wanglab/gogpt-training-data huggingface dataset:
Protein: NADH-cytochrome b5 reductase 2 (EC 1.6.2.2) (Mitochondrial cytochrome b reductase) (p34/p32) [Cleaved into: NADH-cytochrome b5 reductase p34 form; NADH-cytochrome b5 reductase p32 form] (P36060)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The outer membrane form may mediate the reduction of outer membrane cytochrome b5. The soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals. May play a minor role in complementing the function of CBR1 as a DPH3 reductase in the first step of diphthamide biosynthesis and tRNA Wobble base mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine) formation.
Subcellular location: [NADH-cytochrome b5 reductase p32 form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:8001120}.; SUBCELLULAR LOCATION: [NADH-cytochrome b5 reductase p34 form]: Mitochondrion outer membrane; Single-pass membrane protein. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:8001120}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Cytochrome b5
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- C-22 sterol desaturase ERG5
Sequence:
MFSRLSRSHSKALPIALGTVAIAAATAFYFANRNQHSFVFNESNKVFKGDDKWIDLPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKESTHLFVCGPPPFMNAYSGEKKSPKDQGELIGILNNLGYSKDQVFKF
Protein: Large ribosomal subunit protein eL28 (60S ribosomal protein L28) (P17702)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P46779}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL34
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Large ribosomal subunit protein uL13
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MSAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEAWPDGKGVVVVMKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVVVKRKRTRPTKSS
Protein: Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) (Q14974)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In association with IPO7, mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11891849}. Nucleus envelope {ECO:0000269|PubMed:11891849}.
Interaction partners:
- Importin subunit alpha-5
- GTP-binding nuclear protein Ran
- Importin subunit alpha-1
- Snurportin-1
- Nuclear pore complex protein Nup153
- Importin subunit alpha-7
- Importin subunit alpha-3
- E3 SUMO-protein ligase RanBP2
- Importin subunit alpha-4
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
Protein: Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Calcium-independent phospholipase A2-zeta) (iPLA2-zeta) (EC 3.1.1.4) (P0C548)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (By similarity). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (By similarity). Also possesses acylglycerol transacylase and phospholipase A2 activities (By similarity). Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides (By similarity). Regulates adiposome size and may be involved in the degradation of adiposomes (By similarity). May play an important role in energy homeostasis (By similarity). May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion (By similarity).
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:Q96AD5}. Cell membrane {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BJ56}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Lipoprotein lipase
- Perilipin-5
- Hormone-sensitive lipase
- Hepatic triacylglycerol lipase
- Pancreatic triacylglycerol lipase
- Gastric triacylglycerol lipase
- Endothelial lipase
Sequence:
MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVTEERTGGEDRILEHLPARLNEALLEACVEPKDLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGDHLPSRLSEQVELRRAQSLPSVPLSCATYSEALPNWVRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPDALRMRAPASPTATDPATPQDPSGLPPC
Protein: Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (P49740)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Interaction partners:
- CTP synthase
- Thymidylate kinase
- Ribonucleoside-diphosphate reductase large chain
- Uridylate kinase
- Inosine triphosphate pyrophosphatase
- Adenylate kinase
- Guanylate kinase
- Ribonucleoside-diphosphate reductase small chain
- Small ribosomal subunit protein uS10m
- Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
Sequence:
MSTEQTFIAVKPDAVQRGLIGYIISKFELKGYKLRALKFLVPSRDLVEEHYAEHKGKPFYEKLVGFMASGPVCAMIWEGKQAVKTGRLMLGASNPLDSAPGTIRGDYGIDLGRNVCHGSDSIESANREIKLWFQPSEIQVYDRTIEPWIYE
Protein: EG214403 protein (B2RUG5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGFCSMLLLSNILLTAWLSTAKGEVKSCEFPQFKYGRLYYEEILRPNFPVSIGNKYSYKCDNGFSPPSGIFWDYLRCTVQGWEPEVPCVRKCVFHYVENGQSAYWEKIYVQGQSLKVQCYNGYSLQNGQDTMTCTENGWSPPPKCIRIKTCSVSDIEIENGFFSESFRTYALNRETSYRCKQGYVTNTGETSGSITCLQNGWSPQPSCIKSCERPVFENSVTKNNSTWFKLNDKLDYECLIGYENEYKHTKGSITCTYYGWSDTPSCYEIECSVPILDRKLVVSPRKEKYRVGDLLEFSCRSGHRVGPDSVQCYHFGWSPSFPTCKGQVASCAQPPEIPNGEINGAKRVEYSHGEVVGYDCKPRFLLKGPNKIQCVDGMWTTLPVCVEEERTCGDIPELEHGSVKFSVPPYHHGDSVEFTCAETFTMIGLGSVFCLSGKWTQLPKCVATDQLEKCRVLKSTDIEAIKPKRKEFQHNSTMYYKCRDKQEYEHSICINGKWNPEPNCIRKISCPPPPQIPNTQVIETTVKYLDGEKLSVLCQDNYLTQDPEEMMCKDGRWQSLPHCIEKIPCSQPPTIEHGSIKLPRTSEKRRKSIEFSSHEHGTTFSYVCDDGFRIPEENGVACYMGKWSTPPRCVGLPCGPPPSIPLGTVSLELESYQHGEEVTYHCSTGFGIDGPALIKCEGGKWSDPPKCIKTDCDILPTIENAIIRGKNKKSYRTGEQVTVRCQSPYQMNGSDTVTCINGRWIGKPVCKDSRGKCGPPPPIDNGDITSLSLPEYEPFSSVDYQCQKYYLLKGKKTITCRNGKWSEPPTCLHACIIPENIMEARKIILKWRHTKNIYSHSGEDIEFECKYGYHKARGSPPFRTKCISGTINYAICE
Protein: Transcription factor MYB80 (Myb-related protein 80) (OsMYB80) (Q7XQN1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Essential for tapetum development in anthers and microsporogenesis. May regulate the timing of tapetal programmed cell death (PCD) which is critical for pollen development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MGRVPCCEKDNVKRGQWTPEEDNKLLSYITQYGTRNWRLIPKNAGLQRCGKSCRLRWTNYLRPDLKHGEFTDAEEQTIIKLHSVVGNRWSVIAAQLPGRTDNDVKNHWNTKLKKKLSGMGIDPVTHKSFSHLMAEIATTLAPPQVAHLAEAALGCFKDEMLHLLTKKRPSDFPSPAVHDGAGAGASASALAAPCFPAAPPHHPQADDTIERIKLGLSRAIMSDPSTASAAAAAAAPSAPAEDKPWPPGDMSEGLAGMYATYNPAAHAHAQAQAEFRYDGASAAQGYVLGGDGDQGTSMWSHQSLYSGSSGTEEARRELPEKGNDSVGSSGGDDDAADDGKDSGKGAASDMSGLFASDCVLWDLPDELTNHMV
Protein: Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (RIP-homologous kinase) (Receptor-interacting serine/threonine-protein kinase 5) (Sugen kinase 496) (SgK496) (Q6XUX3)
Organism: Homo sapiens (Human)
Function: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death. In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to UV stress in a range of dermal cell types.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17123648, ECO:0000269|PubMed:23862974}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000269|PubMed:23862974}. Basolateral cell membrane {ECO:0000269|PubMed:23862974}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}. Note=Detected at apical cell-cell junctions. Colocalized with FGF receptors to the cell membrane (By similarity). Detected in basolateral and apical membranes of all tubular epithelia. {ECO:0000250|UniProtKB:Q6XUX1, ECO:0000269|PubMed:23862974}.
Interaction partners:
Sequence:
MEGDGVPWGSEPVSGPGPGGGGMIRELCRGFGRYRRYLGRLRQNLRETQKFFRDIKCSHNHTCLSSLTGGGGAERGPAGDVAETGLQAGQLSCISFPPKEEKYLQQIVDCLPCILILGQDCNVKCQLLNLLLGVQVLPTTKLGSEESCKLRRLRFTYGTQTRVSLALPGQYELVHTLVAHQGNWETIPEEDLEVQENNEDAAHVLAELEVTMHHALLQEVDVVVAPCQGLRPTVDVLGDLVNDFLPVITYALHKDELSERDEQELQEIRKYFSFPVFFFKVPKLGSEIIDSSTRRMESERSPLYRQLIDLGYLSSSHWNCGAPGQDTKAQSMLVEQSEKLRHLSTFSHQVLQTRLVDAAKALNLVHCHCLDIFINQAFDMQRDLQITPKRLEYTRKKENELYESLMNIANRKQEEMKDMIVETLNTMKEELLDDATNMEFKDVIVPENGEPVGTREIKCCIRQIQELIISRLNQAVANKLISSVDYLRESFVGTLERCLQSLEKSQDVSVHITSNYLKQILNAAYHVEVTFHSGSSVTRMLWEQIKQIIQRITWVSPPAITLEWKRKVAQEAIESLSASKLAKSICSQFRTRLNSSHEAFAASLRQLEAGHSGRLEKTEDLWLRVRKDHAPRLARLSLESCSLQDVLLHRKPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSIAVLLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSVKLPEAFERCASKDHLWNNVRRGARPERLPVFDEECWQLMEACWDGDPLKRPLLGIVQPMLQGIMNRLCKSNSEQPNRGLDDST
Protein: Probable anion transporter 4, chloroplastic (Phosphate transporter PHT4;3) (Q66GI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inorganic phosphate and probable anion transporter.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable inorganic phosphate transporter 1-6
- Mitochondrial phosphate carrier protein 1, mitochondrial
- Inorganic phosphate transporter 2-1, chloroplastic
- Putative defensin-like protein 288
- Alpha/beta-Hydrolases superfamily protein
- F-box/FBD/LRR-repeat protein At1g13570
- Defensin-like protein 268
- ATG8-interacting protein 2
- Defensin-like protein 286
- Probable transcription factor At4g00390
Sequence:
MCYSLSIQSSIDFHNRNALKIHGDRAILTSNLPTLRRIPFLPERDRRRKLVLCTGRVVNSLKFTGNTSVDLCGIPRHRLRVSCSDARRTPEETAAELTAQPNFSEFITSERVKVVAMLALALALCNADRVVMSVAIVPLSLSRGWSKSFSGIVQSSFLWGYLISPIAGGTLVDRYGGKVVMAWGVALWSLATFLTPWAADSSLWALLAARAMVGVAEGVALPCMNNMVARWFPPTERSRAVGIAMAGFQLGNVVGLMLSPILMSQGGIYGPFVIFGLSGFLWLLVWLSATSSAPDRHPQITKSELEYIKQKKQISTMENKRISTSGIPPFGRLLSKMPTWAVIVANSMHSWGFFVILSWMPIYFNSVYHVNLKQAAWFSAVPWSMMAFTGYIAGFWSDLLIRRGTSITLTRKIMQSIGFIGPGIALIGLTTAKQPLVASAWLSLAVGLKSFSHLGFLINLQEIAPEYSGVLHGMCLTAGTLAAIVGTVGAGFFVELLGSFQGFILLTAILYLLSALFYNIYATGERVDFDTTA
Protein: Interleukin-1 receptor-associated kinase 1 (A0A0G2JYX9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGGPGPGEPVVPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPASVLPPSTGAPRPSSISAGSETEDWSPRKLQSSASTFLSPAFPGSQTHSESELLQVPLSDSLGPPLQSSAPSSIKQPSPESPVSGLQRARPSPFCWPFCEISQGTCNFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAEEVGVTLKSTQPTLWMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGLQAVPPWKLEVAGHGSPSPQENSYMSTTGSAQSGDEPWQPLVVTTRAPAQAAQQLQRSPNQPVESDESVPGLSATLHSWHLTPDSHPSPVSFREASCTQGGTTRESSLRSGPGFQPTTMEGSSMGSSSLLSSEPPQIIINPARQKMVQKLALYEEGVLDSLQLLSSGFFPGLDLEPEKRKRPEESDEFQS
Protein: Thioredoxin domain-containing protein (Q57VQ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSAPRRRHLVAGFRLSALGGACGSHCSGTYSYRFIRCSISGSRCAQIMGRNPICVSSRSIAYKTDASSFEREVIQSQQAICLVYYRPDSSGCNAYLAHTERLVDRLNEQACGGKNGEGTEASMQRAWLKLCTINADENRNLASAFSVERAKLPITYFIMQGTIIDKVTGQVTETRLEGILRKFLDHYQQQLNVDLMGGSPNKQNPLPAAAGADLLHGASTQYLQNQIMAALLGTECIRLPEESEKLDGLRKTIQQAKKKAFDELQELRRELGVDVRRLGEAEMMERYYKSSQYSATAVLSGLEALFLARVHATIGNISAENVLFAVKAIQRDFEPALGDNTVKRLISLCEALVLRAELHLERKLESESGGEAHVAKLLRWIDELVDARLVPERYPSSEVEEMFNLLKLYIPQARRAQGSNKEECLSAKRVRQVKTCLLGVLQLFHDDPKSQEARLRLSSLLY
Protein: C3H1-type domain-containing protein (Q386W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RRM domain-containing protein
- Mago nashi-like protein,putative
- MI domain-containing protein
- RNA-binding protein, putative
- RNA helicase
- MI domain-containing protein
- PRP8 protein homologue
- RNA-binding protein, putative
- PinX1-related protein 1
- U5 small nuclear ribonucleoprotein component, putative
Sequence:
MSSAVDSLLVRLKIPDLIPKFREMNVDRIISLRKLSEEELRTAVPDDDQRNRIIEAIKNRGSSEKRTQAPAASINPPRSTDDGGRGGMSYPRGAPRGGGPVRGRGRGGTGSAGEGGFHGSGSNNANMFPSRQRVCNHFLNGDCRYGDSCRYSHNKALCQEAAESVPRRNHDATSLSEDFSETCIIPTHRIKYLLANRADRLRSIHSKNRTHNKSFQHIDPTIEKFELVIYGADQQSVQESKKMILACIGVTREEEQKNRVQYTMNELSSNQRAAKFLAACNMKNEGTVRELSEASLRNIISFFRFEKQQDIRHFWVNTNSEHSKLDIIANIVAQLQGVQAIMFCDQKRVVDMSKVASKITRYFNGVSPLFLHRAIPKEERMKMLQTFKDGKPNENGIRERLLVTNEDYAKLARKTIVPYVNLVINYSVPRSEEYYLLQSLVAGRSDTVGVSIVCVFPHEQSLFQELQRNIPFEELEEEGNFKDAAVKLVYDTVDEPLTGEDADPPSNWHEQLKPKTL
Protein: Small ribosomal subunit protein eS26A (40S ribosomal protein S26-A) (Q9UT56)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS27
- Elongation factor 3
- Small ribosomal subunit protein uS15
- mRNA export factor elf1
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS21
Sequence:
MTQKRRNCGRNKHGRGHTKFVRCINCSRAVPKDKAIKRWNIRNMVETAAIRDLSEASVYSEYAIPKIYVKLQYCVSCAIHARVVRVRSREGRRIRTPPPRVRYNRDGKRVNPAAIAKTAL
Protein: Large ribosomal subunit protein eL14 (60S ribosomal protein L14) (A0A1D8PFL9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL37
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL18
Sequence:
MSSTVKAANWRFVEVGRVVLVDNKELATIVEIIDQKRVLIDGPKIQRQAIALAKIVLTPIVLPNLPRGSRTATVTKKWAAADIDAKWAASGWAKKLANKERRSQLSDFERFQVMVLKKQRRFATKKALVKA
Protein: Kinesin-like protein KIF15 (Kinesin-like protein 2) (hKLP2) (Kinesin-like protein 7) (Serologically defined breast cancer antigen NY-BR-62) (Q9NS87)
Organism: Homo sapiens (Human)
Function: Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Detected during the interphase in the cytoplasm as finely punctuate pattern and irregularly shaped dots. Detected during mitosis on the mitotic spindle. Colocalizes with TPX2 in mitosis. Localizes at the central spindle at anaphase (By similarity). Localizes at the sites of invaginating cell membranes, a position that corresponds to the location of the contractile actomyosin ring of dividing cells (By similarity). Colocalizes with actin in interphase (By similarity). Colocalizes in dendrites and in growth cone of axons with microtubules (By similarity). {ECO:0000250}.
Interaction partners:
- Kinesin-like protein KIF11
- KIF-binding protein
- Abnormal spindle-like microcephaly-associated protein
- Dual specificity protein kinase TTK
- Centromere protein F
- DNA topoisomerase 2-alpha
- Targeting protein for Xklp2
- Kinesin-like protein KIF2C
- Kinesin-like protein KIF18A
- Kinesin-like protein KIF20A
Sequence:
MAPGCKTELRSVTNGQSNQPSNEGDAIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSES
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FTS5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MAPPLAKKAKLAGKDRVIRACDVCRKRKVKCDGDQPCSSCMTASTVCIYNGVAFPHVKSFYHRDNDLYRELRLLYKSAKALSRNEKIKASGQLCKTLTEIENSISNLQSQVDLDINDETIADYDGEGSLERQFIETSTVRLNRFSNVDMTKNNVPNITPYFGIYSTLAIFSKYGFSWMFKKLMSYSNNTSTRETMYIYMKFLDMAQLHYEEDINQKTTPIEWCFDKYAVNCDCKTLDGLFAILNIQVNPTKNDDILTKDVYEELARRPIEFFSKLIEYAWETCYLYYTGVGQSFQMSSKIFELEDIMTCLALEFSSKILYADMHHEIIIPATLRWVRICHWHEELYTVGKFLACAIRRALDLGLNSWEYYISLPEVAAEKNRLIWWECYWWDKWFSLSAGKSPLIDDAKITCLLPRRLMESGLDESMTCLEMMERCNFRHMSESEIRIFGYIMLGKYIEYINSEILFKKEYTDYRLFASVKKPIDVTINKFYDEYRSAIDLLNKMENFFVSLTGVDVDTDELTEFMTYFIETKMKCLIAMGSLIYRLKGVEVSGSELLDKCLKISLTNIYQCSLTGLRRVSNFNSFLIERYLLHINLMILNLMLSIIESPENEPVENILLMCNVVHLLGNANALKNCSNSKNMPLSELICRQSLSLSYICCRVYVQLAVKRNSSISEEEILRVLQRSNPHFATIYNQLNDISSDIFKSLLELNVAGSYQAHLIDHFREMMGDKILQKMKQLESEVQSSATPSSIEATSTVSSTVHQDHIDTNYKMNGGPAQELQDVTFEALLNSDSFASVYTDFLESLDLRKPSGNDTMPSLSLDHHADMNNPSL
Protein: Protein disulfide-isomerase SCO2 (EC 5.3.4.1) (Protein SNOWY COTYLEDON 2) (Q93YN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein disulfide-isomerase involved in chloroplast development in cotyledons. Involved in the process of vesicle-derived thylakoid formation, probably at the level of the integration and folding of LHCB proteins at the initial location of integration. Acts only in germinating seeds after dormancy, during the transition from heterotrophic to autotrophic growth.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:17921316, ECO:0000269|PubMed:18209955}; Peripheral membrane protein {ECO:0000269|PubMed:17921316, ECO:0000269|PubMed:18209955}. Note=Associates with multiple thylakoid complexes.
Interaction partners:
- Protein disulfide-isomerase LQY1, chloroplastic
- Elongation factor G, chloroplastic
- GTP-binding protein OBGC, chloroplastic
- Probable transmembrane GTPase FZO-like, chloroplastic
- Protein THYLAKOID FORMATION 1
- Protein SNOWY COTYLEDON 3
- Membrane-associated protein VIPP1, chloroplastic
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- CAAX amino terminal protease family protein
- Thiol-disulfide oxidoreductase LTO1
Sequence:
MFRLYPNCSLPSHRPLVFLPRLPSRSLRCRAAADIPLGDGIRLPREADSTSDTARSRDVSVAAGGNGEGAKWRKRRLLWSKSGESYLVDDGDALPLPMTYPDTSPVSPDVIDRRLQCDPVVEDCREVVYEWTGKCRSCQGSGTVSYYKKRGKEVICKCIPCQGIGYVQKITSRTDIEVMEDLDNEPS
Protein: FATH protein (Q6X4A1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KMISRKKKRQAEPEDKRLGPTTAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESMHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEAIDEHTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAPDELPPLPPEFSDQFESIHPPRDMPAAGSLGSSSRSRQRFNLNQYLPNFYPADMSEPQKQGAGENSPCREPYTPYPPGYQRNFEAPTIENMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV