wanglab/gogpt-training-data huggingface dataset:
Protein: Prolyl endopeptidase (EC 3.4.21.-) (Q38AG2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine peptidase, putative serine peptidase, Clan SC, Family S9D
- Pyroglutamyl-peptidase I
Sequence:
MRLAYPTARRSAASYVLHNVTVPEPYDYLEDPENNETKSFVKAQNDLFGEYMRSTEALGNKLYNRISQTFDFPRTSNPSFRNGRYYFYHNTGLQNQSVLKRATSLTDSNPTTFLDPNILSNDGTTALKATAWSEDESLFAYSASDKGSDWQHIHVRRADTAEDTEDVIEWAKFTGISWLHNTGFFYTRFPALKGDVDKGAETDAAKDPFVCFHRLGTKQDEDVVVLSLPEHPHWGVSAEVSNCHSYLVVSITDGCEPKNLIWITKLPIDGAEKLSPSTLTYNKLFNEFVGSFEYLGNDGTTFYFVTTRDAPRKKIISVDIATGKEQIVVGEREAVLDHAALVKNTLILVYLEDVKSTLYYCCLDKPELKKITIPIGAISSLFADRKVDLVSFKVTSFLLPGRSFVLDINDPEGSLRVFKDDNIEGLSADDFITEQKFYNSADGTRIPMFIIHRKGIVTSESPVLLYGYGGFNISLTPSFSSSRVVFLQHLRGVLAVPNIRGGGEYGEAWHNAGRLTSKQNCFTDFIEAAKFLHGNGYGNPATTAIMGGSNGGLLVAAVANQAPELFRCVICQVGVLDMYKFHKFTIGHAWRSDFGDPDKEEDFKVLQKYSPLHNIKSGVKYPAILVVTGDHDDRVVPLHSLKYIAALQHENPTEGGPFLARVEVAAGHGAGKPTSKIMQESADIYTFIAKNTNAQWTD
Protein: Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45) (P04157)
Organism: Rattus norvegicus (Rat)
Function: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:P08575}. Synapse {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:P08575}.
Interaction partners:
- B-cell receptor CD22
- Proto-oncogene tyrosine-protein kinase LCK
- Leukosialin
- Tyrosine-protein kinase HCK
- T-cell surface glycoprotein CD4
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase Fyn
- Galectin-3
- Leukocyte surface antigen CD47
- Semaphorin-4D
Sequence:
MYLWLKLLAFSLALLGPEVFVTGQGTTDDGLDTTEIVLLPQTDPLPARTTEFTPPSISERGNGSSETTYLPGFSSTLMPHLTPQPDSQTPSARGADTQTLSSQADLTTLTAAPSGETDPPGVPEESTVPETFPGGTPILARNSTAPSPTHTSNVSTTDISSGANLTTPAPSTLGFASNTTTSTEIATPQTKPSCDEKFGNVTVRYIYDDSSKNFNANLEGDKKPKCEYTDCEKELKNLPECSQKNVTLSNGSCTPDKIINLDVPPGTHNFNLTNCTPDIEANTSICLEWKIKNKFTCDIQKISYNFRCTPEMKTFALDKHGTLWLHNLTVRTNYTCAAEVLYNNVILLKQDRRVQTDFGTPEMLPHVQCKNSTNSTTLVSWAEPASKHHGYILCYKKTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAYVIGRVQRNGPAKDCNFRTKAARPGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGSLVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGEYLGDPEIKPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSNLDEQQELVERDEEKQLINVDPIHSDLLLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEMSKESEAESDESSDEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIYPTQNGQVKKANSQDKIEFHNEVDGAKQDANCVQPADPLNKAQEDSKEVGASEPASGSEEPEHSANGPMSPALTPSS
Protein: Protein LPA2 (Protein LOW PSII ACCUMULATION 2, chloroplastic) (F4KDA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein LPA3
- Protein LOW PSII ACCUMULATION 1
- Protein PAM68, chloroplastic
- Thylakoid membrane protein TERC, chloroplastic
- Inner membrane protein ALBINO3
- Photosystem II D1 precursor processing protein PSB27-H2, chloroplastic
- Photosystem II stability/assembly factor HCF136
- Rieske
- Chloroplast protein HCF243
- Photosystem II CP43 reaction center protein
Sequence:
MALQIHSPCSFSTRPYHLFFTTRNPRFAIKCQNSQIESDTTEDPSRSKNSSSSGVGFGSPASSSSPAKKLSAATSGNKKGKGKREVNRRAPVEKPVFMSEEGAAKAEEQRQNENAFLLTWLGLGIVILIEGIILAASGFLPEELDKLFVKYVYPVFTPSVVLFVAGTTAYGVLKYIQNEKMKGQE
Protein: Protein tyrosine phosphatase Pps1, putative (AFU_orthologue AFUA_5G11690) (Q5BH51)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MATVVVQQPLRHTTPPPGTVAPALTLNRTSSPVPNKHIPVCPTGPSPVSSRTSSPAPKDDVVLPTSSPLHPPDAFPKISESPLLYSIEIEILVAAVDHCSSQPLPDPNLMFPWLHGLHPENHLQVGFFTNRRRSLRRTPKCWRGLTIVKVGGDLSTSRLKGAITPDAILAPSGLEFLATDPREGFSVRNFQIQTAKVAPLSDIVVYGEDGVTAKQLLEVASRIATAQHHWRLKHDHEQTLPSYNTFVVSCPFSDIERRAPNLVAVNSSGQLTNQVVDLCESTECCARIRSNKRLVQLERLEMCTMSRATEFAHNVWQGPTPDYLLQAGASGTPSADAFDLMIDANDLAGIPGPRYLANLAKRLAKEPQRMEFPSSGSLLTPSGESRDLDDLINTLRWIYYLANPEVVETDAEGDVSMDIPPRKTRRILIHCPDGYTESSLLVIAYTMFAEGISASEAWLRLHREKKRNFFAYPSDVAYLKNVQERILQESPANPPTYRVSDPQWFKYCDGSLPSRILPYMYLGNLSHANNPEMLWELGIRRVLSIGEAVTWSDSDIARMGAENLMHITKVQDNGIDPLTQEFDRCLEFIRKGKSDGAATLVHCRVGVSRSATICIAEVMASLNLSFPRAYCYVRARRLNVIIQPHLRFVYELLKWEELQQKKNKQPVKRELEWATVAREIALMNKPYSR
Protein: Cytochrome P450 2B3 (EC 1.14.14.1) (CYPIIB3) (P13107)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- UDP-glucuronosyltransferase 1A1
- Cytochrome P450 7A1
- UDP-glucuronosyltransferase 2B15
- Cytochrome P450 2E1
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 2U1
- Cytochrome P450 3A1
- UDP-glucuronosyltransferase 2B37
Sequence:
MDTSVLLLLAVLLSFLLFLVRGHAKVHGHLPPGPRPLPLLGNLLQMDRGGFRKSFIQLQEKHGDVFTVYFGPRPVVMLCGTQTIREALVDHAEAFSGRGIIAVLQPIMQEYGVSFVNEERWKILRRLFVATMRDFGIGKQSVEDQIKEEAKCLVEELKNHQGVSLDPTFLFQCVTGNIICSIVFGERFDYRDRQFLRLLDLLYRTFSLISSFSSQMFEVYSDFLKYFPGVHREIYKNLKEVLDYIDHSVENHRATLDPNAPRDFIDTFLLHMEKEKLNHYTEFHHWNLMISVLFLFLAGTESTSNTLCYGFLLMLKYPHVAEKVQKEIDQVIGSQRVPTLDDRSKMPYTEAVIHEIQRFSDVSPMGLPCRITKDTLFRGYLLPKNTEVYFILSSALHDPQYFEQPDTFNPEHFLDANGALKKCEAFMPFSIGKRMCLGEGIARSELFLFFTTILQNYSVSSPVDPNTIDMTPKESGLAKVAPVYKICFVAR
Protein: Alpha-galactosidase AgaA (EC 3.2.1.22) (Q9ALJ4)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.
Interaction partners:
Sequence:
MSVAYNPQTKQFHLRAGKASYVMQLFRSGYLAHVYWGKAVRDVRGARAFPRLDRAFSPNPDPSDRTFSLDTLLQEYPAYGNTDFRAPAYQVQLENGSTVTDLRYKTHRIYKGKPRLNGLPATYVEHEQEAETLEIVLGDALIGLEVTLQYTAYEKWNVITRSARFENKGGERLKLLRALSMSVDFPTADYDWIHLPGAWGRERWIERRPLVTGVQAAESRRGASSHQQNPFIALVAKNADEHQGEVYGFSFVYSGNFLAQIEVDQFGTARVSMGINPFDFTWLLQPGESFQTPEVVMVYSDQGLNGMSQTYHELYRTRLARGAFRDRERPILINNWEATYFDFNEEKIVNIARTAAELGIELVVLDDGWFGERDDDRRSLGDWIVNRRKLPNGLDGLAKQVNELGLQFGLWVEPEMVSPNSELYRKHPDWCLHVPNRPRSEGRNQLVLDYSREDVCDYIIETISNVLASAPITYVKWDMNRHMTEIGSSALPPERQRETAHRYMLGLYRVMDEITSRFPHILFESCSGGGGRFDPGMLYYMPQTWTSDNTDAVSRLKIQYGTSLVYPISAMGAHVSAVPNHQVGRVASLKTRGHVAMSGNFGYELDITKLTETEKQMMKQQVAFYKDVRRLVQFGTFYRLLSPFEGNEAAWMFVSADRSEALVAYFRVLAEANAPLSYLRLKGLDSNQDYEIEGLGVYGGDELMYAGVALPYRSSDFISMMWRLKAVQQ
Protein: Uncharacterized protein (Q387S8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pseudouridylate synthase RPUSD4, mitochondrial
- 50S ribosomal protein L17, putative
- Mitochondrial RNA binding complex 1 subunit
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
- GTP-binding protein, putative
- Uncharacterized protein
- KOW domain-containing protein
- Uncharacterized protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MPNIKGGVGSFLMRRAAPKSIRQKYQTGPQFYKRKFFQFQKGHHRLHRRISGVQTGSPTHQREYERFHHLPGDVRTRPQFDFTFGETRADRVMFAWRKRGDLQLYQMSGRGETFVCYRCGYPVRSQLVAVKADNWDYRMCYRCYTNTVHRGMENDT
Protein: POU domain, class 4, transcription factor 1 (Brain-specific homeobox/POU domain protein 3A) (Brain-3A) (Brn-3A) (P20266)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional transcription factor with different regions mediating its different effects. Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor. Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain). Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins. Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity. May positively regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord. Plays a role in TNFSF11-mediated terminal osteoclast differentiation. Negatively regulates its own expression interacting directly with a highly conserved autoregulatory domain surrounding the transcription initiation site (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P17208}. Cytoplasm {ECO:0000250|UniProtKB:P17208}.
Interaction partners:
- Visual system homeobox 2
- RNA-binding protein, mRNA-processing factor.
- Insulin gene enhancer protein ISL-1
- Cellular tumor antigen p53
- Neurogenin-1
- Melanopsin
- Paired box protein Pax-6
- Recoverin
Sequence:
MMSMNSKQPHFAMHPTLPEHKYPSLHSSSEAIRRACLPTPPLQSNLFASLDETLLARAEALAAVDIAVSQGKSHPFKPDATYHTMNSVPCTSTSTVPLAHHHHHHHHHQALEPGDLLDHISSPSLALMAGAGGAGAAGGGGAPTRPRGAGGPGGGGGPGGGGPGVAGRRRGPGGGGGGPGGGLLGXSAHPHPHMHGXGHLSHPAAAAAMNMPSGLPHPGLVAAAAHHGAAAAAAAAAAGQVAAASAAAAVVGAAGLASICDSDTDPRELEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEGAQREKMNKPELFNGGEKKRKRTSIAAPEKRSLEAYFAVQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKFSATY
Protein: Protein sepa-1 (Suppressor of ectopic P granules in autophagy) (G5EC37)
Organism: Caenorhabditis elegans
Function: Adapter protein that connects P-granules in somatic cells with the autophagic machinery. Association with other adapters such as epg-2 and P-granule components such as pgl-3 is required for the accumulation and degradation of P-granules by autophagy in somatic cells. This ensures exclusive localization of the P-granules in germ cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00311}. Cytoplasm {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24140420}. Cytoplasmic granule {ECO:0000305|PubMed:19167332}. Note=Diffuse cytoplasmic localization, but also localized to cytoplasmic aggregates throughout development (PubMed:19167332, PubMed:21802374). Co-localizes with epg-2 and lgg-1 in cytoplasmic aggregates (PubMed:19167332, PubMed:24140420). {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24140420}.
Interaction partners:
- Protein lgg-1
- Guanyl-specific ribonuclease pgl-3
- Ectopic P granules protein 2
- Very Early Transcript
- Guanyl-specific ribonuclease pgl-1
- ZZ-type domain-containing protein
- F-box C protein
- PhosphoLipase A2 Group
Sequence:
MTPLSALTSNPAPSPPPKFALGKCPATAIHVVSVLRPNRQRFCYEKTDAGDLIPHKCLICQPILTEKHISPYYAVYSDLLEDFVLFGYNTMTGKMEQFIYAFKTDCFVEVNRPEIKYNPAFLVKGNVVVALNGPEGELVVIERDCRGLLSKESTSYGQFRTLPTAALRTLTLQDLERDRWDRAANSDEVKISSGNESFDRLYAEYQKNLPRFQVRQCLHLNKEFLCVYSKTSGDYTRLEYIDETGDFQKISCTLCTCEVTESNLIPLYVERNASELVIHVHNTENNQIEQYIYDVRTFGFVQVKRNLVYDPKKITSGLNLFMAENIDNRKVYMIMRGRDGRLQKETSGSGGFEKMQPVAVKTFQVQWVEMKTEFEKKKASTERVEPQHPVQTEGEDIMETVLAMVESFNCDLRKELGLTQDQEIPRKAPRVESAETEENIVKNLEKLQIAKDPEEPTTAASEGGNTYGYQELDDTMSEGLLEKEAESKHQDANEPEPVKNVTYEPDVAAMDKKKKRRELKSRLNKINAQIDELEKRRMERAGKKQVVSSSVPSEEAAQVEAPASPALAENTNQISNEETPKIDIFEGYNGSFLFGTNTSKEWIVEDIRNHMVGKLLKAFWPRIQNVEEMNGELFKKLIANARKCETEILEASNDRDEYYRLMQLTVDQILKKTLKKDQRATEHNHQQPTQSSDELAKNHEKN
Protein: Uncharacterized ABC transporter ATP-binding protein TM_0288 (Q9WYC4)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter, ATP-binding protein
- Oligopeptide ABC transporter, ATP-binding protein
- Oligopeptide ABC transporter, ATP-binding protein
- Sugar ABC transporter, ATP-binding protein
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Conserved hypothetical protein
Sequence:
MPEIRRRPHGPILEKPALKNPTATLRRLLGYLRPHTFTLIMVFVFVTVSSILGVLSPYLIGKTIDVVFVPRRFDLLPRYMLILGTIYALTSLLFWLQGKIMLTLSQDVVFRLRKELFEKLQRVPVGFFDRTPHGDIISRVINDVDNINNVLGNSIIQFFSGIVTLAGAVIMMFRVNVILSLVTLSIVPLTVLITQIVSSQTRKYFYENQRVLGQLNGIIEEDISGLTVIKLFTREEKEMEKFDRVNESLRKVGTKAQIFSGVLPPLMNMVNNLGFALISGFGGWLALKDIITVGTIATFIGYSRQFTRPLNELSNQFNMIQMALASAERIFEILDLEEEKDDPDAVELREVRGEIEFKNVWFSYDKKKPVLKDITFHIKPGQKVALVGPTGSGKTTIVNLLMRFYDVDRGQILVDGIDIRKIKRSSLRSSIGIVLQDTILFSTTVKENLKYGNPGATDEEIKEAAKLTHSDHFIKHLPEGYETVLTDNGEDLSQGQRQLLAITRAFLANPKILILDEATSNVDTKTEKSIQAAMWKLMEGKTSIIIAHRLNTIKNADLIIVLRDGEIVEMGKHDELIQKRGFYYELFTSQYGLVVEKE
Protein: Ets variant gene 6 (TEL oncogene) (Transcription factor ETV6) (Q7ZU22)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MSDSPSQQLIIKERSAFSPSASPLPNSTSSPGHVPLAPNTARTEEETSRLPAHLRMQPVFWSREDVCVWLRWAEREFALRPISSGSFQMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPHAYFPISPFHTLNDTPPQQHKHEETVRRPVRGTDSAVSLQPPTIELRHRSRSPLHHHHHHLHHLHHRPTSAEDPQQMSAPLPDSNHHLPEDSYPLSVSPAAAANGHCPARDAPPPASPGPEESAPPRVIQLLPSAIMHPLMLSPARGPPAPPQNGRESKAQHQHSGSGGHYSLSAQLPLLDDRHYRNHISLQDEQATPMGRIADCRLLWDYVYQLLSDSRYENYIRWEDRDTKVFRIMDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLSRFMKTPDEIMSGQTERLEHLESDTDDQIYVKEEC
Protein: Transcription initiation factor TFIID subunit 10 (Transcription initiation factor TFIID 24 kDa subunit) (TAFII-24) (TAFII24) (dTAF(II)24) (Q9U5W9)
Organism: Drosophila melanogaster (Fruit fly)
Function: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10669741}. Nucleus {ECO:0000269|PubMed:10669741}.
Interaction partners:
- TBP-associated factor 3
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 2
- TATA-box-binding protein
Sequence:
MASDGEDISVTPAESVTSATDTEEEDIDSPLMQSELHSDEEQPDVEEVPLTTEESEMDELIKQLEDYSPTIPDALTMHILKTAGFCTVDPKIVRLVSVSAQKFISDIANDALQHCKTRTTNIQHSSGHSSSKDKKNPKDRKYTLAMEDLVPALADHGITMRKPQYFV
Protein: Repressor of RNA polymerase III transcription MAF1 homolog (Q9D0U6)
Organism: Mus musculus (Mouse)
Function: Plays a role in the repression of RNA polymerase III-mediated transcription in response to changing nutritional, environmental and cellular stress conditions to balance the production of highly abundant tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and maintenance (By similarity). Also plays a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation. Mechanistically, associates with the RNA polymerase III clamp and thereby impairs its recruitment to the complex made of the promoter DNA, TBP and the initiation factor TFIIIB. When nutrients are available and mTOR kinase is active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged in transcription. Stress-induced MAF1 dephosphorylation results in nuclear localization, increased targeting of gene-bound RNA polymerase III and a decrease in the transcriptional readout. Additionally, may also regulate RNA polymerase I and RNA polymerase II-dependent transcription through its ability to regulate expression of the central initiation factor TBP (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20543138}. Cytoplasm {ECO:0000250|UniProtKB:Q9H063}.
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEDESPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLRWVVNAVNCSLFSAVREDFKALKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNALDLELGAEEADEESGGGGGEGRAEETSTMEEDRVPVICM
Protein: Kugelkern, isoform A (Kugelkern, isoform B) (Kugelkern, isoform C) (LD09231p) (Q8SX89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSKMASNTSGGGGTTSGTGTGRRLPLSLSGGSTVTRLQQSSGSNGRSNSPQNGNKKITESFLPVKKSNQPRTTSTGSTGSSQNGVSKPTNGKDKSQNGSSTGKDQKVEKSKDKLPEKKAKEVGAENKDKDGAAEMTDMEVVVENKQKEVVSENKQNEVVSENKEVVSENKEVVSENKEVASEKKVVVAEVPSDKDDNGETKKDDATVESTAPASQTPADAAVIIDEVVFIPDLSTPTKDRKSTRKSGSQQKSPISKASNASPVQKIKTEAVSSSTSGSLTPQEDVDMEPLQVDASPIRSVHGNLNAVPTATSTPGRSLFSFRGSNKQSTEVELAAQTSSSPAGTPARTFAQISGRRSIRPIDSLTPSKIGTYRCGNSDLDTSNCTNASMNATVGSEIPNSSSFSFSFFGRGRKRERTPPPLTASQSTSDLGHDVDMSPPKRARFDLFSLNLASPFSLLRSRFSKATIGTPTRLRLEPNSSGVEEQHLNTSTTGVPEEVDVEEEQPAEDVTVGQEAGAEEIPAKKDVEDKNVNGQDGDKESSDGENIDPVVEVADVAAVAAEGRSICSIM
Protein: DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha) (Q72CF4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein bL17
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS3
- DNA-directed RNA polymerase subunit beta
- Small ribosomal subunit protein uS4
- DNA-directed RNA polymerase subunit omega
Sequence:
MLIKQGDRLINTRNWSELVKPEQISRDGEVSDTMYGKFVCEPLERGYATTIGNAMRRVLLSSLQGAAFVAVKISGVQHEFTTIPGVLEDVTDVVLNLKQVRLAMDTEEPQYLELKVDKRGAITAGDVRTNQHVMVLNPDQHIATLTEDIELTFELEVRMGKGYVPADMHEGLSEEIGLIKLDASFSPVRKVAYTVEQARVGQMTNYDKLILEVWTDGSVSPEDAIAYSAKIIKDQISVFINFDERISGENSNGSADSGEFNEHLFKSIDELELSVRATNCLKSANIALVGELVQKSENEMLKTKNFGRKSLDEIRRVLGDMGLDFGTKVDGFEKKYQEWKRKQQHEA
Protein: Cyclin-U4-3 (CycU4;3) (Cyclin-P4.2) (CycP4;2) (Q9FKF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ATP-dependent DNA helicase 2 subunit KU80
- DNA ligase 6
- Transmembrane protein
- Inorganic pyrophosphatase 2
- DNA ligase 4
- Inorganic pyrophosphatase 1
- Serine/threonine-protein kinase AtPK2/AtPK19
- ATP-dependent DNA helicase 2 subunit KU70
Sequence:
MADQIEIQRMNQDLQEPLAEIMPSVLTAMSYLLQRVSETNDNLSQKQKPSSFTGVTKPSISIRSYLERIFEYANCSYSCYIVAYIYLDRFVKKQPFLPINSFNVHRLIITSVLVSAKFMDDLSYNNEYYAKVGGISREEMNMLELDFLFGIGFELNVTVSTFNNYCCFLQREMAMLMKMKSLFLEPSSFKISSKTKLVMYPHEEDSLSTHHNKKQLAAA
Protein: Amino acid ABC transporter membrane protein (Q9I487)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Amino acid ABC transporter periplasmic binding protein
- Amino acid ABC transporter ATP binding protein
- Probable permease of ABC transporter
- Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase
- Amino acid ABC transporter ATP binding protein
- Probable ATP-binding component of ABC transporter
- Probable ATP-binding component of ABC transporter
- Amino acid ABC transporter periplasmic binding protein
- L-arginine-binding protein
- Arginine/ornithine transport ATP-binding protein AotP
Sequence:
MFTTSLTANDLLFLLQGAWTTLAITAMAMLIGTLLGVVFGLLRALLPRASLPLAALLDVFRSVPLLIQFVLLNSFKSILGLDWSAFAVACLVLGVYAAAYCAEVVRGGVLSVPPSVRRAARSLGLSYRQDLFHIVLPMAARVAFPGWVNLTLSVMKDTSLVLWIGIVELLRASQTIVTRIQEPLFVLCIAGLVYYLMSWVVARLGARLERRWQQ
Protein: Cell cycle checkpoint control protein family (F4J7B7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell cycle checkpoint protein RAD17
- Checkpoint protein
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 5
- DNA repair endonuclease UVH1
- Serine/threonine-protein kinase ATR
- Transcription coactivator
- BRCT domain-containing protein At4g02110
- Exonuclease 1
Sequence:
MELSISGNALKTLSRSIICLARVGNELVVQASPTQLALHTLNASRSAYQCITFQSSFFDVYTVSGPQAHFSVLLKAVCSVLRTPLASIDHMSVQLPDHDASKVKWTLQCYSAVLCKNLDVACFRPVHNSMKKTYWITCNVEPDIQHLSLDRGRFPSTLVMHPRNLSKLLGNFQSSLQEITIIATDQTSFPSDAASEIGGKAVEFRSYVDPTKDGDSLLHTQLWIDPSEEFLQYTHAGDPVDITFSLKELKAFLAFCEGCEADIHLFFEKAGEPILMAPKFGLGDGSSSSFDATLVLATMLVSQLQEGIPAEPPEAANSTGGHAAEQVGSRPQERSRQNASEHPSDHTRVWSELSGTATKSVNGTEDRPQAQGQPDLDIHRIRNMEISKGGPVGDTAPAAPPKSQRPTQIDHAEGSRVRVQNQSFSQHHPSNWVDANEEEEDDDEGVEATPPHNEDY
Protein: Diadenylate cyclase CdaS (DAC) (EC 2.7.7.85) (Cyclic-di-AMP synthase) (c-di-AMP synthase) (D5TM67)
Organism: Bacillus thuringiensis (strain BMB171)
Function: One of 3 paralogous diadenylate cyclases (DAC) in this bacteria catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). It has slow DAC activity with ADP as a substrate and may have weak ADPase activity. Required for efficient spore formation, whereas in B.subtilis, it is required for efficient spore germination. It is produced under the control of different sigma factors in the two bacteria. It is also required for parasporal crystal formation.
Interaction partners:
Sequence:
MHEWGLSEELKIQTKQMIEIAEKELSIMRNAIDKEDECILCKMEDIHHMLANVQTLAATYYIQAYLSPYTESSSFITTAIQHLSARKHGALIVVERNETLEALIQTGTTLNAHLTAPLLESIFYPGNPLHDGAVLVKNNHIVSAANILPLTKSTEVDPELGTRHRAAIGLSEKSDALILVVSEETGRTSFALNGILYTISL