wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-binding transcriptional dual regulator OxyR (Hydrogen peroxide-inducible genes activator) (Morphology and auto-aggregation control protein) (P0ACQ4)
Organism: Escherichia coli (strain K12)
Function: Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability.
Interaction partners:
- HTH-type transcriptional regulator PerR
- Catalase-peroxidase
- Redox-sensitive transcriptional activator SoxR
- Alkyl hydroperoxide reductase C
- Regulatory protein SoxS
- Catalase HPII
- RNA polymerase sigma factor RpoS
- Glutaredoxin 1
- Alkyl hydroperoxide reductase subunit F
- Superoxide dismutase
Sequence:
MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGMLLVDQARTVLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCVILALVKESEAFIEVPLFDEPMLLAIYEDHPWANRECVPMADLAGEKLLMLEDGHCLRDQAMGFCFEAGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPPERKRDGVVYLPCIKPEPRRTIGLVYRPGSPLRSRYEQLAEAIRARMDGHFDKVLKQAV
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FY79)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Adenylosuccinate lyase
- Phosphoribosylglycinamide formyltransferase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase
- Phosphoribosylformylglycinamidine synthase
- Serine hydroxymethyltransferase, cytosolic
- Amidophosphoribosyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, mitochondrial
Sequence:
MYKKTAILSVYDKTGLLDLAKGLIENDVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHGGILARNLESDEKDLKDQHIDKVDFVVCNLYPFKETVAKVGVTVPEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYAIFLHELKEHGEVSQELRNRLALKAFEHTADYDAAISDFFRKQYSENRAQLPLRYGANPHQRPAQAFVTQLEELPFKVLSGSPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGIPLSDVEKQIYFVSDIENLSPLACAYARARGADRMSSFGDWIALSNIVDVPTATIISKEVSDGVIAPGFEPEALEILKKKKNGKYCILQIDPNYIPDAMESRDVYGITLQQKRNDAIINQSSFKEIVSANKNLTEQAVIDLTVASLALKYTQSNSVCYAKNGMVIGLGAGQQSRIHCTRLAGDKADNWWLRQHPKVLAFKWAKGVKRPDKSNAIDLYVTGQIPEEDPEKSEYESKFAEIPTPLTPEERKEWLSKLNNVSLSSDAFFPFPDNVYRAVKSGVKYIAAPSGSVQDKAVFAAADSFDLVYVENPIRLFHH
Protein: Stretchin-MLCK (Q9GV79)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
IPNDYGVEAAAASVAVEGPPEPPSAQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERCQPEQLLAAKVIKCIKSQDRQKVLEEISIMRALQHPKLLQLAASFESPREIVMVMEYITGGELFERVVADDFTLTEMDCILFLRQVCDGVAYMHGQSVVHLDLKPENIMCHTRTSHQIKIIDFGLAQRLDTKAPVRVLFGTPEFIPPEIISYEPIGFQSDMWSVGVICYVLLSGLSPFMGDTDVETFSNITRADYDYDDEAFDCVSQEAKDFISQLLVHRKEDRLTAQQCLESKWLSQRPDDSLSNNKICTDKLKKFIIRRKWQKTGNAIRALGRMANLSVSRRNSAIAMGVLSSPRPSISGLGMLTTSAIGGGTSSQMTSLHEEEDDFSGEMPPVEKRTVLKLRDKSQCSERSDSGYSECSNCSGAQETLLLSLAKSKLEAIAKASTLPTVVHDTEQPVSLELPTKGEAIMRSDFTNTIKMRKKSLEDSAAREKPRSKPQVKPLLCESKLKVSQLKDRFQVSPAPASASASASAANKPPLAYGPFKIAKVASVGRISRTEEPGRSGRGAPSVSGKGKSPQVRSMPSSPLPQRSATPTRLMSQRVREAAERLAQQHTVASAQRHLGNGRGTGNGNGNGNSNSNGNGNGNTAETNRESRARRLINRFNSETQHITS
Protein: Cytochrome c oxidase copper chaperone 1 (Cytochrome c oxidase 17 copper chaperone) (AtCOX17) (Q9LJQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Copper chaperone for cytochrome c oxidase (COX). Binds 2 copper ions and delivers them to the Cu(A) site of COX (By similarity). Can complement the yeast mutant cox17.
Subcellular location: Mitochondrion intermembrane space.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40 homolog
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase copper chaperone 2
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM9
- Protein SCO1 homolog 1, mitochondrial
- FAD-linked sulfhydryl oxidase ERV1
- Cytochrome c oxidase 19-1
- Heme A synthase COX15
- Mitochondrial import inner membrane translocase subunit TIM8
Sequence:
MTDQPAQNGLIPPPTSEPSKAAASAETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHKICLRAEGFNV
Protein: Guanine nucleotide exchange protein SMCR8 (Smith-Magenis syndrome chromosomal region candidate gene 8 protein) (Q8TEV9)
Organism: Homo sapiens (Human)
Function: Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and inhibiting its protein kinase activity. As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro. Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates. In addition to its activity in the cytoplasm within the C9orf72-SMCR8 complex, SMCR8 also localizes in the nucleus, where it associates with chromatin and negatively regulates expression of suppresses ULK1 and WIPI2 genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:28195531}. Nucleus {ECO:0000269|PubMed:28195531}. Presynapse {ECO:0000250|UniProtKB:Q3UMB5}. Postsynapse {ECO:0000250|UniProtKB:Q3UMB5}. Note=Localizes mainly in the cytoplasm. {ECO:0000269|PubMed:28195531}.
Interaction partners:
- Guanine nucleotide exchange factor C9orf72
- WD repeat-containing protein 41
- Ras-related protein Rab-39B
- Ras-related protein Rab-8A
- Serine/threonine-protein kinase ULK1
- Serine/threonine-protein kinase TBK1
- TRAF family member-associated NF-kappa-B activator
- ADP-ribosylation factor 1
- Serine/threonine-protein kinase ULK2
- Autophagy-related protein 101
Sequence:
MISAPDVVAFTKEEEYEEEPYNEPALPEEYSVPLFPFASQGANPWSKLSGAKFSRDFILISEFSEQVGPQPLLTIPNDTKVFGTFDLNYFSLRIMSVDYQASFVGHPPGSAYPKLNFVEDSKVVLGDSKEGAFAYVHHLTLYDLEARGFVRPFCMAYISADQHKIMQQFQELSAEFSRASECLKTGNRKAFAGELEKKLKDLDYTRTVLHTETEIQKKANDKGFYSSQAIEKANELASVEKSIIEHQDLLKQIRSYPHRKLKGHDLCPGEMEHIQDQASQASTTSNPDESADTDLYTCRPAYTPKLIKAKSTKCFDKKLKTLEELCDTEYFTQTLAQLSHIEHMFRGDLCYLLTSQIDRALLKQQHITNFLFEDFVEVDDRMVEKQESIPSKPSQDRPPSSSLEECPIPKVLISVGSYKSSVESVLIKMEQELGDEEYKEVEVTELSSFDPQENLDYLDMDMKGSISSGESIEVLGTEKSTSVLSKSDSQASLTVPLSPQVVRSKAVSHRTISEDSIEVLSTCPSEALIPDDFKASYPSAINEEESYPDGNEGAIRFQASISPPELGETEEGSIENTPSQIDSSCCIGKESDGQLVLPSTPAHTHSDEDGVVSSPPQRHRQKDQGFRVDFSVENANPSSRDNSCEGFPAYELDPSHLLASRDISKTSLDNYSDTTSYVSSVASTSSDRIPSAYPAGLSSDRHKKRAGQNALKFIRQYPFAHPAIYSLLSGRTLVVLGEDEAIVRKLVTALAIFVPSYGCYAKPVKHWASSPLHIMDFQKWKLIGLQRVASPAGAGTLHALSRYSRYTSILDLDNKTLRCPLYRGTLVPRLADHRTQIKRGSTYYLHVQSMLTQLCSKAFLYTFCHHLHLPTHDKETEELVASRQMSFLKLTLGLVNEDVRVVQYLAELLKLHYMQESPGTSHPMLRFDYVPSFLYKI
Protein: L-propargylglycine--L-glutamate ligase (EC 6.3.2.-) (G8XHD8)
Organism: Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057) (Streptomyces cattleya)
Function: Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes the ATP-dependent ligation of L-propargylglycine to L-glutamate to form the dipeptide L-gamma-glutamyl-L-propargylglycine. Is selective for L-propargylglycine over norvaline, allylglycine and the standard proteinogenic amino acids, except L-cysteine which can be used as a substrate to a lesser extent.
Interaction partners:
Sequence:
MYGAGVVTRMNEAERFHMTDPGSTKILIYAFNYADRMLEEVPYLRYSAERSLCFLGDLRDPGTRLVVITSEAVDPATLDYHLRDVFRFDEPALADVRRRLTLLTPASRAARPLDSLVLEDEALVETLRRAVAERPAGTIVDFSASPATDELGRRTGATPEEGDHAFVARWGSKSGGKEICLRAGVAVPGGTSEVLRSEAEVVEAIHRLSCGTAAARRAMVKLDAITWAASIGNVLIDRDKLRHTGDLVGSAEVIRLPAEEFRRELAEQGAIVEEFLEEITDSPSGLGHIERDGTVRVVACHDQVLSGGQYWGCRFPADERWRPEITDAVRRTGEVLSGLGHRGAFGVDFVVAGERGLLAVEINLRKVGPSHVVRYAEALVGARVGADGMLRGADGRPVYYTHGRLLEPETLGKLNPRTAVERLRAEGLLYRHDTGEGVALHVLGALNACGFVELTALARSPEAADGYSRAAQALLTGPYPSA
Protein: Neuronal PAS domain-containing protein 3 (Neuronal PAS3) (Basic-helix-loop-helix-PAS protein MOP6) (Member of PAS protein 6) (Q9QZQ0)
Organism: Mus musculus (Mouse)
Function: May play a broad role in neurogenesis. May control regulatory pathways relevant to schizophrenia and to psychotic illness.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15347806}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
Sequence:
MGRAGAAANGTPQNVQGITSYQQRITAQHPLPNQSECRKIYRYDGIYCESTYQNLQALRKEKSRDAARSRRGKENFEFYELAKLLPLPAAITSQLDKASIIRLTISYLKMRDFANQGDPPWNLRMEGPPPNTSVKGAQRRRSPSALAIEVFEAHLGSHILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYVHPGDHVEMAEQLGMKLPPGRGLLSQGTTEDAASSASSSSQSETPEPVETTSPSLLTTDNTLERSFFIRMKSTLTKRGVHIKSSGYKVIHITGRLRLRVPLSHGRTVPSQIMGLVVVAHALPPPTINEVRIDCHMFVTRVNMDLNIIYCENRISDYMDLTPVDIVGKRCYHFIHAEDVEGIRHSHLDLLNKGQCVTKYYRWMQKNGGYIWIQSSATIAINAKNANEKNIIWVNYLLSNPEYKDTPMDIAQLPHLPEKASESSETSDSESDSKDTSGITEDNENSKSDEKGNQSENSEDPEPDRKKSGSACDNDMNCNDDGHSSSNPDSRDSDDSFEHSDFEHPKAAEDGFGALGPMQIKVERYVESEADLRLQPCESLTSDSAKDSDSANEAGAQASSKHQKRKRRRKRQKGGSASRRRLSSASSPGLDAGLVEPPRLLSSPHSASVLKIKTEIAEPINFDNESSIWNYPPNREISRNESPYSMTKPPTSEHFPSPQGQGGSIGGGGALHVAIPDSVLTPPGADGTAGRKTQFSGTAPVPSDPLSPPLSASPRDKHPGGGAGSGGGGPGASNSLLYTGDLEALQRLQAGNVVLPLVHRVTGTLAATSTAAQRVYTTGTIRYAPAEVTLAMQGNLLPNAHAVNFVDVNSPGFGLDPKTPMEMLYHHVHRLNMSGPFGGAVSAASLTQMPGGNVFTTAEGLFSTLPFPVYSNGIHAAQTLERKED
Protein: Endochitinase Ziz m 1.0101 (EC 3.2.1.14) (Allergen Ziz m 1) (allergen Ziz m 1.0101) (Q2VST0)
Organism: Ziziphus mauritiana (Indian jujube)
Function: Defense against chitin containing fungal pathogens (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:16122801}.
Interaction partners:
Sequence:
MVPQAKLVVASLILTSALIQTSEAVGGIATYWGQYTETEEGSLAEACASNLYSYINIAYLNIFGEGRYLSLNISGHCSDCTFLGEEIKACQSQGVKIFLSLGGPYGDYHLTTDGDADRVAEQLWSSFLGGSKSTGVYQPLLGDVELDGIDLDIQIGPPEEYDVLARNLKDLTKDRTRPFYLSAAPKCSAYNDSDAYLWTAVETGLFDFVWVKFYNDTSCQYNNDTAAGLDAFYRSWYDWTVSLAEGNKLLIGIPASNETDNSPLGGYIPSDVLNDQIVSVIMTSSKFGGVNVWNRYYDLKTNYSSSIILEYVNSGTKYLPLRTKFMYQNA
Protein: Mandelamide hydrolase (EC 3.5.1.86) (Q84DC4)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Hydrolyzes both the R- and the S-enantiomers of mandelamide, and phenylacetamide. Has lower activity on 3-phenylpropionaide and lactamide. Does not hydrolyze benzamide. Hydrolyzes esters and amides with little steric bulk. Preferentially hydrolyzes aromatic substrates.
Interaction partners:
Sequence:
MRHPVDMPEKVGTDAKRLFAQPEHLWELTLTEASALVRHRRITSRQLVEAWLSRIADFSELNAFISVDAAAALKQADSYDHYLEAGGDPLPLGGVPIAVKDNIQVVGFANTAGTPALSKFFPTCNARVIEPLLKAGAIVVGKTNMHELAFGTSGYNTAYHIPGVIGVRNAFDHSCIAGGSSSGSGTAVGALLIPAALGTDTGGSVRQPGAVNGCVGFRPTVGRYPVDGITPISPTRDTPGPIARSVEDIVLLDSIITGALPAEVPAAESIRLGVVDQLWADLSEPVRKLTEDALRKLEQQGVQIVRVSMSEIFEMSHAVSMPLALHECRSALTEYLSANETGVSFDELVAGISSPDVRTIFEDYILPGRLGELEGQSVDLEQAYATAMKDARPKLIQSFEFLFKEHQLDAIIHPTTPDLAIKSNPAATSFEAFARMIRNADPASNAGMPGISLPAGLSQQEGLPVGIEIEGLPGSDARLLSIANFIESILGRGPTPTRSGVESKISM
Protein: Immunoglobulin kappa variable 6-14 (A0A140T8P1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEFQTQVFVFVLLWLSGVDGDIVMTQSQKFMSTSVGDRVSITCKASQNVRTAVAWYQQKPGQSPKALIYLASNRHTGVPDRFTGSGSGTDFTLTISNVQSEDLADYFCLQHWNYP
Protein: Recoverin (G3V6G4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Rhodopsin kinase GRK1
- Rhodopsin
- Cone-rod homeobox protein
- Arrestin-C
- Aryl-hydrocarbon-interacting protein-like 1
- Visual system homeobox 2
- Photoreceptor-specific nuclear receptor
- G protein subunit alpha transducin 1
- Short-wave-sensitive opsin 1
- Phosphodiesterase
Sequence:
MGNSKSGALSKEILEELQLNTKFTEEELSAWYQSFLKECPSGRITRQEFESIYSKFFPDSDPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTTAGKPTQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMIKPEDVKNLPDDENTPEKRAEKIWAFFGKKDDDKLTEEEFIEGTLANKEILRLIQFEPQKVKERIKEKKQ
Protein: BARBU (LD05688p) (Twin of m4) (Q9V3S6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bearded
- Brother of bearded A
- Enhancer of split mgamma protein
- Enhancer of split mdelta protein
- Protein spalt-accessory
- GEO09613p1
- LD15563p
- Enhancer of split m7 protein
- GEO04221p1
- Enhancer of split m4 protein
Sequence:
MSFITREYKFESSKVMEPKSDQHTMAMRSLRKLVKPLLRLVKKKQLLRKTLAEIQNQNAVNASLEDMRKDPAASCDNMANEELEQRLYTDLRQCPTNVAMIVQQGQQQSIVPVHPEQTFIPVHFARTTSGTFFWTSAEGARQHHEQQLRQQFDRWVQA
Protein: Ribosome biogenesis protein BOP1 homolog (Q7K0Y1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03027}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03027}.
Interaction partners:
- Ribosome biogenesis protein WDR12 homolog
- LD47540p
- Nucleolar complex protein 2
- Pescadillo homolog
- Probable ATP-dependent RNA helicase pitchoune
- Guanine nucleotide-binding protein-like 3 homolog
- Putative rRNA methyltransferase
- Ribosomal RNA processing protein 1 homolog
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein BRX1 homolog
Sequence:
MTKKLALKRRGKDSEPTNEVVASSEASENEEEEEDLLQAVKDPGEDSTDDEGIDQEYHSDSSEELQFESDEEGNYLGRKQSSSAEEDEESSDEEDNEEEESTDGEEVEDEEKDSKSKQTDDKPSGSGAASKKALTAELPKRDSSKPEYQDSDTSDEEDIRNTVGNIPMHWYDEYKHIGYDWDAKKIIKPPQGDQIDEFLRKIEDPDFWRTVKDPLTGQDVRLTDEDIALIKRIVSGRIPNKDHEEYEPWIEWFTSEVEKMPIKNVPDHKRSFLPSVSEKKRVSRMVHALKMGWMKTTEEVEREKQAKRGPKFYMLWETDTSREHMRRIHDPVSAPKRDLPGHAESYNPPPEYLFDAKETKEWLKLKDEPHKRKLHFMPQKFKSLREVPAYSRYLRERFLRCLDLYLCPRAKRVKLNIDAEYLIPKLPSPRDLQPFPTVESMVYRGHTDLVRSVSVEPKGEYLVSGSDDKTVKIWEIATGRCIRTIETDEVVRCVAWCPNPKLSIIAVATGNRLLLVNPKVGDKVLVKKTDDLLAEAPSQDVIESERIKTAVQWSNAEADEQEKGVRVVITHFKPIRQVTWHGRGDYLATVMPEGANRSALIHQLSKRRSQIPFSKSKGLIQFVLFHPVKPCFFVATQHNIRIYDLVKQELVKKLLTNSKWISGMSIHPKGDNLLVSTYDKKMLWFDLDLSTKPYQTMRLHRNAVRSVAFHLRYPLFASGSDDQAVIVSHGMVYNDLLQNPLIVPLKKLQTHEKRDEFGVLDVNWHPVQPWVFSTGADSTIRLYT
Protein: Flagellar hook-length control protein (P26416)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Controls the length of the flagellar hook.
Interaction partners:
- Basal-body rod modification protein FlgD
- Flagellar FliJ protein
- Peptidoglycan hydrolase FlgJ
- Flagellar M-ring protein
- Flagellar motor switch protein FliG
- Flagellar hook-basal body complex protein FliE
- Flagellar hook-associated protein 1
- Flagellar protein FliO
- Flagellar hook protein FlgE
- Flagellar assembly protein FliH
Sequence:
MITLPQLITTDTDMTAGLTSGKTTGSAEDFLALLAGALGADGAQGKDARITLADLQAAGGKLSKELLTQHGEPGQAVKLADLLAQKANATDETLTDLTQAQHLLSTLTPSLKTSALAALSKTAQHDEKTPALSDEDLASLSALFAMLPGQPVATPVAGETPAENHIALPSLLRGDMPSAPQEETHTLSFSEHEKGKTEASLARASDDRATGPALTPLVVAAAATSAKVEVDSPPAPVTHGAAMPTLSSATAQPLPVASAPVLSAPLGSHEWQQTFSQQVMLFTRQGQQSAQLRLHPEELGQVHISLKLDDNQAQLQMVSPHSHVRAALEAALPMLRTQLAESGIQLGQSSISSESFAGQQQSSSQQQSSRAQHTDAFGAEDDIALAAPASLQAAARGNGAVDIFA
Protein: mRNA cap guanine-N(7) methyltransferase (EC 2.1.1.56) (RG7MT1) (mRNA (guanine-N(7))-methyltransferase) (mRNA cap methyltransferase) (hCMT1) (hMet) (hcm1p) (O43148)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Subcellular location: Nucleus {ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:15767670}.
Interaction partners:
- RNA guanine-N7 methyltransferase activating subunit
- mRNA-capping enzyme
- RNA guanine-N7 methyltransferase-activating subunit-like protein
- Peripheral myelin protein 22
- Gap junction beta-1 protein
- Eukaryotic translation initiation factor 4E
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- Eukaryotic translation initiation factor 4E type 2
- Transcription elongation factor SPT5
Sequence:
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Protein: WW domain-binding protein 2 (WBP-2) (Q8R478)
Organism: Rattus norvegicus (Rat)
Function: Acts as transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation. In presence of estrogen, binds to ESR1-responsive promoters. Required for YAP1 coactivation function on PGR activity. Synergizes with WBP2 in enhancing PGR activity (By similarity). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q969T9}. Nucleus {ECO:0000250|UniProtKB:Q969T9}. Note=Translocates from cytoplasm to nucleus when phosphorylated. {ECO:0000250|UniProtKB:Q969T9}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Ubiquinol-cytochrome c reductase, complex III subunit X.
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Transcriptional coactivator YAP1
- WW domain-containing E3 ubiquitin protein ligase 2.
Sequence:
MALNKNHSEGGGVIVNNTESILMSYDHVELTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLSKGKDAMRSFMMPFYLMKDCEVKQPVFGANFIKGTVKAEAGGGWEGSASYKLTFTAGGAIEFGQQMLQVASQASRGEVPNGAYGYPYMPSGAYVFPPPVANGMYPCPPGYPYPPPPPEFYPGPPMMDGAMGYVQPPPPPYPGPMEPPVVSGPSAPPTPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQ
Protein: Lens fiber major intrinsic protein (Q4ZJI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Beaded filament structural protein 1.
- Beaded filament structural protein 2, phakinin
- Crystallin, gamma MX,-like 1
- Transporter
- Alpha-crystallin A chain
Sequence:
MWEFRSMMFWRAVFAEFFGTMFFVFFGMGAALRWTTGPYHVFHTALCFGFAAATLIQSIGHISGGHINPAVTFAYLVGSQMSVFRAFFYICAQCLGAMAGAAALYGVTPNNMRGTMALNTLQPGMSLGMATTVEVFLTMQLVVCVFAVTDERRNGRLGSAALSIGFSVTMGHLMGMYYTGAGMNPARSFAPAVITRNFINHWVYWVGPMIGAAMGAIFYDFFLFPRMRGFSERLATLKGSRPPEAENQQETRGEPIELKTQTL
Protein: Protein BTG2 (BTG family member 2) (NGF-inducible protein TIS21) (Q04211)
Organism: Mus musculus (Mouse)
Function: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors. Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth (By similarity).
Interaction partners:
- Protein arginine N-methyltransferase 1
- CCR4-NOT transcription complex subunit 7
- Homeobox protein Hox-B9
- CCR4-NOT transcription complex subunit 8
- Nuclear receptor subfamily 4 group A member 1
- CCR4-NOT transcription complex subunit 1
- Transcription factor Jun
- Dual specificity protein phosphatase 1
- Cyclic AMP-dependent transcription factor ATF-3
- Krueppel-like factor 6
Sequence:
MSHGKRTDMLPEIAAAVGFLSSLLRTRGCVSEQRLKVFSRALQDALTDHYKHHWFPEKPSKGSGYRCIRINHKMDPIISKVASQIGLSQPQLHRLLPSELTLWVDPYEVSYRIGEDGSICVLYEEAPVAASYGLLTCKNQMMLGRSSPSKNYVMAVSS
Protein: Senescence-associated carboxylesterase 101 (EC 3.1.1.1) (Q4F883)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyl hydrolase that triggers the leaf senescence onset. Can use triolein as substrate to produce oleic acids.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22072959}. Cytoplasm {ECO:0000269|PubMed:22072959}. Note=Can move to the cytoplasm when in complex with PAD4 and EDS1.
Interaction partners:
- Protein EDS1
- Lipase-like PAD4
- Toll/interleukin-1 receptor-like protein
- Alpha/beta-Hydrolases superfamily protein
- Disease resistance protein ADR1
- Isochorismate synthase 1, chloroplastic
- Disease resistance protein RRS1
- Regulatory protein NPR1
- Senescence associated gene 20
- Senescence-associated protein 13
Sequence:
MESSSSLKGSALGKLVVTSGLLHSSWSKILEIHNPPYSNHDPGLQVSKKKKDSGLEFQIHREEKFTLVVFSAPPICRSSSSDSTLLHVKDKENPFPFLCSENNPSFSLHTPAFNLFTSASTSLTYLKSELLQTLKSEKPVIITGAALGGSVASLYTLWLLETIEPTLKRPLCITFGSPLIGDASLQQILENSVRNSCFLHVVSAQTRIKMDFFKPFGTFLICFDSGCVCIEDHVAVTELLNGVHDSGLVDYSQVLNRLDQSMLSLADSRLIPEDVIKGIEKRAEMKNLRFDMMFKKLNDMKISMAYIEWYKKKCKEVKIGYYDRFKTQLAFPSKEFDINIKNHHKSELNRFWKSVVEEVERRPQSDASILKRRFLFSGNNYRRMIEPLDIAEYYLEGRKEYRTTGRSHHYVMLEKWFGMESILIEKERCKKRDLSDLLTFDSCFWAEVEDSLIVINQLNTTVGMRDDVREVLTRKLVEFEGYVWEIITKREVSPEIFLEESSFMKWWKEYKKIKGFNSSYLTEFMNTRKYESYGKSQ
Protein: Formin-binding protein 1 (Formin-binding protein 17) (hFBP17) (Q96RU3)
Organism: Homo sapiens (Human)
Function: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Actin nucleation-promoting factor WASL
- Formin-binding protein 1-like
- Cell division control protein 42 homolog
- Sequestosome-1
- Sorting nexin-2
- F-BAR domain only protein 1
- F-BAR domain only protein 2
- tRNA-splicing endonuclease subunit Sen2
- Dynamin-2
Sequence:
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS
Protein: Spindlin-4 (Q56A73)
Organism: Homo sapiens (Human)
Function: Exhibits H3K4me3-binding activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36927955}. Nucleus {ECO:0000269|PubMed:36927955}.
Interaction partners:
Sequence:
MSPPTVPPMGVDGVSAYLMKKRHTHRKQRRKPTFLTRRNIVGCRIQHGWKEGNEPVEQWKGTVLEQVSVKPTLYIIKYDGKDSVYGLELHRDKRVLALEILPERVPTPRIDSRLADSLIGKAVEHVFEGEHGTKDEWKGMVLARAPVMDTWFYITYEKDPVLYMYTLLDDYKDGDLRIIPDSNYYFPTAEQEPGEVVDSLVGKQVEHAKDDGSKRTGIFIHQVVAKPSVYFIKFDDDIHIYVYGLVKTP