wanglab/gogpt-training-data huggingface dataset:
Protein: Sorting nexin-6 [Cleaved into: Sorting nexin-6, N-terminally processed] (Q6P8X1)
Organism: Mus musculus (Mouse)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity (By similarity). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R. May function as link between transport vesicles and dynactin. Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity). In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B. May contribute to transcription regulation (By similarity).
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:20228253}; Peripheral membrane protein {ECO:0000269|PubMed:20228253}; Cytoplasmic side {ECO:0000269|PubMed:20228253}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9UNH7}. Cytoplasm {ECO:0000250|UniProtKB:Q9UNH7}. Nucleus {ECO:0000250|UniProtKB:Q9UNH7}. Note=Interaction with SNX1 or SNX2 promotes location at endosome membranes (By similarity). Only a minor proportion is seen in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9UNH7}.
Interaction partners:
- Sorting nexin-1
- Sorting nexin-2
- Sorting nexin-5
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26A
- Sorting nexin-27
- Sorting nexin-32
- Sorting nexin-3
- Dynactin subunit 1
Sequence:
MMEGLDDGPDFLSEEDRGLKAINVDLQSDAALQVDISDALSERDRVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT
Protein: Hydrogenase maturation factor HybG (Hydrogenase-2 operon protein HybG) (P0AAM7)
Organism: Escherichia coli (strain K12)
Function: Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor. HybG delivers iron-bound CO(2) to HypD where reduction to CO probably occurs. In complex with HypD, accepts the cyanide ligand generated by HypF and HypE, and also coordinates the carbon monoxide ligand (By similarity). Involved in the maturation of the hydrogenase 2. Also participates in the maturation of hydrogenase 1.
Interaction partners:
- Hydrogenase maturation factor HypD
- Carbamoyl dehydratase HypE
- Hydrogenase maturation factor HybF
- Hydrogenase-2 large chain
- Hydrogenase 2 maturation protease
- Carbamoyltransferase HypF
- Hydrogenase-2 operon protein HybE
- Hydrogenase maturation factor HypB
- Hydrogenase-1 large chain
- Hydrogenase-2 small chain
Sequence:
MCIGVPGQVLAVGEDIHQLAQVEVCGIKRDVNIALICEGNPADLLGQWVLVHVGFAMSIIDEDEAKATLDALRQMDYDITSA
Protein: Succinate dehydrogenase subunit 4, mitochondrial (Q941A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Succinate dehydrogenase subunit 8
- Succinate dehydrogenase subunit 7B
- Succinate dehydrogenase subunit 7A
- Succinate dehydrogenase subunit 3-2
- Succinate dehydrogenase subunit 5
- Succinate dehydrogenase subunit 3-1
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
Sequence:
MSLRRTILDLHRQTQRATLSKSLPFSMSHISSASATAAVRNPLGRDLSSIPFAQAQKLKPDSTNLVTDRSISSSIGQSELNKAAKFSRQSSSRGYTNGSFLRKIPVVFHIHEGMEEILADYVHQEMTRNLIVMSLGLFQIIVLKDIILFLL
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (P49153)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MAKKVKSKVDTINTKIQLVMKSGKYVLGTQQSLKTLRQGRSKLVVISANCPPIRKAEIEYYCTLSKTPIHHYSGNNLDLGTACGRHFRACVLSITDVGDSDITSA
Protein: L-prolyl-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14) (Flavoprotein desaturase PigA) (L-prolyl-PCP dehydrogenase) (Q5W271)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the desaturation of the L-prolyl-[PigG] to yield 1H-pyrrole-2-carbonyl-[PigG].
Interaction partners:
- Electron transfer flavoprotein subunit alpha
- enoyl-CoA hydratase
- enoyl-CoA hydratase
- NADH-quinone oxidoreductase subunit C/D
- Enoyl-CoA hydratase/isomerase family protein
- Electron transfer flavoprotein
- Enoyl-CoA hydratase/isomerase family protein
- 3-hydroxybutyryl-CoA dehydrogenase
- Pyruvate-flavodoxin oxidoreductase
- Non-ribosomal peptide synthetase
Sequence:
MDFNLSNSQSDIYESAYRFACDVLDQDAQTRISQKILSTELWKKAAAYGFAHGPVSHQFGGSELGALDTALMIEALGKGSRDIGLSFSLCAHLCACVIPLYRFGSSELKDKYLESLVTGKLIAANAATEPDAGSDIYNMQATAQPCEGGYILNGKKIFITNAPIADVFIIYAKTNPDHGFLGVSAFLIEKGTPGLNVGEVIPKDCLSNCPWSEIVFNDIFIPQSQRIGMEGAGGAIFHDSMIWEKGCLSALFVGGLARLLETTLEYAKARQQFGKAIGQFQSVSNRIIDMKLRLEQCRLMLYRACWKHDQGQDAEADIAMSKLLISEYAVQSGLDAIQTFGGAAMDQELGLVRHLLNMIPSRIFSGTNDIQKEIIARKLGLRGTSS
Protein: Ribonucleoside-diphosphate reductase subunit M2 (EC 1.17.4.1) (Ribonucleotide reductase small subunit) (P48592)
Organism: Drosophila melanogaster (Fruit fly)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Proliferating cell nuclear antigen
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm2
- DNA replication licensing factor MCM4
- DNA replication licensing factor Mcm7
- Thymidylate kinase
- Thymidylate synthase
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm6
Sequence:
MASKENIADNMEKFSLKSPSKKILTDSTNNVRKMSIGHEANGQLAKESSTVNGIGKSANSLMEKSVTPFDPSLEPLLRENPRRFVIFPIQYHDIWQMYKKAEASFWTVEEVDLSKDLTDWHRLKDDERHFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENVHSEMYSVLIDTYIRDPHQREYLFNAIETMPAVKRKADWALSWISSKSANFGERIIAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFAVLMFQHLVQRPKRERIIEIIRDAVAIEQEFLTDALPVNLIGMNCDLMSQYIEFVADRLLVELGVGKIYNTKNPFNFMEMISLDGKTNFFEKKVGEYQRMGVVSNPLDNVFTLDADF
Protein: Non-structural protein 4b (ns4b) (Accessory protein 4b) (P19740)
Organism: Human coronavirus 229E (HCoV-229E)
Interaction partners:
Sequence:
MQGKCWFLENKALKPFVCFYGGDQFLYIGDRIVSYFSTNDLYVALRGRIDKDLSLSRKVELYNGECVYLFCEHPAVGIVNTDFKLEIH
Protein: LIM homeobox transcription factor 1-alpha (LIM/homeobox protein 1.1) (LMX-1.1) (LIM/homeobox protein LMX1A) (Q9JKU8)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Nuclear receptor subfamily 4 group A member 2
- Hepatocyte nuclear factor 3-beta
- Homeobox protein OTX2
- Neurogenin-2
- Achaete-scute homolog 1
- Tyrosine 3-monooxygenase
- G protein-activated inward rectifier potassium channel 2
- Sonic hedgehog protein
Sequence:
MLDGLKMEENFQSAIETSASFSSLLGRAVSPKSVCEGCQRVISDRFLLRLNDSFWHEQCVQCASCKEPLETTCFYRDKKLYCKYHYEKLFAVKCGGCFEAIAPNEFVMRAQKSVYHLSCFCCCVCERQLQKGDEFVLKEGQLLCKGDYEKERELLSLVSPAASDSGKSDDEESLCKSAHGAGKGASEDGKDHKRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRQQQQQQDQQNTQRLTSAQTNGSGNAGMEGIMNPYTTLPTPQQLLAIEQSVYNSDPFRQGLTPPQMPGDHMHPYGAEPLFHDLDSDDTSLSNLGDCFLATSEAGPLQSRVGNPIDHLYSMQNSYFTS
Protein: Fructose dehydrogenase small subunit (Fructose dehydrogenase subunit III) (M1VB40)
Organism: Gluconobacter japonicus
Function: Subunit of fructose dehydrogenase, an enzyme that catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161}.
Interaction partners:
Sequence:
MEKIADSGPVQIFLSRRKLLAFSGASLTVAAIGAPSKGSTQDVVASNRDSISDFMQLSAFATGHKNLDLNIGSALLLAFEAQKHDFSTQIKALREHITKNNYQDVEALDAAMKDDPLHPTLIQIIRAWYSGVIEDETNAKVYAFEKALMYQPSRDVVVIPTYAHNGPNYWVSEPASVDVMPAF
Protein: RNA-binding protein, putative (Q582F3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pab1p-dependent poly
- Probable eukaryotic initiation factor 4A
- Nuclear cap-binding protein subunit 2
- Regulator of nonsense transcripts 1, putative
- PAB1-binding protein 1
- Eukaryotic release factor 3, putative
Sequence:
MSLFSFTPTGGSNMPRTTSTEENTTSDCQTSLNHPPPKMTFTDMLNTKIQNSNKHSSEDKNSNCSTVDEVLDCCDYGYGCVHGNALVEEGAEEMRRRYFLEMQRNLLDDVDTDNEEQIDSKIVSTCRSTTSVSARDSSEVLGPIPLPHDGGDVLSFNPFASSVTYSPLSDENGCVENLSPNPSSRTPLSSSTSGAQLPNGSFSSISPSLSTHPTGRLATRKNVYVSELPTHWNTEKLRSVCATFGNIVSAKVMHDSNTNESRGYGFVMFETDEQAALCVRTLNSCKVDGRMLSCRFAHEKAMPSFAHSDRIPWQEFGRSPNSTTPSLSKDKLTDVKTQPDQQQGGNSLPNMELLKGAHVACFGDRSRPMVQRSHNIFIQGLPLQWNTDKLRSLCGTFGKVELAKVVRDATTSLSCGHGFVLFEREEAAALCVERLNGATVEGRTLTCRFARDKRGPGVATGAAPSPPVRPSGNDFLKNTAPLLVRMVDAQESPSMLLQSAVGSNKWSTVTVPQNCHTAVYSQSPLLVAGGVSPLLGLSPVVSPMVPSGVMTEMTEPPHGMQSFGCNIAGLQCLIAVPYHQTRIVSGFSNGDGGTFAALT
Protein: Cadherin domain-containing protein (Q3UTF9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAAMPGTVRSWVEIWWGATLLFLFCHLGYVYGQIRYPVPEESQEGTFVGNVAQDFLLDTESLSARRLQVAGEVNQRHFRVDLDSGALLIKNPIDREALCGLSASCIVPLEFVTEGPLEMYRAEVEIVDVNDHAPRFPRQQLDLEIGEAAPPGQRFPLEKAQDADVGSNSISSYRLSSNEHFALDVKKRSDGSLVPELLLEKPLDREKQSDYRLVLTAVDGGNPPRSGTAELRVSVLDVNDNAPAFQQSSYRISVLESAPAGMVLIQLNASDPDLGPSGNVTFSFSGHTPDRVRNLFSLHPTTGKLTLQGPLDFESENYYEFDVRARDGGSPAMEQHCSLRVDLLDVNDNAPHITVTSELGTLPESAEPGTVVALISVQDPDSGSNGDVSLRIPDHLPFALKSAFRNQFSLVTAGPLDREARSSYDIMVTASDAGNPPLSTHRTIFLNISDVNDNPPSFFQRSHEVFVPENNRPGDLLCSLAASDPDSGLNALISYSLLEPRNRDVSASSFISLNPQTGAVHATRSFDYEQTQTLQFEVQARDRGSPPLSSTVTVRLFVLDLNDNAPAVLRPRARPGSLCPQALPPSVGAGHLVTKVTAVDLDSGYNAWVSYQLLEAPDPSLFAVSRYAGEVRTAVPIPADLPPQKLVIVVKDSGSPPLSTSVTLLVSLEEDTHPVVPDLRESSAPREGESRLTLYLAVSLVAICFVSFGSFVALLSKCLRGAACGVTCFPAGTCACLTRSRRREGLPPSNGILRIQLGSEDPIKFVDVGGHSHGCTPLASAPTRSDSFMMVKSPSAPMAGEPVRPSCPPSDLLYGLEVRPLQAQPMLEGDCDPAMWLGRVPEGTDLPVRAHRGATIFVSSNCVVNSVLYKWFQN
Protein: E3 ubiquitin-protein ligase MPSR1 (EC 2.3.2.27) (Protein MISFOLDED PROTEIN SENSING RING E3 LIGASE 1) (RING-type E3 ubiquitin transferase MPSR1) (Q9LQX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in protein quality control (PQC) under proteotoxic stress. Is essential to plant survival under proteotoxic stress. Functions by removing damaged proteins before they form cytotoxic aggregates. Recognizes misfolded proteins selectively and tethers polyubiquitin chains to the proteins directly for subsequent degradation by the 26S proteasome pathway. Targets misfolded proteins independently of cytoplasmic chaperones. Associates with the 26S proteasome and sustains the structural integrity of the proteasome complex at the initial stage of proteotoxic stress. Under normal conditions, MPSR1 becomes highly unstable by its autoubiquitination activity and is stabilized during proteotoxic stress by conjugating ubiquitins on misfolded proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29087340}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- E3 ubiquitin-protein ligase CHIP
- DNA ligase 6
- Ubiquitin-conjugating enzyme E2 8
- E3 ubiquitin-protein ligase AIRP1
- Chloride conductance regulatory protein ICln
- E3 ubiquitin-protein ligase AIRP2
- Pyruvate, phosphate dikinase regulatory protein 2
- Heat shock protein 90-1
Sequence:
MATEQEAEVGTETSSVSGRFLRNRDLYLFLPFLLGFSDQESSNGDDDDVASSRERIILVNPFTQGMIVLEGSSGMNPLLRSLLESREEGRPPASKASIDAMPIVEIDGCEGECVICLEEWKSEETVKEMPCKHRFHGGCIEKWLGFHGSCPVCRYEMPVDGDEIGKKRNDGNEIWVRFSFNDGRRIRDFSAQDGGNSDGVESEN
Protein: Variant surface glycoprotein (VSG), putative (Q38CP0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MAKKVLGFAQLATLIVVLSPSSIYANVGPGDNAAEFTTLCQLISLAEGAAQPPAATTAPSAEYDELMRLNMTLSDEAWHDMFIKSKADKTWHDAIPATAKDPGGWAEAWPTWRKAAEELTQEDKMANIKSLNVNAANPKQKAMIITEIRKMADAAQELMKKRHTLDKSIEKPPQEYAAALKTLAYGDKTKNRKTVTAADAFKGGSTSFSTDCGGAAASNKIKTVAATITCLCHKANTQNEDQVCGRTVKITTNTWTVNGAIGSAGVITEPLGFCSVEQGTDLTSSEITAILRQLKSLIKVTSNDGILGASDNGSCDADKTHGICIKLTNWAADGKVDITKLEWAKQAVELAKELSRREHAAASAAEIDSAIRNLHRQAFRTTLYTAHIQHNPHQTATPLDSTSKNDKGMEDKKKECEKHKNNKTSCTNAKCIWEGKDGKSDTEGECKPKDGGKGTAQTNAGTGDGTAGTGPNCASQTKKEDCEKENVGKTTPVCGWRIGKDNEPDKDKEMCRNGSFLVNKQFALSVVSAAFVALLF
Protein: Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) (P07222)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a chaperonin for the core histones H3, H2B and H4. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. It may function in the assembly and/or transport of ribosome. May stimulate endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA. May inhibit endonuclease activity on AP single-stranded RNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
Sequence:
MEDSMDMDNIAPLRPQNFLFGCELKADKKEYSFKVEDDENEHQLSLRTVSLGASAKDELHVVEAEGINYEGKTIKIALASLKPSVQPTVSLGGFEITPPVILRLKSGSGPVYVSGQHLVALEDLESSDDEDEEHEPSPKNAKRIAPDSASKVPRKKTRLEEEEEDSDEDDDDDEDDDDEDDDEEEEETPVKKTDSTKSKAAQKLNHNGKASALSTTQKTPKTPEQKGKQDTKPQTPKTPKTPLSSEEIKAKMQTYLEKGNVLPKVEVKFANYVKNCFRTENQKVIEDLWKWRQSLKDGK
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (Oligosaccharyl transferase 48 kDa subunit) (Protein DEFECTIVE GLYCOSYLATION 1) (Q944K2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Dol-P-Glc:Glc
Sequence:
MVNLSRSVALISVFLLPLLSFSFSVDNPTDRRVLVLLDDLSLKSSHSIFFNTLKSRGFDLDFKLAEDSKLALQRYGQYLYDGLIIFAPSTERFGGSLDSKSIADFVDSGRDLILSADTAASDLIRGIATECGVDFDEDSSAMVIDHTSFSVSDVDGDHTLIAADDLVKSDVILGKTKIEAPVLFRGVAHSLNPTNNLVLKVLSASPSAYSANPSSKLSSPPQLTGSSISLVSVMQARNNARVVISGSVQLFSDRLIRSGVQKAGSPNQYEKSGNEQFVTELSKWVFHERGHLKAGNLVHHRVGETDEPAIYRIKDDLEFSVEIYEWSGKSWEPYVANDVQVQFYMMSPYVLKTLSTDKKGLFHTSFKVPDVYGVFQFKVEYEKLGYTTLSLSKQIPVRPYRHNEYERFIPTAYPYYGACFTTMAGFFVFSFVYLYHK
Protein: DNA damage response protein kinase DUN1 (EC 2.7.11.1) (P39009)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transducer of the DNA damage signal. Phosphorylates SML1 on serine residues. Cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Subcellular location: Nucleus.
Interaction partners:
- Serine/threonine-protein kinase MEC1
- Serine/threonine-protein kinase RAD53
- Ribonucleotide reductase inhibitor protein SML1
- RFX-like DNA-binding protein RFX1
- Ribonucleoside-diphosphate reductase large chain 1
- Serine/threonine-protein kinase TEL1
- DNA repair protein RAD9
- Ribonucleoside-diphosphate reductase small chain 1
- Serine/threonine-protein kinase CHK1
- General transcriptional corepressor CYC8
Sequence:
MSLSTKREHSGDVTDSSFKRQQRSNKPSSEYTCLGHLVNLIPGKEQKVEITNRNVTTIGRSRSCDVILSEPDISTFHAEFHLLQMDVDNFQRNLINVIDKSRNGTFINGNRLVKKDYILKNGDRIVFGKSCSFLFKYASSSSTDIENDDEKVSSESRSYKNDDEVFKKPQISATSSQNATTSAAIRKLNKTRPVSFFDKYLLGKELGAGHYALVKEAKNKKTGQQVAVKIFHAQQNDDQKKNKQFREETNILMRVQHPNIVNLLDSFVEPISKSQIQKYLVLEKIDDGELFERIVRKTCLRQDESKALFKQLLTGLKYLHEQNIIHRDIKPENILLNITRRENPSQVQLGPWDEDEIDIQVKIADFGLAKFTGEMQFTNTLCGTPSYVAPEVLTKKGYTSKVDLWSAGVILYVCLCGFPPFSDQLGPPSLKEQILQAKYAFYSPYWDKIDDSVLHLISNLLVLNPDERYNIDEALNHPWFNDIQQQSSVSLELQRLQITDNKIPKTYSELSCL
Protein: Atrochrysone carboxyl ACP thioesterase (ACTE) (EC 3.1.2.-) (Endocrocin synthesis protein B) (Q4W945)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA. The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA. The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC. The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself.
Interaction partners:
- Atrochrysone carboxylic acid synthase
- Anthrone oxygenase encC
Sequence:
MDQYSNLFAFEDYLGAQARSIPDLPEVDVLSPRVVRVLGGNPGQMQLQGTNTYILGTGAERLLIDSGQGRARWEQLMASLAAEHKFRISTVLLTHWHLDHTGGVPHLFRIFPELRGANAIYKYHPDPSQQAIVDGQVFSVEGATVRAVFTPGHSTDHMCFLLQEEEAIFTGDTVLGHGTTGVEDLEEYMQSLRKIQSLGCRIGYPGHGAVIENMQQKVQQEIDRKQRRERQVLLALQNIQREKRTVGDANGAATQAELIEAIFGRLPADVADRFFAPYMKDILMKMARDKQVGFRFKGGQKHWFANVSQENPVCR
Protein: Oligoribonuclease, mitochondrial (EC 3.1.15.-) (RNA exonuclease 2 homolog) (Small fragment nuclease) (Q9Y3B8)
Organism: Homo sapiens (Human)
Function: 3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides. Binds and degrades longer oligonucleotides with a lower affinity. Plays dual roles in mitochondria, scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that are produced by the degradosome and clearing short RNAs that are generated by RNA processing. Essential for correct initiation of mitochondrial transcription, degrading mitochondrial RNA dinucleotides to prevent RNA-primed transcription at non-canonical sites in the mitochondrial genome. Essential for embryonic development (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:23741365}. Mitochondrion matrix {ECO:0000269|PubMed:23741365}. Mitochondrion {ECO:0000269|PubMed:32365187}. Cytoplasm {ECO:0000269|PubMed:23741365, ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}.
Interaction partners:
- RNA exonuclease 5
- RNA exonuclease 1 homolog
- RNA exonuclease 4
- Exonuclease 1
- Phosphoglucomutase-like protein 5
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Sequence:
MLGGSLGSRLLRGVGGSHGRFGARGVREGGAAMAAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNILAEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTITLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKIDEKKRKIIENGENEKTVS
Protein: Rap guanine nucleotide exchange factor 5 (A8MQ07)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAIGVWQLLLDMGIMLSVDQHLYFQDTYVFYQFSSDECSYLYCEFEREEEWQNGVKLLLQLVPLIPARGGICELSHQKIEDSEESSDEILVRLTSAVQRELAAVIALKARKSAIEQDEENNDKHVAVTEAESVPDSQAGVMCKLQERDEIGRIELVQKLAKENYQFLQTDKKEQEKSEHQDDEVTTVQVKEQDQSVLVLKKVQCCGPAPTAGSAESHWRYVVVSGTPEKILEHLLNDLHLEEVQDKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQGKEENSDVPRRKRKVLHLVSQWIALYKDWLPEDEHSKMFLKTIYRNVLDDVYEYPILEKELKEFQKILGMHRRHTVDEYSPQKKNKALFHQFSLKENWLQHRGTVTETEEIFCHVYITEHSYVSVKAKVSSIAQEILKVVAEKIQYAEEDLALVAITFSGEKHELQPNDLVISKSLEASGRIYVYRKDLADTLNPFAENEESQQRSMRILGMNTWDLALELMNFDWSLFNSIHEQELIYFTFSRQGSGEHTANLSLLLQRCNEVQLWVATEILLCSQLGKRVQLVKKFIKIAAHCKAQRNLNSFFAIVMGLNTASVSRLSQTWEKIPGKFKKLFSELESLTDPSLNHKAYRDAFKKMKPPKIPFMPLLLKDVTFIHEGNKTFLDNLVNFEKLHMIADTVRTLRHCRTNQFGDLSPKEHQELKSYVNHLYVIDSQQALFELSHRIEPRV
Protein: Lipoyl amidotransferase LIPT1, mitochondrial (EC 2.3.1.200) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase) (Lipoyltransferase 1) (EC 2.3.1.-) (Q8VCM4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O46419}.
Interaction partners:
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Acyl-coenzyme A synthetase ACSM1, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- U5 small nuclear ribonucleoprotein 40 kDa protein
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Sequence:
MLIPLSMKNCFRLLCQHKVPAAGFKSPPTHGLILQSISNDVYENLAFEDWIHDHIHLEGKPILFLWRNSPSVVIGRHQNPWQECNLHLMRQEGIKLARRKSGGGAVYHDMGNINLTFFTTKTKYDRMENLKLIVRALNAVQPQLDVQPTKKFDLLLDGQFKISGTASKIGRTAAYHHCTLLCSTNRTALSSSLKSPYCGIKSNATPSIPSAVKNLLERDSTLTCEVLMSAVAAEYAAHHQVDGHVNLINPADETMFPGINRKVKELQSWEWVYGRTPKFTVDTTFHVPYEQAHLEIQVFMDVKNGRIETCAIKAPDHWLPLEIGEKLNSSFIGSKFCPVETTLLTNVLLRTCPGDHHLHSKWYILCEKIRGIM
Protein: Probable sugar phosphate/phosphate translocator At5g25400 (Q3E6T0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GDP-fucose transporter 1
- UDP-rhamnose/UDP-galactose transporter 2
- UDP-galactose/UDP-glucose transporter 3
- At4g32290
- GDP-mannose transporter GONST1
Sequence:
MGKGGSLSEGVIKNIIISYTYVAIWIFLSFTVIVYNKYILDKKMYDWPFPISLTMIHMSFCSTLAFLLIKVFKFVEPVSMSRDTYLRSVVPIGALYSLSLWLSNSAYIYLSVSFIQMLKALMPVAVYSIGVLFKKEGFKSETMMNMLSISFGVAIAAYGEARFDVWGVILQLGAVAFEATRLVMIQILLTSKGITLNPITSLYYVAPCCLAFLFIPWIVVEFPILRDTSSFHFDYLIFGTNSFCAFALNLAVFLLVGKTSALTMNVAGVVKDWLLIAFSWSVIKDTVTPINLFGYGIAFLGVAYYNHAKLQALKAKEAQKTAQQVDEETGRLLEEREGNEGGRKNEPED