wanglab/gogpt-training-data huggingface dataset:
Protein: D-mannonate dehydratase CC2812 (ManD) (EC 4.2.1.8) (Q9A4L8)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Mannitol 2-dehydrogenase
- SAF domain-containing protein
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- D-mannonate dehydratase CC0532
- 2-dehydro-3-deoxygluconokinase
- Uronate isomerase
- Carbohydrate kinase, pfkB family
- Ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase A
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
Sequence:
MPKIIAAKTIVTCPGRNFVTLKIMTDEGVYGLGDATLNGRELAVEAYLTQHVIPCLIGRDAHQIEDIWQYLYRGCYWRRGPVTMAAIAAVDTALWDIKGKIAGLPVYQLLGGACRVGVMVYGHANGETIDETLDNAAVYAQQGYKAIRLQTGVPGMSGTYGVSKDKFFYEPADSDLPKETIWSTERYLRSTPALFEAARERLGDDLHLLHDVHHRLTPIEAARLGKDLEPYRLFWMEDATPAENQASFRLIRQHTTTPLAVGEIFNSIWDCKQLIEEQLIDYIRATVVHAGGITHLKKLASFADLHHVRTGCHGATDLSPVCMGAALHFDLSIPNFGVQEYMRHTPETDAVFPHAYTFKDGMLHPGDAPGLGVDIDEDLAAKYPYQRAYLPIARRLDGSMHDW
Protein: Slr2144 protein (P73681)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr1160 protein
- Sll1549 protein
- High light-inducible protein HliD
- Ycf51-like protein
- Sll1632 protein
- Sll0359 protein
- Uncharacterized protein sll0944
- Sll1274 protein
- Sll0822 protein
- Slr1302 protein
Sequence:
MPSPLTSPWLIRSHRHPSSTALKFDQNMISQPQGFTRLSRSSHRFFPARWLMAFGWGVGLMALGSLPLNAATIAQGNVTERQVRALIEQFDAVANQHNTDRLGEIYSPEFSNSDGLTFAQMETTLQQLWETYGNLTYSTELKNWKQDGQAVVVETLTTIQGERPWLGRTAQLNGQITSRQTFVQNKLVRQEVLTEKMTLTAGDNPPEVDVNLPQQVQAGQEFDFDVVLRQPIGDDLLAGTAFSQKIDPNNYVDPSQVKLELLQAGGLFKRAIAGNDPQWLSALLVTPEGMVLVTQRLAVVP
Protein: Lipid phosphate phosphatase gamma (AtLPPG) (EC 3.1.3.-) (Phosphatidic acid phosphatase gamma) (Plastidic phosphatidic acid phosphatase gamma) (Q6NLA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a primary role as PAP in plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:17652095}; Multi-pass membrane protein {ECO:0000305|PubMed:17652095}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichol kinase EVAN
- dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- At3g57220
- Lipid phosphate phosphatase epsilon 2, chloroplastic
- Lipid phosphate phosphatase epsilon 1, chloroplastic
- Dolichol-phosphate mannose synthase subunit 2
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
Sequence:
MDLIPQQLKAVTLTHVRYRPGDQLGHFLAWISLVPVFISLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLEACDSHGWPSSHSQFMFFFATYFSLMGCKGIGFWFGLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVNSVLYPFFPVIEESVLGRWLYVKDTSHIPDVLKFEYDNARAARKDMDSAKSD
Protein: Protein asunder (Cell cycle regulator Mat89Bb) (Integrator complex subunit 13) (Maternal transcript 89Bb) (Set apart in position or space protein) (Q9VEX5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1 and U5. Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus-centrosome coupling that occur upon meiotic progression of primary spermatocytes. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:9799434}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19357193}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes (PubMed:19357193). Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M (PubMed:23904267). {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23904267}.
Interaction partners:
- Integrator complex subunit 1
- Integrator complex subunit 3
- Integrator complex subunit 5
- Integrator complex subunit 14
- Integrator complex subunit 9
- Integrator complex subunit 6
- Integrator complex subunit 11
- Integrator complex subunit 10
- Integrator complex subunit 4
- Integrator complex subunit 7
Sequence:
MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIVSDTAAHIVNTWRPSTQNMAHVMNAMLIVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADFGTDELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPSKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISPLLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGATYETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSLCITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRVVPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLPHFLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLESLQSLRAAYGDAPLKSEPGASLLRTYTESPLSPERLEPISSVGASGSSSSNSLLKASKRRMSSCGQRSLLDIISSAERSQSNKRLDFSGRLCTPLGQVAKLYPDFGTKDKDTVTTGASITPNVKEESVRS
Protein: G-protein coupled receptor family C group 6 member A (Odorant receptor ZO6) (Q5U9X3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Olfactory receptor that is activated by amino acids that act as potent odorants in fish. Displays preference for acidic amino acids such as Glu over basic amino acids.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8K4Z6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8K4Z6}.
Interaction partners:
- Olfactory receptor C family, b1
- Calcium-sensing receptor.
- Phosphoinositide phospholipase C.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- PH_14 domain-containing protein.
- G protein-coupled receptor 158a
Sequence:
MDLMSFILLWAGLMKVAEASIAQFSQLGASAPGNIIIGGLFPIHEAVVPVNYTGNNSISAPEHPDCIRFYTKGLNQALAMINAVEMANKSPMLSSLNITLGYRIYDTCSDVTTALRAVHDIMRPFSDCESPEDSSQPVQPIMAVIGTTSSEISIAVARDLNLQMIPQISYASTATILSDKSRFPAFMRTVPSDEYQTCAMAKLLKSNKWSWVGIIITDGDYGRSALEGFIQHTETEGICIAFKAILPDSLADQQKLNTDIENTLNIIENNPKVRVVISFAKSSQMQLLFKGLQSRNISNNMVWVASDNWSTAKHILNDGSITDIGKVLGFTFKSGNFTSFHQYLKNLQFESEDEMNNSFLKEFLKLNAGNASNTVLELMKSTNLDKIFSIEMAVTAVANAVAKLCAERQCQDSTALQPWELLRQLRSITFENGGEMYKFDANGDINLGYDLFLWEGDQSDEHADDIIAEYDPTKGGFHYIHNDLSEIKKVVSRCSNSCQPGQYKKTAEGQHTCCYECLTCVENHYSNITDADECSPCDSESMWSLANSTECHPKVFEYFDWNSGFAIVLLILAALGVLLLFFMSALFFWQRHSPVVKAAGGPLCHLILVSLLGSFISVVFFVGEPSDLTCRARQVIFGFSFTLCVSCILVKSLKILLAFEMNFELKELLCMLYKPYMIVSVGMGVQIIICTVWLTLYKPFKDKEVQTESILLECNEGFYVMFWLMLGYIALLALFCFTFAYIGRKLPQKYNEAKFITFSMVICLMAWIIFIPIHVTTSGKYVPAVEMVVILISNYGILSCHFLPKSYIILFKKEHNTKDAFMKNVYEYARKSAENIKGLTGTEPQFKQENSVYTISNLSFVPEEKHE
Protein: 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) [Cleaved into: PEX] (P33436)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 3
- Matrix metalloproteinase-14
- Metalloproteinase inhibitor 1
- Vascular endothelial growth factor A
- Endothelin-1
- NADPH oxidase 2
- Proto-oncogene tyrosine-protein kinase Src
- Cytochrome b-245 light chain
- Neutrophil cytosolic factor 1
Sequence:
MEARLVWGVLVGPLRVLCVLCCLLGHAIAAPSPIIKFPGDVSPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNGDGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKVWCATTTNYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSNDDIKGIQELYGPSPDADTDTGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFSGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
Protein: Uncharacterized amino-acid permease C777.04 (O74543)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative arrestin-related trafficking adapter C2D10.04
- Ribose-phosphate pyrophosphokinase 1
- Large ribosomal subunit protein eL36B
Sequence:
MSSIKSKTIIEPSENDIEKGEVDFVSSSISNFEEAYEEGPSLKREFKSRHVNMISVAGAIGTGLVIGSGSALLKGGPGSLFIAYLMTGINLYVVLISLGEMAAFSSDDKGFSGFSSRYVDKALGFATGWNYFFKYAIVYPTNLTAVGIVIHYWRPDLNVGIWVAVFLVVILAINLLHVKYFGEVEFWLSAVKILVLVTLIITCIVITSGGTPVHHKIGFHYWRDPGAFAPYLVEGSTGRFLGFWACLVQSCFAYVGSEVVGIAFGEAPNPEKTIRKSSFQSLFRIATFYVIGVFVLGLCVPYDSDILSSNASKGNAAASPFVVAIKLAQIKVMPDVINACLLVFIISSANSDIYIGSRTLYALAKEGYAPKILMLQTKQGIPWVGCLVTSSFGLLAFMNTKSSSATIFGYFSSAVTVFGTINWINILLSYICYHRATIVQQIPTERIPFRSWGQPYIAYASLIFTGLITFFNGYNAFIHGFKYRSFITSYIGIAAYVIMILGWKFTFKAKRVTSSTVDFRK
Protein: Calmodulin-binding receptor-like cytoplasmic kinase 1 (EC 2.7.11.1) (Q9FIL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- O-fucosyltransferase 20
Sequence:
MPMRSKTPTPLRFSNGKHQRDDSEYSWTDVGTGEKARNVSVLGAIRRAAKKVFVIIFLGQRKLKPTECRSDPGESSTHDRESTLSGWTGYSSPSSFGRSTERKVSGQYRFSGSRFQSPGKDSSSSKSWHQGPVIFSFGELQRATANFSSVHQIGEGGFGTVFKGKLDDGTIVAIKRARKNNYGKSWLLEFKNEIYTLSKIEHMNLVKLYGFLEHGDEKVIVVEYVANGNLREHLDGLRGNRLEMAERLEIAIDVAHALTYLHTYTDSPIIHRDIKASNILITNKLRAKVADFGFARLVSEDLGATHISTQVKGSAGYVDPDYLRTFQLTDKSDVYSFGVLLVEILTGRRPIELKRPRKDRLTVKWALRRLKDDEAVLIMDPFLKRNRAAIEVAEKMLRLASECVTPTRATRPAMKGIAEKLWAIRREMKETMICSSASNSSCSSTTHSFIGRDSDRYALPRIEDNENSIE
Protein: Mediator of RNA polymerase II transcription subunit 1.1 (Mediator complex subunit 1.1) (Suppressor of pal-1 protein 3) (Q9N4G4)
Organism: Caenorhabditis elegans
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 14
- Putative guanine nucleotide exchange factor MSS4 homolog
- Glutamine/asparagine-rich protein mdt-30
- Mediator of RNA polymerase II transcription subunit 13
Sequence:
