wanglab/gogpt-training-data huggingface dataset:
Protein: Histone-lysine N-methyltransferase SMYD3 (EC 2.1.1.354) (SET and MYND domain-containing protein 3) (Zinc finger MYND domain-containing protein 1) (Q9CWR2)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H7B4}. Nucleus {ECO:0000250|UniProtKB:Q9H7B4}. Note=Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M. {ECO:0000250|UniProtKB:Q9H7B4}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 2
- Estrogen receptor
- Probable helicase with zinc finger domain
- Cellular tumor antigen p53
- Histone H3.1
- Histone H3.2
- Histone-lysine N-methyltransferase SETD1B
- Inactive histone-lysine N-methyltransferase 2E
- Histone-lysine N-methyltransferase SETD1A
- Actin-histidine N-methyltransferase
Sequence:
MEALKVEKFTTANRGNGLRAVAPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLMRCSQCRIAKYCSAKCQKKAWPDHRRECSCLKSCKPRYPPDSVRLLGRVIVKLMDEKPSESEKLYSFYDLESNISKLTEDKKEGLRQLAMTFQHFMREEIQDASQLPPSFDLFEAFAKVICNSFTICNAEMQEVGVGLYPSMSLLNHSCDPNCSIVFNGPHLLLRAVREIEAGEELTICYLDMLMTSEERRKQLRDQYCFECDCIRCQTQDKDADMLTGDEQIWKEVQESLKKIEELKAHWKWEQVLALCQAIINSNSNRLPDINIYQLKVLDCAMDACINLGMLEEALFYAMRTMEPYRIFFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMKVTHGREHSLIEDLILLLEECDANIRAS
Protein: Signal-induced proliferation-associated 1 (E9PSX8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- Ribosomal RNA processing 1B
Sequence:
MWAGGVGSPRRGMAPAPTDDLFARKLRQPARPPLTPHTFEPRPARGPLLRSGSDAGEVRPPTPASPRARAHSHEDTSRPAATPTRLFTDPLALLGLPAEEPEPTFPPVLEPRWFAHYDVQSLLFDWAPRPRATGSHTESNSGTLALAEDQTTTSDLLLGAPGFVSELGGEGELGLGGPISPPVPPALPNASVSVLEEPQTRTTAYSLEHADLGAGYYRKYFYGKEHQNFFGLDEALGPVAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPRLSPTCLRLGSASPKVPRTLLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGAAFMQFLTLLGDVVRLKGFENYRAQLDTKTDSTGTHSLYTTYQDHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHAPCTPHTSYRVAVSRTQDTPAFGPALPEGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSLGGRRRATPRSPGAELQAAGALMWGVRAAPGARVSAGAETGGPDHAEVPCLLGISAETLVLVTPRDGRVVFNCACRDVLAWTFSDHQLDLYHGRGEAITLRLDGAPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFITHVERFTFAETTGLRPGARLLRVCGQTLPKLGPEAAAQMLRSASKVCVTVLPPDESGRPRRSFSELYTLSLKEPSRRAAPEPEQDETEKLVTLPAAKQLLHFCLKDGGSPPGPGDLTEERTEFLHSHNSLSPRSSMSDEAPVLPNTTPDLLLVTAVTTLAPGTDRETPPSQDQSGSSSSHEDTSDSAPELRASILPRTLSLRNSISKIMSEAGSETLEDEWQSISEIASTCNTILESLSREGQPILESGDPKETSKCNSEPEPGSLSEKVSHLESMLRKLQEDLQREKADRAALEEEVRSLRHNNQRLLAESESAATRLLLASKQLGSPTTDLA
Protein: Probable cytochrome P450 6a17 (EC 1.14.-.-) (CYPVIA17) (Q9V770)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- NADPH--cytochrome P450 reductase
Sequence:
MLLLALIVVILSLLVFAARRRHGYWQRRGIPHDEVHPLFGNIKDWPNKRHIAEIFRDYYFKYKNSDYPFAGFFFFFTRTAVVTDMELLKRVLIKDFNHFENRGVFYNEIDDPLSATLFSIEGQKWRHLRHKLTPTFTSGKMKNMFPIVVKVGEEMDKVFRSKTAADRGQVLEVVDLVARYTADVIGNCAFGLNCNSLYDPKAEFVSIGKRAITEHRYGNMLDIFLFGFPKLSRRLRLKLNIQEAEDFYTKIVRETIDYRLRTKEKRNDFMDSLIEMYKNEQSGNSEDGLTFNELLAQAFIFFVAGFETSSTTMGFALYELARNQDVQDKLREEIGNVFGKHNKEFTYEGIKEMKYLEQVVMETLRKYPVLAHLTRMTDTDFSPEDPKYFIAKGTIVVIPALGIHYDPDIYPEPEIFKPERFTDEEIAARPSCTWLPFGEGPRNCIGLRFGMMQTCVGLAYLIRGYKFSVSPETQIPMKIVVKNILISAENGIHLKVEKLAK
Protein: Uncharacterized protein YLR177W (Q06251)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein PDC2
Sequence:
MELPSINSTTSISDNQELRNYYDKLLFKNNSGKSLADLPGKMADFNDNSAAAHPRSRVDFINGYIGFREDKQSLLGQKNTKRASFSAFADEGRKQSEMSINGKSPNLSLFSFEFNGTPTQDRKPYKQDYLNVMNTSPNNILSPLNNSSQKYYPQKQQQQQQQQQQQQQQSIFDPGRRSSYISDALIHGNAATQQPQYSQPVYINNNPSLQVPYTAPSEYTQQQQYSSPFNARRNTQPVLNLHPAAAPTNDAGLAVVDGKNLTSSKELHDLYLDCGSNYFASDKVYKFIDSIKGTLRGDNVSASSSRIIEFLDFLKNCNLNYNPQSDAFISTAVSNASSTGAAKSKNSTSMHLHYKPLVLVSLKNGKLELLSKPQTATLILKRGDLVIIDGDRGKDLVLVVEPVVDINLALFINFLKKKIHFDSLITNSQQHFPNDQFIKTLVDTTNGKPVAHELNPKLYDIIELTQLIIPSKQVLRFATPWESSTNLHNKFQDELKALHIAQLKLRSLNNNNSGGGLNIKILNAEFQFDRKKLTFYYICQERNDFRDLIKELFKFYKTRIWLCAIPNNLSIDSKFYDSNKFEWEMYQDMMSHYSMDNTGIVVAPELNRLKLDDFQIGVYMELVKVLFG
Protein: Arogenate dehydratase 1 (PhADT1) (EC 4.2.1.91) (D3U715)
Organism: Petunia hybrida (Petunia)
Function: Converts L-arogenate produced from the shikimate-chorismate pathway into phenylalanine (Phe). Involved in floral volatile benzenoids and phenylpropanoids (FVBP) production.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:20215586}.
Interaction partners:
Sequence:
MQSLTPSSGVNLKSIIRKTSLPPGQTRFITGRVIKCGYQVDSANTVNTAGAPASYNSGHVGASRADWQSSCAILASKVVSQQPDTEKTGGAGNITAVNGHKTLDLVSIDNLPKALTITDLSPAPMHGSTLRVAYQGVPGAYSEAAAGKAYPNCEAIPCDQFEVAFQAVELWIADRAVLPVENSLGGSIHRNYDLLLRHRLHIVGEVQLPVHHCLLALPGVRKEYLTRVISHPQALAQCELTITKLGLNVAREAVDDTAGAAEYIAANNLRDTAAVASARAAELYGLQILAEGIQDDSSNVTRFVMLAREPIIPRMDRPFKTSIVFAHEGTGVLFKVLSAFAFRNISLTKIESRPHRNRPIRLVDDANVGTAKHFEYMFYVDFDASMADVRAQNALAEVQEFTSFLRVLGSYPMDMTPCCPSRDE
Protein: Methyltransferase like 17 (G3V3X6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MENQVQTLTSYLWSRHLPVEPEELQRRARHLEKKFLENPDLSQTEEKLRGAVLHALRKTTYHWQELSYTEGLSLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQSLREYMCVDRSAA
Protein: Peroxisomal membrane protein PEX13 (Peroxin-13) (Q92266)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P80667}; Single-pass membrane protein {ECO:0000250|UniProtKB:P80667}.
