wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein eL27 (60S ribosomal protein L27) (Q7ZV82)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the large ribosomal subunit.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61353}. Cytoplasm {ECO:0000250|UniProtKB:P61353}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:A1XQU5}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A1XQU5, ECO:0000250|UniProtKB:P61353}.
Interaction partners:
- Ribosomal protein L18
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS15
- 40S ribosomal protein S24
- 60S ribosomal protein L37a
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL6
Sequence:
MGKFMKPGKVVMVLAGRYAGRKAVIVKNIDDGTADRPYSHALVAGIDRYPRKVTATMGKKKIAKRSKIKAFVKVFNYNHLMPTRYSVDIPLDKTVVNKDVFRDPALKRKARREAKVKFEERYKTGKNKWFFQKLRF
Protein: Uncharacterized protein (Q580T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Multidrug resistance protein E
- Trans sialidase, putative
Sequence:
MPFWKYFVITKPEVDDDDLPLAKHRIYDDDGNLKPLTVDSIQRKVNTAQGKPKTSPKKEITLTPKTRARILRSVGVSPTGPRRVPEPSTPITEALTTPESVKKRAVRPSVENSDTARALYTSNAETSTPDQKAKGGKGSLKTTPKKSETPKRSASTPSKSPKKEEPKTQPTTATEPAAKLSPKKRSAASKETTPRKSASPQKENNKRKADSPVNVTPPAKKPAASKKAKRSRSASPQKEKEEKSPVAQTSPKAKAKGAASKRSRSETEKAVEEVSPQWSWSIDSLRAFAAERKIDISQCKKKVDIFNKIKDAL
Protein: Small ribosomal subunit protein RACK1 (J3KPE3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
Protein: Late cornified envelope protein 2A (Late envelope protein 9) (Q5TA79)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 1C
- Late cornified envelope protein 2C
- Late cornified envelope protein 2B
- Late cornified envelope protein 1B
- Late cornified envelope protein 1A
- Late cornified envelope protein 1F
- Late cornified envelope protein 6A
- Late cornified envelope protein 1D
- Late cornified envelope protein 3A
- Late cornified envelope protein 4A
Sequence:
MSCQQNQQQCQPPPKCPPKCPPKCPPKCRPQCPAPCPPPVSSCCGPSSGGCCGSSSGGCCSSGGGGCCLSHHRPRLFHRHRHQSPDCCECEPSGGSGCCHSSGDCC
Protein: Beta-glucosidase 16 (Os4bglu16) (EC 3.2.1.21) (Q7XSK2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes glycosides and monolignol glucosides. Can hydrolyze para-nitrophenyl beta-D-glucopyranoside (pNPGlc) in vitro. Hydrolyzes para-nitrophenyl beta-D-fucopyranoside, para-nitrophenyl beta-D-galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in vitro. Hydrolyzes the monolignol glucosides coniferin and syringin with high catalytic efficiencies.
Interaction partners:
- Beta-glucosidase 6
- Beta-glucosidase 24
- Beta-glucosidase 25
- Endoglucanase 8
- beta-fructofuranosidase
- Beta-glucosidase 34
- glucan endo-1,3-beta-D-glucosidase
- glucan endo-1,3-beta-D-glucosidase
- Endoglucanase 11
- Os06g0656000 protein
Sequence:
MAVAAATRIAVVVVVLALAVLAPAARGLRRDDFPPGFLFGAATSAYQIEGAYLDDNKGLNNWDVFTHTQAGRISDGRNGDVADDHYHRYTEDVDILHNLGVNSYRFSISWARILPRGRLGGVNSAGIAFYNRLINALLQKGIQPFVTLNHFDIPHELETRYGGWLGAAIREEFEYYSDVCFNAFGDRVRFWTTFNEPNLSTRHQYILGEFPPNHCSPPFGNCSSGDSRREPYAAAHNILLSHAAAVHNYKTNYQAKQGGSIGIVIAVKWYEPLTNSTEDVRAARRALAFEVDWFLDPIFFGDYPREMREILSSNLPKFTPEEKKLLQNNKVDFIGINHYTAIYAKDCIYSPCTLDTYEGNALVYAIGRRNGKIIGKPTALHGYFVVPEAMEKVVMYVNDRYRNTTIYITENGYSQHSDTSMEDLINDVERVNYMHDYLKYLSSAIRKGANVGGYFAWSIVDNFEWVYGYTVKFGLYQVDFDTQERIPRMSAKWYRDFLTSSSLTDGLQVRSRRADS
Protein: Pluripotency associated transcript 25 (A0A1Y7VIZ1)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transmembrane protein 239
Sequence:
MEKNAVTYKDVHVNFTQEEWALLDPSQKKLYKDVMLETYRNLIAIGFNWDDKNIEEHCQSFGRHTRHERIQSAEKPSEYTQGGKAFALHAHSHAQRHERIHREKKPHGVIQFVEAFAQHSLQLRKRVQTGKKLYEWKQCGKAFEDHSHLKSYEGILMGEKPYECHQWEKAFSSHSNLLQPKGRHTGEKCYECDLCGKAFSQHSRLKRHGRIHTGEKPYKCDQCGKAFSEHCNLQKHKRIHTGEKPYKCHQCDKAFSQHHSLQKHKRIHTGEKPYKCNECDKVFRQSSDLQKHRRIHTGEKPYKCNQCDKAFSQHHSLQIHKRTHTGEKPYKCNQCDKVFSRHSTLQIHIRIHAGEKPFKCNECEKAFSQHSNLQSHRRIHTGKKPYKCNECEKAFSQHSNLQSHRRIHTGKKPYKCNTCEKAFSKHSILHSHRRIHTGEKSYKCNHCEKVFLGHYDLQRHKGIHTG
Protein: Specificity protein transcription factor 1 (Q93727)
Organism: Caenorhabditis elegans
Function: Probable transcription factor which modulates gene expression, thereby acting as an ASJ sensory neuron terminal selector gene.
Interaction partners:
- Uncharacterized protein R07B1.9
- Thioredoxin-1
- Sulfotransferase ssu-1
Sequence:
MGGASSPRIPSRRSAPYFTSLAFFGSSYIKVKNNRNKMLNPTDAASVALSFSVPFQMSGENPLSKLVEHCNKFVPGADIKMKAEPAKPESLLLPTDMNAYSPYLATPNWWVDQTGWPQLYPTVTTASSVDVYQNYLASSQLGGLLSSSVSAVASQLPAGINAQSALNITSQQRTIAKSFQHTKPMASSSSIPSVLTASNSSANSLVSSGSESVSARGTSGSGGTGKYPSSRTANKCECPNCHEIEKFGPNAIAARKRGVHNCHIAGCGKVYNKSSHLKAHLRWHSGERQMKKRSGDSS
Protein: Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (J3KN38)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFLKSFPPPGPAEGLLRQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAKFEVEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSIRDYEDGMEVDTTPTVAGQFEDADVDH
Protein: Membrane-associated protein (Q38B63)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCGKVSFSIFVLLTYRPSRISPLSFPFNPRLINVCKKHRRMTPGAMYLSSVTLTLCIVLLATGARQSAAAAAAVGETVILDQGSSESIRIVESGGSTTDASFDFVGLWPHGEHRESDAMFFDEEDAKYEKWMVKEREKKRKQEKEKREEKQKAMNKSKDKPRKPPKGASTFQLTQAAVRARTTERRSRLRALRKPNSLLFDAAWSAVLEDSDNLRKLLSADSIMRSREGEGNNPESQYVQLLSTAFSHTVRNLTTESRSDWISPLIYALPFPVLLDNGALVSAEQEVRALMTDLQVMKATPVPQPSSNGSEKKVPSSTDVEATTQLVEDNLRIASTTISASKSAHRVVAQLALPIMGHAKSSVSDQLREVEKQIRANDESTVAKRRELKDLAKLKKVVKATKDRIHAADGELRNAYFSTTPMLSKSSFLISLALICRLRLSRNTYVDAVDMLPGIDAFADFTGSMRAELYSFLFYPLGVGVAVSAATTWCLLSTRQLITKKLKRQAGRLLQQTSTSGGRPGKVSGITMFALRANLLLEALSPLFVPLVTFYIINRTLTKDLLYPIVITVKPAQRLVLGFVVISVLVASVIVSRVLTAVDRWSLNRHNANKRKVQ
Protein: Protein-L-isoaspartate O-methyltransferase (EC 2.1.1.77) (A0A384MDK7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Protein: FAD-binding monooxygenase prhJ (EC 1.14.13.-) (Paraherquonin biosynthesis cluster protein J) (A0A1E1FFN7)
Organism: Penicillium brasilianum
Function: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B. The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK. Finally, prhA leads to berkeleydione via the berkeleyone B intermediate. PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione. Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable).
Interaction partners:
Sequence:
MAIGPKPESIIGSCDHPPQAEAQTGARLAAINGNNSPVSRLKDFTTDPWLTSTDQPQPGSTTNVPYSPPDSTKHARILIVGAGYGGLLFAVRLLQSGFTLEDILLVDSAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETKNIPSQKYVSGEELRTHAERIAEKWKLGARTLFRTTVSDLTWDDNKLQWIATASCSSNERKQAGCTYTINADFAILANGTLSKPKVPDLPGIDDYTGRIFHTARWDYDYTGGSPAIPAMDQLRTKKVGVIGTGSTAVQVIPQLARWAGELTVFQRTPGAVGLQINRETDHAWWRDNVQLAGPEWQRKRCENFNAFITNPYRASLDAEDLVKDGWTKHPSFSVALGGARNLQADFLDLAKKIDKERREIGQQHINSTVRDPATAEALFNPTYGWCKRPCFHQGYFETYNRENVRLVSTPGQGITKLTRNGIMWGHQEFELDLIVLATGYELGSLCPANRARLSIHGRGRVSMSQKWASGPATLHGVMTRGFPNLFFPGTSQAGVTANQSYMFDRAAEHIAYIIQNARPRTAASAVNPKVRIEPSLEAEELWAMETVSRAKAFAATKTCSAGSYTISARLGESVDESQMARHMPWGEGMASYVKILEEWRKKRDMHGLEVVYD
Protein: Putative C-1-tetrahydrofolate synthase,cytoplasmic (EC 1.5.1.5, EC 3.5.4.9) (Q4Q9F9)
Organism: Leishmania major
Interaction partners:
- formate--tetrahydrofolate ligase
- Adenylosuccinate lyase
- Large ribosomal subunit protein eL18
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Isocitrate dehydrogenase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Adenylosuccinate synthetase
- Aminomethyltransferase
- Aminomethyltransferase
Sequence:
MPSAQIIDGKAIAAAIRSELKDKVAALRELYGGRVPGLASIIVGQRMDSKKYVQLKHKAAAEVGMASFNVELPEDISQEVLEVNVEKLNNDPNCHGIIVQLPLPKHLNENRAIEKIHPHKDADALLPVNVGLLHYKGREPPFTPCTAKGVIVLLKRCGIEMAGKRAVVLGRSNIVGAPVAALLMKENATVTIVHSGTSTEDMIDYLRTADIVIAAMGQPGYVKGEWIKEGAAVVDVGTTPVPDPSRKDGYRLVGDVCFEEAAARAAWISPVPGGVGPMTIAMLLENTLEAFKAALGVS
Protein: Acid phosphatase, putative (AFU_orthologue AFUA_4G03660) (Q5AX38)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Purple acid phosphatase
- 3-phytase
- Alkaline phosphatase
- Thiamine biosynthetic bifunctional enzyme, putative
- Acid phosphatase
- Riboflavin synthase
- Acid phosphatase, putative
- FAD synthase
- Riboflavin kinase
Sequence:
MYTKTLTVLLGGLSLALAQTSSEQTPSAPEIAAARATVMPYSPVSNVQGKSFQRFVNIWLENTDYDVAASEKHLARLAKKGLTLTNFWAVTHPSEPNYCASQGGDTFGMDNDDFNQIPANISTIADMFDTKNISWGEYQEHMPYPGYQGFRYPTSGDNDYVRKHNPAILYDSITEDPTRLRQIKNFTSFYEDLKTHRLPQYSFITPNMTNDGHDTDISFSGRWTWEFLIDLLDNEYFTNDTLILLTFDENDTYELGNKIFSFLLGGAVPKDLIGKEDDTFYTHYSIISSLSANFGLPSLGRWDCGANLLSFLAEKVGYTNYEVDTSNLYLNVSYNGPMAAGEYSQKTYEWPIPATEGQCSGGYGILDVVRKTYAGLTATHDYTSPVPFDVKTGNSVGIEYSRTLKGGRHERYVTGFGKTNETSGARKSS
Protein: Meiotic central spindle, isoform B (M9PF60)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVGRSSGKMERSVDASMGKNCRACAEHSSILVDLFSKEISDPPIWEMLNSILPEICRVKRDEMPQKICPTCLVAAQNAFHFRHKCEQSFQFFSQLLQLDKSNSNLSRSHCRRGTMNPLIPFEIVGCEDPLDTNVTKLDANRPDVKTDIDEPTDGKATNVTMNDIKTEDEVSIQETFEDAFDEENDNNNTDSEREDSDQWTVGSTEDQDEPWIPGGGGRQTVGGNNQSLLCTECGVSYSTQKALARHVAKHKEQGDTQKPHLCDFCGRGFRTNAQLTTHRRRHTGERPFKCPLCPKAYTHGPTLKSHMHTHDEEKGHKCPQCDKTFYTRGNLRAHIQRHTGERPYKCPDCPQTFAKNSGLKLHSRLHKEERPFKCELCGKGFVQNQHLITHLRVHNGDRQFKCPDCDKSFFEKSNMMKHQRTHSGIKPFKCEECGQAFSHNHHLKSHLRIHTGEKPYKCDQCGKGFSANQSLMKHTLWHVDNNDRPFKCSQCPKAYDTQQSLRGHEKTHKNPDEPKTLHQCPHCDVRFALKKTLDKHITSHKIRPHPCPQCPEGFFSQKSLKKHLRLHNLKK
Protein: Inorganic pyrophosphatase 2, mitochondrial (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 2) (PPase 2) (Q91VM9)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes inorganic pyrophosphate. This activity is essential for correct regulation of mitochondrial membrane potential, and mitochondrial organization and function.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9H2U2}.
Interaction partners:
- Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
- Potassium-transporting ATPase alpha chain 2
- Potassium-transporting ATPase alpha chain 1
- Potassium-transporting ATPase subunit beta
- Inorganic pyrophosphatase
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- V-type proton ATPase 21 kDa proteolipid subunit c''
- ATP synthase F
Sequence:
MRALLPLLSVGRGWRVGAAARPPRRVMSLYRTEELGHPRSQDYRLFFKHVAGHYISPFHDIPLKADCKEEHDIPRKKARNDEYENLFNMVVEIPRWTNAKMEIATEEPLNPIKQDIKNGKLRYTPNIFPHKGYIWNYGALPQTWEDPHLRDKSTDCCGDNDPIDVCEIGSKVLSRGDVVHVKILGTLALIDQSETDWKIIAINVNDPEAEKFHDIDDVKKFKPGYLEATLNWFRLYKVPDGKPENKFAFNGEFKNKAFALDVINSAHERWKEMVMKKCDKGAISCVNVHICDSPFHCTMEEARSLVESVPTPSMNKESNVEEEVWHFLRN
Protein: Protein LlR18B (EC 3.1.27.-) (LlPR10.1B) (allergen Lup l 4) (P52779)
Organism: Lupinus luteus (European yellow lupine)
Function: Class II ribonuclease (RNase), with low activity on single-strand RNA. Binds to cytokinins (By similarity). Interacts with melatonin (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9LLQ2}.
Interaction partners:
Sequence:
MGVFAFEDEHPSAVAQAKLFKALTKDSDDIIPKVIEQIQSVEIVEGNGGPGTVKKITASHGGHTSYVLHKIDAIDEASFEYNYSIVGGTGLDESLEKITFESKLLSGPDGGSIGKIKVKFHTKGDVLSDAVREEAKARGTGLFKAVEGYVLANPNY
Protein: Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (Activating transcription factor 2) (cAMP response element-binding protein CRE-BP1) (Q00969)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type (By similarity).
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-34 is required for its nuclear localization and negatively regulates its mitochondrial localization. Colocalizes with the MRN complex in the IR-induced foci (IRIF) (By similarity). {ECO:0000250}.
Interaction partners:
- Transcription factor Jun
- Mitogen-activated protein kinase 14
- Cyclic AMP-responsive element-binding protein 1
- mitogen-activated protein kinase
- Histone lysine acetyltransferase CREBBP
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 3
- cAMP responsive element binding protein 5
- Mitogen-activated protein kinase 1
Sequence:
MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTNDEKEIPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRAQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKTEAGATSVLTQMADQSTEPALSQIVMAPSSQAQPSGS
Protein: NFX1-type zinc finger-containing protein 1 (Q8R151)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses. Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response. Also required for immunity against some bacteria, such as mycobacteria (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:31685995}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9P2E3}.
Interaction partners:
- Ubl carboxyl-terminal hydrolase 18
- Protein mono-ADP-ribosyltransferase PARP12
- UMP-CMP kinase 2, mitochondrial
- Signal transducer and activator of transcription 2
Sequence:
MEDRRPHLEARPRNPPANHRGPMDGELPPRARNQTNNPAATNHAGRHLRASNHPAPFRQREERFRAMGRNPHQGRRNQEGHTSDEARDQRQSQNDTRRRNDDQEGRSHRPPWSSDTFQQWHTPPQKPGEQPQQTKRLGYKFLESLLQKEPSEVAITLATSLGLKELLSHSSMKPSFLQLICQVLRKACSSRIDRQSILHVLGILNNSKFLRVCLPAYVVGMITEPSPDIRNQYPEHISNIISLLQDLVSVFPASSMQETSMLISLLPTSLNALRASGVDIEEETEKNLEKVQAIIKYLQEKRRQGSLRVDTYTLVQAEAEGEVESYRAMPIYPTYNEVHLDEKPFLRPNIISGKYESTAVYLDTHFRLLREDFVRPLREGILKLLQSFEDQCLRKRKFDDIRIYFDARIITPMCSASGIVYKVQFDTKPLKLVRWQNSKRLLYGSLVCMSKDNFETFLFATVSNREHEDLCQGIVQLCFNEQSQQLLADVQPSDSFLMVETTAYFEAYRHVLEGLQEVQEEDVPFQRNIVQCDSYVRNPRYLLMGGRYDFTPLMENPSAMRKSLRGAEALRHPRINVFDFGQWPSKEALKLDDSQMEALQFALTKELAIIQGPPGTGKTYVGLKIVQALLTNKSVWQINTQTFPILVVCYTNHALDQFLEGIYGCQKTSIVRVGGRSNSEILKQFTLRELRNKREFRRTLPMHLRRAYMSIVTEMKESEQKLQEGAQTLECTMHGVLREQHLEKYISAQHWESLMSGPVQDADWVCVQPSKHSMILEWLGLGVGSFTQSASPAGPENTAQAEGEEEEEGEEEGSLIEIAEEADLIQADRVIEEEEVVRPRRRKKEENGTDQELAKMLLAMRLDQEVPGTTAGPEQATEEWETQRGQKKKMKRRVKVELRKLNTMTKAEANGIQDVWQLDLSSRWQLYRLWLQMYQADTRRRILSYERQYRTWAERMAELRLQEDLHILKDAEVVGMTTTGAAKYRQILQQVEPRIVIVEEAAEVLEAHTIATLSKACQHLILIGDHQQLRPSANVYDLAKNFNLEVSLFERLVKVNIPFVRLNYQHRMRPEIARLLTPHIYQDLENHPSVLKYEQIKGVSSNLFFVEHNFPEQEIQEGKSHQNQHEAHFVVELCQYLLCQEYLPSQITILTTYTGQLFCLRKLMPVKTFAGIKVHVVDKYQGEENDIILLSLVRSNQEGKVGFLQIPNRICVALSRAKKGMYCIGNMQMLAKVPLWSRIIHTLRENNQIGPSLRLCCQNHPETHTLVSKASDFQKVPEGGCSRPCEFRLACGHVCTRACHPYDSSHKEFQCMKPCQKVLCQDGHRCPNVCFQECQPCQVKVPKIILKCGHKQMVPCSMSESEFCCQEPCSKILRCGHRCSHLCGEDCVRLCSERVTVELKCGHSQLVKCGNVEDIKYGLPVKCTTKCDTTLDCGHPCPGSCHSCFEGRFHERCQQPCKRLLICSHKCQEPCTGECPPCQRTCQNRCVHSQCKKKCGELCSPCVEPCVWRCQHYQCTKLCSEPCNRPPCYVPCTKLLACGHPCIGLCGEPCPKKCRVCQPDEVTQIFFGFEDEPDARFVQLEDCSHIFEVQALDRFMNEQKDDEVAIKLKVCPICQVPIRKNLRYGTSIKQRLEEIEIVKEKIQGSAGEISTSQEQLKALLKSKTLFHQLRPEEFLILQEKLAQKNLSVKDLGLVENSIRFYDHLANLEGSLEKVHCGEQQSVRTRLEQVHEWLAKKRLSFSSQELSDLQSEIQRLTYLVNLLMRCKMAEKVKGSIAEEVSSIRNILEKTSKFTQEDEQLVQKKMDALKTTLPCSGLGISDEERVQIVTAMGVPRGHWFKCPNGHIYVITECGGAMQRSTCPECQEVIGGENHTLERSNHLASEMDGAQHPAWSNTANNFMNFEEIHRMM
Protein: ATP-dependent DNA helicase (EC 3.6.4.12) (Q4QH47)
Organism: Leishmania major
Interaction partners:
Sequence:
MAKPKKPASRRCTQRETATPTPAAVTAAEAPVAPANPAADAFRESLDEESFFSSLLQPGKGVSGIADPRESTLVYNALTGRMTSETSVTMQCLRELGFDVNDQRQVIMKHPEVLNALAERVRAGTAALPTKWPVTVARVISAVVMNRHISDPAKALEQMIQVKTNSVMRSRYTSVVSAVNSDLDAAMAQTTAAEQAGMNGGHDPDQAIELNDEQKRVIDIALRGHHLYIGGSAGTGKTVLLRAVARRLQGHRLRVAMTATTGVAGCHIGGSTFHHALGVTSRGEFMRRSIILDYDVIIIDEVSMFPQSLFEEFDRVLREEAGTPDLPFGGVQIILCGDFLQLGCINEKSLIGSPLFHKNFVKIRLETQVRQTANSQFANDLQLMRLGIVPSDLPTTVQLLPPGTMVDSAVNLLPTNKEVHAANERQLQELPGDSLTLTPETGITSLQCETTATLLLRTTPDFNEAEFARHTRSLLQATLDLPRASLLSLYRVYEDGHVMRVMLPPGESVAWRDAMRERFLEIAGLLNDLELGATVTEIIPNGDGLHTPEIEDYLHKVMSKHPIAQPLALKKGCRVLLRSNLSSNLVNGSIGTVVDFVECKEESFPEYIKTESVRRCIDRYRVFCFTECGMPVPMVPVVQFHSGEQIAVPPWEFSVGGGPNTHFYSLSSVALPLSLAYAFTVHKVQGLTLVGRVHLELSRMWPCEHLLYVAMSRVRNPEQLSMSSFTASMVVANETCVHFDKELRGALQLTVADVAKYPISAWKRCNDTIYHLRCRGASLRRLLEGVTSMSGSISPLMVSGSGSSQAHDSRLDRSGRSFASRSRSDGEDDHEALSAHEMTSTSDGSRVMVRVGKHGSGGTGVAGEVNTDDPAFNLEHLSAIQQSVLVARRMRKLVRHVERVARLTEARHRTKSNGRNSKGPAAPEGAAHAASAAVAVVNGSDDASSRRDGAEAEEMDSDEPCDVERAASVMVASVAAAAAASPAISLAVGEEHTF
Protein: TSC22 domain family protein 1 (Regulatory protein TSC-22) (TGFB-stimulated clone 22 homolog) (TSC22-related inducible leucine zipper 1b) (Transforming growth factor beta-1-induced transcript 4 protein) (P62500)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor (By similarity). Acts on the C-type natriuretic peptide (CNP) promoter (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1587811, ECO:0000269|PubMed:19745830}. Nucleus {ECO:0000269|PubMed:1587811, ECO:0000269|PubMed:19745830}. Cell membrane {ECO:0000250|UniProtKB:Q15714}; Peripheral membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250|UniProtKB:Q15714}. Nucleus {ECO:0000250|UniProtKB:Q15714}. Mitochondrion {ECO:0000250|UniProtKB:Q15714}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q15714}. Nucleus {ECO:0000250|UniProtKB:Q15714}. Mitochondrion {ECO:0000250|UniProtKB:Q15714}.
Interaction partners:
- TSC22 domain family protein 4
- Nuclear receptor-binding protein
Sequence:
MHQPPESTAAAAAAADISARKMAHPAMFPRRGSGGGSASALNAAGTGVSGAAPSSEDFPPPSLLQPPPPAASSTQGPQPPPPQSLNLLSQAQLQGQPLAPGGTQMKKKSGFQITSVTPAQISASISSNNSIAEDTESYDDLDESHTEDLSSSEILDVSLSRATDLGEPERSSSEETLNNFQEAETPGAVSPNQPHLPQPHLPHLPQQNVVINGNAHPHHLHHHHHPHHGHHLHHGHHHSSHAAVAGPSIPGGPPSSPVSRKLSTTGSSDGGVPVAPPPAVPSSGLPASVMTNIRTPSTTGSLGINSVTGTSATNNVNIAAVGSFSPSVTNSVHGNANINTSNIPNAASISGGPGVTSVVNSSILSGMGNGTVSSSPVANSVLNAAAGITVGVVSSQQQQQQQQQPTVNTSRFRVVKLDSTSEPFKKGRWTCTEFYEKENAVPATEGVAINKVVETVKQTPTEASSSERESTSGSSVSSSVSTLSHYTESVGSGEMMGAPAVVAPQQPPLPPAPPGLQGVALQQLEFSSPAPQSIAAVSMPQSISQSQMSQVQLQPQELSFQQKQTLQPVPLQATMSAATGIQPSPVSVVGVTAAVGQQPSVSSLAQPQLPYSQTAPPVQTPLPGAPPQQLQYGQQQPMVPAQIAPGHGQPVTQNPTSEYVQQQQQPIFQAALSSGQSSSTGTGAGISVIPVAQAQGIQLPGQPTAVQTQPAGAAGQPIGQAQTAVSTVPTGGQIASIGQQANIPTAVQQPSTQVTPSVIQQGAPPSSQVVLPAPTGIIHQGVQTRASSLPQQLVIAPQSTLVTVPPQPQGVETVAQGVVSQQLPTGSPLPSASTISVTNQVSSAAPSGMPSVPTNLVPPQNIAQPPATQNGSLVQSVSQSPLIATNINLPLAQQIPLSSTQFSTQSLAQAIGSQMEDARRPAEPSLGGLPQTMSGDSGGMSAVSDGSSSSLAAPASLFPLKVLPLTTPLVDGEDESSGASVVAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPPAQPASQGSGSTA
Protein: V-type proton ATPase subunit D (V-ATPase subunit D) (Vacuolar proton pump subunit D) (P34462)
Organism: Caenorhabditis elegans
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B 1
- V-type proton ATPase subunit C
- Probable V-type proton ATPase subunit H 2
- V-type proton ATPase subunit B 2
- Probable V-type proton ATPase subunit F
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit
- Probable V-type proton ATPase subunit G
Sequence:
MSGGGKDRIAVFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAGDFSHTVIQNVSQAQYRVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNRRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANKKKLKEQEAAQKALEGPGPGEDAAHSENNPPRNLLASEEDNLPVLFN