wanglab/gogpt-training-data huggingface dataset:
Protein: Filamin A (A0A8I5Y6H8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSSHSRSGQSAAGASPAGGIDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVNNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGIGEVEVVIQDPTGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPTACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPTIPGTYTVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGIVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIREAPQDFHPDRVKARGPGLEKTGVAINKPAEFTVDAKHAGKAPLRVQVQDNEGHSVETTVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCTEAGQGDVSIGIKCAPGVVGPTEADIDFDIIRNDNDTFTVKYTPCGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLNRTGVELGKPTHFTVNAKTAGKGKLDVQFSGLAKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVSVTYGGDHIPKSPFSVGVSPSLDLSKIKVSGLVDKVDVGKDQEFTVKSKGAGGQGKVASKIVSPSGAAVPCKVEPGLGADNSVVRFVPREEGPYEVEVTYDGVPVPGSPFPVEAVAPTKPSKVKAFGPGLQGGNAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTDTYVQDCGDGTYKVEYTPYEEGVHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGSYSISVLYGEEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPTVQTPLRPQQLPSQYTYPQGSQQTWIPERPMVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPSITDNKDGTVTVRYSPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHITAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNDQHIPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGMHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFGIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGRFVGTAPNVDIQP
Protein: Epididymis secretory sperm binding protein (A0A384MTQ8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
Protein: RNA helicase (EC 3.6.4.13) (Q17978)
Organism: Caenorhabditis elegans
Interaction partners:
- MUTator
- MUTator
- PAP-associated domain-containing protein
- Exonuclease mut-7
- SH2 domain-containing protein
- RNA-directed RNA polymerase
- RNase NYN domain-containing protein
- Argonaute protein wago-1
- Zc3h12a-like Ribonuclease NYN domain-containing protein
- RNA helicase
Sequence:
MSYPWSNKNGEAASSSKTTVAPPLSPPRYEKVLDFSTLDTQRHRYEVRDQANQRAVVSSAKAESSMIDKFCKENTRIQTNPGIDLPDDYGTDAIVANAIGDQRIVNNLKCVHVTTFNAVQQMSIQVIREGRGLVVEAPTGIGKTYAFLIPAIEAALKNRQSNCFEYTKPSPSILIMASTSALVDQLFNRCELILGLQCMDNVEPIRDIKIDKLVANHPFTKGQCDIAFCTIGKLKATIECGDVCLDNLKTIILDEADKMIDNCAFGPDINWILDQLKEENLENLQSCFFSATYNKNANGTIALTVLQMRMLGEDDPWSVIICPRMSGYITQRVVRVGRGRPNDIRSHPWVIKMGIIRKLIDDDLKETGCSKDGPYNETIAIFCETVQRVTQVTMALRQLGYNFKPVCSMITKNQQLVTVNDLEFRKIHGVVCTNILARGIDVSSVKHTIIMEMSADFDTYKHRIGRVGRDGCGGKSTVLVEHHQLQGGPASNVIEQLYNFMKESKEDIPQWMQEWIVARRNNNIDSWA
Protein: Protein WHAT'S THIS FACTOR 1, chloroplastic (B6TTV8)
Organism: Zea mays (Maize)
Function: RNA-binding protein involved in the chloroplastic group II intron splicing. Binds specific group II introns and promotes their splicing. Functions in the context of a heterodimer with the ribonuclease III domain-containing protein RNC1.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19251672}.
