wanglab/gogpt-training-data huggingface dataset:
Protein: Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2) (P36896)
Organism: Homo sapiens (Human)
Function: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Activin receptor type-2B
- Protein Cripto
- Activin receptor type-2A
- Inhibin beta A chain
- Growth/differentiation factor 8
- TGF-beta receptor type-1
- Activin receptor type-1
- Mothers against decapentaplegic homolog 2
- Activin receptor type-1C
- Mothers against decapentaplegic homolog 4
Sequence:
MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI
Protein: DNA gyrase subunit B (EC 5.6.2.2) (O08399)
Organism: Treponema pallidum (strain Nichols)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
Interaction partners:
- DNA gyrase subunit A
- Uncharacterized lipoprotein TP_0136
- McbG protein, putative
- DNA replication and repair protein RecF
- Beta sliding clamp
- Ribonucleoside-diphosphate reductase subunit alpha
- DNA polymerase I
- ATP-dependent DNA helicase RecQ
- Methionine--tRNA ligase
- DNA primase
Sequence:
MGIEYSASSITVLEGLEAVRKRPGMYIGSTGPNGLHHLVYEVVDNCIDEAMAGYCDRITVVLEQGNVVRVEDNGRGIPVDVHPHEGVSALEVVLTKLHAGGKFDKKSYKVSGGLHGVGVSVVNALSLWVEVTVYRDGAEYYQKFNVGMPLAPVEKRGVSEKRGTIIRWQADPSIFKETVAYDFDVLLTRLRELAFLNSTVVIQLRDERLATAKQVEFAFEGGIRHFVSYLNRGKSVVPERPLYIEGSKSDVLVEVALQYHDGYTENVQSFVNDINTREGGTHLEGFKSALTRVANDFLKKSPKLAKKIEREEKLVGEDVRAGLTVVLSVKIPEPQFEGQTKTKLGNSEVRGIVDSLVGERLTLYFEQNPGVLTKILEKSIAEAQARLAARRAKEAARRKSGMDSFGLPGKLADCSLKDPAKCEVYIVEGDSAGGSAKKGRDSKTQAILPLWGKMLNVEKTRLDKVLHNEKLQPIIATLGTGVGKDFDLTRIRYHKVIIMADADVDGSHIRTLLLTFFFRYLPQIIEAGYVYLAMPPLYRIAWSKKELYVYSDTERDEALESIGKKSGVAVQRYKGLGEMDGTQLWETTMNPVRRKMMQVVLSDAVEADRVFSTLMGEDVEPRRKFIEENAIYARLDV
Protein: Fanconi-associated nuclease 1 (EC 3.1.21.-) (EC 3.1.4.1) (FANCD2/FANCI-associated nuclease 1) (mFAN1) (Myotubularin-related protein 15) (Q69ZT1)
Organism: Mus musculus (Mouse)
Function: Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates (By similarity). Not involved in DNA double-strand breaks resection. Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL. Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap (By similarity). Also has endonuclease activity toward 5'-flaps.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}. Note=Localizes at sites of DNA damage following recruitment by monoubiquitinated FANCD2. Localizes to stalled replication forks via its UBZ4-type zinc finger. {ECO:0000250|UniProtKB:Q9Y2M0}.
Interaction partners:
- Fanconi anemia group D2 protein homolog
- DNA mismatch repair protein Mlh1
- Fanconi anemia group I protein homolog
- Mismatch repair endonuclease PMS2
- Structure-specific endonuclease subunit SLX1
- Fanconi anemia group M protein homolog
- Structure-specific endonuclease subunit MUS81
- DNA cross-link repair 1A protein
- E3 ubiquitin-protein ligase FANCL
- Myotubularin-related protein 10
Sequence:
MPSQRKSPDQKRPRRSLSTSKTAKSQCHSITSYFNSAPPAKLACSTCHKMVPRYDLIRHLDESCANNGVGDDVQVEPAQAGLMSPTVPTSDLPSGPLENVTPQKLSPPKRSLISVQCGSKLGIQQQTSPYFKDALVSKDQNELPNQSVEIMPLGSLTSKLSRRYLNAKKSLAKNEGLASQCPQTSPSTPGTSLTDNCPEMEDKDEVLNSSQKENIYSCAPLKEENASEQKVKNNKITGDESQKASCGEPALTPASAEHASILLSSDSTLVSNTKSSPGDTLVKQESARRADVGLAEPLEVRSHKEVQMTFDAAAKTLVSGEAESNGPTDVDMSDMTTWSNNQELVREAGSVLHCPLEQGSSCGGPSETAQLALSHPYYLRSFLVVLQALLGNEEDMKLFDEQEKAIITRFYQLSASGQKLYVRLFQRKLTWIKMSKLEYEEIASDLTPVVEELKDSGFLQTESELQELSDVLELLSAPELKALAKTFHLVSPGGQKQQLVDAFHKLAKQRSVCTWGKTQPGIRAVILKRAKDLAGRSLRVCKGPRAVFARILLLFSLTDSMEDEEAACGGQGQLSTVLLVNLGRMEFPQYTICRKTQIFRDREDLIRYAAAAHMLSDISAAMASGNWEDAKELARSAKRDWEQLKSHPSLRYHEALPPFLRCFTVGWIYTRISSRAVEVLERLHMYEEAVKELENLLSQKIYCPDSRGRWWDRLALNLHQHLKRLEEAIRCIREGLADPHVRTGHRLSLYQRAVRLRESPSCRKYKHLFSRLPEVAVGDVKHVTITGRLCPQHGMGKSVFVMESGDGANPTTVLCSVEELALGYYRQSGFDQGIHGEGSTFSTLCGLLLWDIIFMDGIPDVFRNAYQASPLDLLTDSFFASREQALEARLQLIHSAPAESLRAWVGEAWQAQQGRVASLVSWDRFTSLQQAQDLVSCLGGPVLSGVCRRLAADFRHCRGGLPDLVVWNSQSHHCKLVEVKGPSDRLSCKQMIWLYELQKLGADVEVCHVVAVGAKSKGLG
Protein: Secreted effector protein PipB2 (Type III effector PipB2) (Q8ZMM8)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Involved in the reorganization of late endosome/lysosome (LE/Lys) compartments in mammalian cells. Necessary and sufficient to link kinesin-1 onto the Salmonella-containing vacuole (SCV) membrane. Required for centrifugal extension of lysosomal glycoprotein-rich membrane tubules, known as Salmonella-induced filaments (Sifs), away from the SCV and toward the cell periphery. Required for virulence, but not for intracellular survival and replication in phagocytic cells.
Subcellular location: Secreted. Host membrane. Note=Secreted via the type III secretion system 2 (SPI-2 T3SS), and delivered into the host cell. In phagocytic cells localizes to the Salmonella-containing vacuole (SCV) and tubular extensions from the SCV, Salmonella-induced filaments (Sifs). In epithelial cells localizes to peripheral vesicles, in addition to SCVs and Sifs. Concentrates in detergent-resistant microdomains (DRMs), present on the intracellular membranes of SCVs and Sifs.
Interaction partners:
- Secreted effector protein SseJ
- Secreted effector protein SifA
- Secretion system effector
- Secretion system effector
- Secreted effector protein sopD2
- E3 ubiquitin-protein ligase SspH2
- Deubiquitinase SseL
- Secreted effector kinase SteC
- E3 ubiquitin-protein ligase SlrP
- Secreted effector protein SseI
Sequence:
MERSLDSLAGMAKSAFGAGTSAAMRQATSPKTILEYIINFFTCGGIRRRNETQYQELIETMAETLKSTMPDRGAPLPENIILDDMDGCRVEFNLPGENNEAGQVIVRVSKGDHSETREIPLASFEKICRALLFRCEFSLPQDSVILTAQGGMNLKGAVLTGANLTSENLCDADLSGANLEGAVLFMADCEGANFKGANLSGTSLGDSNFKNACLEDSIMCGATLDHANLTGANLQHASLLGCSMIECNCSGANMDHTNLSGATLIRADMSGATLQGATIMAAIMEGAVLTRANLRKASFISTNLDGADLAEANLNNTCFKDCTLTDLRTEDATMSTSTQTLFNEFYSENI
Protein: Somatostatin (Growth hormone release-inhibiting factor) [Cleaved into: Somatostatin-28; Somatostatin-14 (SST-14); Neuronostatin (NST)] (P61278)
Organism: Homo sapiens (Human)
Function: Inhibits the secretion of pituitary hormones, including that of growth hormone/somatotropin (GH1), PRL, ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-stimulated secretion of GH1 and LH; the inhibition of ghrelin-stimulated secretion of GH1 can be further increased by neuronostatin.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P60042}.
Interaction partners:
- Somatostatin receptor type 4
- Somatostatin receptor type 5
- Somatostatin receptor type 1
- Somatostatin receptor type 2
- Somatostatin receptor type 3
- Gastrin
- Cortistatin
- Pro-glucagon
- Pro-neuropeptide Y
- Pancreatic polypeptide prohormone
Sequence:
MLSCRLQCALAALSIVLALGCVTGAPSDPRLRQFLQKSLAAAAGKQELAKYFLAELLSEPNQTENDALEPEDLSQAAEQDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC
Protein: Kunitz-type serine protease inhibitor RsTIQ7 (P84555)
Organism: Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus)
Function: Serine protease inhibitor. Inhibits trypsin, elastase, plasmin and kallikrein.
Interaction partners:
Sequence:
EDFDSQCVPTADPGPCKAYIPMWWYNVLS
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) (P06858)
Organism: Homo sapiens (Human)
Function: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:24291057, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:27811232}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
Interaction partners:
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Apolipoprotein C-II
- Angiopoietin-related protein 4
- Angiopoietin-related protein 3
- Prolow-density lipoprotein receptor-related protein 1
- Apolipoprotein E
- Apolipoprotein C-III
- Gastric triacylglycerol lipase
- Patatin-like phospholipase domain-containing protein 2
- Monoglyceride lipase
Sequence:
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
Protein: Mannan-binding lectin associated serine protease 2 (Q6Q1Q9)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MRLLLLLAVLCGGANSSIVLQKMYGRITSPDFPNNYPNHKERTWNVTVPKGYAVRIYFTHFNLELSYQCEYDYVKLSSSGKTLATLCGQDSTDTEEAPGNKTYISIDNTLTVVFRSDYSNEKPFTGFEAFYAAEDIDECKQLFDGEPLCSHHCHNYVGGYYCSCRIGYVLHENKRTCTAQCQNQIFTQRTGEIASPDYPAPYPPLSTCSYNIQVEDGFLITLEFVETFNVETHPEVLCPYDVLKMETPKKQFGPFCGKILPAKIETQTSVVNITFITDVSGAHTGWKVNTQRSLPCPSPEAPPYGHIAPVQAQYTVGDHYALSCDVGYVLLENENVVMSFVAECEKNASWNKPMAKCIIVDCGQPEDIDSGAILYLTGPEKTTYSAAIQYQCAAPFYTMRANSSGKYICSDDGFWKNTEGEITLPVCEPVCGMQRMRALERIYGGRRANPGQFPWQVMLITEHGELGSGSLLYDSWVLTAAHVVAEQRNPSTLRIKLGILNRYSVHYEEVHAVKIFIHEGYKNDLVNFDNDIALIKLERKVPVSTTISPICLPGKEEFQIKANDTVTVAGWGRTETRSSSVVLLYTELMIINQKECADAYANKSHNGNPLVITENMLCAGAEEGGRDACHGDSGGPLVVLDAQTRKWFVIGIVSWALDCAVAGQYGVYTKVMNYMPWIESTITNNS
Protein: Glutathione peroxidase (D6XK31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase
- Glutathione peroxidase
- Glutathione peroxidase
- Tryparedoxin
Sequence:
MSAASSIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATTLYNKYKSQGFTVLAFPCNQFGGQEPGTEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILKTKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEKKLIPLLESTQSA
Protein: Golgi phosphoprotein 3 like (Q5T5I6)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004344}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004344}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004344}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004546}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004546}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004546}.
Interaction partners:
Sequence:
MTTLTHRARRTEISKNSEKKMESEEDSNWEKSPDNEDSGDSKDIRLTLMEEVLLLGLKDKEANINSWITRWLTPVIPALWGAEGYTSFWNDCISSGLRGGILIELAMRGRIYLEPPTMRKKRLLDRKVLLKSDSPTGDVLLDETLKHIKATEPTETVQTWIELLTGETWNPFKLQYQLRNVRERIAKNLVEKGILTTEKQNFLLFDMTTHPVTNTTEKQRLVKKLQDSVLERWVNDPQRMDKRTLALLVLAHSSDVLENVFSSLTDDKY
Protein: Meiosis-specific protein PAIR3 (Protein HOMOLOGOUS PAIRING ABERRATION IN RICE MEIOSIS 3) (B9G5N1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plays a crucial role in homologous chromosome pairing and synapsis in meiosis. Does not seem required for cytokinesis. Is essential for meiotic bouquet formation, homologous chromosome pairing and normal recombination, and synaptonemal complex (SC) assembly. Required for the proper association of PAIR2 with chromosomes.
Subcellular location: Chromosome {ECO:0000269|PubMed:21119003, ECO:0000269|PubMed:27436711}. Nucleus {ECO:0000269|PubMed:21119003}. Note=During interphase-early leptotene, distributed as numerous punctuate foci throughout the chromatin. Associates with chromosomal axes at leptotene, zygotene and pachytene (PubMed:21119003). Associates with chromosomal axes at zygotene (PubMed:27436711). {ECO:0000269|PubMed:21119003, ECO:0000269|PubMed:27436711}.
Interaction partners:
- Synaptonemal complex protein ZEP1
Sequence:
MEVELTNIQKATSSDYWSLASNQYPCGKFPKVSVGVTIPRTSSVSRGRDAASTAAFEKNLSQGTDGRSRPPKMDNASLQVSPEAANHGGSAKEVPKPVPAKVSVSQPDDNAIEQTGTFSFGTRREQDSHLDQLDRPPLVSSQGKRQVESADKNKPNSEMLRMKLWEILGGTSQNKEAVASPNPEDIETPCQPKSQIANGPSSGRQKVFTSPVPYNIKTPAQFNSQTANKPSSDPIESDSDSPQVVEVRPITRSLGRKKEPTGSTHQDKSGSAKKPLSTHRSTPKQKILDNVFAFNDKCTPKTVGKSANGESGSLRNLRSLSRRAKVEPKKAHCSDRISHKTTQDDMERKVPSKYIPSEKKGEKTNSFSSLSRTGKTAESCSRSPKRERRVNTMANVGARKMQLSENLLVKTLNDGEHKLSSPQLTSFKSKGKCSSISPQQKENDNTHIPEASDRTAARNSFNSTPSPAANPSPVLRKYSWEHDENPAINGKSGQKDASPLADRFSDMPDDFASPTFAANIKISPHRSKMLDDDLFSSKYPKGVNRSRSTSFTSDPESEPLDKMEKTNELPGSESPNSQEERQNRKQPHLSPLSPIESEGAQISIPSFRKGYKSHKWLSDVDSPDKSSIEHLGRKSHLKEGRKGKRQLTSPTHFATSGTQETMSDKEPEKVPENYLTRAFDQLVVVLGRFQTKIKSETRNKSSKILAATGEIIRQHLEGVEGQMQADVDKLVNAGKSKRKRLESTFEEQQEKLRILHEKFKEEVNQQLLGCKNSVEDFEAYHAELKGVADKQKASHKKLLQNAEKTVGAQLSDAETKIAEVQKRARKRMKGLKFVLKELIAETAE
Protein: Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.155) (EC 2.3.1.16) (TP-beta) (F5GZQ3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Protein: Protein EOLA1 (Endothelial-overexpressed lipopolysaccharide-associated factor 1) (Endothelium and lymphocyte associated ASCH domain 1) (Q8TE69)
Organism: Homo sapiens (Human)
Function: May play a role in cell protection during the inflammatory response. In epithelial cells, negatively regulates IL6 production and apoptosis through the regulation of MT2A expression.
Interaction partners:
- Protein EOLA2
- Metallothionein-2
Sequence:
MKFGCLSFRQPYAGFVLNGIKTVETRWRPLLSSQRNCTIAVHIAHRDWEGDAWRELLVERLGMTPAQIQALLRKGEKFGRGVIAGLVDIGETLQCPEDLTPDEVVELENQAVLTNLKQKYLTVISNPRWLLEPIPRKGGKDVFQVDIPEHLIPLGHEV
Protein: Glycerol-3-phosphate acyltransferase, chloroplastic (GPAT) (EC 2.3.1.15) (Q43307)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate (Probable). The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. This is an oleate-selective acyltransferase.
Subcellular location: Plastid, chloroplast stroma.
Interaction partners:
- Glycerol-3-phosphate 2-O-acyltransferase 6
- Glycerol-3-phosphate 2-O-acyltransferase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Glycerol-3-phosphate acyltransferase 1
- Glycerol-3-phosphate acyltransferase 5
- Probable glycerol-3-phosphate acyltransferase 8
- Glycerol-3-phosphate acyltransferase 7
- Probable glycerol-3-phosphate acyltransferase 3
- Glycerol kinase
- Probable glycerol-3-phosphate acyltransferase 2
Sequence:
MTLTFSSSAATVAVAAATVTSSARVPVYPLASSTLRGLVSFRLTAKKLFLPPLRSRGGVSVRAMSELVQDKESSVAASIAFNEAAGETPSELSHSRTFLDARSEQDLLSGIKKEAEAGRLPANVAAGMEELYWNYKNAVLSSGASRADETVVSNMSVAFDRMLLGVEDPYTFNPYHKAVREPFDYYMFVHTYIRPLIDFKNSYVGNASIFSELEDKIRQGHNIVLISNHQSEADPAVISLLLEAQSPFIGENIKCVAGDRVITDPLCKPFSMGRNLICVYSKKHMNDDPELVDMKRKANTRSLKEMATMLRSGGQLIWIAPSGGRDRPNPSTGEWFPAPFDASSVDNMRRLVEHSGAPGHIYPMSLLCYDIMPPPPQVEKEIGEKRLVGFHGTGLSIAPEINFSDVTADCESPNEAKEAYSQALYKSVNEQYEILNSAIKHRRGVEASTSRVSLSQPWN
Protein: RNA polymerase sigma factor sigA (Os-sigA) (Sigma factor A) (Protein YELLOW-GREEN LEAF 13) (RNA polymerase sigma factor sig1) (OsSIG1) (Sigma factor 1) (Q0J7T6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released (Probable). Controls the transcription of the psaA and psaB genes in chloroplast, and thus maintains the abundance of the core protein complex PsaA-PsaB of photosystem I (PSI) in the thylakoid membrane. Maintains PSI activity, sufficient rate of electron transfer from PSII to PSI, and photochemical efficiency.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA1
- Os12g0540700 protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I and III subunit RPAC1
- Os02g0723600 protein.
- Os09g0110400 protein
- Os07g0463100 protein
- DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide, putative, expressed
- Os08g0426000 protein
- Proliferating cell nuclear antigen
Sequence:
MTATPAVIGLSAGNRLLSASFGPTDLMPDKVSLGVGGGGGGGGGGGGGDAMSFAPPAPATPKLTAVAAHRLKLSPHGRAQVMRALRHHSSAAAALAPPPPPPPPPTPSPASRAAHAHDLESSLEAIVLLQRSMLEKQWELPFDDDNHAMAIGLAEDDDDTSKATVVVARSSVSARQRRMSGRRRGRTKNGAAHFAVSPELIQSRNRIYLRGTVSKELLTHKQVVHLSHKIKDGIWLQQQRSKLKEKLGNEPSYKQLAHSLKISPPELRSRMHESFLAREMLTMSNLRLVISIAQKYDNLGVELADLIQGGLIGLLRGIEKFDASRGFRISTYVYWWIRQGVSRALAENSKTFRLPTYLHERLIAIRGAKYELEDQGIAPTIENIAGSLNISEKKVLNATEAVNKVLSLDQQAFPSLNGLPGETLHSYIEDQNVANDPWHGFEEWYLKEEVNKLLNSTLNERERDIIRLYHGIGKQCHTWEDISRQFGLSRERVRQVGLIAMEKLKHAARRKNLEALLEDY
Protein: Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66) (O15371)
Organism: Homo sapiens (Human)
Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDESSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQILPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGKERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSDEDEEEEEEEEEEEEEEET