wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Sp1 (P08047)
Organism: Homo sapiens (Human)
Function: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.
Interaction partners:
- Estrogen receptor
- Histone acetyltransferase p300
- Transcription factor Jun
- Cellular tumor antigen p53
- TATA-box-binding protein
- CREB-binding protein
- Histone deacetylase 1
- Estrogen receptor beta
- Transcription factor E2F1
- Mothers against decapentaplegic homolog 3
Sequence:
MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF
Protein: RNA-binding motif, single-stranded-interacting protein 2 (Suppressor of CDC2 with RNA-binding motif 3) (Q15434)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Complement factor H-related protein 3
- Complement factor H
Sequence:
MLLSVTSRPGISTFGYNRNNKKPYVSLAQQMAPPSPSNSTPNSSSGSNGNDQLSKTNLYIRGLQPGTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPSAAQKAVTALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELEGMLKPFGQVISTRILRDTSGTSRGVGFARMESTEKCEAIITHFNGKYIKTPPGVPAPSDPLLCKFADGGPKKRQNQGKFVQNGRAWPRNADMGVMALTYDPTTALQNGFYPAPYNITPNRMLAQSALSPYLSSPVSSYQRVTQTSPLQVPNPSWMHHHSYLMQPSGSVLTPGMDHPISLQPASMMGPLTQQLGHLSLSSTGTYMPTAAAMQGAYISQYTPVPSSSVSVEESSGQQNQVAVDAPSEHGVYSFQFNK
Protein: Methyltransferase (O26771)
Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Interaction partners:
Sequence:
MSCYIYWDKIKRIASRLEGMNYHFDEMDTSGVMPLLDEIEEIAHDSTIDFESAKHILDDAEMNHALSLIRKFYVNLGMKLEMEKAQEVIESDSPWETLRSFYFYPRYLELLKNEAALGRFRRGERAVFIGGGPLPLTGILLSHVYGMRVNVVEIEPDIAELSRKVIEGLGVDGVNVITGDETVIDGLEFDVLMVAALAEPKRRVFRNIHRYVDTETRIIYRTYTGMRAILYAPVSDDDITGFRRAGVVLPSGKVNNTSVLVFKCPD
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 1) (1-AGP acyltransferase 1) (1-AGPAT 1) (Lysophosphatidic acid acyltransferase alpha) (LPAAT-alpha) (O35083)
Organism: Mus musculus (Mouse)
Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99943}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipid phosphatase 2
- Lysocardiolipin acyltransferase 1
- Phospholipid phosphatase 3
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Glycerol-3-phosphate acyltransferase 4
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
Sequence:
MELWPGAWTALLLLLLLLLSTLWFCSSSAKYFFKMAFYNGWILFLAILAIPVCAVRGRNVENMKILRLLLLHAKYLYGIRVEVRGAHHFPPTQPYVVVSNHQSSLDLLGMMEVLPDRCVPIAKRELLWAGSAGLACWLAGIIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIIPIVMSSYQDFYSKKERRFTSPGRCQVRVLPPVSTEGLTPDDVPALADSVRHSMLTIFREISTDGLGGGDCLKKPGGAGEARL
Protein: Neuromedin B (D4A1W6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Gastrin-releasing peptide
- Neuromedin-B receptor
- Gastrin-releasing peptide receptor
- Bombesin receptor subtype-3
- Elongator complex protein 3
- Elongator complex protein 5
- Elongator complex protein 1
- Epsilon-sarcoglycan
- Sarcoglycan, alpha
Sequence:
MTRQAGSTWLLRGLLLFALFVSGITPFSWDLPEPRSRASKIRVHPRGNLWATGHFMGKKSLEPPSLSLVGTAPPITQREQRLQLSHDLLRILLLQKALGMNLSGPAPPIQYRRLLQK
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (P9WGE9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Uncharacterized protein Rv2876
- Cytochrome bc1 complex cytochrome b subunit
- Superoxide dismutase
- Catalase-peroxidase
- Putative glutamate--cysteine ligase 2
- Probable cytochrome c oxidase subunit 1
- Alkyl hydroperoxide reductase C
- Cytochrome c oxidase subunit 2
- Probable cytochrome c oxidase subunit 3
Sequence:
MPKPADHRNHAAVSTSVLSALFLGAGAALLSACSSPQHASTVPGTTPSIWTGSPAPSGLSGHDEESPGAQSLTSTLTAPDGTKVATAKFEFANGYATVTIATTGVGKLTPGFHGLHIHQVGKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQVRGDGSAMLVTTTDAFTMDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 (Complex I-MNLL) (CI-MNLL) (NADH-ubiquinone oxidoreductase MNLL subunit) (Q02378)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 subunit C2
Sequence:
MNLLQVVRDHWVHVLVPMGFVFGYYLDRKNDEKLTAFRNKSLLYKRELKPNEEVTWK
Protein: FI07418p (Rab39, isoform A) (Rab39, isoform B) (Q9W3Q0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00025701}; Lipid-anchor {ECO:0000256|ARBA:ARBA00025701}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00025701}.
Interaction partners:
- LD44762p
- SD08447p
- Rab GDP dissociation inhibitor
- Geranylgeranyl transferase type-2 subunit alpha
- Rab proteins geranylgeranyltransferase component A
- non-specific serine/threonine protein kinase
Sequence:
MVEPIFEYQFRLILIGDSTVGKSSLLKFFTDGKFAELSDPTVGVDFFARLIEMKDGTQIKLQLWDTAGQERFRSITKSYYRNSVGVLLVYDISNHASFEHIPLWMMEAQRHIEPHRPVFALVGCKLDLINAGGHREVTTEEAQKFAKQHGLHFVETSARSGANVEEAFRMVTQEVYARIRSGEYKAEDGWDGIKSGFSRPNSLDFNLVVAEPEKSSCC
Protein: DNA-directed RNA polymerases II, IV and V subunit 8B (RNA polymerase Rpb8) (Q9M1A8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerase V subunit 7
- DNA-directed RNA polymerase IV subunit 7
- DNA-directed RNA polymerases IV and V subunit 2
- DNA-directed RNA polymerases IV and V subunit 5B
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 11
Sequence:
MASNIIMFEDIFVVDKLDPDGKKFDKVTRVEARSHNLEMFMHLDVNTEVYPLAVGDKFTLAMAPTLNLDGTPDTGYFTPGAKKTLADKYEYIMHGKLYKISERDGKTPKAELYVSFGGLLMLLQGDPAHISHFELDQRLFLLMRKL
Protein: Protein-toxin resistance protein KTD1 (Killer Toxin Defense 1) (P39548)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:36800387}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:36800387}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:36800387}; Multi-pass membrane protein {ECO:0000255}. Note=Overexpressed protein is predominantly vacuolar. A small amount of protein also localizes to the cell periphery, possibly the cell membrane or cortical endoplasmic reticulum. {ECO:0000269|PubMed:36800387}.
Interaction partners:
- DUP240 protein DFP2
- ULP1-interacting protein 3
- SRP-independent targeting protein 2
Sequence:
MQTPSENTDVKMDTLDEPSAHLIEENVALPEDTFSSHLSYVLYEIAHCKPIMFMIIIIVSLISLIVLFHDNDGCTVILVMSLIVASMALMVVAAFTFGKAITEQEFMIKLLVEVIARKPAGKEWGTVAYNMNQYLFMKRLWYTPYYFYSGKKCHEFFTTLIKEVNSGSHSDSSSNSAEDTQSPVSAGKTSNGLNNFYSIRSDPILMAYVLKATQIEKEAQSEYWRKQYPDADLP
Protein: Killer cell lectin-like receptor subfamily E member 1 (Q80ZC8)
Organism: Rattus norvegicus (Rat)
Function: Lectin-like receptor for natural killer (NK) cells. Can either inhibit or activate NK cell cytotoxic activity, depending on its binding partner. Heterodimer formation with KLRI1 mediates NK cell inhibition whereas heterodimer formation with KLRI2 mediates NK cell activation. Plays a role in allogeneic recognition by the immune system (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12782717, ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Killer cell lectin-like receptor subfamily I member 2
Sequence:
MNQTLIICSTLNVNSQQKSKAKNSMKNTFHSNELSSIEQRQKYQKHLKKDKKTAEDITGVGNCSPPWRLISSVLFVVCLLLMAVAMVMTIFTTRLSSERSSSNIHQEGLHHPCPENWVWFRCSCYYFSKEKLVWRESQRACLSFNSSLIRMNKEEMDFFSLKSFFWVGVYYDETSKQWLWDDHSVLPSGMFSGLESSPKNFCASYKSKEAYLAENCSTKLMYICKK
Protein: Fructose-2,6-bisphosphatase TIGAR B (EC 3.1.3.46) (TP53-induced glycolysis and apoptosis regulator B) (Q7ZVE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. May play a role in mitophagy inhibition.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BZA9}. Nucleus {ECO:0000250|UniProtKB:Q9NQ88}. Mitochondrion {ECO:0000250|UniProtKB:Q8BZA9}.
Interaction partners:
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
- 6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase 3
- 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2a.
- 6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase 1
- Mannose-6-phosphate isomerase
- Probable fructose-2,6-bisphosphatase TIGAR A
- ATP-dependent 6-phosphofructokinase
- Triosephosphate isomerase A
- ATP-dependent 6-phosphofructokinase
- ATP-dependent 6-phosphofructokinase
Sequence:
MLTFALTIVRHGETQYNRDKLLQGQGIDTPLSDTGHQQAAAAGRYLKDLHFTNVFVSNLQRAIQTAEIILGNNLHSSATEMILDPLLRERGFGVAEGRPKEHLKNMANAAGQSCRDYTPPGGETLEQVKTRFKMFLKSLFQRMLEEHGSALSSAPSEADQPVIAGLADDGAQNVPVHALMVSHGAFIRISVRHLVEDLQCCLPAGLKMNQVFSPCPNTGISRFIFTIHREESVLRATRIQGVFINRKDHLEEVKNSD
Protein: Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (3-ketoacyl-CoA reductase) (3-ketoreductase) (KAR) (Microsomal beta-keto-reductase) (Q10245)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03107}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03107}.
Interaction partners:
- Putative enoyl reductase C646.07c
- Probable very-long-chain
- Probable acyl-CoA desaturase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Putative fatty acid elongase 1
- Putative fatty acid elongase 2
- 3-keto-steroid reductase erg27
- AP-1-like transcription factor
- Lanosterol synthase erg7
- Acetyl-CoA acetyltransferase
Sequence:
MDGEVLANKSCCGAVVTAFSVIGIVFTILKFTSFASFVYKTFFAKGVKLSVYGAKKGYWAVVTGATDGIGKEYATQLAMSGFNVVLISRTQEKLDALAKELETVAKVKTRTIAIDYTKTTAETFEKLHQDLVGTPITVLINNVGQSHYMPTSFAETTVKEMDDIMHINCFGTLHTTKAVLSIMLRERQKNEKGPRCLILTMGSFAGLLPSPYLSTYAGSKAFLSNWSASLGEEVKKQGIDVWCFNSYLVVSAMSKVRRPTLTIPTPKKFVRAALSSIGLQRGGTNPYISQPYPSHAVMSWSLEQLLGSAKGFVVSQVAAMHLSIRKRALRKEARLQAQNQA
Protein: Exportin-6 (Exp6) (Ran-binding protein 20) (Q924Z6)
Organism: Mus musculus (Mouse)
Function: Mediates the nuclear export of actin and profilin-actin complexes in somatic cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96QU8}. Cytoplasm {ECO:0000250|UniProtKB:Q96QU8}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q96QU8}.
Interaction partners:
- Profilin-4
- Profilin-1
- E3 SUMO-protein ligase RanBP2
- Profilin-3
- Profilin-2
- Importin-9
- Profilin
- Exportin-7
- Transformation/transcription domain-associated protein
- Exportin-4
Sequence:
MASEEASLRALESLMTEFFHDCTTNERKREIEELLNNFAQQVGAWRFCLYFLSSTRNDYVMMYSLTVFENLINKMWLGVPSQDKMEIRSCLPKLLLAHHKTLPYFIRNKLCKVIVDIGRQDWPMFYHDFFTNILQLIQSPVTTPLGLIMLKTTSEELACPREDLSVARKEELRKLLLDQVQTVLGLLTGILETVWDKHSVTAATPPPSPTSGESGDLLSNLLQSPSSAKLLHQPIPILDVESEYVCSLALECLAHLFSWIPLSASITPSLLTTIFHFARFGCDTRARKMASVNGSSQNCVLGQERGRLGVLAMSCINELMSKNCVPMEFEEYLLRMFQQTFYLLQKITKDNNAHTVKSRLEELDESYIEKFTDFLRLFVSVHLRRIESYSQFPVVEFLTLLFKYTFHQPTHEGYFSCLDIWTLFLDYLTSKIKSRLGDKEAVLNRYEDALVLLLTEVLNRIQFRYNQAQLEELDDETLDDDQQTEWQRYLRQSLEVVAKVMELLPTHAFSTLFPVLQDNLEVYLGLQQFVVTSGSGHRLNITAENDCRRLHCSLRDLSSLLQAVGRLAEYFIGDVFAARFNDALTVVERLVKVTLYGSQIKLYNIETAVPSVLKPDLIDVHAQSLAALQAYSHWLAQYCGEAHRQNTQQFVTLISTTMDAITPLISTKVQDKLLLSACHLLVSLATTVRPVFLISIPAVQKVFNSIIDASAQRLTDKAQVLVCRALSNTLLLPWPNLPESEQQWPLRSINHASLISALSRDYHSLKPSATAPQRKVPLGDTKVIIHQTLSVLEDIVENISGESTKSRQICYQSLQESVQVSLALFPAFIHQSDVTDEMLSFFLTLFRGLRVQMGVPFTEQIIQTFLNMFTREQLAESILHEGSTGCRVVEKFLKILQVVVQEPGQVFKPFLPSIIALCMEQVYPIIAERPSPDVKAELFELLFRTLHHNWRYFFKSTVLASVQRGIAEEQMENEPQFSAIMQAFGQSFLQPDIHLFKQNLFYLETLNTKQKLYHKKIFRTTMLFQFVNVLLQVLVHKSHDLLQEEIGIAIYNMASVDFDGFFAAFLPEFLTSCDGVDANQKNVLGRNFKMDRDLPSFTQNVHRLVNDLRYYRLCNDSLPPGTVKL
Protein: Hal9p (A0A1D8PNC6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
Sequence:
MDPAYDIQSHEKQVLVNDPLIPEDNAQNPSLPSRGSSNSTITQSSSSSSEVKPILKKKRTRISKACEYCRKKKVKCNGCQPCLNCLQSNNGNCEYAVDDEKKPKISKKKKSTSSKSKSNRDRQNKALDERLSKIEGILAQLAAGIGTNDNTSTLSPVSGSNVPNGKEAKTDKSSPLQLPKEIREESANGHDEKHDPKVESNFHGSHSVINIFCKKSVEWLFRPVLSKCNQDIEVFKDIAKVNDLYIQAFLDTISQPIKARINRRNDLMDNTFANAKIPLEILSCYDDIFLVSYVCKGDDIRKLFQTYFEEPDQNGSRRRSFLWSELLLMTAAVGICISVLIDDRNNTKDTDKPKYSCSLSNQQLIEINFKCFYSMIFYHRRLCVIGEGFSTVTAFVLLIMYFDFAVPISHATFLAVSTVMHYARQLGLHRSEAYREMGLEEQRTRRILWWFCEYLHIQYCFEKGYALDIGDEDMMSFSGDDATTKALIKSNWNLIQSAKNSDTPIDALTINQIKETKANHICASYTMHSLSKIRVKSYQLLYSSKAQKKTLSTILTFVDELNSEMKDLCSDLPGPMAILFYDEPGFLSNSAINSEILLNLDNGYENTLMIQFEYFSHLLTINRLSLQEFPQDMDNKFLTHKCLYHRNIANRSARTILYIARNLAEKKVDFILINWFSYSIFAAFVYLGSMCLEDPQSPEVISDIDLLIDISYSFLAFENQSFKVSRFSLQRYVYDIYTRCILKLYLKVAKEETRNMFYEKYKNLHNHLRLEETFHEFFFNENLGFDPSKTYQALNKLFRPFWIKSNEKPNRTQANAADDATSNQMSSTPLESSSSSSGILYGNSSSSSTSFQPPMVHQRNSVSSHQFDYTQDFPHNGGKPLEISYLVHPQMKHFDAAIGSVTKRNGSPNDKELSETFDPQAISVINAAQMQQQQQQQQQQQQQQPPFFTPPPPPPQQSLLPSQYQQQSQQQQQQQEQPLSNRFNSNFTSLEEMIEENYVGDLNFPDIFYN
Protein: Membrane progestin receptor beta (Progestin and adipoQ receptor family member VIII) (Q801G3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSGVLGRLSTLTLSLQQLGQLPHLSNWLPRLPRRQATVHASEVPSLFREPYILSGYRPVHQEWRSYFCSLFQCHNELLNVWTHLLAIPAVLLQFSFFAGAWGLTLNLASLPLFLYVLSSLTYLSFSVAAHLLQSHSELAHYSLFFVDYVGVAVYQYGCSMGHYFYCSEPEWRHSLVGVLFLPGAAMLAWLSCASCCYSKFRYRRPYPFHRKICQIIPTSLAYLLDISPVAHRLLTKSWDEPVLVFHAMQVAFFLLAALFFSCPVPERFFPGRCDIVGHGHQIFHIFLVLCTMCQLEAMFRDFLVHQQSVVDAHGEHFILLAGGSFFLLVLCSILTAVLMRGAVQRQLRKKD
Protein: ATP citrate synthase (EC 2.3.3.8) (Q5BAJ5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- ATP citrate synthase
- Citrate synthase, mitochondrial
- 2-methylcitrate synthase, mitochondrial
- Acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate carboxylase
- malate dehydrogenase
- malate dehydrogenase
- Malate dehydrogenase
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
Sequence:
MSAKSIFEADGKAILNYHLTRAPVIKPTPLPPSNTHNPPPKLASLYFPDDLSVKDVLDQAEVTYPWLLTPGSKFVAKPDQLIKRRGKSGLLALNKTWAEAREWIEARATKEQQVETVVGVLRHFLVEPFVPHPQETEYYINIHSVREGDWILFTHEGGVDVGDVDAKAEKLLIPVNLKNYPSNEEIASALLSKVPKGIHNVLVDFISRLYAVYVDCQFTYLEINPLVVIPNADATSADVHFLDLAAKLDQTAEFECGTKWAVARSPANLGLAALPTSDKVNIDAGPPMEFPAPFGRELSKEEKFISDMDAKTGASLKLTVLNPNGRVWTLVAGGGASVVYADAIASAGFVSELANYGEYSGAPTETQTFNYARTILDLMLRSPIHPDGKVLFIGGGIANFTNVASTFKGVIRALREVAPVLNEHKVQIWVRRAGPNYQEGLKNIKAVGEELGLNMHVYGPEMHVSGIVPLALQGKQTDIKEFGTA
Protein: Transcription factor TT8 (Basic helix-loop-helix protein 42) (AtbHLH42) (bHLH 42) (Protein TRANSPARENT TESTA 8) (Transcription factor EN 32) (bHLH transcription factor bHLH042) (Q9FT81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2. Involved in the control of flavonoid pigmentation. Plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). Not required for leucoanthocyanidin dioxygenase (LDOX) expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein TRANSPARENT TESTA GLABRA 1
- Transcription factor TT2
- Transcription factor MYB75
- Transcription factor MYB114
- Transcription factor MYB113
- At1g71030/F23N20_2
- Transcription repressor MYB5
- Transcription factor MYB90
- Dihydroflavonol 4-reductase
- WRKY transcription factor 44
Sequence:
MDESSIIPAEKVAGAEKKELQGLLKTAVQSVDWTYSVFWQFCPQQRVLVWGNGYYNGAIKTRKTTQPAEVTAEEAALERSQQLRELYETLLAGESTSEARACTALSPEDLTETEWFYLMCVSFSFPPPSGMPGKAYARRKHVWLSGANEVDSKTFSRAILAKSAKIQTVVCIPMLDGVVELGTTKKVREDVEFVELTKSFFYDHCKTNPKPALSEHSTYEVHEEAEDEEEVEEEMTMSEEMRLGSPDDEDVSNQNLHSDLHIESTHTLDTHMDMMNLMEEGGNYSQTVTTLLMSHPTSLLSDSVSTSSYIQSSFATWRVENGKEHQQVKTAPSSQWVLKQMIFRVPFLHDNTKDKRLPREDLSHVVAERRRREKLNEKFITLRSMVPFVTKMDKVSILGDTIAYVNHLRKRVHELENTHHEQQHKRTRTCKRKTSEEVEVSIIENDVLLEMRCEYRDGLLLDILQVLHELGIETTAVHTSVNDHDFEAEIRAKVRGKKASIAEVKRAIHQVIIHDTNL
Protein: Netrin receptor UNC5 (F1QXJ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367033}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367033}.
Interaction partners:
Sequence:
MLSTWIHRDQSPASLLGLLLLSSTLVIHADGSDYSEVLPDSFPSAPAEPLPEFQSEPEDAFIVKNRPVKLSCKAAPATQIYFKCNGEWVNQNDHVTKESLDHITGLVVREVDISVSRTQVEELFGLEDYWCQCVAWSSAGTTKSRRAYVRIAYLRKNFEQEPLGREVRLEQEVLLQCRPPEGSPPAEVDWLKNEELIDPALDSNFLITIEHDLIIKQARLSDTANYTCVARNVVAKRRSSTATLIVYVSGGWSSWTEWSECNAQCGRGWQRRTRSCTNPAPLNGGAFCDGPPFQRVTCTTLCPVDGGWTEWAKWSACGTECTHWRSRECQAPPPRNGGRHCSGSMMESKNCTEGLCARTLGSGTGVAVYAGLVGALLLCVILVLCVGILVYRRSCRHLHGEITDSSSALTAAFHPGNYKPPRQDNPHLLHPTAPPDLTASAGTFRGPLFSLQQATLDSHHKIPMTTSPLLDPLPSLKIKVYNSSTMSSLELPTGLGSVDGDIMSLKTVGSGPKDHHGHTLPREPSHSASATLGSLGGRLTIPNTGVSLLVPPGTIPQGKFYEMYLIINKWEKTTLPSDGSQTVLSPVVSCGPSGMLLSRPVVLTLPHCAQLEPPDWTLTLKMQNHQGAWEEVLTVGEESLSSPCYLQVEEQSCHILMEQLGTYGLVGQSAPPRPACKRLQLALFAPRAPCLSLDYSLRVYCIQDTPHALKEVLEVERSLGGVLLEDPKPLLFKDSYHNMRLSIHDIPHSHWRSKLLAKYQEIPFYHIWSGSQRPLHCTFSLERGSLVVSQLTCKICVRQVEGEGQIFQLNTDIQETLPPHSPLPAGGSCLPSSQVGPYAFRLPVSIRQKICASLDAPSARGCDWRMLARSLAFDRYLNYFATKPSPTGVLLDLWEACHQGDADLVSLATALEEMGKSEVLVVMTTDGDC
Protein: Cyclin-T1-3 (CycT1;3) (Q8LBC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase C-1
- Cyclin-dependent kinase C-2
- Cyclin-dependent kinase D-2
- Cyclin-H1-1
- Protein RTF1 homolog
- Transcription elongation factor SPT4 homolog 1
- Pentatricopeptide repeat-containing protein At4g30825
- Transcription elongation factor SPT4 homolog 2
- Protein RNA-directed DNA methylation 3
- FACT complex subunit SSRP1
Sequence:
MGEEHPRKRSRQHFEAEARNVSLFESPQCETSKWYFSREEIERFSPSRKDGIDLVKESFLRSSYCTFLQRLGMKLHVSQVTISCAMVMCHRFYMRQSHAKNDWQTIATSSLFLACKAEDEPCQLSSVVVASYEIIYEWDPSASIRIHQTECYHEFKEIILSGESLLLSTSAFHLDIELPYKPLAAALNRLNAWPDLATAAWNFVHDWIRTTLCLQYKPHVIATATVHLAATFQNAKVGSRRDWWLEFGVTTKLLKEVIQEMCTLIEVDRRRNMPPPPPPPRRELSWAIPAAVKPVHMARAYPFHSYPLQSYRQAGIW