wanglab/gogpt-training-data huggingface dataset:
Protein: Protein DETOXIFICATION 47, chloroplastic (AtDTX47) (Multidrug and toxic compound extrusion protein 47) (MATE protein 47) (Protein ENHANCED DISEASE SUSCEPTIBILITY 5) (Protein EDS5) (Protein IMPORTANT FOR THE ARR PATHWAY 1) (Protein IAP1) (Protein SALICYLIC ACID INDUCTION DEFICIENT 1) (Protein SID1) (Protein SUSCEPTIBLE TO CORONATINE-DEFICIENT PST DC3000 3) (Protein SCORD3) (Q945F0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a multidrug and toxin extrusion transporter in the export of salicylic acid (SA) from the chloroplast to the cytoplasm. Plays an essential function in plant defense via the pathogen-induced salicylic acid (SA) accumulation. Acts also as a key component of the Age-related resistance (ARR) pathway.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:23333976, ECO:0000269|PubMed:23757404}; Multi-pass membrane protein {ECO:0000269|PubMed:23333976, ECO:0000269|PubMed:23757404}.
Interaction partners:
- Isochorismate synthase 1, chloroplastic
- Protein DETOXIFICATION 19
- Lipase-like PAD4
- Protein EDS1
- Regulatory protein NPR1
- 4-substituted benzoates-glutamate ligase GH3.12
- Protein DETOXIFICATION 18
- Isochorismate synthase 2, chloroplastic
- Protein DETOXIFICATION 51
- Immune-associated nucleotide-binding protein 9
Sequence:
MLIKSQRLTLFSPLLSKTRRIPVNSHQTLVAESVITRRTLGAITATPSFHKNPVVIRRRIKLERVTRNCVRIDREIDEEEEEEEKERGDLVKQSIWEQMKEIVKFTGPAMGMWICGPLMSLIDTVVIGQGSSIELAALGPGTVLCDHMSYVFMFLSVATSNMVATSLAKQDKKEAQHQISVLLFIGLVCGLMMLLLTRLFGPWAVTAFTRGKNIEIVPAANKYIQIRGLAWPFILVGLVAQSASLGMKNSWGPLKALAAATIINGLGDTILCLFLGQGIAGAAWATTASQIVSAYMMMDSLNKEGYNAYSFAIPSPQELWKISALAAPVFISIFSKIAFYSFIIYCATSMGTHVLAAHQVMAQTYRMCNVWGEPLSQTAQSFMPEMLYGANRNLPKARTLLKSLMIIGATLGLVLGVIGTAVPGLFPGVYTHDKVIISEMHRLLIPFFMALSALPMTVSLEGTLLAGRDLKFVSSVMSSSFIIGCLTLMFVTRSGYGLLGCWFVLVGFQWGRFGLYLRRLLSPGGILNSDGPSPYTVEKIKSI
Protein: Rav2p (A0A1D8PQ08)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- RAVE complex protein Rav1 C-terminal domain-containing protein
- H
- V-type proton ATPase subunit B
- E3 ubiquitin ligase complex SCF subunit
Sequence:
MTANILNNKTFIDTVLSIQSTQNDKELHWYIINIILPDLPQIIETLQICSNLLMYNSPQEPDSKQCIEKGPSIKLPLSLTNQQDSVNGIITRDGPYITDLNLTVKNHYFNKHFHKLRLIKPMVLEQLVNVLNLIKDSIGILQNLQSIDKELTLLSEKEENEHTIKHDQLICDFKKLLVNIHDSKTNLQLPSDPNLVFPLQVTDGENFEPQLSDRIAVDFYLSQNQVCIDLKSLHRITEKPWCEIDANGKSFVDKLKEEMKNKRSSIGDKSTSDAINQNNNTNIFSNMMSHLSLRHKYDTMDYITRCITYNNMVVVVNKKFEVSTEDPILISCFTKLDSLESIINGYISSLNSFSM
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (Q9KKF0)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
Sequence:
