wanglab/gogpt-training-data huggingface dataset:
Protein: Cold shock-induced protein TIR1 (Serine-rich protein 1) (TIP1-related protein 1) (P10863)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cell wall. Required for anaerobic growth.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Cell wall protein DAN1
- Eukaryotic translation initiation factor 5A-2
Sequence:
MAYTKIALFAAIAALASAQTQDQINELNVILNDVKSHLQEYISLASDSSSGFSLSSMPAGVLDIGMALASATDDSYTTLYSEVDFAGVSKMLTMVPWYSSRLEPALKSLNGDASSSAAPSSSAAPTSSAAPSSSAAPTSSAASSSSEAKSSSAAPSSSEAKSSSAAPSSSEAKSSSAAPSSSEAKSSSAAPSSTEAKITSAAPSSTGAKTSAISQITDGQIQATKAVSEQTENGAAKAFVGMGAGVVAAAAMLL
Protein: Zinc finger protein 7 (Q39266)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q39261}.
Interaction partners:
- Protein trichome birefringence-like 41
- Zinc-finger homeodomain protein 8
- At3g49930
- Basic leucine-zipper 70
Sequence:
MTESDDASRETPASRGGEASSNQDLSKPESNHVSLDLKLNDTFNDDTKSTKCEANPRVFSCNYCRRKFYSSQALGGHQNAHKRERTMAKRAMHMGRMFGHHHRPYTYTSSSLGMQAHSGLLHHTLSQPQPLVSRFHHQGYFGNTVPLFFDYDDGGSDFFWPGSFRQVVEEAEAPVVVVASTESGLDLNSVAANGGVDNNSSKPDLTLRL
Protein: UDP-glycosyltransferase 85C2 (EC 2.4.1.-) (Q6VAB0)
Organism: Stevia rebaudiana (Stevia) (Eupatorium rebaudianum)
Function: Involved in the biosynthesis of steviol glycosides in leaves. Converts steviol to the mono-glycoside steviolmonoside. Converts the mono-glycoside steviolmonoside to the bi-glycoside rubusoside.
Interaction partners:
Sequence:
MDAMATTEKKPHVIFIPFPAQSHIKAMLKLAQLLHHKGLQITFVNTDFIHNQFLESSGPHCLDGAPGFRFETIPDGVSHSPEASIPIRESLLRSIETNFLDRFIDLVTKLPDPPTCIISDGFLSVFTIDAAKKLGIPVMMYWTLAACGFMGFYHIHSLIEKGFAPLKDASYLTNGYLDTVIDWVPGMEGIRLKDFPLDWSTDLNDKVLMFTTEAPQRSHKVSHHIFHTFDELEPSIIKTLSLRYNHIYTIGPLQLLLDQIPEEKKQTGITSLHGYSLVKEEPECFQWLQSKEPNSVVYVNFGSTTVMSLEDMTEFGWGLANSNHYFLWIIRSNLVIGENAVLPPELEEHIKKRGFIASWCSQEKVLKHPSVGGFLTHCGWGSTIESLSAGVPMICWPYSWDQLTNCRYICKEWEVGLEMGTKVKRDEVKRLVQELMGEGGHKMRNKAKDWKEKARIAIAPNGSSSLNIDKMVKEITVLARN
Protein: Beta lactamase like protein (O86336)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible hydrolase
- Possible penicillin-binding lipoprotein
- Probable conserved lipoprotein
- Conserved protein
- Phosphate acetyltransferase
- F420-dependent glucose-6-phosphate dehydrogenase
- Acetate kinase
Sequence:
MVATRGTRLAALALAPRLAGMAELVQITDKVHLARGHAVNWVLVTDDTGVLLIDAGYPGDRAEVLASLNKLGYTPGDVRAIVLTHAHIDHLGSAIWFAREHSTPVYCHAEEVGHAKREYRENASVFDVALRSWRPRVAVWGIHLLRRGGLTGDGIPTAQPLTAEAAAGLPGQPMAIFTPGHTSGHCSYVVDGVLASGDALITGHPMLRHRGPQLLPAVFSHSQQNSIRSLAALALLETNILAPGHGELWHGPIRKATDEALERAQKSNHVFR
