wanglab/gogpt-training-data huggingface dataset:
Protein: Deoxyribodipyrimidine photo-lyase, mitochondrial (EC 4.1.99.3) (DNA photolyase) (Photoreactivating enzyme) (P05066)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Subcellular location: Nucleus. Mitochondrion.
Interaction partners:
- 1,3-beta-glucanosyltransferase GAS1
- 1,3-beta-glucanosyltransferase GAS2
- 1,3-beta-glucanosyltransferase GAS5
- 1,3-beta-glucanosyltransferase GAS4
- Probable 1,3-beta-glucanosyltransferase GAS3
- Casein kinase I homolog HRR25
- DNA damage-responsive transcriptional repressor RPH1
- Uncharacterized protein YOR385W
Sequence:
MKRTVISSSNAYASKRSRLDIEHDFEQYHSLNKKYYPRPITRTGANQFNNKSRAKPMEIVEKLQKKQKTSFENVSTVMHWFRNDLRLYDNVGLYKSVALFQQLRQKNAKAKLYAVYVINEDDWRAHMDSGWKLMFIMGALKNLQQSLAELHIPLLLWEFHTPKSTLSNSKEFVEFFKEKCMNVSSGTGTIITANIEYQTDELYRDIRLLENEDHRLQLKYYHDSCIVAPGLITTDRGTNYSVFTPWYKKWVLYVNNYKKSTSEICHLHIIEPLKYNETFELKPFQYSLPDEFLQYIPKSKWCLPDVSEEAALSRLKDFLGTKSSKYNNEKDMLYLGGTSGLSVYITTGRISTRLIVNQAFQSCNGQIMSKALKDNSSTQNFIKEVAWRDFYRHCMCNWPYTSMGMPYRLDTLDIKWENNPVAFEKWCTGNTGIPIVDAIMRKLLYTGYINNRSRMITASFLSKNLLIDWRWGERWFMKHLIDGDSSSNVGGWGFCSSTGIDAQPYFRVFNMDIQAKKYDPQMIFVKQWVPELISSENKRPENYPKPLVDLKHSRERALKVYKDAM
Protein: Uncharacterized protein (E7DN73)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MKKVQTYQEYLKLVEFKRQLSLNLREGKIGVDEAVIQLFTFYSFNNIEEPPFIVLKMQEAAVNGTYEAKLNMLKRFKII
Protein: Leucine-rich repeat-containing protein 41 (Protein Muf1) (Q8K1C9)
Organism: Mus musculus (Mouse)
Function: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-5
- Rho-related BTB domain-containing protein 3
Sequence:
MAAPEAWRARSCWFCEVAAATTMEATSREAAPAKSSASGPSAPPALFELCGRAVSAHMGVLESGVWALPGPILQSILPLLNIYYLERIEETALKKGLSTQAIWRRLWDELMKTRPSSLESVTCWRAKFMEAFFSHVLRGTIDVSSDKRLCDQRFSPLLHSSRHVRQLTICNMLQGATELVAEPNRRVLETLASSLHTLKFRHLLFSDVAAQQSLRQLLHQLIHHGAVSQVSLYSWPVPESALFILILTMSAGFWQPGPGSLPCRLCGEASRGRAPSRDEGSLLLGSRRPRRDAAERCAAALMATRRKSEVKQMPRAVPPTRVTRRSTQESLAIGGTDSKLYLPATSYEASGTKQPSAPAAASASSSTSSKRAPASSASQPKPLKRFKRAAGKKGPRTRQGSGAESEDLYDFVFIVAGEKEDGEEMEIGEVACGALDGSDPSCLGLPALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWVSLESLTLSYNGLGSNIFRLLDSLRALSGQAGCRLRALHLSDLFSPLPILELTRAIVRALPLLRVLSIRVDHPSQRDNPAVPENAGPPGHIVGDEEIPENCLEQLEMGFPRGAQPAPLLCSVLKASGSLQQLSLDSATFASPQDFGLVLQTLKEHNLSLKRLSFHDMNLADCQSEVLFLLKNLTLQEITFSFCRLFEKRPVQFLPEMVAAMKGNSTLKGLRLPGNRLGNAGLLALADVFSEDSSSSLCQLDISSNCIKPDGLLEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRATCHVVSDSWDSTQAFADYVSTM
Protein: Indoleamine 2,3-dioxygenase 1 (IDO-1) (EC 1.13.11.52) (Indoleamine-pyrrole 2,3-dioxygenase) (P14902)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P28776, ECO:0000303|PubMed:25691885}.
Interaction partners:
- Tryptophan 2,3-dioxygenase
- Kynureninase
- Kynurenine formamidase
- Tryptophan 5-hydroxylase 1
- Tryptophan 5-hydroxylase 2
- Cytochrome P450 1A1
- L-amino-acid oxidase
- Amine oxidase [flavin-containing] A
- Cytochrome P450 1B1
- Amine oxidase [flavin-containing] B
Sequence:
MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
Protein: General negative regulator of transcription subunit 3 (O13870)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000305|PubMed:16823372}.
Interaction partners:
- Poly
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 1
- Cell differentiation protein rcd1
- General negative regulator of transcription subunit 2
- Putative general negative regulator of transcription C16C9.04c
- Putative ATP-dependent RNA helicase ste13
- ABC transporter domain-containing protein C20G4.01
- Deadenylation-dependent mRNA-decapping factor pdc2
- Mitochondrial division protein 1
Sequence:
MSARKLQVEIEKTFKKVTDGIAIFDEVYEKLSASNSVSQKEKLEGDLKTQIKKLQRLRDQIKTWASSNDIKDKKALLENRRLIEAKMEEFKAVEREMKIKAFSKEGLSIASKLDPKEKEKQDTIQWISNAVEELERQAELIEAEAESLKATFKRGKKDLSKLSHLSELESRIERHKWHQDKLELIMRRLENSQISPEAVNDIQEDIMYYVECSQSEDFAEDENLYDELNLDEASASYDAERSGRSSSSSHSPSPSASSSSSSENLLQDKAEAEEKVSADASVQDIAEKESLDADKELATNDQEDDEEENQAETQKDGAISNNENMQSEVQTTNPSASTSAVTNITKPTLIQNPSTPLSVSNSKVASPETPNATHTAPKVEMRYASAAAAAAAALAKESPSHHYIMQQVRPETPNSPRLNSTVIQSKWDSLGHTASPKMQTQPVRSVSQSSATTETNVKPTKEENADVPVSSPDYLKDLVNALNTSKEQHKGAIDKEKLTEALNISCVYVPDATDAAKPQYYIPKDPYPVPHYYPQQPLPLFDSSEMTELVDPDTLFYMFYYRPGTYQQYIAGQELKKQSWRFHKKYTTWFQRHEEPKMITDEFESGSYRYFDFEGDWVQRKKADFRFTYQYLEDDDDWTR
Protein: UBQ, helicase-c and DEAD-like helicase domain-containing protein (F4K9K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MENERRSGGGDSVPISVRSINGESTTVQVSSDGTIRDLKKALKSCFPPASSSSNFHLYIKGEKLKLDTRVAAITINDGDILGLFPFKKKELRQTPKPDLSKPSSLSSRTSTMKDENAKRAEDHCVGEKRKRDEEACPYGFFNDDLESECKDAFKGQNTEKLAEVLKSRNCLTSPGSTKCLMSWDSSSSLCSCPDWESLSRLAMSGVRVRIQDVKNLSVICPKVITDDYEAVNYENAIVIADYLEMDEKSGRKKIPLAKLFSAMKKREASFKSDFWESIRSLLNKNTGESGIAISLEGLLKFASEGRADGGNEARQAGKGTCPTSGSRKFQTLCHATNSLLPSEMVEHLRNGIGSKGQVVHVEVIKARKSAYVEMSDKLSETTKSALKRIGLNTLYSHQAEAISAALAGKNVAVATMTSSGKSLCYNVPVFEELCKDTNSCALYLFPTKALAQDQLRALSDLIKGFEASINMGVYDGDTPYKDRTRLRSNARLLITNPDMLHISILRRHKEQFSRILSNLRYIVIDEAHIYKGPFGCHMALILRRLRRLCSHVYGVNPSFIFCTATSANPREHCMELANLSELELVTIDGSPSSEKLFVLWNPSAPPTSKSEKSSKVVSSSEAAADKPSGAAVDTLSGPASEVSHLFAEMVQHGLRCIAFCPSRKLCELVLCLTREILAETAPHLVEAITSYRGGYIAEDRRKIESDLFGGKLCGIAATNALELGIDVGHIDVTLHLGFPGSIASLWQQAGRSGRRQKPSLAVYVAFLGPLDQYYMSFPDKLFGSPIECCHIDSQNKHVLMQHLACAALEHPLSLQYDQQHFGSGLSDPLAELRNKGFLSFDPSRDSSSRIWNYIGREKNPARIVSIRAIETVRYRVMEKKSKDVLDEIEESKAFFHVYEGAIYMNQGRNYLVTSLDIKEKVALCELVNVDYYTRTRDYTDIKVTGGDTAYPVKAPKKPTPQTHACRVTTKWFGFLRIRRRNNEVIDDVELSLPSYTYQSQAVWIQVPMSVKLAVETANLPFRAGLHAACHALVNVVPTRVTCNYSDIAPECPNPQEQRYFPARILVYDRHPGGTGISAKICPLFFELLKDARDLLRSCEKCPPETGCPKCAQTFGCRGYNELLHKKAAIMIMQGVLDAKED
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain) (A8MTJ3)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8015379}. Note=Dual distribution pattern; plasmalemmal pattern with apical region localization and cytosolic pattern with localization throughout the cytoplasm.
Interaction partners:
- Taste receptor type 1 member 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Taste receptor type 1 member 2
- Taste receptor type 1 member 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Taste receptor type 2 member 38
- Taste receptor type 2 member 4
- Taste receptor type 2 member 46
- Taste receptor type 2 member 10
Sequence:
MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Cellular retinoic acid-binding protein 1 (Cellular retinoic acid-binding protein I) (CRABP-I) (P62964)
Organism: Bos taurus (Bovine)
Function: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Retinoic acid receptor beta
- Voltage-dependent T-type calcium channel subunit alpha
Sequence:
MPNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCRSLPTWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE
Protein: Kelch domain-containing protein 7B (Q96G42)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVLRSHPFPRQDRPQGSVPRAVPGSPVGPSTSTHSEDRHGPSSSVGTVIGTGTGGLVEAGGQPQPRSSETNGSPSPDPPPGLRGEGTREKSLDPLPQAAMPRGPAQPPAQRPPGPAASSSARRSQPVPQLRKRSRCEIAPSSEQEVRPAASGDPQGEAPGEGGSPAGRSGALTEKQEEARKLMVFLQRPGGWGVVEGPRKPSSRALEPATAAALRRRLDLGSCLDVLAFAQQHGEPGLAQETYALMSDNLLRVLGDPCLYRRLSAADRERILSLRTGRGRAVLGVLVLPSLYQGGRSGLPRGPRGEEPPAAAPVSLPLPAHLHVFNPRENTWRPLTQVPEEAPLRGCGLCTMHNYLFLAGGIRGSGAKAVCSNEVFCYNPLTNIWSQVRPMQQARAQLKLVALDGLLYAIGGECLYSMECYDPRTDAWTPRAPLPAGTFPVAHEAVACRGDIYVTGGHLFYRLLRYSPVKDAWDECPYSASHRRSSDIVALGGFLYRFDLLRGVGAAVMRYNTVTGSWSRAASLPLPAPAPLHCTTLGNTIYCLNPQVTATFTVSGGTAQFQAKELQPFPLGSTGVLSPFILTLPPEDRLQTSL
Protein: RTX-I toxin-activating lysine-acyltransferase ApxIC (EC 2.3.1.-) (APX-IC) (Cytolysin IC) (CLY-IC) (HLY-IC) (RTX-I toxin determinant C) (Toxin RTX-I-activating protein C) (P55132)
Organism: Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)
Function: Protein-lysine acyltransferase that catalyzes fatty acylation of the protoxin, thereby converting it to the active toxin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSKKINGFEVLGEVAWLWASSPLHRKWPLSLLAINVLPAIESNQYVLLKRDGFPIAFCSWANLNLENEIKYLDDVASLVADDWTSGDRRWFIDWIAPFGDSAALYKHMRDNFPNELFRAIRVDPDSRVGKISEFHGGKIDKKLASKIFQQYHFELMSELKNKQNFKFSLVNS
Protein: Myomesin and myosin binding protein (Q9VZT8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGNQPGKLHTHPQGGRPKKNVHWKSAERPSPPGRPILTPVALPEQQPDVVNLRWDRPLHDGGSPITGYTVEHRRMGSPHWVRATPTPVDRCDVCISGLEPGWRYQFRCFAENIVGRSDASELSDPLTVTLQRNAITVPRFIDELVDTNAVEDERIEFRVRILGEPPPEINWFKDGYEIFSSRRTKIVNDNEASVLVIHQVALTDEGEIKCTATNRAGHVITKARLMVQAPPKIRLPRTYEDGLIVEADEVLRLKVGVAGQPPPAITWLHEGEVIAPGGRFEVSNTEKNSLLKIDNVLREDRGEYMVKAWNRLGEDSTSFLVTVTARPNPPGTPKLNMSFGKSATLSWTAPLDDGGCKIGNYIVEYFRVGWNVWLKAATTRALSTTLHDLIEGSEYKFRVKAENPYGLSEPSGESELLFIPDPKRGITKPKSATRIAGDEKDKPKTGAGGMQVPPRRKTLSPPRPQADASTGMSPKQSPSAKRKPKPQLIDNEQLTHEMSYGTSDHALKMDVRKSPSLNSADSANKPTTDSSNPKLNLTLVTTTLAPLDKSVPSPKAPRTPATSPLKLFNPKPSGAPKDRSPVQPKPQPLPTPPMETPDKASPNPKRSLSPPNKRQPPPLRKSPTPPEPIKVTPALLRSAEPVQLGVNQNVRRFSGQTLSPARNVPTLALAVASGVSAVIGEKLPTIEISAPPTPQEEEPPVLERSPSPEPAPKSQSNARRFSRSADKHDDVHTSNEFMLVVFDKNSKVKDKDKQDSFELDLEDAIQPPPISISAPDLAFLEFTNLHTTFPLRRSVSSTELLYERAMARFYEAVELEQASKSRKTSRDKLVTPVPHQTPANLRKRLGSISEAERLSFERRSEMRRQSADVVSISRKWDSRENVNEMGNLTRIHTTGQLPFETRKDLRESEAEEEHEEGEEEHLTESTADDSEDMDLDYDEDLDVDYPPQKKLQQQSSNDLGSDYTESTASSEQDSIEKFKMELLARTRSPSPRDLETYHPRTMGAGTFTPYRAPTPEQAAVVLNRPVPLPSPDFVPKPILKRSSNEHMEQAVSPLPSSFASEAPTIIVPPTATVANSNPSTLKMDLAKGIKSFFSRDKRSATEKNTEANEEISNPLERTNAAAIAADLEVKRKAKEEEELRRKEEERLMQEEAHAAVDHYSDLVKEVGSSHKYHTPLYLDRDELKRAAAKAAAETDEEDMLTHAEELKKRRATGGSEDLFLAPPVVRERRLSISEREQLVHVRDAASSLAFHRSPEKPESDQEHESPKSQQDEEPEYPTVLVVPPPKSKNKNESETESVMSEMVEARPDARGRTRLVKVKRVIRRRVPSSTRSRDASLTRPAIAEVEGSQQTSLVLSAADRDLLQKAATLAILQSEEQAHEKVRSALSYCTDLVLFLVACYVYLFKDARLVLPILGLIIYRQLGEAVRGYVPGWLRRRFTGNGS
Protein: WD repeat and SOCS box-containing protein 1 (WSB-1) (SOCS box-containing WD protein SWiP-1) (Q9Y6I7)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes type II iodothyronine deiodinase/DIO2. Confers constitutive instability to HIPK2 through proteasomal degradation.
Interaction partners:
- Cullin-5
- Elongin-B
- Elongin-C
- Type II iodothyronine deiodinase
- E3 ubiquitin-protein ligase RBX1
- Transcriptional repressor CTCF
- RING-box protein 2
- Homeodomain-interacting protein kinase 2
- Neurofibromin
- Ubiquitin carboxyl-terminal hydrolase 33
Sequence:
MASFPPRVNEKEIVRLRTIGELLAPAAPFDKKCGRENWTVAFAPDGSYFAWSQGHRTVKLVPWSQCLQNFLLHGTKNVTNSSSLRLPRQNSDGGQKNKPREHIIDCGDIVWSLAFGSSVPEKQSRCVNIEWHRFRFGQDQLLLATGLNNGRIKIWDVYTGKLLLNLVDHTEVVRDLTFAPDGSLILVSASRDKTLRVWDLKDDGNMMKVLRGHQNWVYSCAFSPDSSMLCSVGASKAVFLWNMDKYTMIRKLEGHHHDVVACDFSPDGALLATASYDTRVYIWDPHNGDILMEFGHLFPPPTPIFAGGANDRWVRSVSFSHDGLHVASLADDKMVRFWRIDEDYPVQVAPLSNGLCCAFSTDGSVLAAGTHDGSVYFWATPRQVPSLQHLCRMSIRRVMPTQEVQELPIPSKLLEFLSYRI
Protein: Protein c-Fos (Cellular oncogene fos) (Fos proto-oncogene, AP-1 transcription factor subunit) (G0/G1 switch regulatory protein 7) (Proto-oncogene c-Fos) (Transcription factor AP-1 subunit c-Fos) (P01100)
Organism: Homo sapiens (Human)
Function: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.
Subcellular location: Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30.
Interaction partners:
- Protein FosB
- Transcription factor JunD
- Transcription factor Jun
- Transcription factor JunB
- Estrogen receptor
- Transcription factor Maf
- Nuclear factor of activated T-cells, cytoplasmic 2
- Fos-related antigen 2
- Cyclic AMP-responsive element-binding protein 1
- Fos-related antigen 1
Sequence:
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
Protein: Small ribosomal subunit protein mS77 (rPPR2) (Protein NUCLEAR FUSION DEFECTIVE 5, mitochondrial) (Q8LEZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus.
Subcellular location: Mitochondrion {ECO:0000303|PubMed:36423343, ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g19525
- Alba DNA/RNA-binding protein
- DEAD-box ATP-dependent RNA helicase 32
- Pentatricopeptide repeat-containing protein At1g15480
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- UBP1-associated proteins 1B
- Pentatricopeptide repeat-containing protein At3g02490
- Pentatricopeptide repeat-containing protein At4g02820
- rRNA
- Polynucleotidyl transferase, ribonuclease H-like superfamily protein
Sequence:
MKSFLLSRQAIHRISLLSSKTPTFCRNFSAITSTISHSDRHLRSYDEQTPFQNVEIPRPISSFNRYFHFTRESRLSESSAAIDDSNDQEEDDEDGTTNEFLSRFVWIMRGKVSEAYPDCDKKMIDGMLLLIVEKVVEEIERGGFNKVGSAPPSPSSEFSDDLWATIWEVSNTVLKDMEKERKKEKMKQYVQSPEVMEMCRFAGEIGIRGDLLRELRFKWAREKMDDAEFYESLEQQRDLDNSIRESETVDGEVEEEGFVPSDEVESRSISLPKRKGKLKYKIYGLELSDPKWVEMADKIHEAEEEADWREPKPVTGKCKLVMEKLESLQEGDDPSGLLAEWAELLEPNRVDWIALINQLREGNTHAYLKVRL
Protein: EF-hand domain-containing protein (Q57Y22)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- C2 domain-containing protein
- Uncharacterized protein
Sequence:
MSDTESIQFNEVTDNEEPNVSVGSRAMPQGVDKTGSAQQFNRPPLHGVLSPTARKGQMYSSSASTPKFVVLNDEGVGDSDHTESLQFKELTDVDSPSTRGEAKALSRSISNRPVTQESKRPPLHSAVPQASRRSHGQSSEGTSLHFVVHGDAEGDDDFDDSDSIQFHTEGASRNVSFKVQSTTSMAETKRGASAVRGQQLVNMETADDSLVFFVEDTQSSIGKKINSQRENSHDDTISFVVEDPVTGGGEGTSSAEKSISFVIASADEASEKSPPVPLAAGGKRISTSPSPKSPSEKVSKRAAGSGNAQRKSKRTSVSKKAQGPKEVGTGSARANSRGSTPQHVSNGGAGEGATFNVYKVGGKHTLNKAGATALRPAAEGGLAPRTTNLAGGRVLNERQAAEDNETIASLVPNAATLLPLPFPQTPGRKVSLKAPDVEEMVLQAKVHTEYWRMFNDVQREEVVQLTERIVRTREGGTNVWEGKAEKERPSQTSRPLCFSDLFKKTRKDSNRSGNRGRTNAGGAHTSPGAMSTGCGRLTDENKPSANHLGGCYETGIGTLRIPSPNKRRWPLTRKARRPRPPKTEKTGNSRFENISKEVRDDALAKFAELSGVAWPPSSRDELFFLTGVRLTPKQREQFYESMQLYTVASWKVNMNVYAACEQETAPSNAREVKRKVRVTRTTLLRKAFAVMDIEKTGVISVALLPSVRQLLEEERRNLQDALSGRKTQEAFLTRSRNEKAKLSGRVNTTVSQKKTEGDDDVKAVSALRIYRLVLDVLLPLLGASGLLTFDFTTVGLLVFGTLGLSTAGASPSFLKWREATLRCFDSLLKHPV
Protein: Thymic stromal lymphopoietin (Q969D9)
Organism: Homo sapiens (Human)
Function: Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11418668}.
Interaction partners:
- Cytokine receptor-like factor 2
- Interleukin-7 receptor subunit alpha
- Interleukin-33
- Interleukin-13
- Cytokine receptor common subunit gamma
- Interleukin-4 receptor subunit alpha
- Interleukin-4
- Interleukin-13 receptor subunit alpha-1
- Interleukin-7
- Interleukin-5
Sequence:
MFPFALLYVLSVSFRKIFILQLVGLVLTYDFTNCDFEKIKAAYLSTISKDLITYMSGTKSTEFNNTVSCSNRPHCLTEIQSLTFNPTAGCASLAKEMFAMKTKAALAIWCPGYSETQINATQAMKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLKQQ
Protein: Cousin of atonal (RT01061p) (Q0IGT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Achaete-scute complex protein T4
Sequence:
MSYYYSSASEEDGSSQYLGSPNYNLTQLPPVSGQDYGQGAFLSPEWQFLDAAGGTQTELGPIMEAQGQHTQPQTKRRSNSFTGSDGRKSSPEQTNLSPTVQKRRRQAANARERKRMNGLNAAFERLREVVPAPSIDQKLSKFETLQMAQSYILALCDLLNNGDVEVDAAAYTIFGDSDSGFGLSGGSLS
Protein: Lantibiotic paenibacillin (P86013)
Organism: Paenibacillus polymyxa (Bacillus polymyxa)
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacks antibacterial activity against Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:17071789, ECO:0000269|PubMed:18625234}.
Interaction partners:
Sequence:
MKVDQMFDLDLRKSYEASELSPQASIIKTTIKVSKAVCKTLTCICTGSCSNCK
Protein: Nicolin 1, tubulin polyglutamylase complex subunit (cDNA FLJ52908, highly similar to Nicolin-1) (B4DX77)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRVLVPCHVKGSVALQVGDVRTSQGRPGVLVIDVTFPSVAPFELQEITFKNYYTAFLSIRVRQYTSAHTPAKWVTCLRDYCLMPDPHSEEGAQEYVSLFKHQSPSVTFPKWLSHPVPCEQPALLREGLPDPSRVSSEVQQMWALTEMIRASHTSARIGRFDVDGCYDLNLLSYT
Protein: Phospholipase D zeta 1 (PLDzeta1) (EC 3.1.4.4) (Phospholipase D p1) (AtPLDp1) (Phospholipase D1 PHOX and PX-containing domain protein) (Q9LRZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Phosphatidylcholine-selective. Regulates root-hair morphogenesis. Contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis in phosphorus-starved roots. Involved in root elongation during phosphate limitation.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:12775839}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Non-specific phospholipase C5
- Non-specific phospholipase C4
- Phosphatidate phosphatase PAH2
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Non-specific phospholipase C1
- Non-specific phospholipase C2
- Non-specific phospholipase C6
- Phosphatidate phosphatase PAH1
Sequence:
MASEQLMSPASGGGRYFQMQPEQFPSMVSSLFSFAPAPTQETNRIFEELPKAVIVSVSRPDAGDISPVLLSYTIECQYKQFKWQLVKKASQVFYLHFALKKRAFIEEIHEKQEQVKEWLQNLGIGDHPPVVQDEDADEVPLHQDESAKNRDVPSSAALPVIRPLGRQQSISVRGKHAMQEYLNHFLGNLDIVNSREVCRFLEVSMLSFSPEYGPKLKEDYIMVKHLPKFSKSDDDSNRCCGCCWFCCCNDNWQKVWGVLKPGFLALLEDPFDAKLLDIIVFDVLPVSNGNDGVDISLAVELKDHNPLRHAFKVTSGNRSIRIRAKNSAKVKDWVASINDAALRPPEGWCHPHRFGSYAPPRGLTDDGSQAQWFVDGGAAFAAIAAAIENAKSEIFICGWWVCPELYLRRPFDPHTSSRLDNLLENKAKQGVQIYILIYKEVALALKINSVYSKRRLLGIHENVRVLRYPDHFSSGVYLWSHHEKLVIVDNQVCFIGGLDLCFGRYDTFEHKVGDNPSVTWPGKDYYNPRESEPNTWEDALKDELERKKHPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPYEDSIPLLMPQHHMVIPHYMGRQEESDIESKKEEDSIRGIRRDDSFSSRSSLQDIPLLLPHEPVDQDGSSGGHKENGTNNRNGPFSFRKSKIEPVDGDTPMRGFVDDRNGLDLPVAKRGSNAIDSEWWETQDHDYQVGSPDETGQVGPRTSCRCQIIRSVSQWSAGTSQVEESIHSAYRSLIDKAEHFIYIENQFFISGLSGDDTVKNRVLEALYKRILRAHNEKKIFRVVVVIPLLPGFQGGIDDSGAASVRAIMHWQYRTIYRGHNSILTNLYNTIGVKAHDYISFYGLRAYGKLSEDGPVATSQVYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVLIEDTELVDSRMAGKPWKAGKFSSSLRLSLWSEHLGLRTGEIDQIIDPVSDSTYKEIWMATAKTNTMIYQDVFSCVPNDLIHSRMAFRQSLSYWKEKLGHTTIDLGIAPEKLESYHNGDIKRSDPMDRLKAIKGHLVSFPLDFMCKEDLRPVFNESEYYASPQVFH