MAKEIKFSEETRRALEAGVNKLADTVKVTLGPKGRNVILDKKFGSPLITNDGVTIAKEIELEDRFENMGAQLVKEVATKTNDVAGDGTTTATVLAQAIIREGLKNVTAGANPILLRKGIQKAVTVAVEELKNQSRIVETQEAISQVASISAGDEEVGKLIAEAMEIVGKDGVITVEESQTMNTELDAVEGMQFDRGFVSAYMVTDVDKMEAVLNDPYILITDKKISNIQELLPVLEQIVQQGKKLLIIAEDVEGEALSTLVVNKLRGTFDVVAVKAPGFGDRRKEMLQDIAILTGAQVISEELGYDLKEADLSMLGRASSVKVTKESTTIVDGSGDKKAIEDRVTQIKHQVEQTTSDFDREKLMERLAKLAGGVAVVKVGAATEVELKERKLRIEDALNATRAAVEEGIVAGGGTAFVSVIPAIGTLIESLEGEVKLGAQIVKKALEEPLRQIAINAGLEGAVIVQNVVNSEAETGFDALNEKYVNMIEAGIVDPTKVSRSALQNAASIASTFLTTEAAVADLPEKEDAGMPGTGMDGMY
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratsysase) (P28297)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in storage lipid mobilization during the growth of higher plant seedling.
Subcellular location: Glyoxysome {ECO:0000269|PubMed:19246395}.
Interaction partners:
- Malate synthase
- Aconitate hydratase 1
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 3, mitochondrial
- Glycolate oxidase 2
- Serine--glyoxylate aminotransferase
- Glycolate oxidase 3
- Peroxisomal
- Glycolate oxidase 1
- Peroxisomal
Sequence:
MAASFSVPSMIMEEEGRFEAEVAEVQTWWSSERFKLTRRPYTARDVVALRGHLKQGYASNEMAKKLWRTLKSHQANGTASRTFGALDPVQVTMMAKHLDTIYVSGWQCSSTHTSTNEPGPDLADYPYDTVPNKVEHLFFAQQYHDRKQREARMSMSREERTKTPFVDYLKPIIADGDTGFGGTTATVKLCKLFVERGAAGVHIEDQSSVTKKCGHMAGKVLVAVSEHINRLVAARLQFDVMGTETVLVARTDAVAATLIQSNIDARDHQFILGATNPSLRGKSLSSLLAEGMTVGKNGPALQSIEDQWLGSAGLMTFSEAVVQAIKRMNLNENEKNQRLSEWLTHARYENCLSNEQGRVLAAKLGVTDLFWDWDLPRTREGFYRFQGSVAAAVVRGWAFAQIADIIWMETASPDLNECTQFAEGIKSKTPEVMLAYNLSPSFNWDASGMTDQQMVEFIPRIARLGYCWQFITLAGFHADALVVDTFAKDYARRGMLAYVERIQREERTHGVDTLAHQKWSGANYYDRYLKTVQGGISSTAAMGKGVTEEQFKESWTRPGADGMGEGTSLVVAKSRM
Protein: Exocyst complex component 8 (Exocyst complex 84 kDa subunit) (Q8IYI6)
Organism: Homo sapiens (Human)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
Interaction partners:
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 6
- Exocyst complex component 4
- Exocyst complex component 1
- Ras-related protein Ral-B
- Exocyst complex component 3
- Ras-related protein Ral-A
- Exocyst complex component 5
- Exocyst complex component 6B
Sequence:
MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGVGGAGGRDHLRGQAGFFSTPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYSLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEDTKRALSEKRRREQEEAAAPRGPPQVTSKATNPFEDDEEEEPAVPEVEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVEERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFEIDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGDIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV
Protein: Catenin alpha-3 (Alpha T-catenin) (Cadherin-associated protein) (Q65CL1)
Organism: Mus musculus (Mouse)
Function: May be involved in formation of stretch-resistant cell-cell adhesion complexes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, desmosome {ECO:0000269|PubMed:17535849}. Note=Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2. Colocalizes with PKP2 at intercalated disks in the heart (PubMed:17535849). {ECO:0000250, ECO:0000269|PubMed:17535849}.
Interaction partners:
- Catenin beta-1
- Plakophilin-2
- Vinculin
- Cadherin-1
- Afadin
- Tight junction protein 1
- Alpha-actinin-1
- Alpha-actinin-4
- Actin, cytoplasmic 1
- Catenin alpha-2
Sequence:
MSAETPITLNMDTQDLQIQTFTVEKLLEPLIIQVTTLVNCPQNPSNRKKGRSKRARVLLASVEEATWNLLDKGEMIAKEATVLKEELAAALQEVRKESKALKVSAERFTDDPCYLPKREAVVQAARALLAAVTRLLVLADMIDVMCLLQHVSSFQRTFESLKNVSNKSDLQRTYQKLGKELESLDYLAFKRQQDLKSPSQRDEIAGARATLKENSPLLHSICSACLEHSDVASLKASKDTVCEEIQNALDVISNASQGIQNAPAPPEPQAATLGSAFDELENLIVLNPLTVTEEDVRPSLEKRLEAIISGAALLADSSCTRDLHRERIIAECNAIRQALQDLLTEYMSNTGKTERSNTLNTAIVNMSKKTRDLRRQLRKAIIDHISDSFLDTTVPLLVLIEAAKNGRVKEIKDYAAIFHEHTGRLVEVANLACSMSTNEDGIKIVRIAANHLETLCPQIINAALALASRPKSQVVKNTMEMYKRTWEHYIHVLTEAVDDITSIDDFLAVSESHILEDVNKCIIALRDQDADNLDRAAGAIRGRAARVAHIVAGEMDSYEPGAYTEGVMRNVNFLTSTVIPEFVTQVNVALDALSKNSLTALDDNQFVDISKKIYDTIHDIRCSVMMIRTPEELEDVSDLEDDHEVRSHTSIQTEGKTDRAKMTQLPEAEKEKIAEQVADFKKVKSKLDAEIEIWDDTSNDIIVLAKKMCMIMMEMTDFTRGKGPLKHTTDVIYAAKMISESGSRMDVLARQIANQCPDPPCKQDLLAYLEQIKFYSHQLKICSQVKAEIQNLGGELIVSALDSVTSLIQAAKNLMNAVVQTVKMSYIASTKIIRIQSSAGPRHPVVMWRMKAPAKKPLIKREKPEETWAAVRRGSAKKKIHPVQVMSEFRGRQVY
Protein: Ubiquitin-like protein 5 (Q9BZL1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11161819, ECO:0000269|PubMed:23726919, ECO:0000269|PubMed:37315790}. Nucleus {ECO:0000269|PubMed:23726919, ECO:0000269|PubMed:37315790}. Nucleus, Cajal body {ECO:0000269|PubMed:37315790}.
Interaction partners:
- U4/U6.U5 tri-snRNP-associated protein 1
- Pre-mRNA-processing-splicing factor 8
- Microfibrillar-associated protein 1
- Pre-mRNA-splicing factor 38A
- Zinc finger matrin-type protein 2
- WW domain-binding protein 11
- Thioredoxin-like protein 4A
- WD40 repeat-containing protein SMU1
- WW domain-binding protein 4
- Pre-mRNA-processing factor 6
Sequence:
MIEVVCNDRLGKKVRVKCNTDDTIGDLKKLIAAQTGTRWNKIVLKKWYTIFKDHVSLGDYEIHDGMNLELYYQ
Protein: RNA helicase (EC 3.6.4.13) (D7F7X0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
ADFGLYEYQEEVVQRALRGENIIIWLPTGGGKTRAAVYVAKKHLENNPGAKVAVLVNKVHLVDQHYNNEFNPYLGSDYSLVSISGDCDQKDFFGCEVKNSDLVICTAQILENALTNQEEGKHVELSQFTLLIIDECHHTHKEGVYNKIMARYVAQKLKGERRLPQILGLTASPGTGGAKSIKGAVEHVLQICANLDSVIVSSKVYAPELKKKVPRPRKRFDIVDRRPQDPFGDHLKFMMQFIHDFMALGPEFPVREFGTQEYEADVVILEKKGVTDRNRLLAQCALHLRQYNDALLINDTVRMVDAFRVLESYYSTKSSTAMDGTDFFLLGLYQENEVELRKLSGDARFENPKMGKLQNTLLEQFVQGGHSRGILFSKTRKSICCLYDWVSNNPALQRAGIRAAILTGAGNGINYMTQNEQKDTIRNFRLGSLNLLISTSVAEEGLDIPECNLVVRYGLLTNEIAQQQASGRARASDSVYSVVAQAGGREARRELLNECLEDLTGRAIGEVQRMEPRDFQMKITDLQTEALLTRQLAEQLKLKKRSRFNAATVQLSCRGCFLPVALGHDIKVIENAHHVNINPDFERYYKTGGQPALKTFEDWEPGRVISCAACGRVRLTFNL
Protein: Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (POMGnT2) (EC 2.4.1.312) (Extracellular O-linked N-acetylglucosamine transferase-like) (Glycosyltransferase-like domain-containing protein 2) (Q8NAT1)
Organism: Homo sapiens (Human)
Function: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23929950, ECO:0000269|PubMed:27066570}; Single-pass type II membrane protein {ECO:0000269|PubMed:23929950}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Dystroglycan 1
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannose kinase
- Ribitol 5-phosphate transferase FKRP
- Ribitol-5-phosphate transferase FKTN
- Beta-1,4-glucuronyltransferase 1
Sequence:
MHLSAVFNALLVSVLAAVLWKHVRLREHAATLEEELALSRQATEPAPALRIDYPKALQILMEGGTHMVCTGRTHTDRICRFKWLCYSNEAEEFIFFHGNTSVMLPNLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPVFVPDVALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAHEARLFFMEGWGEGAHFDLYKLLSPKQPLLRAQLKTLGRLLCFSHAFVGLSKITTWYQYGFVQPQGPKANILVSGNEIRQFARFMTEKLNVSHTGVPLGEEYILVFSRTQNRLILNEAELLLALAQEFQMKTVTVSLEDHTFADVVRLVSNASMLVSMHGAQLVTTLFLPRGATVVELFPYAVNPDHYTPYKTLAMLPGMDLQYVAWRNMMPENTVTHPERPWDQGGITHLDRAEQARILQSREVPRHLCCRNPEWLFRIYQDTKVDIPSLIQTIRRVVKGRPGPRKQKWTVGLYPGKVREARCQASVHGASEARLTVSWQIPWNLKYLKVREVKYEVWLQEQGENTYVPYILALQNHTFTENIKPFTTYLVWVRCIFNKILLGPFADVLVCNT
Protein: Mitochondrial processing peptide beta subunit, putative (Q38F91)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Mitochondrial processing peptidase alpha subunit, putative
- Mitochondrial processing peptidase alpha subunit, putative
- Cytochrome c1, heme protein, mitochondrial
- Reiske iron-sulfur protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Electron transfer protein, putative
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Uncharacterized protein
- Acyl carrier protein
Sequence:
MLRPSFCRCLPVLNCTLSAPQCAAAIDRCTPVVYSSLPNGCRVATEYLPNCQFATVGVWIDAGSRFEDINNNGVAHFLEHMNFKGTAKYSKRAVEDLFEHRGAHFNAYTSRDRTAYYVKAFKYDVEKMIDVVSDLLQNGRYDPSDVELERPTILAEMREVEELVDEVLMDNLHQAAYDPAHCGLPLTILGPVENISSRINRDMIQEFVRVHYTGPRMSFISSGGIHPEEAHRLAEKFFGNLPAANNSPLLQSQYRGGYTVMWNEQMATANTAFAYPICGAIHDDSYALQLVHNVIGQVREGQHDQFAHQRLNPRLPWEKLSNLVQLRPFYTPYKETSLLGYQLVTMRTAVADANGGVQRDESQTVLLDHMLKLFNELSTKAVDAALLEEAKSEYKSSVMMMRDSTTNSAEDLGRQMIHLGRRVPLREVFERVDAVTPAVFRDTLAKYVQAVQPTVSYIGSASAVPRFDALTQVKHIL
Protein: Leukotriene B4 receptor 2b (E7F4K9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Adhesion G protein-coupled receptor F6
- Guanine nucleotide-binding protein
- Leukotriene A
Sequence:
MALENGSFSMENITTASPKLKSVVDNSTSATFGALILSIAILLGIPGNLFIIWSILARARKRSVTTLLILNLAFADGCLMFLTIFFIIYLAKQNWIFGEVLCKLLFYLCNTNMYASIMIITLMSLHRLVAVMWPSYLSVCTRRLTVLLVLGGLWVAVFLLAMPVLMFRAEKTIGNKRIVCETHHNRTEQAVFQYTLETMVGFLVPYVIIVSSYVCILRRLRQTKFKRMIRSENLIQAIIVTFCIFWLPYHILNVVQVMAALTPEGMPLKTQLKNIWESSRAVTSTLAFISSCANPVLYAFAGRSYIKADGLAFMARLFEGTVLDYSARKNQQTRDVIRL
Protein: Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP type I receptor) (PTH/PTHr receptor) (Parathyroid hormone 1 receptor) (PTH1 receptor) (Q03431)
Organism: Homo sapiens (Human)
Function: Receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:8397094}; Multi-pass membrane protein {ECO:0000269|PubMed:20172855}.
Interaction partners:
- Parathyroid hormone-related protein
- Parathyroid hormone
- Guanine nucleotide-binding protein G
- Low-density lipoprotein receptor-related protein 6
- Beta-arrestin-1
- Beta-arrestin-2
- Tuberoinfundibular peptide of 39 residues
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MGTARIAPGLALLLCCPVLSSAYALVDADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM
Protein: Uncharacterized protein (Q386C8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRWPRGTVALHPAGLLGCNFVSSARRLLYCSSVPFSLYRSTHGSMKSVAAQLKSDWVFIRRRRMESPPPDRTEGEQAVSAEGDDSNDNNNAAMKCFDHWSSDMNGCTAEEFLQGAKQSYRSLGVLLETLREAASHNGPTGRPVAREVALAKLQGLLLKNYSVKEDIVGEAVISSEKGSAKGTDAFHKTVSKALKQVLPLSQGLSEHLSEMWDKQRTLDFNIFDIAAPDDYVIDADMKLFNPFLVKSSDDLLEYAAWKKNGEECPKPVSVDATTGGACSSPPLKCSFSSGKFDPEKVGERETWSIGCLQRVLKPAPKLMPIAFVSLDVVMPPQRYCEAFDWFYQRTCGYSSEYERVEAARLYTSPSFFLGIFRQCLFLVDFVKRMFVGRPLQLDCTRLVQKLHGNSVDIRRSPPAVRKLLCFYMEGDGRWTLFDVFILERVLVPVSPTASSK
Protein: Protein PIGMENT DEFECTIVE 338, chloroplastic (Protein PETB/PETD STABILIZING FACTOR) (Protein PHOTOSYSTEM BIOGENESIS REGULATOR 1) (Protein rbcL RNA S1-binding domain) (Q9M9H4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RNA-binding protein that acts as an RNA chaperone to remodel RNA structure and activates their translation. Required for seed pigmentation. Necessary for chloroplast development and subsequent photosynthetic electron flow, as well as for non-photochemical quenching (NPQ). Rubisco regulatory factor which regulates the concerted biogenesis of NDH, PSI (including PsaA, PsaB, PsaD, PsaF, PsaL, PsaG, PsaK and NdhH) and Cytb(6)f (including PetA, PetB, PetC and PetD) complexes. Binds specifically to and involved in the post-transcriptional regulation of plastid-encoded mRNAs (e.g. rbcL, petA, petB, petD and Ycf1), thus modulating expression, cellular localization/compartmentalization, and photosynthetic function.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24053212, ECO:0000269|PubMed:30962391}.
Interaction partners:
- Uncharacterized protein At3g06530
- Nucleolar protein
- Nucleolar-like protein
- F18K10.11 protein
- KRR1 small subunit processome component
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- Periodic tryptophan protein 2
- Putative WD-repeat membrane protein
- Ribosomal RNA-processing 7 protein
Sequence:
MQTLLCQPCKSLPILTASSSSSLIRSSGDVRECIDFRASEKVSKFQFHVTLSPFAFRGFSICREFAVRGAYGIRFCSREDVSGVGNGGIVAEEEIELLNKPNPLPKSENEESGKADDDAILEPFLKFFKPEEEGEGIESEVSDETDRVSVEYYDPKPGDFVVGVVVSGNENKLDVNIGADMLGTMLTKEILPLYDKELDYLLCDLKYDAEEFLVNGKMGIVKDDDEGVEIAEFARQGRPVVEIGTVVFAEVLGRTLSGRPLLSSRRYFRRIAWHRVRQIKQLNEPIEVKITEWNTGGLLTRIEGLRAFIPKQELVKKVNTFTELKENVGRRFLVQITRLNEDKNDLILSEKVAWEKLYLREGTLLEGTVVKILPYGAQVKLGDSSRSGLLHISNITRRRIGSVSDVLQVDESVKVLVVKSLFPDKISLSIADLESEPGLFISDREKVFTEAEEMAKKYREKMPLVATSPISDRPPITSSFPQGKDEEIYANWEWFKFESQ
Protein: Type II secretion system protein H (T2SS minor pseudopilin H) (General secretion pathway protein H) (Protein transport protein HofH) (Putative general secretion pathway protein H) (P41443)
Organism: Escherichia coli (strain K12)
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q00515}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Type II secretion system core protein G
- Putative type II secretion system protein K
- Type II secretion system protein J
- Putative type II secretion system protein F
- Putative type II secretion system protein L
- Putative type II secretion system protein I
- Putative type II secretion system protein C
- Putative type II secretion system protein E
- Putative type II secretion system protein M
- Prepilin leader peptidase/N-methyltransferase
Sequence:
MNQQRGFTLLEMMLVLALVAITASVVLFTYGREDVASTRARETAARFTAALELAIDRATLSGQPVGIHFSDSAWRIMVPGKTPSAWRWVPLQEDAADESQNDWDEELSIHLQPFKPDDSNQPQVVILADGQITPFSLLMANAGTGEPLLTLVCSGSWPLDQTLARDTRP
Protein: Signal transducer and activator of transcription (B5X3E8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MAQWCQLQLLESKYLEQVDQLYDDSFPMDIRQYLSKWIESIDWENVAVQDSLATVRFHDLLAQLDDQHSRFALENNFLLQHNIRKIKRNLQDHFQEDPVHMAMIISRNLKEEQKILAAAKSIETDRENTQTSMVLEKQKLDNKVKDMKNKVQEADQNVKSLEYLQDEHDFKENTLKNREHEMNGLTQKQLEHEKLQIAEMCFKLKFKRGEVVGQLAEVLNIAEAVQSDLISEELAEWKKRQQISCIGGPPNACLDQLQNWFTAVAESLQQVRQQLKELQELEQKYTYDNDPIKQQKGFLEGRALSLFRNLLEHSLVVERQPCMPTHPQRPLVLKTQVQFTVKLRFLVKLQEFNYQLKVKALFDKDVTEKKGFRKFNILGTNTKVMNMEESNGSLAAEFRHLQLKEQKVAGNRTNEGPLIVTEELHCICFESELNQSGLELKLETISLPIVVISNVSQLPSGWASILWYNMLTSEPKNLKFFLSPPAASWGQLSEVLSWQFSSVTKRGLNEEQLGMLADKLLGQKAQRNPEGLVPWTKFCKSLSEKSFPFWLWIEAILDLIKRHLLSLWNDGCILGFVSKEREKALLTGKCPGTFLLRFSESSRDGAITFTWVEHDQYDKPVFHAVEPYTKKELSAVSLPDIIRTYKVMAAENIPENPLRFLYPDIPKDKSFGKYYARASEASEPMDVESSSSTGYMKTELISVSEVHPSRLQDNMMPMSPDVFGELKRSVAPVFQCWTGPKEIDAVASDLGEFLAEEFQMFENTPDLDRN
Protein: Histone H2B.3 (HTB3) (Q9SI96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- E3 ubiquitin-protein ligase BRE1-like 1
- E3 ubiquitin-protein ligase BRE1-like 2
- Histone H3.3
- Histone H3.1
- Histone H3-like centromeric protein CENH3
- Histone H3-like 5
- Histone H3-like 1
- Histone H3-like 2
- Histone H3-like 4
Sequence:
MAPKAGKKPAEKKPAEKAPAEEEKVAEKAPAEKKPKAGKKLPKEAVTGGVEKKKKRVKKSTETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQEASKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
Protein: Peroxidase 50 (Atperox P50) (EC 1.11.1.7) (ATP9a) (PRXR2) (Q43731)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Toll/interleukin-1 receptor-like protein
Sequence:
MVVVNKTNLLLLLLSLCLTLDLSSAQLRRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLAGDGFDTVIKAKEALDAVPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQQGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAFN
Protein: E3 ubiquitin ligase TRAF3IP2 (EC 2.3.2.27) (Adapter protein CIKS) (Connection to IKK and SAPK/JNK) (E3 ubiquitin-protein ligase CIKS) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2) (O43734)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase that catalyzes 'Lys-63'-linked polyubiquitination of target protein, enhancing protein-protein interaction and cell signaling. Transfers ubiquitin from E2 ubiquitin-conjugating enzyme UBE2V1-UBE2N to substrate protein. Essential adapter molecule in IL17A-mediated signaling. Upon IL17A stimulation, interacts with IL17RA and IL17RC receptor chains through SEFIR domains and catalyzes 'Lys-63'-linked polyubiquitination of TRAF6, leading to TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways.
Interaction partners:
- TNF receptor-associated factor 3
- Interleukin-17 receptor A
- TNF receptor-associated factor 6
- NF-kappa-B essential modulator
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Interleukin-17 receptor C
- Interleukin-17A
- TNF receptor-associated factor 5
- Interleukin-17 receptor B
- Heat shock protein HSP 90-alpha
Sequence:
MPPQLQETRMNRSIPVEVDESEPYPSQLLKPIPEYSPEEESEPPAPNIRNMAPNSLSAPTMLHNSSGDFSQAHSTLKLANHQRPVSRQVTCLRTQVLEDSEDSFCRRHPGLGKAFPSGCSAVSEPASESVVGALPAEHQFSFMEKRNQWLVSQLSAASPDTGHDSDKSDQSLPNASADSLGGSQEMVQRPQPHRNRAGLDLPTIDTGYDSQPQDVLGIRQLERPLPLTSVCYPQDLPRPLRSREFPQFEPQRYPACAQMLPPNLSPHAPWNYHYHCPGSPDHQVPYGHDYPRAAYQQVIQPALPGQPLPGASVRGLHPVQKVILNYPSPWDHEERPAQRDCSFPGLPRHQDQPHHQPPNRAGAPGESLECPAELRPQVPQPPSPAAVPRPPSNPPARGTLKTSNLPEELRKVFITYSMDTAMEVVKFVNFLLVNGFQTAIDIFEDRIRGIDIIKWMERYLRDKTVMIIVAISPKYKQDVEGAESQLDEDEHGLHTKYIHRMMQIEFIKQGSMNFRFIPVLFPNAKKEHVPTWLQNTHVYSWPKNKKNILLRLLREEEYVAPPRGPLPTLQVVPL