Protein: Ubiquitin carboxyl-terminal hydrolase 30 (EC 3.4.19.12) (Deubiquitinating enzyme 30) (Ubiquitin thioesterase 30) (Ubiquitin-specific-processing protease 30) (Ub-specific protease 30) (D3ZPG5)
Organism: Rattus norvegicus (Rat)
Function: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (By similarity). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q70CQ3}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Mitochondrial ubiquitin ligase activator of NFKB 1
- Mitochondrial import receptor subunit TOM20 homolog
- ubiquitinyl hydrolase 1
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Peptidyl-prolyl cis-trans isomerase FKBP8
Sequence:
MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLSLLKALSCQEVTEEEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNPWKSQHPFHGRLSSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTQNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSQGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPKATESPGSALGVQDTQAAPKPGLSQPAAPKTQFFMNGACSPSLLPALPSPMAFPLPVAPDYSSSMYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYERVLSRVQQQGREYRSEE
Protein: Transcription factor E2F7 (E2F-7) (Q5RIX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as e2f1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes (By similarity). Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator and promoting expression of vegfa.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription factor E2F8
Sequence:
MQEVKCLTLKDLLGVRTLVNKTGSDDAASMNDHKENICMDRRKMTPLKSESLTAALNGHGKISSPEITHITPIKLTEKAHPDPWTPTANLKMLINAASPDIRDREMKKTLFKPIENKGKIAEEEEEEELDDSCQYEALDESERRPSRKQKSLGLLCQKFLALYPDYPESSESINISLDEVATCLGVERRRIYDIVNVLESLMLVSRKAKNMYVWHGRSRLPQTLQGLLQAGRDQHYDLLMDQREGNGLHAVQHVQNAHAASSRRKDKSLRIMSQKFVMLFLVSKTQTVTLDMAAKILIEEGQEESYDSKYKTKVRRLYDIANVLTSLNLIKKIHMREEKTRKPVFKWIGPGNFQSSSNSDDLRGQISNSGTERREKMARHSSFQVITAPPVNQRLISSAPSTPHRYSTDEPVDYSRKSGNNSAVCRLQFGDGVHPSVSPAVPSALASLAMPLQADLMPVPASFSHPLAILPQTPLLMLYSGNISDGASSLRKRERSEEDDHQTTKCRRRSASIESDTVESESLSSSTRRSPVCSPEGSPWDEASFGGLHEDDVAASSSKDALLSPHYLYVPNTAGLNSFNFLLPAGHAQGGVPAVAMPYFVVQSPLIAGAMPTSSTEGAAGFSVPTVLSPAQFVMAGGAYGVTEILQSPEHHGNVPATTSSPRAEESPKPAQTQTPVTPKEASLGSKSFFETPGAFGSLVNQSAARKRGSAQRRLDIGHTAAN
Protein: Profilaggrin (Q05331)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MSTLLVFIFAIINLFNEYSKKDKNTDTLSKKELKELLEKEFRQILKNPDDPDMVDVFMDHLDIDHNKKIDFTEFLLMVFKLAQAYYESTRKENLPISGHKHRKHSHHDKHEDNKQEENKENRKRPSSLERRNNRKGNKGRSKSPRETGGKRHESSSEKKERKGYSPTHREEEYGKNHHNSSKKEKNKTENTRLGDNRKRLSERLEEKEDNEEGVYDYENTGRMTQKWIQSGHIATYYTIQDEAYDTTDSLLEENKIYERSRSSDGKSSSQVNRSRHENTSQVPLQESRTRKRRGSRVSQDRDSEGHSEDSERHSGSASRNHHGSAWEQSRDGSRHPRSHDEDRASHGHSADSSRQSGTRHAETSSRGQTASSHEQARSSAGERHGSHHQQSADSSRHSGIGHGQASTAVSDSGHRGYRGSQASDNEGHSEDSDSQSVAGQRQARSRHQSHQESTRGRSRGGSGRSGSFLYQVSTHEQSESSHGWARTSTGRRQGSRHDQAQDSSRHSTSQQGQDTIHAHPGSRRGGRHGYHHEQSADSTGHSGSQHSHTTTQGRSDASRGSSGSRSTSRETRDQEQSGDGSRHSGSHHQEASTRAESSRHSQVGQGESSGSRTSRNQGSSFSQDRDSQAQSEDSERRSASGSRNHRGSAQEQSRDGSRHPGSHQEDRAGHRQSAESSSQSGTHHAENSSGGQAASSQEQARSSAGERHGSGHQQSADSSRHSGIGHGQASSAVRDSGHRGYSGSQASDQEGHSENSDSQSVSGQRQARSHQQSHQESTRGQSRGRSGRSGSFLYQVSTHEQSESAHGRSAPSTRRRQGSHHDQARDSSRHSASQEGQDTIRGHPGSSRGGRQGSHYEQSVDRSGHSGSHHSHTTSQGRSDASHGTSGSRSASRQTRDEEQSGDGTRHSGSHHQEASTQADSSRHSQVGQGQSAGSRTSRNQGSSVSQDRDSEGQSEDSERHSGSASRNHRGSAQEQSRDGSRHPGSHDEDRAGHRQSADSSSQSGTRHTQTSSRRQAASSQEQARSRAGDRHGSGHQQSADSSRHSAIGRGQASSAVRDRGHRGSRGSQASDQEGHSEDSDSQSVSAQRQAGSHQQSHQESTRGRSQGRSGRSGSFIYQVSTHEQSESAHGRTRTSTGRRQGSHHEQARDSSRHSASQEGQDTIRAHPGSRRGGRQGSHHEQSVDRSGHSGSHHSHTTSQGRSDASHGQSGSVDLQVD
Protein: Adenine nucleotide transporter BT1, chloroplastic/amyloplastic/mitochondrial (Protein brittle-1) (P29518)
Organism: Zea mays (Maize)
Function: Probable adenylate translocator that mediates transport of ADP-glucose into endosperm storage plastids during starch synthesis. Transports cytosolic ADP-glucose to amyloplast stroma by counter-exchange with ADP.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein {ECO:0000305|PubMed:21330298}. Plastid, amyloplast inner membrane {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein {ECO:0000305|PubMed:21330298}. Mitochondrion inner membrane {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein {ECO:0000305|PubMed:21330298}. Note=Dually targeted to mitochondria and plastids. The N-terminal extension acts as a plastidic transit peptide. Dual localization of BT1 does not seem to be due to alternative transcription start sites, translation initiation sites or alternative exon splicing (PubMed:21330298). {ECO:0000269|PubMed:21330298}.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic
Sequence:
MAATMAVTTMVTRSKESWSSLQVPAVAFPWKPRGGKTGGLEFPRRAMFASVGLNVCPGVPAGRDPREPDPKVVRAADNCDIAASLAPPFPGSRPPGRRGRGSEEEEAEGRRHEEAAAAGRSEPEEGQGQDRQPAPARLVSGAIAGAVSRTFVAPLETIRTHLMVGSIGVDSMAGVFQWIMQNEGWTGLFRGNAVNVLRVAPSKAIEHFTYDTAKKFLTPKGDEPPKIPIPTPLVAGALAGFASTLCTYPMELIKTRVTIEKDVYDNVAHAFVKILRDEGPSELYRGLTPSLIGVVPYAACNFYAYETLKRLYRRATGRRPGADVGPVATLLIGSAAGAIASSATFPLEVARKQMQVGAVGGRQVYQNVLHAIYCILKKEGAGGLYRGLGPSCIKLMPAAGIAFMCYEACKKILVDKEDEEEEDEAGGGEDDKKKVE
Protein: Tubulin beta chain (B1PBW7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREILHIQGGQCGNQIGAKFWEVICAEHGIDPTGRYNGDLDLQLERINVYYNESSCGRFVPRAVLMDLEPGTMDSIRSGPVGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSNPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYQALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATVDEEEEYEEEGAEYE
Protein: Cytoplasmic polyadenylation element binding protein 2 (D3ZHK8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRDFGFGVLHTALLRSGSPRSSPGGSAYRPFAAGPSATPFGPLSPPPLPVTGFSEAASPFAIPSGGGAASSAAASSSSPLVAHQQAVQDELLLGLTQQPARPLSGAAAAEQLPSHHPGGGTNAGVTHLLPSQDFKPSLHHPSSSSASSCCCCRTSSPQDFSKRQQQQLSSQKRKELSPPHRPHPPDAKPTPPPLHCPGRFSPPPPTPPPPPGPLLQSAPLAQRPQPFSLPHTQHLPPQDFAPRQRPADLPQLPQLPPSPPAAPRRRHGGAGSPRQTPVAGEGSAAEPPNAGLPPSTPPVNPAPGSMESPNHPLLNSPSTLLPGAALGTSAFSSLQSPDLPHPGGGGGGGPPGGGGGGGSASPPPLPGFGTPWSVQTASPPPPQPPPAPQQQPSQQQQPPQQPPQPQPPGSSAATPGGGGGAGGSLSAMPPPSPDSENGFYPGLPSSMNPAFFPSFSPVSPHGCAGLSVPAGGGGGGGGFGGPFSAPAVPAPPAMNLPQQQPPPAAPQQPQSRRSPVSPQLQQQHQAAAAAFLQQRNSYNHHQPLLKQSPWSNHQSSGWGTASMSWGAMHGRDHRRSGNMGIPGTMNQISPLKKPFSGNVIAPPKFTRSTPSLTPKSWIEDNVFRTDNNSNTLLPLQVRSSLQLPAWGSDSLQDSWCTAAGTSRIDQDRSRMYDSLNMHSLENSLIDIMRAEHDPLKGRLSYPHPGTDNLLMLNARSYGRRRGRSSLFPIDDSLLDDGHSDQVGVLNSPTCYSAHQNGERIERFSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQMCDECQGARCGGKFAPFFCANVTCLQYYCEFCWANIHSRAGREFHKPLVKEGADRPRQIHFRWN
Protein: Uncharacterized protein C18G6.01c (Q10102)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosomes element 1
- E3 SUMO-protein ligase nse2
Sequence:
MFGTRFFAYQFCKNWLSKRPGLVFWSSVATINAMYQTRPLYCESVTKTIQQTYEGLVQKRINNEDELFLLGSGPRYVSFLSIHVYDIELYIQKKDVQTVHTILQKEVDPKLGLEMSMKDEEIGSRIVAALLKNEMKYAIKIVPTRNTNFSHLRGGFVRGLQSRMSQNDPAEQAAVSKFRSTFPVNRTCFKETALWMKLYGNDFCYIYKDSEIGHMHDENYMVSNLFLKGYLVGPRVNSEQARESVCLTLRRIMDGTLLF
Protein: Carboxypeptidase A1 (EC 3.4.17.1) (P00730)
Organism: Bos taurus (Bovine)
Function: Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9UI42}.
Interaction partners:
- Proproteinase E
- Chymotrypsin-C
- Chymotrypsin-like elastase family member 2A
- Pancreatic polypeptide prohormone
- Carboxypeptidase B
- Pancreas transcription factor 1 subunit alpha
- Chymotrypsin-like elastase family member 1
- Recombining binding protein suppressor of hairless-like protein
- Bile salt-activated lipase
- SRY-box transcription factor 9
Sequence:
MQGLLILSVLLGAALGKEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSRARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNNLY
Protein: phosphoinositide 5-phosphatase (EC 3.1.3.36) (A0A0R4IPY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}.
Interaction partners:
Sequence:
MMEPSFGISESQCIATVRGHEIRSGQKEPRLLSLLECSGQFKLDILSNPDAIVLSPVSQLSIPINNHFRIIREAEEALLIDIDSISKTVRIRLRGERTPELLLELQDDGQTQSFLEHVTKAKQQAERSSLPRKMEPVVPAPVKDCVPVPPQRGTSKSFSNNINNSTLANPSNTDSTRSLATDFGFEENFNHVLKVEEKKNKQNRLVAQREPPPPPIPPLPPRKGTNTSLTGPATKERPPSVQNATPVRNEFQSVDRSVSWSESPSNSTIRQAMMSSHAGSREGLLKYRLSKKEKEYVDIKNFKFFVGTWNVNGQSPDSSLGPWLSSDPDPPDVYALGFQELDLSTEAFFYMDSSKEQLWVDAVERGLHQKARYIQVRIIRLVGMMLVVYIKKEHKDQIREIASESVGTGLMNKMGNKGGVAVRFVFHNTSFCFVNSHLAAHVDDFERRNQDYKDICARMSFHLLEYPPVSIVKHDVVIWLGDLNYRLCLPDAGEVKRLIAEKELRRLQEYDQLNLQRKTKRVFTDFMEGEINFIPTYKYDAKSDRWDSSGKCRIPAWCDRILWRGSNVKQLHYRSHMELKTSDHKPVSSVFSIGVKMVIEQRYKKIFEEIVRDMDRMENDFLPSLSLTRREFTFENVKFRQLQRQSFLITNDGQVACTFAFIPKLNDSQYCKPWLRAEPCEGVLDPNEKIEIFLEVYVSKDSVTLLNSGEDNIEDILVLHLDRGKDYFITVSGNYLPSCFGTSLETLCRMKKPIREIPITKLIDLGEDSCMEKEKARMTFLLDSAGTEDKPLKIPKEVWLLVNHLYTKACQQEDLFQTPGLQDELQSIIDCLDTSIPDSIPGCNHSVAEALLIFLEALPEPVLCYELFQRCLECSHDSRLCKQLISQLPRAHRNVFRYLMAFLRELLKHSIDNNLNANLLATLFASLLIRPPPNLAGKQTQHDRQKANDFILGFLMAGDED
Protein: Ras association domain-containing protein 2 (Q8BMS9)
Organism: Mus musculus (Mouse)
Function: Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P50749}. Cytoplasm {ECO:0000250|UniProtKB:P50749}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P50749}. Note=Translocates to the cytoplasm in the presence of STK3/MST2 and STK4/MST1. {ECO:0000250|UniProtKB:P50749}.
Interaction partners:
- Serine/threonine-protein kinase 3
- Ras association domain-containing protein 4
- Serine/threonine-protein kinase 4
- Ras association domain-containing protein 7
Sequence:
MDYTHQPALIPCGQDKYMPKSELLLHLKTYNLYYEGQNLQLRHREEEDEFIVEGLLNISWGLRRPIRLQMQDDHERIRPPPSSSSWHSGCNLGAQGTTLKPLTMPTVQISEVDMPVEGLETHSPTDSRGLKPVQEDTPQLMRTRSDVGVRRRGNVRTSSDQRRIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYVVHTSGEKQRLKSSDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPVLKSFIQKLQEEEDREVEKLMRKYTVLRLMIRQRLEEIAETPETI
Protein: Crotonyl-CoA reductase (EC 1.3.1.86) (Q82LU9)
Organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Function: Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It uses only NADP as electron donor. May have a role in providing butyryl-CoA as a starter unit for straight-chain fatty acid biosynthesis.
Interaction partners:
Sequence:
MKEILDAIQSQTATSADFAALPLPDSYRAITVHKDETEMFAGLSTRDKDPRKSIHLDDVPVPELGPGEALVAVMASSVNYNSVWTSIFEPVSTFNFLERYGRLSDLSKRHDLPYHIIGSDLAGVVLRTGPGVNSWKPGDEVVAHCLSVELESSDGHNDTMLDPEQRIWGFETNFGGLAEIALVKSNQLMPKPDHLSWEEAAAPGLVNSTAYRQLVSRNGAGMKQGDNVLIWGASGGLGSYATQFALAGGANPICVVSSEQKADICRSMGAEAIIDRNAEGYKFWKDETTQDPKEWKRFGKRIREFTGGEDIDIVFEHPGRETFGASVYVTRKGGTITTCASTSGYMHEYDNRYLWMSLKRIIGSHFANYREAWEANRLVAKGKIHPTLSKVYSLEDTGQAAYDVHRNLHQGKVGVLALAPREGLGVRDEEKRAQHIDAINRFRNI
Protein: N-alpha-acetyltransferase 40 (EC 2.3.1.257) (Q9USH6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized N-acetyltransferase C663.13c
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase A complex catalytic subunit ard1
- N-terminal acetyltransferase B complex subunit arm1
Sequence:
MHFLKQYLFYSPRRMKTQEIKNVTLEDVDFLKNLGVWVEIYHHLEKGLLQQCFNLVKKNMEALYRQSSFGWDDSEKLKEMEMEKLEYICIFEKTSKKLVGFLSFEDTVEAGLTCLYIYEIQLDEHIRGRNVGKWLLKNASILAYRRNLKYIFLTVFSANLNALNFYHHFDFVPHESSPQEKKFRSGKVIHPDYYILYTKSRKDW
Protein: ATP-dependent molecular chaperone HSC82 (82 kDa heat shock cognate protein) (Heat shock protein Hsp90 constitutive isoform) (P15108)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
- Protein SGT1
- Heat shock protein SSA1
- Co-chaperone protein SBA1
- Hsp90 co-chaperone AHA1
- ATP-dependent molecular chaperone HSP82
- Hsp90 co-chaperone Cdc37
- Heat shock protein STI1
- Mitochondrial protein import protein MAS5
- Peptidyl-prolyl cis-trans isomerase CPR6
- Serine/threonine-protein phosphatase T
Sequence:
MAGETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPKQLETEPDLFIRITPKPEEKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKNNEDEQYIWESNAGGSFTVTLDEVNERIGRGTVLRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLLVTKEVEKEVPIPEEEKKDEEKKDEDDKKPKLEEVDEEEEEKKPKTKKVKEEVQELEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFDKFYSAFAKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKDILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTNLLFETALLTSGFSLEEPTSFASRINRLISLGLNIDEDEETETAPEASTEAPVEEVPADTEMEEVD
Protein: Putative hydroxypyruvate isomerase (EC 5.3.1.22) (Endothelial cell apoptosis protein E-CE1) (Q5T013)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Interaction partners:
Sequence:
MAPLRFSANLSWLFPELSGLPARVRAAGSSGFEAVEVAWPYAETPEALARAAREAGLRLVLINTPPGDQEKGEMGLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRIAVKAEMEAVFLENLRHAAGVLAQEDLVGLLEPINTRITDPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSPGELNFPYLFQLLEDEGYKGFVGCEYQPRGDTVEGLSWLRSYWDRRGHPEAGQ
Protein: Schlafen-like protein 3 (SLFN-like 3) (PUCH complex member slfl-3) (O61766)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:37758951}; Single-pass membrane protein {ECO:0000255}. Note=The localization to the mitochondrion is mediated by the transmembrane domain. {ECO:0000269|PubMed:37758951}.
Interaction partners:
Sequence:
MDSGDFSPMQSNFSLGFMSFEDIPEDARTTEMIDKIVFEEDKEYDHTQDSFRYGRVTTGVSYNLVTGKIPKTVFEQVKAKDDENDNVEFEMEHLEDKETAHKTQTFDELYESQMPKYFDYQSNFSDVNGIWTLLFDQNHYEKMSTFELQAAICAALNSKHFMMICVGIDAFNAVTGVEMSAKDRVVFRMALTRAVAGEFQPPLVKVAPKQLTGVSPMKRDISEVTSSIDVLFVPVIGVTDEVENNRFLIVVRVKEISDKVYQISSGRIYNEQEGRVVEMSDMNEAFHKLIVEKSISDIQTRRGSMFMLEPEPFLEDSAVIFTESNEIPSENHEISRVHVKNCTERSLSQSLLNLLDIQNIGWIFFGTALSFCIYNNAIKPLVK
Protein: Adenylylsulfatase HINT1 (EC 3.6.2.1) (HIS triad family protein 3) (Histidine triad nucleotide-binding protein 1) (Q8GUN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses adenylylsulfatase activity in vitro.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19329564}. Plastid, chloroplast {ECO:0000269|PubMed:19329564}.
Interaction partners:
- Bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein E
- 26S proteasome regulatory subunit
- Probable acyl-activating enzyme 12, peroxisomal
- Acetate/butyrate--CoA ligase AAE7, peroxisomal
- Vacuolar protein sorting-associated protein 53 A
- TATA-box-binding protein 1
- TATA-box-binding protein 2
- Pentatricopeptide repeat-containing protein At4g30825
Sequence:
MSHRVSILSSHFSPASAVMASEKEAALAATPSDSPTIFDKIISKEIPSTVVFEDDKVLAFRDITPQGPVHILLIPKVRDGLTGLSKAEERHIDILGRLLYTAKLVAKQEGLAEGFRIVINDGPQGCQSVYHIHVHLIGGRQMNWPPG
Protein: Chorismate mutase (CM) (EC 5.4.99.5) (P32178)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12455686}.
Interaction partners:
- Chorismate synthase ARO2
- Probable prephenate dehydratase
- Prephenate dehydrogenase [NADP
- Multifunctional tryptophan biosynthesis protein
- Pentafunctional AROM polypeptide
- Anthranilate synthase component 1
- Aromatic/aminoadipate aminotransferase 1
- Aminodeoxychorismate synthase
- Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
- Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-inhibited
Sequence:
MDFTKPETVLNLQNIRDELVRMEDSIIFKFIERSHFATCPSVYEANHPGLEIPNFKGSFLDWALSNLEIAHSRIRRFESPDETPFFPDKIQKSFLPSINYPQILAPYAPEVNYNDKIKKVYIEKIIPLISKRDGDDKNNFGSVATRDIECLQSLSRRIHFGKFVAEAKFQSDIPLYTKLIKSKDVEGIMKNITNSAVEEKILERLTKKAEVYGVDPTNESGERRITPEYLVKIYKEIVIPITKEVEVEYLLRRLEE
Protein: Kappa-type opioid receptor (A0A5F9ZI09)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPVXLVVEMSSYSSSGREEFNDLGLTQITTAV
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q9VD61)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ero1-like protein
- Sulfhydryl oxidase
Sequence:
MIRLLKTLLYCLLLISPADVLGRLNARKSANEASLYSDTDNVIMLDIESLRPALNLKNSKLVQFLNSFCGDCHRFAPVFKTLSRDLYKWRRILRIYAVDCAQERNAQLCREFNIRQTPSLRFFGPDMRKNDDVLGAVIPGQDPEFISSTLAELVSQNDYGPGQPNFRPLKATDYEIFQDQDGETPIQFVALVLQPKNSKIGRDTLLELLPFKELSVRIIEDSQIFNEFGLGPDDQKLAIVDRNGTAQYLTPSSDSSEAYASTIGDFLKNRNIQPDPPLPIAVAPNFTEFLDHQNQAILTKVLTPPLQVYRADLEQAIDKLLHIELRKWVLLEGNSLNALKNIIKIFRYLNPLNKDGKLLLTDLDNSLSSKQSIKGADFGDLVDSLENGRRVFKARRYVGCIGSRPLLRSFTCSMWTLFHHLTVEAAKPPNYFEAGSILKTFHGFAKYFFGCTDCSEHFQQMAIRRNLTSVKTHDEEILWLWAAHNEVNARIAGDSTEDPKFPKIQFPSAENCPTCRSNDSEWRTDEVLKYLKQLYDINNVSFYGLPTPQGYD