MIIEERKNHELNLESIDRDLRMENVRQSAEKLGWEHFARSVRRNLLEKRQTLDARTRLDVLGSLVFMKEHLPIDNDATIARKVQQLSEGLGEHCVFSTQNSGFSIRNPDVTIDIGVAEDQISTCKIGYFGQPLTDAPGALALMKNGEFSKLRDSITAILSSLPKEITLSEKNACKEAFRALDQLLIRDAADSSFTAINTGKYGFYAPRNELRSGRIYYVAEPVLIRLAEKEGKTKADASYLDLLPYIEISFFKHDKPSKLPVFTQTGEWSTFNDANVCICVRFNQGFLLSQQTIRKLSHIVPKSPLVRNYVNFYRYMTGRVGVKSNLKLLTQFPDEGDIQQQYQVDSKMLTKEDDVVAMEMYLSDFRDLSKLIETLRSEWKHASLWESILAICESSKGEQKEVNAVDMQLVLRRTEFFLQFDTDYGSMTMQIFEKSPSNYVVKTTSQITGESPSLDFDKMLTEKLNSTWSIPATLTFAITDLKCRINSVLNCVISFDSSSSSDKQHQNYWSISNNNTQLMQSAAQKSAAKCTKKKVTVLEVGPAIEPTQLVYTRENDEEFQGSLLSSFGEVDDYYVKTSTIGRTRPQPRPKREPNQLTSMDMMSAELDKSRHTMEGSMRDAQTSSFLDAARVRMKQSIGAAHAVGLASHQPPASPVAAAAAAPGGPMRHNSYPSGFEPPPSVAPYDFPADPSKKQRKQRAKKQPGEEPPAGRGKGGKKGRGAGAVGAAAAGGRKSAGGAGENPFGMDPMRPPMLQRSSSEQHNPNPHQMSQYQMQQYQQNQQFRMHQMQQQQQQQFQMQSPKNPLVPAYTDEDSDEECDPPPPPKPQVSTSSRMSSVPSHPPPPPQQLGNPMVGYPGMPLQSPNHLPLTPSPLSAPPKPFSPEQQHHFGMKMRETSYWKELERLETKPDVEKLKQQLSSSSSSSQAEASDPPSTSTEAQDPPKPSSSSAPPPPKKKLGLEAAISKIRGQQEQALQKQLQQQESVESELATPHPGSSGAPPLAPHQVNRARNLNDIFDDEADDSSPTADIKPSLQALQKPTDTSSQSTSSEPPPKKEPADEQPEREKEKLILKIPKMLKPVVDDRREDRKERDRDRDRDRDRDEDREKVRDKEDKAQREKDKKEKERERRRQRDRDRTEQKKSDREKEPSKKRKLEKKDEKEKDRREPERKKGKSDGKEYSKASTTSLIPTLSLKNFRIPKKDTVEEEKKDVKEEAPGPSSSTESKKEPPSAAPITRKESTTAPVAPAVQQQQQRKESFTALPSLPEQQQHHREPLLKKKPPLQPPPPPQMTGPPIGIYPGPPAPGNLPGSSRPSGNRKQPLPPPPPMIRGPPPDQMYRDRSGGGGGSMRGGFPPASHYHGGTSGVNKQVASYAQGLPPGMGPPVVKPHGNNYQASQWVRPPTHRDSSHSYHGMPSLGPPQLQREPPAPPPPQMIPLPKDPPVLREHPREHRAHRGGADDDGPDSPEEGTLRIDDE
Protein: Keratin-associated protein 11-1 (High sulfur keratin-associated protein 11.1) (Q8IUC1)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 8-1
- Keratin-associated protein 3-1
- Keratin-associated protein 7-1
- Keratin-associated protein 2-1
- Keratin-associated protein 17-1
- Keratin-associated protein 24-1
- Keratin, type II cytoskeletal 71
- Keratin, type II cuticular Hb5
- Keratin, type I cuticular Ha5
- Keratin-associated protein 15-1
Sequence:
MSFNCSTRNCSSRPIGGRCIVPVAQVTTTSTTDADCLGGICLPSSFQTGSWLLDHCQETCCEPTACQPTCYRRTSCVSNPCQVTCSRQTTCISNPCSTTYSRPLTFVSSGCQPLGGISSVCQPVGGISTVCQPVGGVSTVCQPACGVSRTYQQSCVSSCRRTC
Protein: DNA polymerase sliding clamp (Proliferating cell nuclear antigen homolog) (PCNA) (O73947)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Unlike its eukaryotic paralog, loads on circular DNA without the replication factor C (RFC) clamp loader, although RFC greatly increases loading efficiency. Stimulates the ATPase activity of replication factor C (RFC) in the presence of ssDNA. Stimulates the helicase activity of Hel308 and may alter its substrate specificity.
Interaction partners:
- DNA polymerase II small subunit
- DNA polymerase
- Flap endonuclease 1
- DNA primase large subunit PriL
- DNA ligase
- DNA primase small subunit PriS
- DNA polymerase II large subunit
- Replication factor C small subunit
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- DNA helicase
Sequence:
MPFEIVFEGAKEFAQLIDTASKLIDEAAFKVTEDGISMRAMDPSRVVLIDLNLPSSIFSKYEVVEPETIGVNMDHLKKILKRGKAKDTLILKKGEENFLEITIQGTATRTFRVPLIDVEEMEVDLPELPFTAKVVVLGEVLKDAVKDASLVSDSIKFIARENEFIMKAEGETQEVEIKLTLEDEGLLDIEVQEETKSAYGVSYLSDMVKGLGKADEVTIKFGNEMPMQMEYYIRDEGRLTFLLAPRVEE
Protein: Heat shock factor-binding protein (AtHSBP) (Q8GW48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of the heat shock (HS) response. Affects negatively HSFA1B DNA-binding capacity in vitro. Involved in acquired thermotolerance but not basal thermotolerance. Crucial for seed development, after fertilization and during embryogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20388662}. Cytoplasm, cytosol {ECO:0000269|PubMed:20388662}. Note=Translocates from the cytosol to the nucleus upon heat shock (HS). {ECO:0000269|PubMed:20388662}.
Interaction partners:
- Heat stress transcription factor A-1a
- Heat stress transcription factor A-2
- Heat stress transcription factor A-1b
- Protein BOBBER 1
- Transmembrane 9 superfamily member 9
- Heat shock 70 kDa protein 4
- Fes1A
Sequence:
MDGHDSEDTKQSTADMTAFVQNLLQQMQTRFQTMSDSIITKIDDMGGRINELEQSINDLRAEMGVEGTPPPASKSGDEPKTPASSS
Protein: Vacuolar-sorting protein SNF8 (Q9VD72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein sorting 20, isoform A
- Charged multivesicular body protein 4
- Vacuolar protein sorting-associated protein 28 homolog
- Tumor suppressor protein 101
- RH72336p
- GH14561p
- Vacuolar protein sorting-associated protein VTA1 homolog
- Multivesicular body subunit 12A
Sequence:
MRRRVGLGAIQQQKLAAEKYKDKGTDLQENQLEQMTKQMEVFRVKLEEFAMKHKEDIRKNSQFRKQFQEMCAAIGVDPLATGKGFWSVLGMGDFYYELGVQVVEVCLAANHKTGGLMELDDLRRRLIAARGQSSVHQEITKEDILMAAKKLSIFGNGFVVHKLGKGKYIVQSIPGELSMEETNILNAASNTEQGCVTQSQLIKDLGWTDYRAQQSLDKVLGEGLCWIDKQAGDEPAYWFPSLFPGRNAQTTAAT
Protein: Increased minichromosome loss 1, isoform C (Q8IRG8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLYKLNTHTRGCNKSYDADLVMNLKDHPNANVGDVVEIYAPDEENGTHLLLQITEFNGSCGRDVISIESGIANAFKMRPYSNVVMRIVKPADVALDSIEITFKDQYMGRSEMWRLKTYLTDTCVYVNKKIDYNDMQIRCQVYEMWSQGERVASGVITEDTKIVFRSSTSMVYLFLQMSSEMWDFDIHGDLYFEKAVNGFLTELFQKWRKLSCNHEVTIVLFSRTFYAAKSLDEFPEHMRDCLQQDYKGRFYEDFYRVAIQNERCDDWCTVLGQLRKLFTSYQATVLRYHERENMKIPPATNSSATQGNFLEVLNISLNTFEKHYLDRTFDRTGQLSVVITPGVGVFSVDRELTNITKQRIIDNGVGSDLVCVGEQPLHAVPLLKFHNKDTTLTSADDYSLPHWINLSFYSTNKKIVYSSFIPRIKLPLFGSQLTLHDGVGDGEGEENERHFLSCNQSEYKHNSLFDYDAYDEQIFQPLPAQSTCSLQRVVRAKKTSVPSLETYAYRNNDWENLTPTQIPAMRRKMSDPDIHHGTSAMLAALQPDTTNLSESLASEKNSRRTIVSIAPIVRPGRALINPFDPSQVTIKLTSNRRRWTHIFPKGPTGVLIQQHHYQAVPAKPTQAGQQRPLQQTQSNNNNDQEDYGCENGEQYDRVSSHSLLNKSDSSQSFVMGDEPIDFFKRRQNSPMNPQPANVPNLTATQAKSYLWGATGEQEWTPAITTGVDWKSLTIPACLPITTDYFPDKRSLNNDYVISDYTLLPDDVNHDYAQSRAVYRKPLSTEEVCKEIVSQRLAQGFQLIVVDEKPPTASGCSSGSAVQPVKLSRETNKEYLLSIGRIFHKISLSGSVITVTGYRPRHPYPPINVDYRYRFHAPQHETYEISGVNFTTEKLENFNWNHMDLYICTRGDVDYPLMESLKYWRYRMYLLPRENIVSKIASCQRCDIFPDVTADNTREQVEDFVRLIEAVSKLKRQYARKARGLTNSPFRERVGSNRLPEKRPSINVRPKLENGRIPRIFPATDAAAAAGVAARDDQDDGFPVDIKFSPNATLPEIFEAMKHPVNGVGFFSQTQSLPSCTFVSYDALMWLKTRLNNGRHPLDLLEAMRKERMICHASGDWKKPVVPGFVFYYVVQQDKNAKDYAPPLDDYSAFVNEWLEIEFQGCSFLWHDEPVTTPVPNFLRDSPAPQSWTETSSNKRVYRQSHLEIDVNQKSDRMEWGHVKHHTVLQPRFAFEIVVEWVTSSGPIVADLIGGWMRKANQFNFLVSVPADPMAEPFTKKSDPLRGPIFIPLCTTFLPNGAALFDEFPEESRSDRMLFFQEAILGKFGFLPCVLEKKYSVGKDLPKEYQYVHCTGNMFALIRCATNNYQVESPILKEANVTRCVYGHTNNTNVPKKVGFLWAWNHMIPNKKWKAQTINNSADGELFQLKMLKDFREFCSNSDQRLSTFWTQSQELKRRAQKFEFNNNNTEENKMK
Protein: Carnitine O-acetyltransferase (Q59T80)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Carnitine O-acetyltransferase
- Carnitine O-acetyltransferase, mitochondrial
- Isocitrate lyase
- Mitochondrial thiamine pyrophosphate carrier 1
- Peroxisomal hydratase-dehydrogenase-epimerase
- Mitochondrial thiamine pyrophosphate carrier 1
- Malate synthase
Sequence:
MSTYRFQETLEKLPIPDLVQTCNAYLEALKPLQTEQEHENTKIAVDKFLNGSNSKTTNNGVVTGSGIGHYLDRELRQYAKTRPSYIEQFWYDSYLNYDSPVVLNLNPFFLLEDDPFTNESSSINPQVKRATNLTLSSLKFIQALKNETLSVDTLKNGKPLCMYQYTKLFGASRIPSQEGCMMQSDPLSNHIVVMSKSQFYWFDVLDSHNNLILNEAELNINFNSIIRDSLNTPSDEIAKSSFGVLTTENRRVWANVRNNLIGNNTINREVLSIIDSALFILCFDDIAIDDLSELSKNMLCGLSILDNGIQVGTCTNRWYDKLQIIVTKNAKAGINFEHTGVDGHTVLRFVSDIYTDSILSFANSINNNAPSLWKSTTKNDVPDYELEEELITIPRKLEWDLTPDLSLVLRFGETRLSDLINQNEFRHLEFKNYGSSQIKKMKFSPDAFVQMAFQATYYALYGKVECTYEPAMTKQYYHGRTEAIRTVSQESNLFVRKFFDSTVSMKEKLQYLSDACKKHSEKTRMSSMGQGVDRYLYAMFCIWKRYLQDYEEEQQQQQHPVEEGSGGEQQMEAVGLSRDDTIVVQMDGEHDDDDSTTVVGTNGGKNLHASGSHGNNDIYDNFDLLKTVPELFADSGWDKLNSTIISTSNCGNPSLRLFGFGPVSANGFGIGYILKDDSISICASSKHRQTQRFLVTLNSYLLEIQSIWKQVETMNKLQDELALKIDISKKQKETEEEQARPKHNINALLGGYGYFDMGEEDIKSRGQSPEPPFLNRANSSFSVREIGKKLRLSEY
Protein: RNA helicase (EC 3.6.4.13) (Q7ZVV8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MANLEQWVSDQLHDILGLSDRYVAQFMIGLVQKSSGPQDFVSRLQDTGTIDIDQRITAFAHELYDKAPKKHVVEKPARAIERQVMEMERKNRTYTLLEDSESDGEAAREGGKEKKSKERDKGKKRKHLRQKRDESPSSSEEDKKKSITFKDEPKKAGKEDEEEEEWERGERERLQDLEERDAFAERVKQKDKDKTRNILERNDKKAYEEAQKRIKMAEEDKRKMLPELRKQSRRQYLSKREQEKLEDLEAEIKDEEYLFSTQNLTDRERKDLEYKRTIRDMAKEYKKAGAKEQEERKNRYYMPEEKRNKSIPQKDMDLEFEETPREGGGEQGRWEEARVATATLQFGARQERERRIKEEQERYQLILEEEEMITFVSTAITMKGTLSEKESEPELSQAEKQKQSIQEVRRSLPIFPYREDLLAAIGDHQILVIEGETGSGKTTQIPQYLLEEGYTKGGMKIGCTQPRRVAAMSVAARVAQEMSVKLGNEVGYSIRFEDCTSERTILKYMTDGMLLREFLTEPDLASYSVIIIDEAHERTLHTDILFGLIKDIARFRPDLKVLVASATLDTERFSSFFDDAPVFRIPGRRFPVDIYYTKAPEADYLEACVVSVLQIHVTQSPGDVLVFLTGQEEIEACCELLQERCRRLGSKISELLVLPIYANLPSDMQAKIFNPTPPGARKVVVATNIAETSLTIDGIIYVIDPGFCKQKSYNAKTGMESLIVTPCSRASANQRAGRAGRVAAGKCFRLYTAWAFKHEMEETTVPEIQRTNLGNVVLLLKSLGINDLIHFDFMDPPPHETLVLALEQLYALGALNHLGELTKLGRRMAELPVDPMLSKMILASEQYKCSEEVLTIAAMLSVNNSIFYRPKDKVVHADNARMNFVVPGGDHLVLLNVYTQWVESGYSTQWCFENFIQFRSMKRARDVRDQLEGLMDRIEVELCSSNGDSMPIRKAVTAGYFYHTARLSKGGYKTVKHQQTVYVHPNSSLFEEQPRWMIYHELVFTTKEFMRQVIEIESGWLLEVAPHYYKNKELEDSSSKKMPRKQGKAREELG
Protein: PH-sensitive chloride channel 1, isoform F (Q2PDY9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCVFEAAKEQPHKPRSRQLRRNQCRGKAEKAAAGTRGKVAVRGNNDKPAEDIKIKDNYQQNHKTQTETQTEVAAVVAIATDAGAETETETEAEAQKEPATGPEHLKAAAQVLLTIRQARQENNKHSSSQVAETHKDEGEDALARQGSIVDTAAGRIGIDIAATTIQVAERHEDGQHWQQHNVRRRRRQPDPAAHPASITKLSAISLHFHALAALAKTLQKHEDLSPVQDRQPLAYRAWQEHPYAETQMPATMSAAIIANVGATAAATSAAAFQYLGQHYKHYSQSISFYAASSVLLMLCYLTTASTAAATQSETGALDKHPIHGIDWSKFDESSSDKEILDLLLEKKRYDKRLLPPVNDEDFCCGLQSPDMATNQNARRPHNRGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLRVDLIFTRDRAFYFTTVFIPGIILVTSSFITFWLEWNAVPARSMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQRLPAVLSRIGVILASPLPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS