wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydropyrimidine dehydrogenase (NADP(+)), chloroplastic (DHPDH) (DPD) (EC 1.3.1.2) (Dihydroorotate dehydrogenase-like protein) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (Protein PYRIMIDINE 1) (Q9LVI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate and the reduction of thymine to 5,6-dihydrothymine (DHT). Involved in the recycling of nitrogen from nucleobases to general nitrogen metabolism.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19413687, ECO:0000269|PubMed:21865177}.
Interaction partners:
- Dihydropyrimidinase
- Beta-ureidopropionase
- Uridine 5'-monophosphate synthase
- Uridine nucleosidase 1
- Uracil phosphoribosyltransferase, chloroplastic
- Aspartate carbamoyltransferase, chloroplastic
- Dihydroorotase, mitochondrial
- Allantoinase
- Nitrate reductase 2
- Nitrate reductase 1
Sequence:
MASMSFALNRFSGLSSKTTLSADFDPSSRRSFLPPTRVGLKISSAAESEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKVINVTPRYARLRTGSNGSAKTDVIGWQNIELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAAVGQDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGGYSYKAVRPIALAKVMNIAKMMKSEFSEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQHNFSTIEEFRGHSLQYFTTHTDLVKRQKEAVEQRKAEKRGLKSDKDWTGDGFVKETESMVSN
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (H0YNW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGGAAPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
Protein: Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (Amplified in breast cancer-1 protein homolog) (AIB-1) (CBP-interacting protein) (p/CIP) (pCIP) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (ACTR) (TRAM-1) (O09000)
Organism: Mus musculus (Mouse)
Function: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Estrogen receptor
- Nuclear receptor coactivator 2
- Histone-arginine methyltransferase CARM1
- Nuclear receptor coactivator 1
- Histone acetyltransferase p300
- Estrogen receptor beta
- Mediator of RNA polymerase II transcription subunit 1
- ETS translocation variant 4
- Progesterone receptor
Sequence:
MSGLGESSLDPLAAESRKRKLPCDAPGQGLVYSGEKWRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISSDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYSILHEPRRKDFLNTYQNPQLMEFLGLMRTRDKKAPYILIVRMLMKTHDILEDVNASPETRQRYETMQCFALSQPRAMLEEGEDLQCCMICVARRVTAPFPSSPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYVHGHAETPVYRFSLADGTIVSAQTKSKLFRNPVTNDRHGFISTHFLQREQNGYRPNPIPQDKGIRPPAAGCGVSMSPNQNVQMMGSRTYGVPDPSNTGQMGGARYGASSSVASLTPGQSLQSPSSYQNSSYGLSMSSPPHGSPGLGPNQQNIMISPRNRGSPKMASHQFSPAAGAHSPMGPSGNTGSHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNISQPSKVSGQDSKSPLGLYCEQNPVESSVCQSNSRDPQVKKESKESSGEVSETPRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDPNCKDSSVSVTSPSGVSSSTSGTVSSTSNVHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSTASCGEGTTRQEQLSPKKKENNALLRYLLDRDDPSDVLAKELQPQADSGDSKLSQCSCSTNPSSGQEKDPKIKTETNDEVSGDLDNLDAILGDLTSSDFYNNPTNGGHPGAKQQMFAGPSSLGLRSPQPVQSVRPPYNRAVSLDSPVSVGSGPPVKNVSAFPGLPKQPILAGNPRMMDSQENYGANMGPNRNVPVNPTSSPGDWGLANSRASRMEPLASSPLGRTGADYSATLPRPAMGGSVPTLPLRSNRLPGARPSLQQQQQQQQQQQQQQQQQQQQQQQMLQMRTGEIPMGMGVNPYSPAVQSNQPGSWPEGMLSMEQGPHGSQNRPLLRNSLDDLLGPPSNAEGQSDERALLDQLHTFLSNTDATGLEEIDRALGIPELVNQGQALESKQDVFQGQEAAVMMDQKAALYGQTYPAQGPPLQGGFNLQGQSPSFNSMMGQISQQGSFPLQGMHPRAGLVRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALEMKMENPAGTAVMRPMMPQAFFNAQMAAQQKRELMSHHLQQQRMAMMMSQPQPQAFSPPPNVTASPSMDGVLAGSAMPQAPPQQFPYPANYGMGQPPEPAFGRGSSPPSAMMSSRMGPSQNAMVQHPQPTPMYQPSDMKGWPSGNLARNGSFPQQQFAPQGNPAAYNMVHMNSSGGHLGQMAMTPMPMSGMPMGPDQKYC
Protein: Chloride intracellular channel protein 3 (Glutaredoxin-like oxidoreductase CLIC3) (EC 1.8.-.-) (O95833)
Organism: Homo sapiens (Human)
Function: Can insert into membranes and form chloride ion channels. May participate in cellular growth control.
Subcellular location: Nucleus. Membrane; Single-pass membrane protein. Cell membrane {ECO:0000269|PubMed:32066374}; Single-pass membrane protein. Cytoplasm. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:28198360}. Note=Predominantly nuclear. Some protein was found in the cytoplasm. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). Secreted into the extracellular matrix by activated fibroblasts. {ECO:0000250, ECO:0000269|PubMed:28198360}.
Interaction partners:
- Mitogen-activated protein kinase 15
Sequence:
MAETKLQLFVKASEDGESVGHCPSCQRLFMVLLLKGVPFTLTTVDTRRSPDVLKDFAPGSQLPILLYDSDAKTDTLQIEDFLEETLGPPDFPSLAPRYRESNTAGNDVFHKFSAFIKNPVPAQDEALYQQLLRALARLDSYLRAPLEHELAGEPQLRESRRRFLDGDRLTLADCSLLPKLHIVDTVCAHFRQAPIPAELRGVRRYLDSAMQEKEFKYTCPHSAEILAAYRPAVHPR
Protein: ADAM metallopeptidase domain 28 (E9PTQ3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQQWRLLVVWFLLSPVPASAIKELPKAKNYEVVYPIRLHLLHKRETKEPEPKETFETELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYYQGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAHALFKDDPKEDQENSNCGVDDALWLQGLHQDVVLPATRLIKLNDGMVQEPKKYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGNDLLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSPLPSDIISTPVCGNQLLEMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRFRVNGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQNEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSGDLPWKGLTIAFLTCKLFDPEDINQGVDMVANGTKCGNNKVCINAECVDMEKTYKSANCSSKCKGHAVCDHELQCQCKEGWAPPDCEDSATVFHFSTVVGVFFPMAVIFVVIAIVIYHQSARRKQRRVQRLPPIKDAKLHRQKCRPQKKDVQPEMSQMKKLHVSDLPTEEQEPPPDVLITEPNFLPPPIPISLRGRAKAPFVKMSHRFSEQIGHTCLVY
Protein: Zinc finger protein pat-9 (Paralyzed arrest at two-fold pat-9) (Q22829)
Organism: Caenorhabditis elegans
Function: Probable transcription factor; required for proper organization of muscle myofilaments and for their recruitment to the M line.
Subcellular location: Nucleus {ECO:0000269|PubMed:22616817}. Chromosome {ECO:0000269|PubMed:22616817}.
Interaction partners:
- F-box domain-containing protein
- Transposase domain-containing protein
- Uncharacterized protein.
- REST corepressor rcor-1
Sequence:
MENRTPMQHHSGYEIVKSEPPSTPKTLIKSSYMENTPEMVFGSFPIHSGFCTQVVTHTDPMNNNNQPKTNANGRALAADRKRPYPCNLCSSKFGSKMELEEHQNSHTGQKPFECDTCNARFNRRSTLWNHKRIHSDAKPFVCTVCQMTFKWKNSLKCHKDMHQRKNETSAHLDNDLRQLTYATAAKRKLQMEQEENGGLPASSSASSVISHPLITTTSGNKKRSKAAKAKQTPSSLATTLSQVHLGAVQPLHASALVPPSDHQIDLDTTSLDSLMQSQNQNFLMQLYGYSDDGRHNGGMLSLDDTMLSNLSDSKSDSGSSSGGLSIQLPMQTINMLNFRNLGTQQLPPVHQLASSLPSVSSGMDYVNVNQHDSHYIVSQPDMMLGNQPLYHNGSFANIEKSNPHNNQFTIDSCVLLPSSRQDYPFDYTMVNQQYPMQEQVHDQTVGVSVVQQHYAEQAHAHGKTVPHEQW
Protein: Succinyl-CoA--L-malate CoA-transferase alpha subunit (EC 2.8.3.22) (Q1KLK1)
Organism: Chloroflexus aurantiacus
Function: Involved in the 3-hydroxypropionate cycle used for autotrophic carbon dioxide fixation. Catalyzes the transfer of CoA moiety from succinyl-CoA to L-malate to yield L-malyl-CoA. It is highly specific for succinyl-CoA as the CoA donor, however it can accept L-citramalate instead of L-malate as the CoA acceptor.
Interaction partners:
Sequence:
MPPTGEEPSGHAESKPPASDPMSTPGTGQEQLPLSGIRVIDVGNFLAGPYAASILGEFGAEVLKIEHPLGGDPMRRFGTATARHDATLAWLSEARNRKSVTIDLRQQEGVALFLKLVAKSDILIENFRPGTMEEWGLSWPVLQATNPGLIMLRVSGYGQTGPYRRRSGFAHIAHAFSGLSYLAGFPGETPVLPGTAPLGDYIASLFGAIGILIALRHKEQTGRGQLIDVGIYEAVFRILDEIAPAYGLFGKIREREGAGSFIAVPHGHFRSKDGKWVAIACTTDKMFERLAEAMERPELASPELYGDQRKRLAARDIVNQITIEWVGSLTRDEVMRRCLEKEVPVGPLNSIADMFNDEHFLARGNFACIEAEGIGEVVVPNVIPRLSETPGRVTNLGPPLGNATYEVLRELLDISAEEIKRLRSRKII
Protein: Perilipin (A0A8I5ZQJ5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MASVAVDPQPSVVTRVANLPLVSSTYDLVSSAYVSTKDQHPYLRSVCEMAEKGVRTVTSVAVTGALPIIQKLEPQIAVANTYACKGLDRMEARLPILNQPTSEIVANARGAVTGAKDVVTTTMAGAKDSVASTVSGVVDKTKGAVTGSVERTKSVVNGGIDTVLGMVQLMSSGVENAISKSELLVDQYLPLTQKELEMEAKKVEGFDMVQKQRYYERLESLSTKICTRAYHQALGRIKDAKQKGQETISQLHSTVHLIEFARKNVHSANQKIQDKLSVSWVEWKRIVGYDDTDESHCAEHIESHTLSMARNLTQQLHTTCQTLLFNVQGLPQNIQDQAKHLGVMAGDIYSAFRNVTSFKEVSDGVLTSSKGQLQKMKESLDEVMDYLVNNTPLNWLMLDFSAFDSTSDTDEVPDIIPLEED
Protein: GTPase-activating protein gyp3 (P87234)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates exocytosis by functioning as a GAP for ypt2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GTPase-activating protein gyp1
- ADP-ribosylation factor 6
- Uncharacterized protein C594.02c
- Uncharacterized membrane protein C18H10.18c
- Probable lipase C14C8.15
- Uncharacterized membrane protein C30D10.09c
- TBC domain-containing protein C23D3.03c
Sequence:
MAGITEHSTIMNDANFKEENAHLSDASIHFGSSEQDKTPSDYELDDVLDLYNDTTEDDADDADDVNNYIMSPSSSLSSESEHALDALVYPIYSHHNILEHENNSDYASITPSNHPAFTSCAYLQNPVVDSNNEYESKFRLSLEIPPTDFLSTSTELSKRESCLSTETSSSKFSAVTAATITNETQSEKRSSQTDPSLPFKTNSLNCDVTYEEGPLTKKLRGPKKYKPSHSSWDIYGFKKANQFYTVDQYNTWYGPYSRYLERREQRWKLFLQENGIDYIHQSPSIFPSRSAKTQRFIRKGIPPEYRGNAWFYYSGGYELLQRNPKLYETLWRCACIKKPSDSDLIERDLYRTFPDNVHFRHKSKHSRNSSDASEHSSEEPDVPMISKLRRVLMTFATYLPENGYCQSLNFLAGFFLLFMSEEKAFWMLVITCRKYLPKMHDANLEGANIDQSVLMASVRESLPAVWSRISLNFDGIPVNDIVAKLPPITLVTAAWFMSAFVGILPTETALRVWDCFFYEGSKVLFMTALCILRLGEDDIKSKSEQTEVFQVIQDLPKSLLDANAFLSLCFRRNFRRTPSQKDIERRREKVAKKRNSSASKLEMSDSSKHHLSRSSSRFSKSHIISQLHNHLKKST
Protein: Protein EARLY FLOWERING 5 (PtELF5) (G3CHK5)
Organism: Poncirus trifoliata (Hardy orange) (Citrus trifoliata)
Function: Involved in the regulation of flowering time (By similarity). Plays an important role during the early flowering of precocious trifoliate orange.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
Sequence:
MKTTKGGKVMNPTDAYRKELRKKELKRNKKERKKVREVGILKKDPEQIREQIEKLEMMKADGALDKARKHKKRQLEDTLNLVLKKRKELQEKMKEKGETPVMFSHLGPPRRRTAEEEERAKHPKPEDSAYYHPTLNPTGAPPPGKPPMYLSSIGPRIPLSSDEASSSKTESDDVALPVPPPPPPLPDSGRLGSGDGSVIPASLPLPPPPPPPKPPTSAGANLGMSLPPPPLPPPPPGPPPKDLVAGQPPLPPSQPLQQSVQPPPPGMSGSEREGSLSALSDDSIFKASAQVPSTLPPPPPPPGMPQKSPNTESGGTASEADGNNLSTTTDLPKMVPPPPPPRQQPTVPGPGLMPSVPADVLPPGLSSFPPPPPPPPLDMRPPLSAPGIPGGANHPGMMVPLVPRPPYGPPPMMRPPLPPGPPPTLQEGEYAANRPTVPQKPSYVKSAAPTVVKRPLAQHTPELTAMVPASVRVRRETALPKAKPKPSVSTTVTTIQPATAPVVRQESIACSAAPKSQGKSIDDSYMAFLEDMKALGALDS
Protein: Uncharacterized mitochondrial carrier C227.03c (Q9UTD6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVDDSLKDAIAGGAAGLASSLVVAPLDVVKTRKQAQKAFYSTGGGKNTMVLGGTLSSMRTIFHNEGIAGLYRGVGPMMLGYLPSWSIYFVVYEKCKVLFGVNKKYTSLHEIDSSKVGIKASLDSSDKQFYRYWGGQIFSAVIAGAASVTLTNPIWVVKTRLVTQSHPRASSFVDKIAAATTVQFRNLQTDAPSVKWRMPRFWLKRRTNVKSSPSQHPVNPPTGPACSPAYNNTFDAFRKIYKYEGLAAFYRGLFPSLFGTLHVGIQFPLYEYFKSFLDDFFGKKSNFHIVLAATLSKIAASTVTYPHEVLRTRLQSLDAPTHNSATLLIRDIWRSEGWRKYYSGMATNFIRTIPASSVTFLSFEIVRKWLN
Protein: Ferrochelatase (O25172)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Methionine--tRNA ligase
- tRNA U34 carboxymethyltransferase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Thioesterase domain-containing protein
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Type 1 capsular polysaccharide biosynthesis protein J
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
Sequence:
MRLGVNEAVELSLGELQNTPSISYFNSIVLSLNKVQKGSLFVAKDHTLIPKALELGAYGILYTGEYPVSDRDVAWIKLKDIEHSLNHLFKFCLLNERVVGALLSPIELEIASKIMVSNFVWCLKESLEDLFIIEGCKIAFFDKLEWLHLFYKQEHLKEDLKESCLIILNQSFFCSALVYEKQEYEFKMPCIFLGSLKRVIQLCEKLQIEFDLNLLGKKEYPLDHCKPFFVNKNLEIAPYGTTARVIVAETSKELFEMMLQKAFEILSWGKIVVFCRKNSAAFFKKTNPYFYTTQNNLKEQLKNLAFNFAFIHGISSHHLESLLNPPFFKKTPTLW
Protein: Aquaporin-12 (AQP-12) (Q8CHJ2)
Organism: Mus musculus (Mouse)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lens fiber major intrinsic protein
- Aquaporin-8
- Aquaporin-7
- Aquaporin-3
- Aquaporin-5
- Aquaporin-4
- Aquaporin-2
- Aquaporin-1
- Aquaporin-6
- Aquaporin-9
Sequence:
MASLNVSLCFFFATCAICEVARRASKALLPAGTYASFARGAVGAAQLAACCLEMRVLVELGPWAGGFGPDLLLTLVFLLFLVHGVTFDGASANPTVALQEFLMVEASLPNTLLKLSAQVLGAQAACALTQRCWAWELSELHLLQSLMAAHCSSTLRTSVLQGMLVEGACTFFFHLSLLHLQHSLLVYRVPALALLVTLMAYTAGPYTSAFFNPALAASVTFHCPGNTLLEYAHVYCLGPVAGMILAVLLHQGHLPRLFQRNLFYRQKSKYRTPRGKLSPGSVDAKMHKGE
Protein: Protein MAINTENANCE OF PSII UNDER HIGH LIGHT 1 (Q9FL44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Interacts with photosystem II (PSII) core complexes and participates in the maintenance of normal PSII activity under photoinhibitory stress. May protect against photodamage or stabilize PSII under high-light stress. Participates in the maintainance of proper PSII function under high-light stress by protecting PSII from photooxidative damage.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:25846821}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein disulfide-isomerase LQY1, chloroplastic
- Protein HHL1, chloroplastic
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244
- PsbP-like protein 1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
- DEAD-box ATP-dependent RNA helicase FANCM
- Light-harvesting complex-like protein OHP2, chloroplastic
- RecQ-mediated genome instability protein 1
- Serine/threonine-protein kinase-like protein At5g23170
- Light-harvesting complex-like protein OHP1, chloroplastic
Sequence:
MSNVLLSPNGYVFASPKPLGRFINSKSGGRKLFFSVVRASSDDADCNAEECAPEKEVGTVSMEWLAGEKTKVVGTFPPRKPRGWTGYVEKDTAGQTNVYSIEPAVYVAESAISSGTAGSSADGAENTAAIVAGIALIAVAAASSILLQVGKDAPTRPKAVDYSGPSLSYYINKFKPSEIVQPSTPSVTEAPPVAELETSLPETPSVAQQETSLPETMASEAQPEASSVPTTSSTS
Protein: Mediator of RNA polymerase II transcription subunit 14 (Glucose repression regulatory protein 1) (Mediator complex subunit 14) (P19263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:11383511, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16630888}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 7
- DNA-directed RNA polymerase II subunit RPB1
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MTTTIGSPQMLANEERLSNEMHALKNRSEQNGQEQQGPVKNTQLHGPSATDPETTATQKESLEMVPKDTSAATMTSAPPPALPHVEINQVSLALVIRNLTVFTMKELAQYMKTNVHTQANEPNSAKKIRFLQLIIFLRTQFLKLYVLVKWTRTIKQNNFHVLIDLLNWFRTTNMNVNNCIWALKSSLNSMTNAKLPNVDLVTALEVLSLGRPNLPTHNFKLSGVSNSMDMVDGMAKVPIGLILQRLKDLNLTVSIKIALMNIPKPLNSYHIKNGRIYFTVPNEFEIQLSTVNRQSPLFFVDLKLLFNTEAEQTVSAVTEATSTNGDSENNEENSSSNGNNLPLNKPRLEKLINEILLKSNDPLLSLYNFLHKYVLTLQLYMVHREFLKLANGGKFSKSNLIHNYDSKKSTITVRYWLNGKMDSKGKITIGIQRTTESLILKWDNQSASRAKNMPVIYNNIVSNIEGILDEIMFNHARIIRSELLARDIFQEDEENSDVLLFQLPTTCVSMAPIQLKIDLLSGQFYFRNPTPLLSNYASKINRAEGPEELARILQQLKLDKIIHVLTTMFENTGWSCSRIIKIDKPIRTQVNTGGESVVKKEDNKYAIAGNSTTNSDVSLLLQRDLFIRLPHWPLNWYLILSIISSKTSCVVEKRIGKIVSQRGKWNLKYLDNSNVMTVKLESITYQKIMILQRTILNRIINHMLIDSLNQLEIRNKICSSEMINEQKLPQYIIQGSNTNDNISIITLELESFLEGSKALNSILESSMFLRIDYSNSQIRLYAKFKRNTMMIQCQIDKLYIHFVQEEPLAFYLEESFTNLGIIVQYLTKFRQKLMQLVVLTDVVERLHKNFESENFKIIALQPNEISFKYLSNNDEDDKDCTIKISTNDDSIKNLTVQLSPSNPQHIIQPFLDNSKMDYHFIFSYLQFTSSLFKALKVILNERGGKFHESGSQYSTMVNIGLHNLNEYQIVYYNPQAGTKITICIELKTVLHNGRDKIQFHIHFADVAHITTKSPAYPMMHQVRNQVFMLDTKRLGTPESVKPANASHAIRLGNGVACDPSEIEPILMEIHNILKVDSNSSSS
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (Q4Q9H8)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Adenosine kinase
- Adenosine kinase
- Adenosine kinase
- Hypoxanthine phosphoribosyltransferase
- Adenylosuccinate lyase
- GMP synthase
- Guanine deaminase
- Guanylate kinase-like protein
- guanylate kinase
- AMP deaminase
Sequence:
MSFKEISPNSFLLEDSHPLSQLLKKNYCWYSPVFSPRNVPRFADVSSITESPETLKAIRDFLVQRYRTMSPAPTHILGFDARGFLFGPMIAVELGIPFVLMRKADKNAGLLIRSEPYEKEYKEAAPEVMTIRYGSISKGSRVVLIDDVLATGGTALSGLQLVEASDAMVVEMVSILCIPFLKAAEKIHSTGHSRYKDIKFISLLSEEALTEDNCGDSKNYTGPRVVSCGDVLSKHSQ
Protein: Ferredoxin-3, chloroplastic (Ferredoxin III) (Fd III) (P27788)
Organism: Zea mays (Maize)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Ferredoxin--NADP reductase, chloroplastic
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Lipoyl synthase, chloroplastic
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Photosystem I reaction center subunit II
Sequence:
MSTSTFATSCTLLGNVRTTQASQTAVKSPSSLSFFSQVTKVPSLKTSKKLDVSAMAVYKVKLVGPEGEEHEFDAPDDAYILDAAETAGVELPYSCRAGACSTCAGKIESGSVDQSDGSFLDDGQQEEGYVLTCVSYPKSDCVIHTHKEGDLY
Protein: Abscisic acid 8'-hydroxylase 4 (ABA 8'-hydroxylase 4) (EC 1.14.14.137) (Cytochrome P450 707A4) (Q9LJK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the oxidative degradation of abscisic acid, but not in the isomerization of the produced 8'-hydroxyabscisic acid (8'-OH-ABA) to (-)-phaseic acid (PA).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Abscisic-aldehyde oxidase
- Beta-D-glucopyranosyl abscisate beta-glucosidase
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- Tetratricopeptide repeat
- Xanthoxin dehydrogenase
- Zeaxanthin epoxidase, chloroplastic
Sequence:
MAEIWFLVVPILILCLLLVRVIVSKKKKNSRGKLPPGSMGWPYLGETLQLYSQNPNVFFTSKQKRYGEIFKTRILGYPCVMLASPEAARFVLVTHAHMFKPTYPRSKEKLIGPSALFFHQGDYHSHIRKLVQSSFYPETIRKLIPDIEHIALSSLQSWANMPIVSTYQEMKKFAFDVGILAIFGHLESSYKEILKHNYNIVDKGYNSFPMSLPGTSYHKALMARKQLKTIVSEIICERREKRALQTDFLGHLLNFKNEKGRVLTQEQIADNIIGVLFAAQDTTASCLTWILKYLHDDQKLLEAVKAEQKAIYEENSREKKPLTWRQTRNMPLTHKVIVESLRMASIISFTFREAVVDVEYKGYLIPKGWKVMPLFRNIHHNPKYFSNPEVFDPSRFEVNPKPNTFMPFGSGVHACPGNELAKLQILIFLHHLVSNFRWEVKGGEKGIQYSPFPIPQNGLPATFRRHSL
Protein: Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) (P07356)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
Interaction partners:
- Protein S100-A10
- AHNAK nucleoprotein
- Tissue-type plasminogen activator
- Protein S100-A4
- Plasminogen
- Annexin A1
- Protein S100-A11
- CD63 antigen
- AHNAK nucleoprotein 2.
- Beta-2-glycoprotein 1
Sequence:
MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAVKTKGVDEVTIVNILTNRSNVQRQDIAFAYQRRTKKELPSALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
Protein: Junction plakoglobin (Desmoplakin III) (Desmoplakin-3) (Q8SPJ1)
Organism: Bos taurus (Bovine)
Function: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:P14923}. Cell junction, desmosome {ECO:0000250|UniProtKB:P14923}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P14923}. Cell membrane {ECO:0000250|UniProtKB:P14923}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14923}. Cytoplasm {ECO:0000250|UniProtKB:Q9PVF7}. Cell junction {ECO:0000250|UniProtKB:Q9PVF7}. Nucleus {ECO:0000250|UniProtKB:Q9PVF7}. Note=Cytoplasmic in a soluble and membrane-associated form. Colocalizes with DSG4 at desmosomes (By similarity). {ECO:0000250|UniProtKB:P14923}.
Interaction partners:
- Cadherin-1
- Desmoplakin
- Lymphoid enhancer-binding factor 1
- Transcription factor 7 like 1
- Catenin beta-1
- Plakophilin-1
- Plakophilin 2.
- Desmocollin-2
- Probable splicing factor YJU2B
- Desmoglein 2
Sequence:
MEVMNLIEQPIKVTEWQQTYTYDSGIHSGANTCVPSLSSKGLIEEDEACGRQYTLKKTTTYTQSVPPGQGDLEYQMSTTARAKRVREAMCPGVTGEDSSLLLTTQVEGQTTNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPMNEPYADDMDATYRPMYSSDVPMDPLEMHMDMDGDYPIDTYSDGLRPPYATADHMLA