin-1
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Calmodulin-like protein 3
Sequence:
MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPPPQQQAQPALAPPSARAVAIETQPAQGELDAVARATGPAPGPTGEREPAAGPGRSGPGPGLGSGSTSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQISAASQASAPILGAPKRRPQSQERWPVQAAAEAREQEAAPGGAGGLAAGKASGADERDTRRKAGPAWIVRRAEGLGHEQTPLPAAQAQVQATGPEAGRGRAAADALNRQIREEVASAVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEASKPTTADNKVIDRRRIRSLYSEPFKEPPKVEKPSVQSSKPKKTSASHKPTRKAKDKQAVSGQAAKKKSAEGPSTTKPDDKEQSKEMNNKLAEAKESLAQPVSDSSKTQGPVATEPDKDQGSVVPGLLKGQGPMVQEPLKKQGSVVPGPPKDLGPMIPLPVKDQDHTVPEPLKNESPVISAPVKDQGPSVPVPPKNQSPMVPAKVKDQGSVVPESLKDQGPRIPEPVKNQAPMVPAPVKDEGPMVSASVKDQGPMVSAPVKDQGPIVPAPVKGEGPIVPAPVKDEGPMVSAPIKDQDPMVPEHPKDESAMATAPIKNQGSMVSEPVKNQGLVVSGPVKDQDVVVPEHAKVHDSAVVAPVKNQGPVVPESVKNQDPILPVLVKDQGPTVLQPPKNQGRIVPEPLKNQVPIVPVPLKDQDPLVPVPAKDQGPAVPEPLKTQGPRDPQLPTVSPLPRVMIPTAPHTEYIESSP
Protein: FK506-binding protein 1 (FKBP) (12-kDa cytosolic FK506-binding protein) (FKBP-12) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (EC 5.2.1.8) (Rapamycin-binding protein) (P20081)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm. Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Serine/threonine-protein kinase TOR2
- Serine/threonine-protein kinase TOR1
- Peptidyl-prolyl cis-trans isomerase
- Calcineurin subunit B
- Target of rapamycin complex 1 subunit KOG1
- Peptidyl-prolyl cis-trans isomerase C, mitochondrial
- FKBP12-associated protein 1
- Peptidyl-prolyl cis-trans isomerase B
- Peptidyl-prolyl cis-trans isomerase CPR6
- Serine/threonine-protein phosphatase 2B catalytic subunit A1
Sequence:
MSEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGSPFQCNIGVGQVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPNSTLVFDVELLKVN
Protein: Caldesmon 1 (F6RGN9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ENQEKEEEKGVKGQAQRQKPRDDKPAFRKEEIKDEKIKKDKEPKEEVKSFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKRLEELRRRRGETENEEFEKLKQKQQEAALELEE
Protein: Thioredoxin-1 (Trx-1) (P29445)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Interaction partners:
Sequence:
MSNRVIHVSSCEELDKHLRDERVVVDFSAVWCGPCRAISPVFEKLSNEFITFTFLHVDIDKLNVHPIVSKIKSVPTFHFYRNGSKVSEFSGASESILRSTLEANK
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (DmPDE5/6) (DmPDE6) (Q9VFI9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Has cAMP phosphodiesterase activity in vitro but not in vivo. Has a role regulating cGMP transport in Malpighian tubule principal cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16232123, ECO:0000269|PubMed:18503409}; Lipid-anchor {ECO:0000269|PubMed:16232123, ECO:0000269|PubMed:18503409}; Cytoplasmic side {ECO:0000269|PubMed:16232123, ECO:0000269|PubMed:18503409}. Note=Expressed on the apical side of the Malpighian tubule principal cell polarized membrane. Loss of prenylation causes protein location to the cytoplasm.