Interaction partners:
Sequence:
MSDSSAPDLPSKPSSLNAGQSSSLQTTNTGIGMGSGMGSGMGMGTYGNSYGSSYGGGYGSSMYGSGGYGMGGYGSSMYGGSRYGMGSYGMGGYGMGGYGMGMNTGMNGMGMAGSLAQGSEATFQLIESIIGAVGGFAQVLEATYMATHSSFFTMISMADQLSHLKTALGSMLGIYTVINWLKRIMGKLMGVKNKLTPDEFRKFQEKQMKKLSNSNNTGGPNKNTNKLSLKPLLLFLAAVVGFPYLLKKLIAHLAETSQMNGNFITSGGSLQGNLDPTKLEFARALYDFNPENEEMELKLARGELMAILSKTEPNSNQESTWWKCRSRDGKVGFVPYNYVEIIERHQRPVPEAQEEPAAAVLAERQQQPIIDSTEFQKMKT
Protein: Ras-related protein RABA1g (AtRABA1g) (Q9LK99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Syntaxin-32
- Kinesin-like protein KIN-14E
- Vesicle transport v-SNARE 12
- Membrin-12
- Geranylgeranyl transferase type-2 subunit beta 1
- Probable phospholipid-transporting ATPase 5
Sequence:
MAAYRADDDYDFLYKVVLIGDSGVGKSNLLSRFTRNEFSLESKSTIGVEFATRSIHVDEKIVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDVTRHVTFENVERWLKELRDHTEANIVIMLVGNKADLRHLRAVSTEDAKAFAERENTFFMETSALEALNVENAFTEVLSQIYRVASKKALDIGDDHTTLPKGQSINVGSKDDVSEVKKVGCCSS
Protein: Dehydration-responsive element-binding protein 2B (Protein DREB2B) (O82133)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates high salinity- and dehydration-inducible transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Low-temperature-induced 78 kDa protein
- Low-temperature-induced 65 kDa protein
- Histone H4
- FACT complex subunit SSRP1
- BURP domain protein RD22
- Floral homeotic protein APETALA 2
- Heat stress transcription factor A-3
Sequence:
MAVYEQTGTEQPKKRKSRARAGGLTVADRLKKWKEYNEIVEASAVKEGEKPKRKVPAKGSKKGCMKGKGGPDNSHCSFRGVRQRIWGKWVAEIREPKIGTRLWLGTFPTAEKAASAYDEAATAMYGSLARLNFPQSVGSEFTSTSSQSEVCTVENKAVVCGDVCVKHEDTDCESNPFSQILDVREESCGTRPDSCTVGHQDMNSSLNYDLLLEFEQQYWGQVLQEKEKPKQEEEEIQQQQQEQQQQQLQPDLLTVADYGWPWSNDIVNDQTSWDPNECFDINELLGDLNEPGPHQSQDQNHVNSGSYDLHPLHLEPHDGHEFNGLSSLDI
Protein: Heat shock factor-binding protein 1 (Q8IIF8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNFNEMLKSNENNIRSDKFNNYCTSFNNSAMSLNSTKQNNISLLNNNNNNINVKVEPKAGEELEIYVENMLNELKTKMQSLSDNLLNKVDNMEKYLDELENTMMNYTTQNNLQ
Protein: Nuclear receptor subfamily 0 group B member 1 (DSS-AHC critical region on the X chromosome protein 1) (Nuclear receptor DAX-1) (P51843)
Organism: Homo sapiens (Human)
Function: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16709599}. Cytoplasm {ECO:0000269|PubMed:16709599}. Note=Shuttles between the cytoplasm and nucleus. Homodimers exits in the cytoplasm and in the nucleus. {ECO:0000269|PubMed:16709599}.
Interaction partners:
- Steroidogenic factor 1
- Nuclear receptor subfamily 5 group A member 2
- Homeobox protein NANOG
- Wilms tumor protein
- Sal-like protein 4
- Sex-determining region Y protein
- Steroidogenic acute regulatory protein, mitochondrial
- Transcription factor SOX-9
- Androgen receptor
- Steroid hormone receptor ERR2
Sequence:
MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI
Protein: Tia1 cytotoxic granule-associated RNA binding protein-like 1 (A0A8I6GIU6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMEDDGQPRTLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGGRQIRTNWATRKPPAPKSTQETNTKQLRFEDVVNQSSPKNCTVYCGGIASGLTDQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYWGKESPDMTKNFQQVDYSQWGQWSQVYGNPQQYGQYMANGWQVPPYGVYGQPWNQQGFGVDQSPSAAWMGGFGAQPPQGQAPPPVIPPPNQAGYGMASFPTQ
Protein: BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (NIP3-like protein X) (NIP3L) (Q9Z2F7)
Organism: Mus musculus (Mouse)
Function: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). May function as a tumor suppressor (By similarity).
Subcellular location: Nucleus envelope {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane. {ECO:0000250}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Microtubule-associated protein 1 light chain 3 beta
- Apoptosis regulator Bcl-2
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor-associated protein-like 1
- FUN14 domain-containing protein 1
- Metalloreductase STEAP3
- GTP-binding protein Rheb
- Bcl-2-like protein 1
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
Sequence:
MSHLVEPPPPLHNNNNNCEEGEQPLPPPAGLNSSWVELPMNSSNGNENGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
Protein: Protein kinase domain-containing protein ppk2 (Q10447)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Located at the cell tip.
Interaction partners:
- Probable Rho-type GTPase-activating protein 3
- Cell division control protein 42 homolog
- RbAp48-related WD40 repeat-containing protein prw1
- Serine/threonine-protein kinase ppk1
- Probable Rho-type GTPase-activating protein 4
Sequence:
MLSNSTFHEHHAKSHFHNNACQSNASSSACRASEDHLVSSFPNDSIIDLQPSRPAPEPPKKKFGYYARRLSGHFLSLIHGSGNSTRSPPFHLQNQKSNGQSEVWHSSDDSGSPKRLNRSRSSKEDMYRRRSLHGLPSLSRRNSKKSSTLSRSISLHLRSESAPISLPIHLYKSYSYNHSPSSLPTVLNSQALSSPPVPTTPDEVSTNRLSSSTSSMNCRNLVPDNFNISIRPNTTNYRSSIQENSNGNRDSISPSAYDAPLLHNVDTQSIDGFVSVASHFSSASTAESLDDGHSATTIQQGDVSSYPLSRSVSTPVPMSPISISPAKPSPQSPKLSQSAVGHPSSSIPAAAMHKVSYSDDLMRFVAREKYYLQIVDCLCTQKDPLFFYTDFTKICQQDTVGTYVARQTLDKEVVVIKRFDISAVTHRRLLLEELQRLSGLSHKNLIRYNESFWYLNNIWSVFEYKDPSTKLSALIPKYFFSELNIASICYEISSGLAFLHNSGIAHHNLTTECIYLTKSSCLKIGNYAFSSPYIERQTNRGAVSHVPDWLIEKNYKEGFMKDVKSLGLVALEIFQGQPNFFRKSIQSIQLTPNANVLVNRVRGLISQEFKEFLLQTLQAETLQGPNINMLLETSSFLEKRQTLNFEICLNNLNLRERKASRYSYL
Protein: N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) (CMP-N-acetylneuraminic acid synthase) (CMP-NeuNAc synthase) (Q90WG6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid.
Subcellular location: Nucleus {ECO:0000305|PubMed:11479279}.
Interaction partners:
Sequence:
MAAAKKRTQSDIEDVRDRKAKVIKDSGEKRHIAALILARGGSKGIPLKNIKVLAGVPLIGWVLRAAVDSKQFDSVWVSTDHDDIEKVAKTWGAQVHRRSPEVSKDSSSSLDTIQEFARLNPEVDVICHIQATSPCLHPFHLKEALEMITKQGFTSVFSVVRRHHFRWQEVKKGGSVATQPLNLDPCNRPRRQDWDGELCENGSFYIYTRATIERGLQGGKWAYYEMLPEYSVDIDVDIDWPVAEQRVLRFGYFGLDKPEVVRLLLCNVSGCLTDGRVLISVSGEEMVSVNTRDTMGIRMLQREGVEVILISSSEDLLTKALADNLSQRTGCEVRQLGKDIQGEVIAMMDDKDLDWKEVAYMGNDAPDVDCLNLAGLSAVPRDAPVVAINAAKYSCHSAAGLGAVREFSEHILLLKKKAKSQMEQDRIHRNTF
Protein: Uncharacterized protein (Q57XV9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSINFSAPYLVTEMEEKVVTSLPSGDTASGSGESTASPPIVISAAVPYTEEEKKLLTEQLRRHQRQQSQGDDDSSWNETTLPFISSMVEKVLQLAAQNRESDSTKDSGSGDENKPQEKANATDDVAGADAVSKVDTFVEDNDYVLEQLRLQPWPFFTLPRLCEILADPYKYNSIGDKLRGEKLQSAIRRCVLVSAPLNCDVRNNSS
Protein: Fructose-bisphosphate aldolase 1, chloroplastic (AtFBA1) (EC 4.1.2.13) (Q9SJU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in glycolysis and gluconeogenesis.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379}. Plastid, chloroplast stroma {ECO:0000269|PubMed:16414959}.
