wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase III subunit RPC8 (RNA polymerase III subunit C8) (DNA-directed RNA polymerase III subunit H) (RNA polymerase III subunit 22.9 kDa subunit) (RPC22.9) (Q9Y535)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVFPGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKFDEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKKEAPYTLVGSISEPGLGLLSWWTSN
Protein: DNA transposase THAP9 (EC 2.7.7.-) (THAP domain-containing protein 9) (hTh9) (Q9H5L6)
Organism: Homo sapiens (Human)
Function: Active transposase that specifically recognizes the bipartite 5'-TXXGGGX(A/T)-3' consensus motif and mediates transposition.
Interaction partners:
- PiggyBac transposable element-derived protein 5
Sequence:
MTRSCSAVGCSTRDTVLSRERGLSFHQFPTDTIQRSKWIRAVNRVDPRSKKIWIPGPGAILCSKHFQESDFESYGIRRKLKKGAVPSVSLYKIPQGVHLKGKARQKILKQPLPDNSQEVATEDHNYSLKTPLTIGAEKLAEVQQMLQVSKKRLISVKNYRMIKKRKGLRLIDALVEEKLLSEETECLLRAQFSDFKWELYNWRETDEYSAEMKQFACTLYLCSSKVYDYVRKILKLPHSSILRTWLSKCQPSPGFNSNIFSFLQRRVENGDQLYQYCSLLIKSMPLKQQLQWDPSSHSLQGFMDFGLGKLDADETPLASETVLLMAVGIFGHWRTPLGYFFVNRASGYLQAQLLRLTIGKLSDIGITVLAVTSDATAHSVQMAKALGIHIDGDDMKCTFQHPSSSSQQIAYFFDSCHLLRLIRNAFQNFQSIQFINGIAHWQHLVELVALEEQELSNMERIPSTLANLKNHVLKVNSATQLFSESVASALEYLLSLDLPPFQNCIGTIHFLRLINNLFDIFNSRNCYGKGLKGPLLPETYSKINHVLIEAKTIFVTLSDTSNNQIIKGKQKLGFLGFLLNAESLKWLYQNYVFPKVMPFPYLLTYKFSHDHLELFLKMLRQVLVTSSSPTCMAFQKAYYNLETRYKFQDEVFLSKVSIFDISIARRKDLALWTVQRQYGVSVTKTVFHEEGICQDWSHCSLSEALLDLSDHRRNLICYAGYVANKLSALLTCEDCITALYASDLKASKIGSLLFVKKKNGLHFPSESLCRVINICERVVRTHSRMAIFELVSKQRELYLQQKILCELSGHINLFVDVNKHLFDGEVCAINHFVKLLKDIIICFLNIRAKNVAQNPLKHHSERTDMKTLSRKHWSSVQDYKCSSFANTSSKFRHLLSNDGYPFK
Protein: Glycosyltransferase (Q54Q41)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
Sequence:
MSLNNNNSNNYESDNDEDEDEDEENLLFKDFQSIERRGNKKINYNNNNNNNSNNNNNNNNNNNNNNNNNNNNNNNKNNDIKNIKNNKITNKNNYNNKNFISKLSIINNNKFKKIKNIILQKKNFKNLIIIILSLFFILFLFYIIITFSINNKIYNYTNNKIINNKNDIINQYCINFLNNNNNNNNNNKGEGEEKKEEEEDDDDEKCSFDLNSPDYSCTPISKNRVINFNYSSNYEERVVNWNKPIVSVIVPFLNTDPQQFNECMESILIRQSFKLIEVILIDDGSTNDKSIKSYREWLKREPIRFRVIVNPFNLGLPHSRNIGVYNSRGDYIFFFDSDDILEPTALEKMVWKLNTSSHIQFTKGYLVGFGHTQYIWLKGFEQADKFLIENQVTISIMYKRSMFGNKLQINQSFQVDDYSYGGSDGDGEYFHYPKELLEFQYDSNIRDGMEDWDFHLKCASAGYWGETIPEILEWYRRKDKKTMEKNWKNTLTSKREKFLNDLKLKYSKLYNIGGGGGGNDNQYKSFPNPIRNENEDSFKINFNFIGGSSGGSGGSCNEIKNPLIKKSSTPRILLILPWLNTGGADKFNLNLCKQLVEKGWEITIVTTIESDNKWLSRFQLYTPDIFLFNEKFLPYSSYPSFINYLIDSRNIDVLFISNSEFGYYLLPFIKSNKYNKDNLIIVDYNHMEEEYWRNGGHPRQSIGMSQFIDLHLVSSNHLKNWMLAKSNQIIDENKILVTYINVDMDEFKKSESSRHEIRKSYDITDKEIVILYAARLTNQKKPLEACEIIKELKESLLNDFENQNQNQNQNQNQNQNQNQNQNQNQNQLFKVLFVGDGYLKSKVELYVKQNGLSDVIKLLGDVPTQDMKSIISACDIVFLPSQFEGVSMIFYESMSIGLVPVGSNVGGQSELVTSDCGFLVDITDIGGGNDIDPLEFTNKFVQVLKQLIKNPKKIASMASKCKKRIKSKFQLHKMGGDMISNFCNTIKKKNNQQPQQQQKQLQQQQTLQLNDGGLFNQEFLIQAIEYLKLTNQFEKKKNDFNQLYSLQSELANLKREIKKLELKQK
Protein: Neuronal acetylcholine receptor subunit beta-3 (Q05901)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:O70174}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O70174}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-6
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit alpha-4
- Acetylcholine receptor subunit epsilon
- Cytochrome P450 2A6
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit delta
- Neuronal acetylcholine receptor subunit alpha-7
Sequence:
MLPDFMLVLIVLGIPSSATTGFNSIAENEDALLRHLFQGYQKWVRPVLHSNDTIKVYFGLKISQLVDVDEKNQLMTTNVWLKQEWTDHKLRWNPDDYGGIHSIKVPSESLWLPDIVLFENADGRFEGSLMTKVIVKSNGTVVWTPPASYKSSCTMDVTFFPFDRQNCSMKFGSWTYDGTMVDLILINENVDRKDFFDNGEWEILNAKGMKGNRRDGVYSYPFITYSFVLRRLPLFYTLFLIIPCLGLSFLTVLVFYLPSDEGEKLSLSTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLLFIMIFVTLSIIVTVFVINVHHRSSSTYHPMAPWVKRLFLQKLPKLLCMKDHVDRYSSPEKEESQPVVKGKVLEKKKQKQLSDGEKVLVAFLEKAADSIRYISRHVKKEHFISQVVQDWKFVAQVLDRIFLWLFLIVSVTGSVLIFTPALKMWLHSYH
Protein: Autophagy-related protein 101 (Q54J54)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Autophagy-related protein 13 N-terminal domain-containing protein
- Serine/threonine-protein kinase atg1
- Protein raptor homolog
- Serine/threonine-protein kinase tor
- Protein LST8 homolog
- Ubiquitin-like domain-containing protein
- Serine/threonine-protein phosphatase 2A catalytic subunit A
- Phosphatidylinositol 3-kinase VPS34-like
- Probable serine/threonine-protein kinase vps15
- Ubiquitin-like-conjugating enzyme ATG10
Sequence:
MNSKQYVLKEINLQYAQLKEVVQCILHSILFQRSLGTVKPKDTTLDCVDFSYVKSDDPSSSKHIEDKSEELLTSIMKRKAKTAQISISFYEKRTKTTIFSNNNNVCWEQWIISFQLVHSMDQKSLFSQLTDTINKIIENVNQEKSIPPITSSNEMPFPFSIQIGSENTGGVVDTIYNMFKPPQITK
Protein: Prominin (Q06PM6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDQRNLTLPTPAATTIMSSSSAAMSAGFASLGGPTTSALTGSTIALATTTTAPPTTTPATFFTYSIPGMDIAPGPFIFTYVSEFLSLITPEELPLDSIRDVLHKNTSLLDFASNAIKIESGFIALMSVFAILALVPLIATCAWCCGRRSTQEEVDHIRNAPCHIRDESLEESLRCRKSAGLVTLWVVFILLTLSDFSIFYANSRLSAGIEMTPEMVKSAVHDVEVFLKDTHLQIKQKLDNGFHVSVERVVKDLEDVDVLLGEPIQAEISAHTGLELAYDSLTTLSLANAELIYRVLMLQETVGRALKLSQEAAARMEELQIQLSVLQRQCTYRDRPLCDTLRIRSFEENGVVDALKTLQEDQSIFRMRYLGEIEFGATVKNLTSEVGVSRSIFSNFPQQVKHDTAYERNYTLEQLASIRHRTTANAQQLTSTVNGLLRRLEDTWSSLQPAYNELKEWADAYWSVGWIAGTVIVWVMLFMLMSYCCFLCESNAKSGVVFFIAVMLICLASICLTIFGVFSLAVGGNAEVFVCRSLYDEDYNMLGKLLDKPGYAYAREPQTGIIGELLRPVGVNRSVVNVGLGQALRGCEQNQASYNVFQLDAFVNTSKIADLRQFPKVSTAIDAISVSGRTLLSLTQSVQNILENMLQTSSFNLTTYRSSVGAPTPEKDLATFIDQMQRVALQIQDVATSSRMTTLGSRSKRLQASILQPLENLQNEILYHLTALELQRDPWAKQVNQTLNHLKSIQSYLENKAGEICHNMTRDYRDRLKAYLTTSKATMESQLGDTTTKCRPFYDTFDASRTFLCRNMVDFINGLTFFIFLTLLLWAIGTPVGLNLITVQTRLNVMQAAQARSKGRHRRSDRSPEHEQRSGSRGRKKQRTSSSATSGRSGKRDQSRERSTSSTARPKPPL
Protein: Non-structural protein NS2 (Q84361)
Organism: Aleutian mink disease parvovirus (strain G) (ADV)
Function: Plays a role in viral DNA replication.
Subcellular location: Host nucleus {ECO:0000269|PubMed:24606679}. Note=Localizes within the viral DNA replication centers.
Interaction partners:
Sequence:
MAQAQIDEQRRLQDLYVQLKKEINDGEGVAWLFQQKTYTDKDNKPTKATPPLRTTSSDLRDYWTKLECHNCHEEYWQLTTYYCKECRKCEHGKLRHTKKECEQCACKAAQETSA
Protein: Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein) (P0C434)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}.
Interaction partners:
- Cytochrome b559 subunit alpha
- Cytochrome b559 subunit beta
- Photosystem II D2 protein
- Photosystem II CP43 reaction center protein
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
- Photosystem II reaction center protein J
- Photosystem II reaction center protein M
- Photosystem II reaction center protein L
Sequence:
MTAILERRESTSLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAALEVPSLNG
Protein: Importin-5 (Imp5) (Importin subunit beta-3) (Karyopherin beta-3) (Ran-binding protein 5) (RanBP5) (O00410)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation (By similarity). In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev.
Subcellular location: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus.
Interaction partners:
- GTP-binding nuclear protein Ran
- Importin-11
- Importin subunit beta-1
- Large ribosomal subunit protein uL23
- Importin-7
- Interferon regulatory factor 3
- THO complex subunit 4
- Exportin-1
- Importin-4
- Sentrin-specific protease 3
Sequence:
MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA
Protein: Zinc finger protein 664 (Zinc finger protein 176) (Zinc finger protein from organ of Corti) (Q8N3J9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Coiled-coil domain-containing protein 92
- Dynein axonemal heavy chain 10
Sequence:
MIYKCPMCREFFSERADLFMHQKIHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCGKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSSHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKPYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI
Protein: Fatty acid-binding protein, adipocyte (AP2) (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (A-FABP) (AFABP) (Fatty acid-binding protein 4) (O97788)
Organism: Sus scrofa (Pig)
Function: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Involved in the regulation of intramuscular fat accretion.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P04117}.
Interaction partners:
- C1q domain-containing protein.
- Gastrotropin
- Fatty acid-binding protein, liver
- Peroxisome proliferator-activated receptor gamma
- Fatty acid-binding protein, intestinal
- Fatty acid-binding protein, heart
- FABP domain-containing protein
- Hormone-sensitive lipase
- Uncharacterized protein.
- Fatty acid synthase
Sequence:
MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNLIITVNGDMITIRSESTFKNTEIAFKLGQEFDEVTADDRKVKSTITLDGGALVQVQKWDGKTTTINRKIVDDKLVVECIMKGVTATRIYERA
Protein: Ataxin 7, isoform A (Ataxin 7, isoform B) (Ataxin 7, isoform C) (Ataxin 7, isoform D) (LD40170p) (Q9VQB6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SAGA factor-like TAF6
- Transcriptional adapter 1-2
- Transcriptional adapter 2b
- Protein will decrease acetylation
- SAGA-associated factor 29kDa
- SAGA complex subunit Spt20
- SAGA complex subunit Spt3
- SAGA-associated factor 11 homolog
- Transcriptional adaptor 3, isoform C
- Ubiquitin carboxyl-terminal hydrolase nonstop
Sequence:
MPLNDVAPAGGGAYPENGTKHKVSGMWKPDSSAGSNSGSGSAGLSLFSLQGQKWQQVFDMEKVIKQLRTAEKTYLRGGKNSSAGADQQAKVQVQRLQSADMAYYDLAPKLASRDIVLCSSCSGCYTKAGFQHHIALQHPSVWEATSSKVNPNPNGTAISSDSRLTATEISQEGGAIVPSSPTDTLSASTLSSCSNGSSSSASLQHPAAAGSSSTTSSSSSSRHKSSSSKSSSSSSSKGSSSTSAGSRSRSKSSKNRHHSSPAPALLESNHKESKGSKKSSAIAAPPVVAAVVKEEPPSVGAAPAAITMFSSSSNSSCSLPPTPTLGAASSEVAMGVNYSPAQLQTDAEKLPELQPKKKLKGSSDHRIKAEKEKNKDKSLVNSYEQQQVLSELDQAVSSITGAVSAEQVAPDEEELPLPNTSDENSISQTLDEMLDSKLINEILNNFDESALDTSQQQSQQQAQNGSLSHPAQATKRLRFEDGTIGEDYAVYQQQAVQQVYGEEEHQQELTTIDAMQLQQLIYQQQQMLEQQQLQEQQQQQQQDQKLQDHEQQRQFSVYNVPSLTDEAMVNPQQQQLEEHMILPSIIYEITESNPVSMLEQKVLAEFLTNAGYENVDVNVVQSGGIQTNLSSGTEANQLADELADFEFSKLETVSDTVKTVKLEAKAASQPPTTNPQINHHPSLANAKYHEDSYFNVMLYSGAPRPLAMNTFGMVKLPQGLGVTFRKNLLTTRKANNNLLSLSGGNHLGVVGQLARTPPPPSPALSNGLPGKNPASGRTIYAQRSNVIAQDRLRCNKRALVGGKAGGGSSGSPGVMTAKRLNELLMGKAKKEEKPPPDSEDGGEQPTKDKERDKEEDNKLTFSFYEKRRRLLAGKLEQLQPLGRPSFTLPLQSNHNASQSQSHSPQQLLKKQLLRTLSDSSSNMNISNMNNISNLNSSNTPSANSNPPWKGNSSNPGGNSTPTSSDLMRVFV
Protein: Biofilm-associated metzincin protease inhibitor (Q9I061)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Inhibitor of the metalloendopeptidase Mep72. Forms a protein-protein complex with the protease, which is the product of its coregulated adjacent gene, and probably prevents premature protease activity until the protein has been secreted.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peptidyl-Asp metalloendopeptidase
- Uncharacterized protein
Sequence:
MAKTWIYAASAAAIGGALIGGWLLDPAPPEASPQARQSPAAQAAAAPTAALAAPAADATRMLAPTPVTTPAPRERVTLWQGELRSREGAQGIPEYLAQVEPALLDTLALGQVLEMSLPGRERPLQARLASTHNSAGLPVWRGGLVDGDEAESLTVVRGSLETHINVATLDGSYSIIVDNRSGKTRVIDENDIAARSDPHGDHVDAPLAELPPMPPPAQG
Protein: Uncharacterized transporter C405.03c (O94654)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MVLQAIGKHALGVVLLLFVVFLWLISSFLTSSLLDDDNFFSPFLITYINTGTFVFYLIPWYFSEKKTRKHRLMSELSMYESVHDSSFNLGTRPNSPLGFRQTAYLSLGFCIIWFAANYFSNSSLGFTNVASFTIISSMSGFFTLGLGTIVNVERFTLSKLLALMASVGGVIIVVTQDAKQADLNDSPPSRPALGNAYALLAALLYGCYSVMVKFHITEESCVSTRLFFGLVGLFDLILLWPFLIILHLYGVERFSLPSTTAGLIVLIINASITFVSDYLWVIAMLMTSPLLVTVGMSLSIPLALFFDILLKGHYLNFSLILGSLLVFAGFIVVNYNQQNII
Protein: Nucleoprotein (EC 3.1.-.-) (Nucleocapsid protein) (Protein N) (P05133)
Organism: Hantaan virus (strain 76-118) (Korean hemorrhagic fever virus)
Function: Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure. As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation. Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). Suppresses apoptosis probably through the inhibition of nuclear import of NF-kappa-B.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12573574}. Host Golgi apparatus, host cis-Golgi network {ECO:0000269|PubMed:24070985}. Note=Internal protein of virus particle. {ECO:0000305}.
Interaction partners:
Sequence:
MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQDPTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFKDDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWLIEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCLFIAGIAELGAFFSILQDMRNTIMASKTVGTSEEKLRKKSSFYQSYLRRTQSMGIQLGQRIIVLFMVAWGKEAVDNFHLGDDMDPELRTLAQSLIDVKVKEISNQEPLKL
Protein: Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (E47 interaction protein 1) (EIP1) (Stimulated by retinoic acid gene 13 protein) (O35185)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2 (By similarity). Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes (By similarity). Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May function as a transcriptional factor for neuronal differentiation. Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (By similarity). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}.
Interaction partners:
- Class E basic helix-loop-helix protein 41
- Basic helix-loop-helix ARNT-like protein 1
- Cryptochrome-1
- Period circadian protein homolog 2
- Circadian locomoter output cycles protein kaput
- Neuronal PAS domain-containing protein 2
- Nuclear receptor subfamily 1 group D member 1
- Nuclear receptor subfamily 1 group D member 2
- Period circadian protein homolog 3
- Cryptochrome-2
Sequence:
MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD
Protein: Mono(2-hydroxyethyl) terephthalate hydrolase (MHET hydrolase) (MHETase) (EC 3.1.1.102) (A0A0K8P8E7)
Organism: Piscinibacter sakaiensis (Ideonella sakaiensis)
Function: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MHET) into its two environmentally benign monomers, terephthalate and ethylene glycol. Does not show activity against PET, bis(hydroxyethyl) terephthalate (BHET), pNP-aliphatic esters or typical aromatic ester compounds catalyzed by the tannase family enzymes, such as ethyl gallate and ethyl ferulate.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26965627}.
Interaction partners:
- NADH-quinone oxidoreductase
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit F
- NAD-dependent formate dehydrogenase, beta subunit
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit B
- NAD-dependent formate dehydrogenase, gamma subunit
- NADH-ubiquinone oxidoreductase, chain E
- NADH-ubiquinone oxidoreductase, chain M
Sequence:
MQTTVTTMLLASVALAACAGGGSTPLPLPQQQPPQQEPPPPPVPLASRAACEALKDGNGDMVWPNAATVVEVAAWRDAAPATASAAALPEHCEVSGAIAKRTGIDGYPYEIKFRLRMPAEWNGRFFMEGGSGTNGSLSAATGSIGGGQIASALSRNFATIATDGGHDNAVNDNPDALGTVAFGLDPQARLDMGYNSYDQVTQAGKAAVARFYGRAADKSYFIGCSEGGREGMMLSQRFPSHYDGIVAGAPGYQLPKAGISGAWTTQSLAPAAVGLDAQGVPLINKSFSDADLHLLSQAILGTCDALDGLADGIVDNYRACQAAFDPATAANPANGQALQCVGAKTADCLSPVQVTAIKRAMAGPVNSAGTPLYNRWAWDAGMSGLSGTTYNQGWRSWWLGSFNSSANNAQRVSGFSARSWLVDFATPPEPMPMTQVAARMMKFDFDIDPLKIWATSGQFTQSSMDWHGATSTDLAAFRDRGGKMILYHGMSDAAFSALDTADYYERLGAAMPGAAGFARLFLVPGMNHCSGGPGTDRFDMLTPLVAWVERGEAPDQISAWSGTPGYFGVAARTRPLCPYPQIARYKGSGDINTEANFACAAPP