Interaction partners:
- Apyrase
- Guanylate kinase
- nucleoside diphosphate phosphatase
- Adenine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- GMP synthase
- Receptor-type guanylate cyclase Gyc76C
- Probable cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Soluble guanylate cyclase 88E
- Guanylate cyclase
Sequence:
MTDVSSPAGGAASPVEMSTTSSSSAATTSASSSKPLTNGANKTAISTAAGGVTPGAVPGPGSGAIPASSSSGNQVKLEHHHRQSNNNRPAVTNRSSETKLMTPTGSSSSPSQSPSQTQASIQTQTSQQDRLAKASTTASQQDVDEVARLFEEKPEAFEKWLTERAPPEALSRLQEFIENRKPHKRPSVTSDLFQQWMAASPTVQQKSPRSLSNSSASSLPECRRHLMDLDEGELFMELIRDVANELDIDVLCHKILVNVGLLTHADRGSLFLAKGTPTNKYLVAKLFDVTQKTALKDAVTRASAEEIIIPFGIGIAGMVAQTKQMINIKEAYKDARFNCEIDLKTGYKTNAILCMPICNYEGDIIGVAQIINKTNGCMEFDEHDVEIFRRYLTFCGIGIQNAQLFEMSVQEYRRNQILLNLARSIFEEQNNLECLVTKIMTEARELLKCERCSVFLVDLDCCEASHLEKIIEKPNQPATRAIKSADSFEEKKMRNRFTVLFELGGEYQAANVSRPSVSELSSSTLAQIAQFVATTGQTVNICDVIEWVRDHNQIRAEDEIDSTQAILCMPIMNAQKKVIGVAQLINKANGVPFTDSDASIFEAFAIFCGLGIHNTQMYENACKLMAKQKVALECLSYHATASQDQTEKLTQDVIAEAESYNLYSFTFTDFELVDDDTCRAVLRMFMQCNLVSQFQIPYDVLCRWVLSVRKNYRPVKYHNWRHALNVAQTMFAMLKTGKMERFMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESPLAILYTTSTMEHHHFDQCVMILNSEGNNIFQALSPEDYRSVMKTVESAILSTDLAMYFKKRNAFLELVENGEFDWQGEEKKDLLCGMMMTACDVSAIAKPWEVQHKVAKLVADEFFDQGDLEKLQLNTQPVAMMDRERKDELPKMQVGFIDVICLPLYRVLCDTFPWITPLYEGTLENRRNWQDLAEKVEMGLTWIDHDTIDKPVEEFAACADEEIKDIEFTVTTLNCNQQSQHGSEDSHTPEHQRSGSRLSMKKTGALGKAVRSKLSKTLYNSMDGSKPKTSLKLLESHVSEDMDDKSPTSPSQPQASGSMGRMSASSSTSSAGGQMVDKSKKRSKLCALL
Protein: Catalytics (F4JI63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase flavoprotein 2, mitochondrial
- At2g29210/F16P2.41
- ETO1-like protein 1
- Ribosome-recycling factor, chloroplastic
- Protein LOW PSII ACCUMULATION 1
- Protein SHORT-ROOT
Sequence:
MLMKSLHLLSSSILLHRFASRSIASLSTLPRRRNIVRIHNPSFSSPFPPILSRPISSGKVLAMAEESSSSSTSSTSQKHTNRLAAEHSPYLLQHAHNPVDWYPWGEEAFEEARKRDVPIFLSIGYSTCHWCHVMEVESFEDEEVAKLLNNSFVSIKVDREERPDVDKVYMSFVQALYGGGGWPLSVFLSPDLKPLMGGTYFPPNDNYGRPGFKTLLKKVKDAWNSKRDTLVKSGTYAIEELSKALSASTGADKLSDGISREAVSTCAKQLSRSYDSEFGGFGSAPKFPRPVEIQLMLYHYKKLKESGKTSEADEEKSMVLFSLQGMANGGMHDHIGGGFHRYSVDECWHVPHFEKMLYDQGQLANVYLDGFSITKDVMYSYVARDILDYLRRDMIAPEGGIFSAEDADSFEFEGAKRKKEGAFYIWTSDEIDEVLGENADLFKEHYYVKKSGNCDLSSRSDPHNEFAGKNVLIERNETSAMASKFSLSVEKYQEILGECRRKLFDVRLKRPKPHLDDKIIVSWNGLVISSFARASKILKAEPESTKYYFPVVNSQPEDYIEVAEKAALFIRGNLYDEQSRRLQHSYRQGPSKAPAFLDDYAFLISGLLDLYENGGGIEWLKWAIKLQETQDELYLDREGGAYFNTEGQDPSVLLRVKEDHDGAEPSGNSVSAINLVRLASIVAGEKAESYLNTAHRLLAVFELRLRELAVAVPLMCCSADMISVPSRKQVVLVGSKSSPELTNMLSAAHSVYDPNKTVIHIDPSSSDEIEFWEEHNSNVAEMAKKNRNSEKVVALVCQHFTCSPPVFDSSSLTRLLSK
Protein: Lin-28 homolog protein (Protein lin-28 homolog B) (S0BDM9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MAEGGPRRGGGSDTARTPPQSLSGSGYCKWFNVRMGFGFISMTSSEGKPVDPPLDVFVHQSKLVMEGFRSLREGEQVEFTFKRSSKGLESLRVTGPGGGPCSGSERRPKAKAPPLKRKPKGDRCYNCGGLDHHAKECGLPPQPKKCHYCQSVTHMVAQCPHKGAPSPSASQDPQRPSTSAQSPEEESRSGSSSSPEEASQRGSRSQRWRKSRD
Protein: Crossover junction endonuclease MUS81 (EC 3.1.22.-) (MMS and UV-sensitive protein 81) (Q04149)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Interacts with MMS4 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.
Subcellular location: Nucleus {ECO:0000269|PubMed:14642571}.
Interaction partners:
- Crossover junction endonuclease MMS4
- ATP-dependent helicase SGS1
- RecQ-mediated genome instability protein 1
- Structure-specific endonuclease subunit SLX1
- DNA topoisomerase 3
- DNA repair and recombination protein RAD54
- Holliday junction resolvase YEN1
- DNA repair and recombination protein RAD52
- ATP-dependent DNA helicase SRS2
- DNA repair protein RAD51
Sequence:
MELSSNLKDLYIEWLQELVDGLTPKQEQLKIAYEKAKRNLQNAEGSFYYPTDLKKVKGIGNTIIKRLDTKLRNYCKIHHISPVEAPSLTQTSSTRPPKRTTTALRSIVNSCENDKNEAPEEKGTKKRKTRKYIPKKRSGGYAILLSLLELNAIPRGVSKEQIIEVAGKYSDHCMTPNFSTKEFYGAWSSIAALKKHSLVLEEGRPKRYSLTEEGVELTKSLKTADGISFPKENEEPNEYSVTRNESSEFTANLTDLRGEYGKEEEPCDINNTSFMLDITFQDLSTPQRLQNNVFKNDRLNSQTNISSHKLEEVSDDQTVPDSALKAKSTIKRRRYNGVSYELWCSGDFEVFPIIDHREIKSQSDREFFSRAFERKGMKSEIRQLALGDIIWVAKNKNTGLQCVLNTIVERKRLDDLALSIRDNRFMEQKNRLEKSGCEHKYYLIEETMSGNIGNMNEALKTALWVILVYYKFSMIRTCNSDETVEKIHALHTVISHHYSQKDLIVIFPSDLKSKDDYKKVLLQFRREFERKGGIECCHNLECFQELMGKGDLKTVGELTIHVLMLVKGISLEKAVAIQEIFPTLNKILMAYKTCSSEEEAKLLMFNVLGDAPGAKKITKSLSEKIYDAFGKL
Protein: Limpet, isoform J (M9MRX0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAEETALTGVGELLFSLLIGYLGALEFAFVARHLYHWTFQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPPRFQEPPEEPMVHKVKTQFGQGSGPEDAYSAKSKTLTFPGVSDEGSSLEPKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQEVQYTEDYLRSLDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSLEEEELRHGDREDYNPIKYTSEPTLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEEEIELERPSRGEDVEEEATNEPKSSSFEEATEAQNEQAVAALKQQLSKEQLDKEAEKDNPQAVDTSDSNKSNLIFSGEYTKAMDKDWHSGHFCCWQCDESLTGQRYVIRDDHPYCIKCYENVFANTCEECNKIIGIDSKDLSYKDKHWHEACFLCFKCHLSLVDKQFGAKADKIYCGNCYDAQFASRCDGCGEVFRAGTKKMEYKTRQWHENCFCCCVCKTAIGTKSFIPREQEIYCAGCYEEKFATRCIKCNKVITSGGVTYKNEPWHRECFTCTHCNITLAGQRFTSRDEKPYCAECFGELFAKRCTACVKPITGIGGTRFISFEDRHWHHDCFVCASCKASLVGRGFITDGPDILCPDCAKQKLM
Protein: Omega-hydroxypalmitate O-feruloyl transferase (EC 2.3.1.188) (Omega-hydroxyacid hydroxycinnamoyltransferase) (Protein ALIPHATIC SUBERIN FERULOYL TRANSFERASE) (Q94CD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of aromatics of the suberin polymer. Specifically affects the accumulation of the ferulate constituent of suberin in roots and seeds, but has no effect on the content of p-coumarate or sinapate.
Interaction partners:
- Cytochrome P450 86B1
- Cytochrome P450 86A8
- Glycerol-3-phosphate acyltransferase 5
- Cytochrome P450 86A2
- Probable fatty acyl-CoA reductase 5
- Cytochrome P450 86A7
- Fatty alcohol:caffeoyl-CoA acyltransferase
- Cytochrome P450 77A4
- Probable fatty acyl-CoA reductase 4
- Cytochrome P450 86A4
Sequence:
MVAENNKNKDVTLSASMDNNNNNIKGTNIHLEVHQKEPALVKPESETRKGLYFLSNLDQNIAVIVRTIYCFKSEERGNEEAVQVIKKALSQVLVHYYPLAGRLTISPEGKLTVDCTEEGVVFVEAEANCKMDEIGDITKPDPETLGKLVYDVVDAKNILEIPPVTAQVTKFKCGGFVLGLCMNHCMFDGIGAMEFVNSWGQVARGLPLTTPPFSDRTILNARNPPKIENLHQEFEEIEDKSNINSLYTKEPTLYRSFCFDPEKIKKLKLQATENSESLLGNSCTSFEALSAFVWRARTKSLKMLSDQKTKLLFAVDGRAKFEPQLPKGYFGNGIVLTNSICEAGELIEKPLSFAVGLVREAIKMVTDGYMRSAIDYFEVTRARPSLSSTLLITTWSRLGFHTTDFGWGEPILSGPVALPEKEVTLFLSHGEQRRSINVLLGLPATAMDVFQEQFLQI
Protein: BCL2 modifying factor 2 isoform X2 (BCL2-modifying factor 2) (U3JAJ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDDEEDEQLPRCCETPLRNKRSEKRDAHGGDVGQTAHRHASTQTAGSVLNSARDADMAPFQGSQREASSLCRVVGARTAFRAPCGTGGLVSLTMGPGARGGPRALFHGNAGFRAHFPALFEPALDGLQNAEQREQDEGRPEEKEEDRDAGISVEVQIGRKLREMGDQFQQEHLQLFTQRGQMGLFQLMTSIYNFLFPQERPQNARAHR
Protein: DNA-(Apurinic or apyrimidinic site) lyase, putative (EC 4.2.99.18) (Q383L5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein artemis
- Endonuclease III homolog lyase)
- Proliferating cell nuclear antigen
- DNA-
- Flap endonuclease 1
- Adenine DNA glycosylase
- Uracil-DNA glycosylase
- Sm protein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MFLISWNVAGWGSTARLIRSDFGTIAEFLRHTQADIVCLQEVKGSWQKLKDEPYAMGAGDGRPVSVEGWESFWSFSGRGQRGFNGVATFARKGLTWWCDSRPFIEADDKEGNSSPDASDKKTSTVEELHDEGRVLVTGHSAFVLVNTYVVNGRNSQRMAFKMRFLSCLKSLLARLKKENGKPVILVGDLNITFRAEDSHWSQRRLGFPSFMRLVHLARSLSNDEWKQSYPYIGQDTVCHLEGYIAEQTLQFLVDESDDPHPNDGRCARVDNLFSGLTKECKTTVTIDGNHLLQELVQKGRELKYHQNKGSGARVTLSELCEAGVTSVFASTLLRMQQTNHNRDIFVLVQYCGLPSHDEAGVEFMKELLVDLNLRDTMLVGLTPEALNDVCPCPYTCWDQSKNKRVVNEGNRIDYILIDASLAPKLAPCRDTENNVVRTLSEGIGHAGEDNGKKVVVDGCENTSSPFFSEFDGASHLLGVQRTAGHGAYPAAAMDGTGLPPLKKEARDLQFRGLPSTGLFVTPPQYSDHCGVCAYFPDLLLEPRPAKVKEIHPCLYRLPASLESFFQKRPRSE
Protein: Heat shock factor protein (HSF) (Heat shock transcription factor) (HSTF) (P22813)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
Subcellular location: Nucleus.
Interaction partners:
- Heat shock protein 83
- Major heat shock 70 kDa protein Ba
- Heat shock protein 83
- Cytosolic Prostaglandin E synthase
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- Heat shock factor-binding protein 1
- Transitional endoplasmic reticulum ATPase TER94
- 14-3-3 protein epsilon
- Protein deacetylase HDAC6
Sequence:
MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYSNQSVEDLLLQGNGTAGGNILVGGAASPMAQSVSQSPAQHDVYTVTEAPDSHVQEVPNSPPYYEEQNVLTTPMVREQEQQKRQQLKENNKLRRQAGDVILDAGDILVDSSSPKAQRTSIQHSTQPDVMVQPMIIKSEPENSSGLMDLMTPANDLYSVNFISEDMPTDIFEDALLPDGVEEAAKLDQQQKFGQSTVSSGKFASNFDVPTNSTLLDANQASTSKAAAKAQASEEEGMAVAKYSGAENGNNRDTNNSQLLRMASVDELHGHLESMQDELETLKDLLRGDGVAIDQNMLMGLFNDSDLMDNYGLSFPNDSISSEKKAPSGSELISYQPMYDLSDILDTDDGNNDQEASRRQMQTQSSVLNTPRHEL
Protein: Alginate biosynthesis protein AlgF (P70799)
Organism: Azotobacter vinelandii
Function: Together with AlgI and AlgJ, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate increases cyst resistance to desiccation.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTRLHRKHRIALGLGLGLLLGFGGTTVQAAGDAALYEAVAPKGSTFVRLYNASNQEVSANVGSINLEDVSPLSSSGFEYLPAGQYSARVGSQNLPVNLSAEHYYTLVTQSGAAPLLVEEPAFKSKQKALLRVQNLSDKPLTLKTADGKTEVVKSVEPKGRGDREINPVKANLALFDGERKVADLKPISLARGEVVCLYVTGTANQLNPVWVKPPVKE
Protein: BAG family molecular chaperone regulator 2 (BAG-2) (Bcl-2-associated athanogene 2) (O95816)
Organism: Homo sapiens (Human)
Function: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release.
Interaction partners:
- Heat shock cognate 71 kDa protein
- BAG family molecular chaperone regulator 1
- Heat shock 70 kDa protein 4
- E3 ubiquitin-protein ligase CHIP
- Heat shock protein 105 kDa
- BAG family molecular chaperone regulator 3
- Hsp70-binding protein 1
- BAG family molecular chaperone regulator 5
- Heat shock 70 kDa protein 4L
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Sequence:
MAQAKINAKANEGRFCRSSSMADRSSRLLESLDQLELRVEALREAATAVEQEKEILLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRNPQQQESLKHATRIIDEVVNKFLDDLGNAKSHLMSLYSACSSEVPHGPVDQKFQSIVIGCALEDQKKIKRRLETLLRNIENSDKAIKLLEHSKGAGSKTLQQNAESRFN
Protein: RE01730p (Secreted Wg-interacting molecule, isoform A) (Secreted Wg-interacting molecule, isoform B) (Q7JWQ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIKCVHLVGLLVLLMGGANALFDHTLKRDFPGPYCARENTCCKDRHDGCSVPISNTLCYCDEFCDRDDSSDCCPDYRSFCIGEVDPIISCEHNGVYFSKYNTTWDNCNECRCLEGGSVQCDEDLCLTDDAIVHSVNSIHRLGWSARKYDQWWGRKYSEGLKLRLGTKEPTYRVKAMTRLKNPTDGLPSSFNALDKWSSYISEVPDQGWCGASWVLSTTSVASDRFAIQSKGKENVQLSAQNILSCTRRQQGCEGGHLDAAWRYLHKKGVVDENCYPYTQHRDTCKIRHNSRSLRANGCQKPVNVDRDSLYTVGPAYSLNREADIMAEIFHSGPVQATMRVNRDFFAYSGGVYRETAANRKAPTGFHSVKLVGWGEEHNGEKYWIAANSWGSWWGEHGYFRILRGSNECGIEEYVLASWPYVYSYYNVKSA