Interaction partners:
- Ribonuclease III domain-containing protein RNC1, chloroplastic
- CRM-domain containing factor CFM3, chloroplastic/mitochondrial
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- CRS2-associated factor 2, chloroplastic
- PORR domain-containing protein
- Tha8
- Uncharacterized protein
- Chloroplast RNA splicing2
Sequence:
MDAKLLLPFPFAPAAATRSPKSLFLGAPLPPPPRPPPFPLRLRPRPAAVVAQAAVKRRKEAPFDTVIQRDKKLKLVLKLRNILVAQPDRVMSLRELGRFRRDLGLTRKRRLIALLRRFPGVFDVVEEGVYSLRFRLTPAAERLYLDELRLRNESEGLAVAKLRKLLMMSQEKRILIEKVAHLKHDLGLPPEFRDTVCLRYPQYFRVVRMDRGPALELTHWDPELAVSAAELAEEESRAREAEERNLIIDRPLKFNRVRLPKGLKLTRGEARRIARFKEMPYISPYADFSHLRSGSDEKEKHACGVVHEILSLTVEKRTLVDHLTHFREEFRFSQSLRGMIIRHPDMFYVSFKGDRDSVFLREAYKDSQLVEKNQLVLLKEKMRALVAVPRFPRRAAVGTGEEAEGMNGSLQSRDQVSDEEYDDEDEGLSDMEDLISELSGGKSDADYEWGDGWFGENDDSPPDFGDDEVKVAMKIADGSANGSAPVPVFPDGRPRERW
Protein: FI17352p1 (Varicose, isoform B) (Q7KT16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein lin-7 homolog
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- Trifunctional purine biosynthetic protein adenosine-3
- X11L, isoform F
- X11Lbeta, isoform A
Sequence:
MVRWSARSRRQARQDKVELLARNNKVNGEDDTSDNAAFRNSTDLSDHDEIFLKGLLRSNSNTPHKELMLNPTEPQPVPLFLPAHLNNKPICDDIIRKFSPSRRLESRELAKLLAQPHFRALLRAHDEIGALYEQRLKAAGGSTSQLEIASQRQTGGYLFTEDVLNTKMPVETIKMVGLRRDPSKPLGLTVELDEFKQLVVARILAGGVIDKQSMLHVGDVILEVNGTPVRTPDELQVEVSRAKENLTLKIGPNVDEEIKSGRYTVSGGQVKQNGIASLETGKKLTCYMRALFTYNPSEDSLLPCRDIGLPFKSGDILQIINVKDPNWWQAKNITAESDKIGLIPSQELEERRKAFVAPEADYVHKIGICGTRISKRKRKTMYRSVANCEFDKAELLLYEEVTRMPPFRRKTLVLIGVSGVGRRTLKNRLINSDVDKFGAVIPHTSRPKRALEENGSSYWFMDREEMEEAVRNNEFLEYGEHNGNLYGTHLQSIKDVINSGRMCILDCAPNALKILHNSQELMPFVIFVAAPGMEQLKTIYADRRATGSNRNLSFDRQSSIRFSSRRARTLESLASLYEDDDLVATVEESSFVQRKYEKYFDMVIVNEDFDETFRQVVETLDQMSHEEQWVPVNWIY
Protein: Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2) (O54902)
Organism: Rattus norvegicus (Rat)
Function: Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1. Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells (By similarity). Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense. Can mediate uncoupled fluxes of either protons or metal ions.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:24448823}; Multi-pass membrane protein {ECO:0000255}. Extracellular vesicle membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49281}.
Interaction partners:
- Ferroportin
- Hepcidin
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Transferrin receptor protein 1
- Natural resistance-associated macrophage protein 1
- Metal cation symporter ZIP14
- Cytoplasmic aconitate hydratase
- Iron-responsive element-binding protein 2
- Solute carrier family 40 protein
- Metalloreductase STEAP3
Sequence:
MVLDPEEKIPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLYGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLRGMFVPSCSGCHTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNEQVVEVCRNSSSPHADLFPNDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLLVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGLSFLDCGRSYHLGLTARPEIYLLNTVDAVSLVSR
Protein: Polyamine oxidase 2 (AtPAO2) (EC 1.5.3.-) (Amine oxidase 1) (Q9SKX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives. Substrate preference is N(1)-acetylspermine > spermine > spermidine. Plays an important role in the regulation of polyamine intracellular concentration (Probable). Involved in abscisic acid-mediated developmental processes. May contribute to nitric oxide-mediated effects on root growth.
Subcellular location: Peroxisome {ECO:0000269|PubMed:18703589}.
Interaction partners:
- Spermine synthase
- Spermidine synthase 2
- Spermidine synthase 1
- N-carbamoylputrescine amidase
- Probable polyamine oxidase 5
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 3 member F1
- Polyamine oxidase 1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MESRKNSDRQMRRANCFSAGERMKTRSPSVIVIGGGFGGISAARTLQDASFQVMVLESRDRIGGRVHTDYSFGFPVDLGASWLHGVCKENPLAPVIGRLGLPLYRTSGDNSVLYDHDLESYALFDMDGNQVPQELVTQIGVTFERILEEINKVRDEQDADISISQAFSIVFSRKPELRLEGLAHNVLQWYVCRMEGWFAADAETISAKCWDQEELLPGGHGLMVRGYRPVINTLAKGLDIRVGHRVTKIVRRYNGVKVTTENGQTFVADAAVIAVPLGVLKSGTIKFEPKLPEWKQEAINDLGVGIENKIILHFEKVFWPKVEFLGVVAETSYGCSYFLNLHKATGHPVLVYMPAGQLAKDIEKMSDEAAANFAVLQLQRILPDALPPVQYLVSRWGSDVNSMGSYSYDIVGKPHDLYERLRVPVDNLFFAGEATSSSFPGSVHGAYSTGLMAAEDCRMRVLERYGELDLFQPVMGEEGPASVPLLISRL
Protein: Probable histone H2A variant 2 (H2A.F/Z 2) (HTA8) (Q9SII0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. May replace conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- SWR1 complex subunit 2
- Histone H4
- SWR1 complex subunit 6
- SWR1-complex protein 4
- RuvB-like protein 1
- Histone H2B.6
- Transcription initiation factor TFIID subunit 14b
- Transcription initiation factor TFIID subunit 14
- Putative high mobility group B protein 11
Sequence:
MAGKGGKGLLAAKTTAAAANKDSVKKKSISRSSRAGIQFPVGRIHRQLKQRVSAHGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLVNKVTKD
Protein: Melanocyte inducing transcription factor a isoform 1 (Melanocyte-inducing transcription factor a) (Microphthalmia-associated transcription factor a) (Microphthalmia-related protein) (Q9PWC2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitochondrial inner membrane protein Mpv17
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Dopachrome tautomerase.
- Tyrosinase.
- Mitogen-activated protein kinase
- Melanocyte-inducing transcription factor b
- Mitogen-activated protein kinase
- Transcription factor SOX-10
- Melanocyte-stimulating hormone receptor
Sequence:
MLEMLEYSHYQVQTHLETPSKYHIQQSQRQQVKHYLSSALGAKLSPQASTGPGPSQPAEHGMTPGPGASAPNSPMALLTLNCEKEMDDVIEDIISLESSYSDDILGFMDAGLQMTNTIPVSANLLDMYSNHALPPAGVSISNSCPSSLPAVKRELSVTPSPGMMHIMDKAGPCGKFDSYQRPDGFPVEAEVRALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQKEQQKAKELENRQKRLEHANRHLLLRIQELEMQARAHGLTVVASSSLYSAELVARAIKQEPGMGDCTSNLYPHLPSPDMSRPTTLDLNNGTISYNDSPTEDGEPGVYDSPNKASTKLEDMLMDNTLSPVGSSDPLLSSGSPVPSNSSGSSSMDEHDNGC
Protein: Achaete-scute homolog 5 (Achaete-scute family bHLH transcription factor 5) (M0QWB7)
Organism: Mus musculus (Mouse)
Function: Transcription factor. Probably binds E-box motifs 5'-CANNTG-3' in complex with transcription factor TCF3/E12. Negatively modulates transcription of target genes such as CDH1/E-cadherin, perhaps by recruiting the PRC2 repressive complex to regulatory elements. Regulates ameloblast development and tooth germ growth, perhaps acting by positively modulating migration of inner enamel epithelium (IEE) cells. Plays a role in enamel formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MNSNFCRALVDRGPPGGMQLGVVAPAGQTPLAATEPLSNVPFLLYPGHSEPPYYDAYTGVFPYVPFPGAFGVYDYPFEPAFIQKRNERERQRVKCVNEGYARLRGHLPGALTEKRLSKVETLRAAIRYIKYLQELLSATPDGAPPPATSPPPAHTGHSNVPQPSSLVAESSGSPFSSSPFLESEEPSL
Protein: Transcriptional activator protein LasR (P25084)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Transcriptional activator of elastase structural gene (LasB). Binds to the PAI autoinducer.
Interaction partners:
- Acyl-homoserine-lactone synthase
- Acyl-homoserine-lactone synthase
- Regulatory protein RsaL
- Response regulator GacA
- LasR-specific antiactivator QslA domain-containing protein
- cAMP-activated global transcriptional regulator Vfr
- Protease LasA
- Multiple virulence factor regulator MvfR
- Elastase
- 2-heptyl-3-hydroxy-4
Sequence:
MALVDGFLELERSSGKLEWSAILQKMASDLGFSKILFGLLPKDSQDYENAFIVGNYPAAWREHYDRAGYARVDPTVSHCTQSVLPIFWEPSIYQTRKQHEFFEEASAAGLVYGLTMPLHGARGELGALSLSVEAENRAEANRFMESVLPTLWMLKDYALQSGAGLAFEHPVSKPVVLTSREKEVLQWCAIGKTSWEISVICNCSEANVNFHMGNIRRKFGVTSRRVAAIMAVNLGLITL
Protein: TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) (P36897)
Organism: Homo sapiens (Human)
Function: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21791611, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:9472030}; Single-pass type I membrane protein {ECO:0000269|PubMed:9472030}. Cell junction, tight junction {ECO:0000269|PubMed:15761148}. Cell surface {ECO:0000269|PubMed:25893292}. Membrane raft {ECO:0000269|PubMed:25893292}.
Interaction partners:
- Activin receptor type-2B
- TGF-beta receptor type-2
- E3 ubiquitin-protein ligase SMURF2
- Peptidyl-prolyl cis-trans isomerase FKBP1A
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 2
- Growth/differentiation factor 8
- Mothers against decapentaplegic homolog 3
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
Sequence:
MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM
Protein: SID1 transmembrane family member 2 (Q8NBJ9)
Organism: Homo sapiens (Human)
Function: Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. Involved in the uptake of single-stranded oligonucleotides by living cells, a process called gymnosis. In vitro, mediates the uptake of linear DNA more efficiently than that of circular DNA, but exhibits similar uptake efficacy toward RNA and DNA. Binds long double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than 100 bp (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:28277980}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319}. Cell membrane {ECO:0000269|PubMed:28277980}. Note=Mainly localizes to lysosomes and only partly to the plasma membrane (PubMed:28277980). Lysosomal localization is required for SIDT2-mediated intracellular degradation of endogenous RNA (By similarity). {ECO:0000250|UniProtKB:Q8CIF6, ECO:0000269|PubMed:28277980}.
Interaction partners:
Sequence:
MFALGLPFLVLLVASVESHLGVLGPKNVSQKDAEFERTYVDEVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGMFQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVSRMDDFVLRTGEQFSFNTTAAQPQYFKYEFPEGVDSVIVKVTSNKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFAEDEPVDQGHRQKTLSVLVSQAVTSEAYVSGMLFCLGIFLSFYLLTVLLACWENWRQKKKTLLVAIDRACPESGHPRVLADSFPGSSPYEGYNYGSFENVSGSTDGLVDSAGTGDLSYGYQGRSFEPVGTRPRVDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLYVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLCALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSIIHIIATLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYVDRMVLLVMGNVINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVLLTLDDDLDTVQRDKIYVF
Protein: Pyridoxal 5'-phosphate synthase subunit PDX2 (PfPDX2) (EC 4.3.3.6) (Pyridoxal 5'-phosphate synthase glutaminase subunit) (EC 3.5.1.2) (Q8IIK4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of Pdx1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16339145}.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit Pdx1
- pyridoxal kinase
- transketolase
- ribose-phosphate diphosphokinase
- NAD
- ribose-phosphate diphosphokinase
- Phosphoglucomutase, putative
- Ribose-5-phosphate isomerase
- Glutamine synthetase, putative
- GMP synthase
Sequence:
MSEITIGVLSLQGDFEPHINHFIKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENDTLYNALVHFIHVLKKPIWGTCAGCILLSKNVENIKLYSNFGNKFSFGGLDITICRNFYGSQNDSFICSLNIISDSSAFKKDLTAACIRAPYIREILSDEVKVLATFSHESYGPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVKNYKYS
Protein: ACB domain-containing protein (Q386F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- BTB domain-containing protein
Sequence:
MKGNKGANIAYPDKYHKVTEFFDREYGDLETCTKLNDCQKLLFYALRQQVEHGPCTSGAPFIWQVRERAKHDAWKQLGAMTKFEAMVHFVTHLEECIGGNVDWGEKLRDLNGMRDQQRVGVENGTGESNANEQTERGVSEAHWDADVQAHLQPSAENIEYLAREVMRLRGELQQVRPNRVVPTPIVVPPRKPIDYVSTKNIVPPARTLATVATRTALLNAQTTNNLVERQPQGWGEWFGLI
Protein: LD15470p (Transforming acidic coiled-coil protein, isoform C) (Q95TU9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDFLANIIKRPKSIATTGISTNQPTTMEALEAASPADECSTPRDKGGVTLVSAHLDSLLESASEELQRLEGKHCELFMESISNPLPAPEDSTDSREEIQKFLSEINFNLNQVSANEMEHLQAMSGELSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEDRHLMQTHILSVTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKIIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFDSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVVQPTKEEEEAKSRRTFCMENENPRRTFCMQQNASPAVEATEDTGADEVMDVDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEQTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNRSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: Pentalenolactone D synthase (EC 1.14.13.170) (Pentalenolactone biosynthesis protein E) (E3VWI7)
Organism: Streptomyces arenae
Function: Catalyzes the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid to pentalenolactone D in the biosynthesis of pentalenolactone antibiotic.
Interaction partners:
Sequence:
MDLEAVREKYRQERDKRGVGRTYQFARGDFSRYARDPYTERREREPLTDEVDVAVVGAGIGGLLTGARLREETGLERIRLIDEAGDVGGTWYWNRFPGVRCDVESYVYMPLLEEIGTIPTEKYSTGPEIFAHLQRIAHRYGLYRDALFQTTVTELRWDEAAARWLVSTDRGDLFRARYVAMSIGLMHRPKLPGLPGLETFAGHSFHTSRWDFGYTGGDSTGGLTGLKDKRVGVIGTGSTTVQLAPHLAEWAERLYIFQRTPAAVDVRGNRPTPPGWADGLDAGWQQRRMENFHALTSGIPQDEDLVQDRWTQTTAELATAILPTGDTGGDPKERALAAERADFRKMEELRARIDSVVTDPATAAALKPYYRVYCKRPCFHDGYLQTFNRPNVTLVDTQGQGVERLTASGVVANGREYPVDCLIFATGYEHEFAVPYTERAGYDIVGRGGVRLSEKWAQGAHTLHGLQVHGFPNCFILSKVQAGRHVNIAYMLGEQTRHLAHIVKCVEERGHRVVEASEAGEKEWVEEILRLASGDLDFLENCTPGLYNNEGDPGGLPLLNSSYGGGSVEFVNILRRWREAGDLAGLELR
Protein: Turgencin-A (C0HLN5)
Organism: Synoicum turgens (Colonial ascidian)
Function: Has antimicrobial activity against Gram-positive bacteria (C.glutamicum ATCC 13032 (MIC=0.4 uM), B.subtilis ATCC 23857 (MIC=0.4 uM) and S.aureus ATCC 9144 (MIC=6.3 uM)) and Gram-negative bacteria (E.coli ATCC 25922 (MIC=0.8 uM) and P.aeruginosa ATCC 27853 (MIC=1.6 uM)).
Subcellular location: Secreted {ECO:0000269|PubMed:31940927}.
Interaction partners:
Sequence:
GPKTKAACKMACKLATCGKKPGGWKCKLCELGCDAV