Interaction partners:
- Sedoheptulose-1,7-bisphosphatase, chloroplastic
- Triosephosphate isomerase, chloroplastic
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Triosephosphate isomerase, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic
- Fructose-1,6-bisphosphatase 1, chloroplastic
- Phosphoglycerate kinase 1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
- Glucose-6-phosphate isomerase 1, chloroplastic
Sequence:
MASSTATMLKASPVKSDWVKGQSLLLRQPSSVSAIRSHVAPSALTVRAASAYADELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPGLGQYISGAILFEETLYQSTTDGKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPNGPSALAVKEAAWGLARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAPNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKANSLAQLGKYTGEGESEEAKEGMFVKGYTY
Protein: Large ribosomal subunit protein eL14y (60S ribosomal protein L14-2) (Q9T043)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL27x
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein eL15z
- Large ribosomal subunit protein eL13z
- Small ribosomal subunit protein eS7z
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL22y
- Small ribosomal subunit protein uS12y
Sequence:
MGFKRYVEIGRVALVNYGEDHGKLVVIVDVVDQNRALVDAPDMERIQMNFKRLSLTDIVIDINRVPKKKALIEAMEKADVKNKWEKSSWGRKLIVQKRRANLNDFDRFKIMLAKIKKAGVVRQELAKLKKEITA
Protein: DNA damage-regulated autophagy modulator protein 1 (Damage-regulated autophagy modulator) (Q8N682)
Organism: Homo sapiens (Human)
Function: Lysosomal modulator of autophagy that plays a central role in p53/TP53-mediated apoptosis. Not involved in p73/TP73-mediated autophagy.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:16839881}; Multi-pass membrane protein {ECO:0000269|PubMed:16839881}.
Interaction partners:
- Cellular tumor antigen p53
Sequence:
MLCFLRGMAFVPFLLVTWSSAAFIISYVVAVLSGHVNPFLPYISDTGTTPPESGIFGFMINFSAFLGAATMYTRYKIVQKQNQTCYFSTPVFNLVSLVLGLVGCFGMGIVANFQELAVPVVHDGGALLAFVCGVVYTLLQSIISYKSCPQWNSLSTCHIRMVISAVSCAAVIPMIVCASLISITKLEWNPREKDYVYHVVSAICEWTVAFGFIFYFLTFIQDFQSVTLRISTEINGDI
Protein: Protein tipE (Temperature-induced paralytic E) (P48613)
Organism: Drosophila melanogaster (Fruit fly)
Function: Enhances para sodium channel function. Required during pupal development to rescue adult paralysis and also protects adult flies against heat-induced lethality.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- IP11896p
- RT03134p
- Sodium channel protein para
- Anoctamin
Sequence:
MGDEQDKRTGKEKLLFYTTAFFILLGTFSLFAFLFLVPFVIEPAFTTIFMQFEEVPALCETYDTEIYYGAKNCSWSSCREGCTKDIYTCTQIRVNYRLNLYNFTDEFNFTEYHINLKEAERILPPVKRTDRYERALRSDYEYDNLGGGTGLDIDLGAGRMEQLNFGDADGSNGYLIEDSEDTRGLSASGTLISDERRPFDEISELNEGLMGNRSMYYYVGARLFPNVKGCGYPPMLNCTIWLKRYTKIGMKFPCYYSKVDPSLVISDLDYWQNTLNLVYSMAIPIPSFIISVIYLTYAYFKIYNEDEETAPLDKNAEDMDIDDIDAVDDSDGAVLADNVAGSQIINMDSTTNDSCLEGVLPNGGPGMTASISQGGSVTTPGPYIAQSPAGSQMTPNSEINSFGHQLKVQMADELSRDSLENGAISTSNSVQGNLSKTMTTSISTPPGPTAAV
Protein: Prefoldin subunit 2 (Gene involved in microtubule biogenesis 4) (Q9LJ98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8. Required for microtubules (MTs) organization and dynamicity (By similarity). Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P57742}. Nucleus {ECO:0000250|UniProtKB:P57742}. Note=In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (By similarity). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (By similarity). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity). {ECO:0000250|UniProtKB:P57742}.
Interaction partners:
- Prefoldin subunit 4
- Prefoldin subunit 1
- Prefoldin subunit 6
- Prefoldin subunit 3
- Prefoldin subunit 5
- Prefoldin chaperone subunit family protein
- Prefoldin chaperone subunit family protein
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- Peptidyl-prolyl cis-trans isomerase CYP18-1
Sequence:
MASKSGSGGLREPPNEQAVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKLYETLEKKKKDLTEFEAKYKIRITKQEDNKEGGNKKEGNAQGVLVGAASSSQ
Protein: B3 domain-containing protein Os04g0676600 (Protein IDEF1 homolog) (Q7XKC5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription regulator that binds specifically to the DNA sequence 5'-CATGC-3' of the IDE1 element found in the promoter of the barley iron deficiency-inducible gene IDS2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
Sequence:
MADTRGSTSSGGGDDRGREGHDDFTGGGQYNRYHRILEAVPSPLVRRENGVHHQYPTGLIHHPSSTMPVAPCSYVPRYTMVPTSAMLPLQHHHRQLQISQENFQDRVPSNNVAAPHLPSNFQDLRPMCNGPPFMSYGQTASNRNVLYQNLTPYSFNAWASNNMPRNPVYTSYHPTAIEDPHATPFHINNHDTDQGFFTVSTSFRVDQSFVHAPSPFPPVSSSSRSFSSAQISNGPIDAKKAKKSDIKDQPIVLRRSDTESEKNDELDQTPASEPSSMSHNSANSTIRFNCREYRVILRKELTNSDVGNIGRIVMPKRDAEAHLPALHQREGVMLKMDDFKLETTWNFKYRFWPNNKSRMYVLESTGGFVKQHGLQTGDIFIIYKSSESEKLVVRGEKAIKPNVIMPIVDCSCKNDLNNSEECGFAISLLTKKT
Protein: Taste receptor type 2 member 7 (T2R7) (Taste receptor type 2 member 130) (Taste receptor type 2 member 6) (T2R6) (Q9JKE9)
Organism: Rattus norvegicus (Rat)
Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MTYETDTTLMFVAVCEALVGILGNAFIALVNFMGWMKNRKITAIDLILSSLAMSRICLQCIILLDCIILVQYPDTYNRGKEMRIIDFFWTLTNHLSVWFATCLSIFYFFKIANFFHPLFLWIKWRIDKLILRTLLACLILSLCFSLPVTENLTDDFRRCVKTKERINSTLRCKLNKAGYASVKVNLNLVMLFPFSVSLVSFLLLILSLWRHTRQMQLNVTGYNDPSTTAHVKATKAVISFLVLFIVYCLAFLIATSSYFMPESELAVIWGELIALIYPSSHSFILILGNSKLKQASVRVLCRVKTMLKGRKY
Protein: TATA box-binding protein (TBP)-associated factor, RNA polymerase I, A (TATA box-binding protein-associated factor RNA polymerase I subunit A isoform X1) (Q5SP02)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- TATA box-binding protein-associated factor RNA polymerase I subunit B
- RNA polymerase I-specific transcription initiation factor RRN3
- TATA-box-binding protein
- Wu:fj64h06.
- Ras-related GTP-binding Ca.
- DNA-directed RNA polymerase I subunit RPA49
- Transcription initiation factor TFIID subunit 12
- Polymerase
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA2
Sequence:
MDDIEAELNIAETHADFTQDESEHRQRLKRPVQLHCQVKDRGFFTGIYFLKCNRKCLELLREAMLHHRWQEAVGYFSSYIQTLEAKTYNSYQSVVAEILWRLGTEILHHLPNTSNEDFNALYEQLKNVGVLNFSKISLEHCYHLLLNGQMDEAKRQLSIAESWRYGRVSRSQSLSKTLITAYCGLLDYLIWNEKKSSVSENEELSSNHEMHSYFRQASVTLKDIISLPGIWDPFVLSYVNMLEFYKQEESALQALENYAYNKEFPSNPNAHVYLYQFLKRHDAPREKLISTLRILHSLVPSHELMLELCNLLLDTLERSDTEEALAVCMDLLEFSSWKTDIRAWDCLLTCLKKIRKKKWQEIIQKEWKVRRSLWVPLHFRDFLSLKDWMDNHKLMMIIKKDCLRIINENMREYCRVAAIAEKEVLLQIRMKRKKKQHKIQTAITELTN