wanglab/gogpt-training-data huggingface dataset:
Protein: Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase) (P46844)
Organism: Rattus norvegicus (Rat)
Function: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53004}.
Interaction partners:
- Heme oxygenase 2
- Heme oxygenase 1
- Biliverdin reductase B
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B1
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 2B37
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MDAEPKRKFGVVVVGVGRAGSVRLRDLKDPRSAAFLNLIGFVSRRELGSLDEVRQISLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTLSFAAAQELWELAAQKGRVLHEEHVELLMEEFEFLRREVLGKELLKGSLRFTASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMTVQLETQNKGLLSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVGVNKNIFLKDQDIFVQKLLDQVSAEDLAAEKKRIMHCLGLASDIQKLCHQKK
Protein: D-serine dehydratase (EC 4.3.1.18) (D-serine deaminase) (Q54XE5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNENNDDINNLNTPCVLVLDSVVRNNCIKMNERAASLGVNVRPHMKTHKTIEIGKYQFEENKNLNKSRGIIVSTLSEGKFFSKEFKDILYATPIAPNKVKDAYQLHLSIDRLNVMFDNIEHLKSMVDYAIKNPNEFQKKWSVFLKIDCGYHRAGADPKLQSTTDLVELIVNGEYNQYFQFQGIYSHSGHSYKCQTPTDIKNLAIEEARVTGDYGKKLKSLGYKVDTVSIGSTPVCSHLPHNLLSEYGVNEIHPGNYTFYDQMQYELGNCKLEDIGVHVLATIVSIYPERNELLVDAGSLALSSDPGCTHLRDLKVINNFGIVYNDTNLRIVAPSQEVSKIQSTNQSPIDFSKYKIGSKIRIIPNHSCLTAAMFSDYHVINNDNQIINSFKPNKHW
Protein: Cancer-associated gene 1 protein (CAGE-1) (Cancer/testis antigen 3) (CT3) (Q8TC20)
Organism: Homo sapiens (Human)
Interaction partners:
- Cancer/testis antigen 1
- Ras-related protein Rab-11B
- Cytosolic non-specific dipeptidase
- Dickkopf-like protein 1
Sequence:
MNKDYQKFWSSPSDPVHFEVDTSHEKVESMSESDTMNVSNLSQGVMLSHSPICMETTGTTCDLPQNEIKNFERENEYESTLCEDAYGTLDNLLNDNNIENYSTNALIQPVDTISISSLRQFETVCKFHWVEAFDDEMTEKPEFQSQVYNYAKDNNIKQDSFKEENPMETSVSANTDQLGNEYFRQPPPRSPPLIHCSGEMLKFTEKSLAKSIAKESALNPSQPPSFLCKTAVPSKEIQNYGEIPEMSVSYEKEVTAEGVERPEIVSTWSSAGISWRSEACRENCEMPDWEQSAESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTTHSNLLPDCSPCEERLNPADIKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKESEKVSDIMLQKLKSLHLKKKTLDKEVIDCDSDEAKSIRDVPTLLGAKLDKYHSLNEELDFLVTSYEEIIECADQRLAISHSQIAHLEERNKHLEDLIRKPREKARKPRSKSLENHPKSMTMMPALFKENRNDLD
Protein: WW domain-containing oxidoreductase (EC 1.1.1.-) (Q803A8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Required for normal bone development. Inhibits Wnt signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NZC7}. Mitochondrion {ECO:0000250|UniProtKB:Q9NZC7}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NZC7}. Lysosome {ECO:0000250|UniProtKB:Q9NZC7}.
Interaction partners:
- Transcription factor AP-2 gamma
- Vesicle amine transport 1-like.
- Receptor protein-tyrosine kinase.
- C-type lectin domain family 3 member A
- Zinc finger protein 592
- Cellular tumor antigen p53
Sequence:
MAALKYAGMEDTDSEDELPPGWEERSTKDGWVYYANHEEMKTQWEHPKTGKKKRCAGALPYGWEQETDDKGQIFYVDHINKRKTYFDPRQAFTVEDMQVKPKRYDGNTGALEILHGQDLSDKVIIVTGANSGIGFETARSFALHGAHVILACRNQSRASKAASLIMGEWSKARVEVLPLDLASLRSVRQFAELFKATKLPLHVLVCNAAVCSQPWRLTEDGFESTFQICHLGHFLLVQLLQDVLRLSAPARVVVVSSESHRFTDLLDSCGNLDLDLLSPPQKNYWSLLAYNRAKLCNLLFSSELHRRMSPHGICCNALHPGSMMFTSIHRSWWLLTLLFSLARPFTKSMQQGAATTVYCAVAPELEGIGGMYFNNCFRCLPSPQAQDPAAALSLWELSERLVQERSTPPQVL
Protein: Molting defective, isoform F (A0A0B4K6J3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSANRRRRSASAASSIAAETATAATAATAEAISTAPSKEQLSPPIAGGSASADEDLLEMPRICRCCCKRDLKLLGLFEASQPTLANTTVASASAAASVASNKSSGTLAKTCATEAETETPQTLSANPVNPGTKATSSPSEAATTLSTSTRPASASFSSTSFSTSTSPMRRRTTNTTAPSASPAPRGRSSDNAVDYTLSGAHSSMDIVLEEMTIWMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQDFAQEISDRQTARQAKRQQKVQKKTHDRWLQLEPTSHEEQQPIRKRRMVSESDGDSTAAAAAAEAATATATTPAKQVRTDFESLPPPKPSPQQHRVRKYRTLSIDCEMERPAASINASSMPWKTKAARKELSENWASSCSTAVMSPNRQRSSTSSSEHMSDLSVGPCCGFESDSNPSSTSNSARRTVILVKQQSPEKTSPMYDLMPRRGRRPRKAPIYMPAKRQRRSLVRKEPLYRKAQPVNEENKKSDQKDIYPKESRMEGLAPSCDEAIDSTSDAPMEVASNVVQKKCDEICLNGLIDSRNQLGAMEMEPVNEMIASNGVDKELTLSVQNNKETTSEEQIFEATSVIKESVQPEQSAEDIQVRTEIESIANDIRAEADLVQSEELTSSTETSESQPKAVEQLESMGKQESYALPQNMEAHESVQQTQTVDESDSADQREIIVSIPLEVLDENLQRRLCVDPETEAANRQSADPKEFALRPDDVNNNENDENFCQSATADSFNSAVALRTNKIEATPPGGTDSDDTDTDEVPIVPSGPTPMDFMAEFAKHCANGIEQLKVTTPVPSPTPSDLVPLNDLEAKQKLEVEMNDVETTLNGILNEMQDQHMYTPNCAHIDEFLTPADYATLTEQESSVSSPPNPFEQSSVAEPKDEKPSATEDPFDNSNFTNELIGFQNDIPCFENIETPEEGQNLHLELTQFLRDLQPSQSDPPAGEQVEKIEMETQPSTVQMDVQSNLPVQAADTQPQNESANHSPFESPISSPQVQSQIELQMEPQIETQMQPQIETRMQHDVLSVQSPQNHQPQVQSHDQSQMQHQIPPQIEPQIEVQNQEQNTLQLVPQAQHQVVPHVQLQSQLVPHVQTQGTTTTVTYEQIYQQHIVQQTVQQSSNKMQVISLPSAGSETTRQWQTQQSQQQQQVQWSSVGGLEAIKSAPVESVAPTTTTYYISASDLYPQQTETYTMLQPASNESYVIEQVNHQQQHCQQQIQMSQQQHQRQHQQQQAQQQQQPIMILIQQPEIQQPVASASNPQQAPLHIYNAATSNDVHQMQHTQRQQIRQQYQHQQYQRLQQPQQTRVVQSHPVLGMPGATSISTKVTPIPVTAARGRPLTLKCRFCHNGPRFSSSLEYSRHIIDLHPAVAPFNCPHCPMAFAGRTKRSQHILSHHVVQQYQCGQCSHVFPAQKALDVHIQRFHMTLKTDPSGAVKVEDVQLQITSERRPRGRPYKPRLQLQQHQLQPQQKLQVQQHQQQQKALQQLPQAQHHQQQQQPQLQQEVLQQVQQLQVQVQPQQHQQHQQVLQVQQPQQQPLMQPQSPHPSSTSGHSHANEQFEELQTLQAPPTVLTPPSTIVSVPSPQPMVYSQHITMPSPEQSEPDSTTTLRQYRKRGVIVGPQGPLHLATPVASPSPSSSPSSSTVDHIPPASPATPASPAPPPSPAVASTVQVSELRTSHHCLYCEERFTNEISLKKHHQLAHGALTTMPYVCTICKRGYRMRTALHRHMESHDVEGRPYECNICRVRFPRPSQLTLHKITVHLLSKPHTCDECGKQFGTESALKTHIKFHGAHMKTHLPLGVFRNEDAASKSPSNNNSHASSDKLENPATPIEETPLTPMSSGGHLYHSPDEYPNSVESCAGNSVALESYATTP
Protein: Uncharacterized protein (Q585K5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- ATP synthase delta chain
- Uncharacterized protein
- ATP synthase subunit beta
- Uncharacterized protein
- ATPase subunit 9, putative
- ATP synthase alpha chain
- Uncharacterized protein
Sequence:
MLRRLGANVSNMARPMNKYAVTVSPRRHLEPMSTWYLASWAMVWYYAFFFWMPMVWTDIMVPSFVYNKLPVIHFLQEKRAEQKLRRVLDETYTEWTEELDQAHVTDAITRSLNI
Protein: DNA-directed RNA polymerase subunit beta' (RNAP subunit beta') (EC 2.7.7.6) (RNA polymerase subunit beta') (Transcriptase subunit beta') (Q8RQE8)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
Sequence:
MKKEVRKVRIALASPEKIRSWSYGEVEKPETINYRTLKPERDGLFDERIFGPIKDYECACGKYKRQRFEGKVCERCGVEVTKSIVRRYRMGHIELATPAAHIWFVKDVPSKIGTLLDLSATELEQVLYFSKYIVLDPKGAILNGVPVEKRQLLTDEEYRELRYGKQETYPLPPGVDALVKDGEEVVKGQELAPGVVSRLDGVALYRFPRRVRVEYVKKERAGLRLPLAAWVEKEAYKPGEILAELPEPYLFRAEEEGVVELKELEEGAFLVLRREDEPVATYFLPVGMTPLVVHGEIVEKGQPLAEAKGLLRMPRQVRAAQVEAEEEGETVYLTLFLEWTEPKDYRVQPHMNVVVPEGARVEAGDKIVAAIDPEEEVIAEAEGVVHLHEPASILVVKARVYPFEDDVEVSTGDRVAPGDVLADGGKVKSDVYGRVEVDLVRNVVRVVESYDIDARMGAEAIQQLLKELDLEALEKELLEEMKHPSRARRAKARKRLEVVRAFLDSGNRPEWMILEAVPVLPPDLRPMVQVDGGRFATSDLNDLYRRLINRNNRLKKLLAQGAPEIIIRNEKRMLQEAVDALLDNGRRGAPVTNPGSDRPLRSLTDILSGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKRMALELFKPFLLKKMEEKGIAPNVKAARRMLERQRDIKDEVWDALEEVIHGKVVLLNRAPTLHRLGIQAFQPVLVEGQSIQLHPLVCEAFNADFDGDQMAVHVPLSSFAQAEARIQMLSAHNLLSPASGEPLAKPSRDIILGLYYITQVRKEKKGAGLEFATPEEALAAHERGEVALNAPIKVAGRETSVGRLKYVFANPDEALLAVAHGIVDLQDVVTVRYMGKRLETSPGRILFARIVAEAVEDEKVAWELIQLDVPQEKNSLKDLVYQAFLRLGMEKTARLLDALKYYGFTFSTTSGITIGIDDAVIPEEKKQYLEEADRKLLQIEQAYEMGFLTDRERYDQILQLWTETTEKVTQAVFKNFEENYPFNPLYVMAQSGARGNPQQIRQLCGLRGLMQKPSGETFEVPVRSSFREGLTVLEYFISSHGARKGGADTALRTADSGYLTRKLVDVTHEIVVREADCGTTNYISVPLFQPDEVTRSLRLRKRADIEAGLYGRVLAREVEVLGVRLEEGRYLSMDDVHLLIKAAEAGEIQEVPVRSPLTCQTRYGVCQKCYGYDLSMARPVSIGEAVGIVAAQSIGEPGTQLTMRTFHTGGVAGAADITQGLPRVIELFEARRPKAKAVISEIDGVVRIEETEEKLSVFVESEGFSKEYKLPKEARLLVKDGDYVEAGQPLTRGAIDPHQLLEAKGPEAVERYLVEEIQKVYRAQGVKLHDKHIEIVVRQMMKYVEVTDPGDSRLLEGQVLEKWDVEALNERLIAEGKTPVAWKPLLMGVTKSALSTKSWLSAASFQNTTHVLTEAAIAGKKDELIGLKENVILGRLIPAGTGSDFVRFTQVVDQKTLKAIEEARKEAVEAKERPAARRGVKREQPGKQA
Protein: Enoyl-CoA delta isomerase 2 (Testicular secretory protein Li 33) (A0A0C4DGA2)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
Protein: Protein shortage in chiasmata 1 ortholog (EC 3.6.-.-) (Protein ZIP2 homolog) (MZip2) (A2ALV5)
Organism: Mus musculus (Mouse)
Function: ATPase required during meiosis for the formation of crossover recombination intermediates. Binds DNA: preferentially binds to single-stranded DNA and DNA branched structures (By similarity). Does not show nuclease activity in vitro, but shows ATPase activity, which is stimulated by the presence of single-stranded DNA (By similarity). Plays a key role in homologous recombination and crossing-over in meiotic prophase I in male and female germ cells. Required for proper synaptonemal complex assembly and homologous chromosome pairing. Required for recruitment of TEX11 and MSH4 to recombination intermediates.
Subcellular location: Chromosome {ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. Note=Localizes to meiotic chromosomes; associates with mid-stage meiotic recombination intermediates (PubMed:29742103). Localization requires meiotic double-strand breaks (DSBs) recombination intermediates catalyzed by DMC1 (PubMed:29742103). {ECO:0000269|PubMed:29742103}.
Interaction partners:
- Testis-expressed protein 11
- MutS protein homolog 4
Sequence:
MALNGRTMFPAFKYYAIDYLQEDIIKERLYRDALLLQIPSCLNQDKNIIDDKYRTPWTRAIPVQEMEDNSVLEQWRTRFCVEGVPEKKTVTGVMINGTFEEIVPSSNPNSPPGIENDKLFPSKDYVDDFIPVKCSLYYPGVKAEHQGLLIDEEMIFMNKAMDNHLPTVNGLLSRLKLYLVKDPFLDFKEELSGKDNFTEYFSVQECSEPFVRDFHMAEETFCKKKLPSVFPSGFKSLISTNPKQEILILPPSKLKKPLNSIPKIMDSVDESECFKGDITSKHEFDTEDIKCNSTENLTFASLCEPECSEPGDLEMPPTHLILPRQHSAVSSLHMGFQTFPFSATCKINLLSAGESANKYCMLWQLGGCRNSWVSFLLTVPRFQEPSSQYSLADMRNIFSVKGDSLVINPAKAKGWRQARLHPIMAETLAHLKAYLCHNGLSSQETKLEIFLPTKVFQLESWLELKSRPLPIVPISEKSTDVHQLHPQKRPIPSSEKEVPHLCLSGESISVKKSKVEANPKNDQEPEARIMQKPENSCVGLGCSSQVPSAESASSSQIQASYDKKQDDLDLLSEFIILRSKHQTFPSEADVDVKSHDHDQNNEFQDKEKYSLTLQEESLVASNSKAPEERCEERTDGVIEIPASDTQCQAYCLLEATANPILKELVCLCTYPAANWKFATVNFDQTRFFLKEQEKKINDATHPDKNDDRKMTFRHAALLHLLITIRDVLLTCNLDTALGYLSNAKDIYKSVLDSRLDNIWRQLKILQFIKEKRPKSNYKIQELQCQILSRLQNQQQMKVLIIIRMDSDGEKHLLIKTLKKIEGLTMTVLRSNDRKKILETTSILKGTNACVVVHNHSIGADFPWSSFSLVVEYNHVGHSCWAEHCQLLDIPFLAFKVAVPDTALQRDALLDGFGGFLLKIPIPYVFFASEGLLNTPEILRLLESNYNITLVERCCCGSLKLFGSTECYVVVTVDEHTAIVVQDLEELHHEKASDNIIMRLMALSFQYSCCWIILYSKETLNSQYHLTEETLRHLAQVYAALVSSGLKSEELDVKLIIAPGVEETALIIRQIADHNLMTSTRDPHEWLDKSWVEVSPSKEEMSLLDFPCINPLVAQLMLHRAPSLHWLLIATPAELQELLPQVPGKVLKHFCSITSLFKISSPSMTKSSQISSLQEDMNQTDLFISQSSAPIIQEQEEYYPYEDSEGTSSSPVELRATPCMLPSAAPHSQRGCWEDPSCGPDPVQNNPSLMNAESKKVTWPSVPSWSDSESDVFSLARTQVSCEPIMTLTDSQRRGTNGFVNCPEAKGPRNMQVSTPVFLPENSQSHLHWDFKKNSCRKQIYSFNPSCGTEQTTYNKWYSWKDDFSSNQPECLWDEMEDVTYRNANAGTRETFWRELPAVPSWDSPCASDSNANQRGFKGLDFCQRAGNYLGQRSLPVSSSNWGDYKTPTDLMYSQVPQPKKRRLMYEKVPGRVDGQTRLKFL
Protein: Eukaryotic translation initiation factor 4E-1 (ZmeIF4E) (eIF-4E-1) (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (O81481)
Organism: Zea mays (Maize)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-2
- Eukaryotic translation initiation factor isoform 4G-2
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 5
- Polyadenylate-binding protein
- RNA helicase
Sequence:
MAEETDTRPASAGSRGRPAPEDDDREEGEITDLACAPSPPATHPLEHSWTFWFDNPQSKSKQAAWGSSIRPIHTFSTVEEFWGLYNNINHPSKLIVGADFHCFKNKIEPKWEDPICANGGKWTISCGRGKSDTFWLHTLLAMIGEQFDYGDEICGAVVSVRGKQERIAIWTKNAANEAAQVSIGKQWKELLDYKDSIGFIVHDDAKKMDKGLKNRYTV
Protein: M protein (Q6V4L5)
Organism: Streptococcus pyogenes
Subcellular location: Secreted, cell wall {ECO:0000256|PROSITE-ProRule:PRU01372}; Peptidoglycan-anchor {ECO:0000256|PROSITE-ProRule:PRU01372}.
Interaction partners:
Sequence:
RKLKTGTASVAVALTVVGAGLASQTEVKANRADDARNEVLRGNLVRAELWYRQIQENDQLKLENKGLKTDLREKEEELQGLKDDVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAERKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKGLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTSETT
Protein: ATP-dependent Clp protease subunit, heat shock protein 100 (HSP100), putative (Q586B8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Chaperone protein DNAJ, putative
- Chaperone protein DnaJ, putative
- Stress-induced protein sti1, putative
- Heat shock protein 20, putative
- GrpE protein homolog
- Uncharacterized protein
- AAA+ ATPase domain-containing protein
Sequence:
MAHSDRQCTNAAQTALSDAVESARKHNNGFVDPAHLALVLFKNEDGLASRVLRKLNAGTVLEPLAARVGALPEQRPAPAVPSPSPAMVVVLNTAEQKRIEWGDSLIAVDHLLIGLFECKEVEAIMKAAHASKKAVEGALLELRKGKKVTSEFQEENYQALEKYATDLCKLAEEGKLDPVIGRTDEVLRTIRVLSRRTKNNPILIGEPGVGKTAIAEGIAQRIVRGDVPDTLLNTRLFSLDLGALIAGSSLRGEFEERLKSVLNEVKESSNGVILFIDEIHLVLGAGKSGGSMDAANLLKPMLARGELRTIGATTLEEYRTYVEKDAAFERRFMPVYVTEPSVEECISILRGLKDRYEAHHGVQITDNAVVVAAQLANRYITNRFMPDKAIDLIDEACANVRVQLSSRPEAIDILERKKRQLEIEAKALERDKEAASRERLKLVKADIQRVEEELQPLVSKYNDERQRIDELQEMQSRLDEKKNKLERAVRDGKMDLAADLQYNVIPLIQDRIRSLKEDIERQKATLVQEKVTEGDVAAVVARWTGIPVVKLSQTDRERLLNLSMHLHRRVKGQDEAVERVADAIIRARAGLSRPNSPTASFLFLGPTGVGKTELVKAVAAELFDDEKHMVRIDMSEYMEQHSVSRLIGAPPGYIGHDEGGQLTEPVRRRPHAVVLFDEVEKAHPNVYNVLLQVLDDGRLTDSRGRTVDFSNTIIVMTSNLGSEHLLNPEETNESYEVLRENVLAAVRSYFRPELINRLDDIVVFRRLRTEDLRGVVDNLIAGVNERLKSSGFSVLLDDGVKDFILEHGHDANMGARPLRRWIEKNIVTEIGRMLIAKELPPNSTLRVSLPEGGNKLTFGVKRGLTSDEWE
Protein: Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (A0A1D8PND1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
Sequence:
MITKCYVQVFRYRRVCHNTKYSFNSVVSIKWLHSAGSSLSQANSSKTSQSSLTSSGFLYYEDPHRYNGSDVSANASETTSTSTAKPVIHSATPYSDKYYQPIISQGAKGFDKLIIPVGFHADNQTVSLEEDKESPIQQDQLQEIVNSFDAPIDVSIGYGSGILPQDGYDKDKSTPNNTANDSKQLDFMFLVKDCGKFHQENLKQNRDHYSIKSLRLIKKVQGTNGMYFNPFIKINEKLVKYGVISSKSALMDLSEWHSLYFAGRLQKPVNFITTNDPRVKFLNQYNLKNAMTIAIFLIDGEGNSRQATFNERQLYEQITKLSYLGDFRMYIGGENPNKSKNIVAKQFHHFKKLYEPILQYFIHKNFLIIVNNDPVNRTFKPNLNVNNRIKLITGLPLKFRQQLYGRYYEKSIKEIVIDDHLSQNLTKIISRTIIISSITQAIRGLLSAGLFNSIKYAVAKQIKFWTSKK
Protein: Probable GDP-mannose transporter 2 (GMT 2) (P0CE11)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Recycles between the Golgi apparatus and the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- Uncharacterized protein YER039C-A
Sequence:
MIYTSSKSLQYLAVPIYTIFKNLTIILIAYGEVLFFGGKVTSMELTSFIMMVLSSVVATWGDQQAIAIKASSLEDLDQELVESTIFVLNPGYLWMFTNCISSALFVLIMRKRIRLTNFKDYDTMFYNNVLALPLLLVFSFIMEDWSTKNLSVNLSADSLAAMVISGLMSVGISYCSGWCVRVTSSTTYSMVGALNKLPIALAGLVFFDAPKNFLSFFSIFLGFLSGLLYAVAKQKKIQQQKVLAATLEK
Protein: DNA-binding protein (A0A087I6S4)
Organism: Vibrio vulnificus
Subcellular location: Cytoplasm, nucleoid {ECO:0000256|ARBA:ARBA00004453}.
Interaction partners:
Sequence:
MSELTKTLLNIRSLRAFSRELTLEQLEEALDKLTTVVAERQEAEAEERAAKAEQEAKLAAIAEQIAKDGIDVEALISALAGETKVKSKGKRAPRPAKYKYVDTNGEEKTWTGQGRTPSAIQAQLDAGKSLEDFEI
Protein: Protein SUGARY ENHANCER 1 (A0A1D6F7U7)
Organism: Zea mays (Maize)
Function: Involved in starch metabolism in endosperm. Acts as a modifier of SUGARY1 (SU1), an isoamylase starch-debranching enzyme involved in amylopectin biosynthesis in endosperm.
Interaction partners:
- Sugary1.
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic
Sequence:
MIRPAPWVGAGHRGRGGEAGACTESLGSESGDVGCDAAEIDQFFPPAPAAGGPDDAGAEPCIPDLAAAAAAGKRRRGGFPPPMPRASGPLFLRAERRGGRLILTEVRADERERRVVFRAERDGGRLRLRFANDGDGPEAAGGGGGAGGGGGELCQVAAGRRGVQVGAVMMGAI
Protein: CRISPR-associated endoribonuclease Cas2 (EC 3.1.-.-) (P45956)
Organism: Escherichia coli (strain K12)
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The Cas1-Cas2 complex is involved in CRISPR adaptation, the first stage of CRISPR immunity, being required for the addition/removal of CRISPR spacers at the leader end of the CRISPR locus. The Cas1-Cas2 complex introduces staggered nicks into both strands of the CRISPR array near the leader repeat and joins the 5'-ends of the repeat strands with the 3'-ends of the new spacer sequence. Spacer DNA integration requires supercoiled target DNA and 3'-OH ends on the inserted (spacer) DNA and probably initiates with a nucleophilic attack of the C 3'-OH end of the protospacer on the minus strand of the first repeat sequence. Expression of Cas1-Cas2 in a strain lacking both genes permits spacer acquisition. Cas2 not seen to bind DNA alone; the Cas1-Cas2 complex preferentially binds CRISPR-locus DNA. Highest binding is seen to a dual forked DNA complex with 3'-overhangs and a protospacer-adjacent motif-complement specifically positioned. The protospacer DNA lies across a flat surface extending from 1 Cas1 dimer, across the Cas2 dimer and contacting the other Cas1 dimer; the 23 bp-long ds section of the DNA is bracketed by 1 Tyr-22 from each of the Cas1 dimers. Cas1 cuts within the 3'-overhang, to generate a 33-nucleotide DNA that is probably incorporated into the CRISPR leader by a cut-and-paste mechanism. This subunit's probable nuclease activity is not required for spacer acquisition.
Interaction partners:
- CRISPR-associated endonuclease Cas1
- CRISPR system Cascade subunit CasC
- CRISPR system Cascade subunit CasD
- CRISPR system Cascade subunit CasE
- CRISPR system Cascade subunit CasA
- CRISPR-associated endonuclease/helicase Cas3
- CRISPR system Cascade subunit CasB
- Crossover junction endodeoxyribonuclease RuvC
- Integration host factor subunit alpha
- Integration host factor subunit beta
Sequence:
MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIREMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTPVDLDGLRLVSFLPV
Protein: Transcription initiation factor TFIID subunit 1-like (TAF(II)210) (TBP-associated factor 1-like) (TBP-associated factor 210 kDa) (Transcription initiation factor TFIID 210 kDa subunit) (Q8IZX4)
Organism: Homo sapiens (Human)
Function: May act as a functional substitute for TAF1/TAFII250 during male meiosis, when sex chromosomes are transcriptionally silenced.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 13
Sequence:
MRPGCDLLLRAAATVTAAIMSDSDSEEDSSGGGPFTLAGILFGNISGAGQLEGESVLDDECKKHLAGLGALGLGSLITELTANEELTGTGGALVNDEGWIRSTEDAVDYSDINEVAEDESQRHQQTMGSLQPLYHSDYDEDDYDADCEDIDCKLMPPPPPPPGPMKKDKDQDAITCVSESGEDIILPSIIAPSFLASEKVDFSSYSDSESEMGPQEATQAESEDGKLTLPLAGIMQHDATKLLPSVTELFPEFRPGKVLRFLHLFGPGKNVPSVWRSARRKRKKHRELIQEEQIQEVECSVESEVSQKSLWNYDYAPPPPPEQCLADDEITMMVPVESKFSQSTGDVDKVTDTKPRVAEWRYGPARLWYDMLGVSEDGSGFDYGFKLRKTQHEPVIKSRMMEEFRKLEESNGTDLLADENFLMVTQLHWEDSIIWDGEDIKHKGTKPQGASLAGWLPSIKTRNVMAYNVQQGFAPTLDDDKPWYSIFPIDNEDLVYGRWEDNIIWDAQAMPRLLEPPVLALDPNDENLILEIPDEKEEATSNSPSKESKKESSLKKSRILLGKTGVIREEPQQNMSQPEVKDPWNLSNDEYYFPKQQGLRGTFGGNIIQHSIPAMELWQPFFPTHMGPIKIRQFHRPPLKKYSFGALSQPGPHSVQPLLKHIKKKAKMREQERQASGGGELFFMRTPQDLTGKDGDLILAEYSEENGPLMMQVGMATKIKNYYKRKPGKDPGAPDCKYGETVYCHTSPFLGSLHPGQLLQALENNLFRAPVYLHKMPETDFLIIRTRQGYYIRELVDIFVVGQQCPLFEVPGPNSRRANMHIRDFLQVFIYRLFWKSKDRPRRIRMEDIKKAFPSHSESSIRKRLKLCADFKRTGMDSNWWVLKSDFRLPTEEEIRAKVSPEQCCAYYSMIAAKQRLKDAGYGEKSFFAPEEENEEDFQMKIDDEVHAAPWNTTRAFIAAMKGKCLLEVTGVADPTGCGEGFSYVKIPNKPTQQKDDKEPQAVKKTVTGTDADLRRLSLKNAKQLLRKFGVPEEEIKKLSRWEVIDVVRTMSTEQAHSGEGPMSKFARGSRFSVAEHQERYKEECQRIFDLQNKVLSSTEVLSTDTDSISAEDSDFEEMGKNIENMLQNKKTSSQLSREWEEQERKELRRMLLVAGSAASGNNHRDDVTASMTSLKSSATGHCLKIYRTFRDEEGKEYVRCETVRKPAVIDAYVRIRTTKDEKFIQKFALFDEKHREEMRKERRRIQEQLRRLKRNQEKEKLKGPPEKKPKKMKERPDLKLKCGACGAIGHMRTNKFCPLYYQTNVPPSKPVAMTEEQEEELEKTVIHNDNEELIKVEGTKIVFGKQLIENVHEVRRKSLVLKFPKQQLPPKKKRRVGTTVHCDYLNIPHKSIHRRRTDPMVTLSSILESIINDMRDLPNTHPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKCLYPSREEFREHLELIVKNSATYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQKMMAVPDSWPFHHPVNKKFVPDYYKMIVNPVDLETIRKNISKHKYQSRESFLDDVNLILANSVKYNGPESQYTKTAQEIVNICYQTITEYDEHLTQLEKDICTAKEAALEEAELESLDPMTPGPYTSQPPDMYDTNTSLSTSRDASVFQDESNLSVLDISTATPEKQMCQGQGRLGEEDSDVDVEGYDDEEEDGKPKPPAPEGGDGDLADEEEGTVQQPEASVLYEDLLISEGEDDEEDAGSDEEGDNPFSAIQLSESGSDSDVGYGGIRPKQPFMLQHASGEHKDGHGK
Protein: UDP-glucuronosyltransferase (EC 2.4.1.17) (Q9V9X9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein {ECO:0000256|RuleBase:RU362059}.
Interaction partners:
Sequence:
MPPIFLLVCLLPGYSEGARILAVFPLPSSSHYFFALPYLKSLASLGHEITSVSPYPQREPFRNIHDIPVPEVFENFNEVLRIASTPRSTWQSSDFINEYVLNLTKTVLNNEGVRRDILGPQKPHFDLVIMDLWRMDVLSGLAAYFDAPIIGMASYGTDWKIDELMGNVSPISYLQSPSSRFYDLEAYGERLLHLMERTFSYMNYKWRHVRKQETLYSQFFPSVAERKPLSEISRNFDLVLVNQHFTLGPPRPYVPNMIQVGGLHVDHSTEALSAELDHFIQGAGESGVIYFSLGTNVKSKSLSEDRRKVLLETFASLPQRIVWKFEDELLPGKPPNVFISKWFPQQAILAHPNVKLFITHGGLLSTIESIHHGKPMLGLPCLFDQFRNMDHVRQVGLGLVLNIKQMTSEEFRSTIIRLLTNKSFEETARITAARYRDQPMKPMETAIWWTEYVLSHKGAAHMQVAGKDLGFVRYHSLDVFGTFLVGALVILGIVTYLLVMTLRKCLFLIKRGKCEAIKKIQ