wanglab/gogpt-training-data huggingface dataset:
Protein: Brm protein (O35846)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PGPPSVSHPLSTMGSADFPQEGMHQLHKPMDGIHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPISGGGPTPPQMPPSQPGRLIPGDPQAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGRPLPETLQLAVQGKRTLPGMQQQQQQQQQQQQQQQQQQQQQPQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSYNRPSGPGQELLLSGQSAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGASVQQPAPG
Protein: Transcriptional regulatory protein rxt3 (O94707)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Putative histone deacetylase complex subunit cti6
- Transcriptional regulatory protein rxt2
- Transcriptional regulatory protein sds3
- Paired amphipathic helix protein pst3
- Histone deacetylase clr6
- Paired amphipathic helix protein pst2
- Paired amphipathic helix protein pst1
- Uncharacterized protein C22E12.19
- Chromatin modification-related protein eaf3
- Chromatin modification-related protein png2
Sequence:
MEEKTPENEQSKKTFDPKDSMKIEETSTNGSSQPSQPSNIKLSIGSILESSNDNGDPEYSENGMGNMNMNTLPMATSTPMSYTKQPSEAKYPNSVWERKGVSDQEENTSSVKRQKTLPTQSSGEEEAKYSHPGAPTATSADSISMESRPSNLSTSLSKTTSYPQFQVRQFVSPIISIDNSALEPFLNRYPASESLFPVTEYEYTPWLEFPLLYSSIGKFVRVTIDIKWLNAAINPRLCRREIWGTDVYTDDSDIATILAHCGCFSLLKPVRKIAVVDLYILPPLVHYKGTRKNQIESRSWSSRQDGISLKIKEVTWKPACASIFENSIHTLTLEERLQARLELSRSSTFKI
Protein: Error-prone DNA polymerase (EC 2.7.7.7) (Q6MQS6)
Organism: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
Function: DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01902}.
Interaction partners:
- DNA polymerase Y family protein
- DNA polymerase III subunit gamma/tau
- Excinuclease ABC subunit C
- DNA polymerase III subunit delta
- Beta sliding clamp
- DNA polymerase III subunit delta'
- DNA polymerase III polC-type
- DNA polymerase III alpha subunit
- DNA polymerase III subunit alpha
- RecA protein
Sequence:
MTNKALIPSQNSRLPAKPRPRAKGFVELLGRSNFSFLQGASSPEEMVSQAVEFGYDGMALCDLNGLYGVVRGFQTIQSPSLFTASPQVKENFHYLIGSELTLTDESSVVLIPMNKQGYSHLCEILTLGKRQAAKGFSKLSLEQIEKYNQGLLCLALPPWTDERYEKLEKIFDNRLYLPLWRDLTWESQEFCRQGFALEEKYKAQLFVTQRPFMHSPERKPLFDVLTCTLHHTTLAEAKNKLIQNSERCLKSLEDISWLWQDRLDLVEKTVEISARVTFSLNEIRYRYPASSLPSGMTPTEYMRHLTLKGAESRYPEGIPDKALKQIEHELELIKDLQYEDYFLTLKEICDFASERKILYQGRGSAANSVVCFCLGLTAIDPVKMDLLFERFLSRERREPPDIDIDFEHSRREEVIQHIYEKYNERHAAMVCTVIRYRSRMAIRETAKVFGMPLAKINAMIKFMGRDGMKRLLDPAVAADFGMEPGPWKMFMALAQQLHGFPRHLGIHTGGFLITQDPITEMVPVEKATMNGRYVIQWNKDDVDFLRLMKIDVLSLGMLTCLRKCFDLLRDVKGRDYSLATLPADDKPTYDMICRAETVGVFQIESRAQMNTLPRMQPRNFYDLVIEIALIRPGPLQGGMVHPFLKLRQNPPKEIKYAHPALEPILKKTMGIPIFQEQVMKMVVAVADFTPGEADELRRVMSSAWKRKATMGGIEQRLRTGFARHGISSEYADQIFKTIEGFANYGFPESHSASFALLTYASCYLKCHYPDVFACGLLNSQPMGFYAPRTIIAEAQRNGVVVAPLDVQKSDYDYTIEKTAAGDLLRVGLRSIYGIPEVLIRRIEDSRKEEGLYIDLADFIRRTQLPRSVLLKLAAAGAFESFNSNVRELIWNLESLSLDQQSFLWGHPKEQFELGEDDDEPEHLPFESNWDRLRREYDSKGYSVESHPMSVLRTYLHSKSEALREKRFVPYFSSEDLKRMKTKTKVRVAGLVAITQRPPTAKGMCFITLEDEFGFVNIVIHPEIYQKDRTTIYTRSLLEIHGQVEKVGAITNIRAERILPLG
Protein: SMC5-SMC6 complex localization factor protein 1 (Ankyrin repeat domain-containing protein 32) (BRCT domain-containing protein 1) (Protein BRCTx) (Q8R3P9)
Organism: Mus musculus (Mouse)
Function: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions.
Subcellular location: Nucleus {ECO:0000269|PubMed:15632077, ECO:0000269|PubMed:22036607}. Cytoplasm {ECO:0000269|PubMed:15632077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15632077}. Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage (PubMed:22036607). Colocalizes with RAD18 in the nucleus and to centrosomes (PubMed:15632077). Associates with chromatin. Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q9BQI6, ECO:0000269|PubMed:15632077, ECO:0000269|PubMed:22036607}.
Interaction partners:
- Cell division control protein 45 homolog
- SMC5-SMC6 complex localization factor protein 2
- 26S proteasome non-ATPase regulatory subunit 12
- TP53-binding protein 1
- E3 ubiquitin-protein ligase RAD18
- DNA replication licensing factor MCM5
- Mediator of DNA damage checkpoint protein 1
- PAX-interacting protein 1
- Serine/threonine-protein kinase ATR
- DNA replication licensing factor MCM3
Sequence:
MEDSATKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTYEWGYKIEKDSHYSPQMQSAPKRWREELKRTGAPGAFHRWKVVLLVRADKRSDSLVRVLEAGKANVILPKNSPSGITHVIASNARISAEREQENFKAPFYPIQYLGDFLLEKEIQNDEHSQISPAWTKYNNQEKGNDVGFPEMKGAGENMYRTQNKMENHNKNVSDRFVLSEHHKKKFKDFRKDIRSVKKRNTLRRHGLENQKETKKKDKNIQRSYILRKKNKKEGYCKTDDAHDTIRSMLKKRGHYREQKEMKNPLLTDGTKESKTKDVKTNMNLIEIKNALKKQIYKDIYRAQAVRYNCIRVDKQPVYNVEVKNSEFPRGILNLIENLIEGQFFKEAIEELSSLQAHYIPPVCLLHAILENVLQDKIDTFSGRYFHILSALLHLHPPWKSPAMLKYYLELFQCPTCMKGAWDFTEVLIRSCLFNEDFCHQISENISTKVVNLTLLKFFFNLLEGEVRHLSQKLCDWSDSQSLKVTEKAILHEIFWSGSETSGLLTKPVNMLLEWTIYSHKEKCKSNDVFKHELSYLLTGILGAAVDYWIFLGIQMGRNVIRHMSDDLGSYISLSCDDFSSKELEIFICSFSSSWLQMFVAEAIFKKLCLQGPTSTCTEPLSLQKIIDSYLPILGKMDIHGAGKMQSPKKLCQRPCLESQRALLMLNGAKRKQAEGRPELLELNRAKCSSSLKKLKKKSEELSCSKENCPSLVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKTQKHFYHQQLEFGSFLLSRMLINFCSIFDLSSEFILAFKGLGHLNELLMACNSDTEASNAHTDWLLDVYARNIKTLKKLPSVLKELPENLNVCPGVHTEALLVTLKMMCQSITELS
Protein: Scarecrow-like protein 4 (AtSCL4) (GRAS family protein 32) (AtGRAS-32) (Q9FL03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18500650}.
Interaction partners:
- Protein PAT1 homolog
- Holliday junction resolvase MOC1, chloroplastic
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Putative scarecrow-like protein 16
- Phytochrome A
Sequence:
MAYMCTDSGNLMAIAQQVIKQKQQQEQQQQQHHQDHQIFGINPLSLNPWPNTSLGFGLSGSAFPDPFQVTGGGDSNDPGFPFPNLDHHHATTTGGGFRLSDFGGGTGGGEFESDEWMETLISGGDSVADGPDCDTWHDNPDYVIYGPDPFDTYPSRLSVQPSDLNRVIDTSSPLPPPTLWPPSSPLSIPPLTHESPTKEDPETNDSEDDDFDLEPPLLKAIYDCARISDSDPNEASKTLLQIRESVSELGDPTERVAFYFTEALSNRLSPNSPATSSSSSSTEDLILSYKTLNDACPYSKFAHLTANQAILEATEKSNKIHIVDFGIVQGIQWPALLQALATRTSGKPTQIRVSGIPAPSLGESPEPSLIATGNRLRDFAKVLDLNFDFIPILTPIHLLNGSSFRVDPDEVLAVNFMLQLYKLLDETPTIVDTALRLAKSLNPRVVTLGEYEVSLNRVGFANRVKNALQFYSAVFESLEPNLGRDSEERVRVERELFGRRISGLIGPEKTGIHRERMEEKEQWRVLMENAGFESVKLSNYAVSQAKILLWNYNYSNLYSIVESKPGFISLAWNDLPLLTLSSWR
Protein: Regulator of G-protein signaling 9-binding protein (RGS9-anchoring protein) (Q148R9)
Organism: Mus musculus (Mouse)
Function: Regulator of G protein-coupled receptor (GPCR) signaling in phototransduction. Participates in the recovery phase of visual transduction via its interaction with RGS9-1 isoform. Acts as a membrane-anchor that mediates the targeting of RGS9-1 to the photoreceptor outer segment, where phototransduction takes place. Enhances the ability of RGS9-1 to stimulate G protein GTPase activity, allowing the visual signal to be terminated on the physiologically time scale. It also controls the proteolytic stability of RGS9-1, probably by protecting it from degradation.
Subcellular location: Membrane {ECO:0000269|PubMed:12119397}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12119397}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 9
- Regulator of G-protein signaling 11
- Regulator of G-protein signaling 7-binding protein
- Regulator of G-protein signaling 6
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 7
- Rhodopsin
- Rod outer segment membrane protein 1
- Aryl-hydrocarbon-interacting protein-like 1
Sequence:
MAREECKALLDALNKTTACYHHLVLTVGGSADTQDLREELQKTRQKARELAVATGARLTVALRDRSLATEERAEFERLWVAFSGCLDLLEADMQRALALGATFPLHAPRRPLVRTGVTGGSSAVAARALSARSLRHEAESDFDVADLPQLEREVLQVGEMIDDMEMKVNVPRWTVQARQAAGAELLSGASAGASSAGGISVEERAGPCDPSKALAATVFSAVLLVAVALALCVAKLS
Protein: Probable 1,4-alpha-glucan branching enzyme Rv3031 (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Branching enzyme) (BE) (P9WQ27)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position (Probable). Is probably involved in the biosynthesis of 6-O-methylglucosyl lipopolysaccharides (MGLP).
Interaction partners:
- Glycogen synthase
- Probable S-adenosylmethionine-dependent methyltransferase Rv3030
- 1,4-alpha-glucan branching enzyme GlgB
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Glycogen phosphorylase
- Glycogen operon protein GlgX homolog
- 4-alpha-glucanotransferase
- Trehalose synthase/amylase TreS
- Probable acetyltransferase Rv3034c
- Diglucosylglycerate octanoyltransferase
Sequence:
MNTSASPVPGLFTLVLHTHLPWLAHHGRWPVGEEWLYQSWAAAYLPLLQVLAALADENRHRLITLGMTPVVNAQLDDPYCLNGVHHWLANWQLRAEEAASVRYARQSKSADYPSCTPEALRAFGIRECADAARALDNFATRWRHGGSPLLRGLIDAGTVELLGGPLAHPFQPLLAPRLREFALREGLADAQLRLAHRPKGIWAPECAYAPGMEVDYATAGVSHFMVDGPSLHGDTALGRPVGKTDVVAFGRDLQVSYRVWSPKSGYPGHAAYRDFHTYDHLTGLKPARVTGRNVPSEQKAPYDPERADRAVDVHVADFVDVVRNRLLSESERIGRPAHVIAAFDTELFGHWWYEGPTWLQRVLRALPAAGVRVGTLSDAIADGFVGDPVELPPSSWGSGKDWQVWSGAKVADLVQLNSEVVDTALTTIDKALAQTASLDGPLPRDHVADQILRETLLTVSSDWPFMVSKDSAADYARYRAHLHAHATREIAGALAAGRRDTARRLAEGWNRADGLFGALDARRLPK
Protein: Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) (Q9WTU6)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P45984}. Nucleus {ECO:0000269|PubMed:29153991}. Note=Colocalizes with POU5F1 in the nucleus. {ECO:0000269|PubMed:29153991}.
Interaction partners:
- Transcription factor Jun
- Dual specificity mitogen-activated protein kinase kinase 4
- C-Jun-amino-terminal kinase-interacting protein 1
- Stress-activated protein kinase JNK
- C-Jun-amino-terminal kinase-interacting protein 2
- Mitogen-activated protein kinase 10
- Transcription factor JunD
- Apoptosis regulator Bcl-2
- Dual specificity mitogen-activated protein kinase kinase 7
- Cellular tumor antigen p53
Sequence:
MSDSKSDGQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMAEMVLHKVLFPGRDYIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVKDQPSDAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR
Protein: Spore wall and anchoring disk complex protein EnP1 (Host cell adhesion protein EnP1) (Q8SWL3)
Organism: Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Function: Spore wall protein involved in the adhesion to host cells surface glycoaminoglycans (GAGs). Microsporidian spore adherence is an integral part of activation and host cell invasion which requires the extrusion at the spore apex of a very long and coiled structure, the polar tube, through which the sporoplasm is pushed to enter into the potential host cell.
Subcellular location: Spore wall {ECO:0000269|PubMed:16368098, ECO:0000269|PubMed:16469199, ECO:0000269|PubMed:17557882}. Spore, perispore {ECO:0000269|PubMed:16469199}. Note=Also localizes at the anchoring disk complex which consists of the polar sac and the anchoring disk, playing a crucial role in the rupture of the spore wall and the subsequent release of the polar tube following activation. {ECO:0000269|PubMed:17557882}.
Interaction partners:
- GUANINE NUCLEOTIDE-BINDING PROTEIN BETA SUBUNIT
- Histone H4
- Histone acetyltransferase type B subunit 2
- Histone H2B
- CHROMOBOX PROTEIN
- Histone H3.1
- Histone H3-like protein
- Uncharacterized LisH domain-containing protein ECU04_1490
- Spore wall protein 1
Sequence:
MKLLGFLIVGLSAISALKTKALHLTCEQELRPYSAVVDANCMAFALNGSNIHEAIKYLQAMNIKKAYVLYWNDHDLRGTPMVLYDNGALAPFDPYTNTAKYVLCVEACPCPGSKAASVGGFQAATSSEKIYVEGSARPAQCSEVCIEPVERRPHYKKIVVNPSPSNCIPCEPECYDSSSSSECNKKRCKTFPRICKEKCGSRRRGCPRKVEVLKSQKTYTFDIEKYRRRGEVVVRVCSKDSKEKFERFILSRNGEIRGNNNKNCILEPLPKCLRCPGQLHKLKKHIERKVCQEVCMYINAKCDIFVLVGDCDFYRVVVNDRRRYRNLHLKKVRGHKLRELIKHGLFGVEFGPLDLDR
Protein: Nuclear fusion protein KAR5 (Factor-induced gene 3 protein) (Karyogamy protein 5) (Q04746)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for nuclear membrane fusion during karyogamy.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
Interaction partners:
- Pheromone-regulated membrane protein 3
- DnaJ-like chaperone JEM1
- Translocation protein SEC66
Sequence:
MFEMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAETRVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNITELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQIIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKKQLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDISEKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIKRYYQWAALLLSIYLGAKTGSLIDF
Protein: Phospholipid scramblase 2 (PL scramblase 2) (Ca(2+)-dependent phospholipid scramblase 2) (Q9DCW2)
Organism: Mus musculus (Mouse)
Function: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.
Subcellular location: Membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}.
Interaction partners:
Sequence:
MEAPRSGTYLPAGYAPQYPPAAVQGPPEHTGRPTFQTNYQVPQSGYPGPQASYTVSTSGHEGYAATRLPIQNNQTIVLANTQWMPAPPPILNCPPGLEYLNQIDQLLIHQQVELLEVLTGFETNNKFEIKNSLGQMVYVAVEDTDCCTRNCCEASRPFTLRILDHLGQEVMTLERPLKCSSCCFPCCLQEIEIQAPPGVPIGYVTQTWHPCLPKLTLQNDKRENVLKVVGPCVACTCCSDIDFEIKSLDEVTRIGKITKQWSGCVKEAFTDSDNFGIQFPLDLEVKMKAVTLGACFLIDYMFFEGCE
Protein: Trihelix transcription factor ASIL1 (6B-interacting protein 1-like 1) (Trihelix DNA-binding protein ASIL1) (Q9SYG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription repressor that binds specific DNA sequence such as the GT-box-like motif 5'-CGTGATT-3' in the AT2S3 promoter. Negative regulator of seed maturation genes during seed germination and seedling development. May target GT-box-containing embryonic genes by competing with the binding of transcriptional activators to this promoter region. Contributes to the maintenance and control of seed filling and may repress the maturation program during early embryogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:19155348}.
Interaction partners:
- At5g63780
- Trihelix transcription factor GTL2
- Trihelix transcription factor GT-1
- Trihelix transcription factor GT-3a
- B3 domain-containing transcription factor FUS3
- B3 domain-containing transcription factor LEC2
- At3g10000
- B3 domain-containing transcription repressor VAL1
- Trihelix transcription factor GT-3b
- Ribonuclease J
Sequence:
MEDDDEIQSIPSPGDSSLSPQAPPSPPILPTNDVTVAVVKKPQPGLSSQSPSMNALALVVHTPSVTGGGGSGNRNGRGGGGGSGGGGGGRDDCWSEEATKVLIEAWGDRFSEPGKGTLKQQHWKEVAEIVNKSRQCKYPKTDIQCKNRIDTVKKKYKQEKAKIASGDGPSKWVFFKKLESLIGGTTTFIASSKASEKAPMGGALGNSRSSMFKRQTKGNQIVQQQQEKRGSDSMRWHFRKRSASETESESDPEPEASPEESAESLPPLQPIQPLSFHMPKRLKVDKSGGGGSGVGDVARAILGFTEAYEKAETAKLKLMAELEKERMKFAKEMELQRMQFLKTQLEITQNNQEEEERSRQRGERRIVDDDDDRNGKNNGNVSS
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Glyoxalase I) (B9DH52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSYSIASAISRISPLIRFVKPYSTGFSFITCACNSTRRPKRFDQLCVFSMASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA
Protein: Psi-producing oxygenase A (Fatty acid oxygenase ppoA) [Includes: Linoleate 8R-lipoxygenase (EC 1.13.11.60); 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (EC 5.4.4.5)] (Q4WPX2)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively. Oxylipins may also serve as activators of mammalian immune responses contributing to enhanced resistance to opportunistic fungi and as factors that modulate fungal development contributing to resistance to host defenses.
Interaction partners:
- Linoleate 10R-lipoxygenase
- Fatty acid oxygenase, putative
- Patatin-like phospholipase domain-containing protein
- Lysophospholipase
Sequence:
MSEKQTGSANGGLGKTLAQLEQVVSASLRPLPSQTGDGTYVTEQVKTGILKDLSHVDLGDLKTLVDVSKSALTGEALDDRKYIMERVIQLSAGLPSTSQIGKELTNTFLTTLWNDLEHPPISYLGRDAMYRRADGSGNNVLWPHIGAAGTPYARSVQPKTVQSPNLPDPETLFDCLLARKEYKEHPNKISSVLFYIASIIIHDLFETDRKDPAISLTSSYLDLSPLYGNNQQEQDLIRTFKDGKLKPDCFSTKRVLGFPPDVGVVLIMFNRFHNYVVEKLAMINEGGRFTKPQESDTAAYAKYDNDLFQTGRLVTCGLYVNIILKDYVRTILNINRTDSIWSLDPRSEMKDGLLGRAAAQATGNQVAAEFNLVYRWHSCISQRDQKWTEDMYQELFPGQDPSKISLQDFLRGLGRWEAKLPGEPRERPFAGLQRKADGSYDDNDLVKIFEESVEDCAGAFGALHVPTVFRSIEALGIQQARSWNLATLNEFRKYFNLAPYKTFEEINSDPYVADQLKRLYDHPDRVEIYPGIIVEDAKESMAPGSGLCTNFTISRAILSDAVALVRGDRFHTVDFTPKHLTNWAYNEIQPQDSVDQTHVFYKLVLRAFPNHFRGDSIYAHFPLVVPSENKKILTKLGTADKYSWDRPNYTPPPQFINSHSACMSILSDQETFKVTWGSKIEFLMRHNNQPYGRDFMLSGDRTPNAMSRQMMGKALYRDKWETEVKRFYENITLKLLHRYSYKLAGVNQVDVVRDIANLAQVHFCASVFSLPLKTESNPRGIFTESELYQIMAVVFTSIFYDADIGKSFELNQAARAVTQQLGQLTLANVELIAKTGFIANLVNSLHRHDVLSEYGVHMIQRLLDSGMPAPEIVWTHVLPTAGGMVANQAQLFSQSLDYYLSEEGSVHLPEINRLAKEDTTEADDLLLRYFMEGARIRSSVALPRVVAQPTVVEDNGQKITLKQGQHIICNLVSASMDPVTFPEPDKVKLDRDMNLYAHFGFGPHQCLGLGLCKTALTTMLKVIGRLDNLRRAPGGQGKLKKLSGPGGIAMYMTPDQTAFFPFPTTMKIQWDGDLPEVKE
Protein: Thermosensitive gluconokinase (EC 2.7.1.12) (Gluconate kinase 1) (P39208)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- L-idonate 5-dehydrogenase
- Phosphogluconate dehydratase
- 5-keto-D-gluconate 5-reductase
- Glyoxylate/hydroxypyruvate reductase B
- 6-phosphogluconolactonase
- Thermoresistant gluconokinase
- High-affinity gluconate transporter
- HTH-type transcriptional regulator IdnR
- Low-affinity gluconate transporter
Sequence:
MAGESFILMGVSGSGKTLIGSKVAALLSAKFIDGDDLHPAKNIDKMSQGIPLSDEDRLPWLERLNDASYSLYKKNETGFIVCSSLKKQYRDILRKGSPHVHFLWLDGDYETILARMQRRAGHFMPVALLKSQFEALERPQADEQDIVRIDINHDIANVTEQCRQAVLAIRQNRICAKEGSASDQRCE
Protein: 40-kDa huntingtin-associated protein (Factor VIII intron 22 protein) (M0RDU0)
Organism: Rattus norvegicus (Rat)
Function: RAB5A effector molecule that is involved in vesicular trafficking of early endosomes. Mediates the recruitment of HTT by RAB5A onto early endosomes. The HTT-F8A1/F8A2/F8A3-RAB5A complex stimulates early endosomal interaction with actin filaments and inhibits interaction with microtubules, leading to the reduction of endosome motility.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23610}. Nucleus {ECO:0000250|UniProtKB:P23610}. Early endosome {ECO:0000250|UniProtKB:P23610}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q00558}. Note=Diffuse presence in the cytoplasm and accumulation in the nucleus (By similarity). In absence of HTT, F8A1/F8A2/F8A3 is concentred in cytoplasm (By similarity). Colocalized with HTT in endosomes (By similarity). In neuron found in intranuclear structures, the intranuclear rodlets (INRs), also known as rodlets of Roncoroni, in association with ubiquitin (By similarity). {ECO:0000250|UniProtKB:P23610, ECO:0000250|UniProtKB:Q00558}.
Interaction partners:
- Huntingtin
Sequence:
MAAGSASSLGGGSWPGSEAGDFLARYRQVSNKLKKRFLRKPNVAEAGEQFAQLARELRAQECLPYAAWCQLAVARCQQALFHGPGEALALTEAARLFLRQECDARQRLGCPAAYGEPLQAAASALGAAVRLHLELGQPAAAAALCLELAAALRAVGQPAAAAGHFQRAAQLHLPLMPLAALQALGDAASCQLLARDYTGALAVFTRMQRLAREHGGHPVQQPELPQQLPSVPQPSLPGPQPRPVLGSTLPLPLPPDHAPGSVAQSPGTLGAFADVLVRCEVSRVLLLLLLQPPPAKLLPEHAQTLEKYSWEAFDGHGQDSSGQLPEELFLLLQSLVMAAHEKDTEGIKKLQVEMWPLLTAEQNHLLHLVLQETISPSGQGV
Protein: Uncharacterized protein C16G5.06 (O60120)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNIRSFLLISIFTAISYLVVDGATPRTFAPSASVSINYGTLSTVFPSLYRRASTSSSSSSSSISTSHDSQPSTSSSSPSSTSTSSSSGTSVITASDVSASNEIISSSTNNSIHQQVSVVTEYVTIQPTTYVTTIFQYTSLASTIAAQSGIASLVPQTYTPYGGVKALIGILVGVVVGSVFLLAIVMVIARIWGPRLLANKDQNNNNEDLDSNLVSKDSEGTPQITYASNF