wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium/potassium-transporting ATPase subunit gamma (Na(+)/K(+) ATPase subunit gamma) (FXYD domain-containing ion transport regulator 2) (Sodium pump gamma chain) (Q04679)
Organism: Rattus norvegicus (Rat)
Function: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Subcellular location: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- FXYD domain-containing ion transport regulator 4
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit beta-3
- Protein ATP1B4
- Phospholemman
Sequence:
MTELSANHGGSAKGTENPFEYDYETVRKGGLIFAGLAFVVGLLILLSKRFRCGGSKKHRQVNEDEL
Protein: Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha binding protein) (IFN-alpha/beta receptor 2) (Interferon alpha binding protein) (Type I interferon receptor 2) (P48551)
Organism: Homo sapiens (Human)
Function: Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:7665574}; Single-pass type I membrane protein {ECO:0000269|PubMed:7665574}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}; Single-pass type I membrane protein {ECO:0000269|PubMed:7665574}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Non-receptor tyrosine-protein kinase TYK2
- Interferon beta
- Interferon alpha-1/13
- Tyrosine-protein kinase JAK1
- Ubl carboxyl-terminal hydrolase 18
- Interferon alpha-2
- Signal transducer and activator of transcription 1-alpha/beta
- Signal transducer and activator of transcription 2
- Interferon omega-1
Sequence:
MLLSQNAFIFRSLNLVLMVYISLVFGISYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLKCTLLPPGQESESAESAKIGGIITVFLIALVLTSTIVTLKWIGYICLRNSLPKVLNFHNFLAWPFPNLPPLEAMDMVEVIYINRKKKVWDYNYDDESDSDTEAAPRTSGGGYTMHGLTVRPLGQASATSTESQLIDPESEEEPDLPEVDVELPTMPKDSPQQLELLSGPCERRKSPLQDPFPEEDYSSTEGSGGRITFNVDLNSVFLRVLDDEDSDDLEAPLMLSSHLEEMVDPEDPDNVQSNHLLASGEGTQPTFPSPSSEGLWSEDAPSDQSDTSESDVDLGDGYIMR
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (O42938)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. May also have a role in cell cycle regulation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Probable transketolase
- Triosephosphate isomerase
- Hexokinase-1
- Hexokinase-2
- Fructose-1,6-bisphosphatase
- Transaldolase
- Enolase 1-1
- Enolase 1-2
Sequence:
MSGETVHGISCYSVVANTEDTYNQTLDFYQKLGFKKVASFGTSDSDNARVCNESLREDWMHVAGNNSAESVTIKFRLVPGELSLSPAAEDSEWRGQKSSLVFYYPNLLDLLKQLSADAIKYQAFPNEKKPDEVYVEDPLGNLIGFSDRYNPFAHANLKKSEESGAASNLESGLATPVVETLKKATTSDKPAGVKKKIAVMTSGGDSPGMNAVVRAVARIAIHRGCDAFAIYEGYEGLVQGGDMIKQLQWGDVRGWLAEGGTLIGTARCMAFRERPGRLRAAKNLISAGIDSIIVCGGDGSLTGADIFRSDWPGLVKELEDTKAITPEQAKLYRHLTIVGLVGSIDNDMSSTDVTIGAFSSLHRICEAVDSISSTAISHSRAFIVEVMGRHCGWLAVLAALATGADFVFIPERPAEVGKWQDELCNSLSSVRKLGKRKSIVIVAEGAIDSELNHISPEDIKNLLVERLHLDTRVTTLGHVQRGGIPCAYDRMLATLQGVDAVDAVLASTPDTPSPMIAINGNKINRKPLMEAVKLTHEVADAIEKKQFAHAMELRDPEFADYLHTWEGTTFIEDESHFVPKDERMRVAIIHVGAPAGGMNSATRAAVRYCLNRGHTPLAIDNGFSGFLRHDSIHELSWIDVDEWCIRGGSEIGTNRDTPDLDMGFTAFKFQQHKIDALIIIGGFEAFTALSQLESARVNYPSFRIPMAIIPATISNNVPGTEFSLGCDTCLNAVMEYCDTIKQSASASRRRVFVCEVQGGRSGYIATVGGLITGASAIYTPEDGISLDMLRKDIDHLKATFALEAGRNRAGQLILRNECASKVYTTEVIGNIISEEAHKRFSARTAVPGHVQQGGNPTPMDRARAARLAMRAIRFFETCRANDLGNDPSSAVVIGIRGTGVSFSSVADVENNETEIEMRRPKNAWWRDMHNLVNILAGKTFAD
Protein: Hyaluronidase (EC 3.2.1.35) (F1MZM9)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Beta-glucuronidase
- ARSB protein
- Alpha-L-iduronidase
- Albumin
- CD44 antigen
- Aggrecan core protein
- Hyaluronan synthase 2
- DERPC proline and glycine rich nuclear protein
- Hyaluronan synthase 1
- Insulin
Sequence:
MLRHQHISFRNFVGSNGAPQAVFTFLLVPCCLALNFTAPPLIPNIPFLWAWNAPTNHCAEIFSMPPDLGLFSLVGSPQKDVTGQPITLFYADRLGYYPKINERTGVHKNGGIPQVASLKKHLDKAEKDIAYYMPIDNVGLAVIDWENWRPTWVRNWKPKDVYKKASIELVLQQNRHFTLKEATKRAKADFEKAAKSFMQETLKLGKFLRPNHLWGYYLFPDCYNHHYNQANYNGSCFDEEKRRNDALNWLWKESTALYPSVYLNTKLKSSPQARLFVRNRVQEAIRLSKVANVKSPLPVFVYTRPVFSDMSSKFLSQDDLVSTIGESIALGASGIIMWGSFNLSLTKQSCMNLSNYLNTILNPYIINVTLAAKMCSQVLCHEEGVCTRKHWNSTDYLHLNPMNFAIQRRKYGKYTIHGKPTLEDLLQFSENFYCSCYANIHCKKRDIKNIHTINVCFAEDVCINASLNSDRSKHSSSQKDISSTTFSTVSSSTPTAKVSARVPGKDHVSLKIRLPGEALSNTIQRGHKSVDWKNIFRQLYFQNIKNETNY
Protein: Methyl-CpG-binding domain-containing protein 6 (AtMBD6) (MBD06) (Methyl-CpG-binding protein MBD6) (Q9LTJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that binds CpG, CpNpN and CpNpG (N is A, T, or C) islands in promoters regardless the DNA methylation status. Plays probably a role in gene silencing. May associate with histone deacetylase proteins (HDAC). Required for nucleolar dominance that consist in the silencing of rRNA genes inherited from one progenitor in genetic hybrids. Recruited to rRNA genes in a DRM2-dependent manner. Maintains gene silencing by interacting with RNA binding proteins (e.g. NTF2, RPS2C, HDA6 and AGO4) and by regulating DNA methylation status.
Subcellular location: Nucleus {ECO:0000269|PubMed:14605234, ECO:0000269|PubMed:15010609, ECO:0000269|PubMed:15805479, ECO:0000269|PubMed:17208509, ECO:0000269|PubMed:18211904, ECO:0000269|PubMed:19061642}. Chromosome {ECO:0000269|PubMed:15010609, ECO:0000269|PubMed:15805479, ECO:0000269|PubMed:17208509, ECO:0000269|PubMed:18211904, ECO:0000269|PubMed:19061642}. Nucleus, nucleolus {ECO:0000269|PubMed:19061642}. Note=Associated with heterochromatin, and particularly at perinucleolar chromocenters and nucleolus organizer regions (NORs) in a DRM2-dependent manner. {ECO:0000269|PubMed:15010609, ECO:0000269|PubMed:15805479, ECO:0000269|PubMed:17208509, ECO:0000269|PubMed:18211904, ECO:0000269|PubMed:19061642}.
Interaction partners:
- Methyl-CpG-binding domain-containing protein 10
- Methyl-CpG-binding domain-containing protein 8
- Increased DNA methylation 3
- Methyl-CpG-binding domain-containing protein 1
- Methyl-CpG-binding domain-containing protein 2
- Methyl-CpG-binding domain-containing protein 11
- Methyl-CpG-binding domain-containing protein 3
- Histone deacetylase 6
- Putative methyl-CpG-binding domain protein 12
- Increased DNA methylation 2
Sequence:
MSDSVAGDFPPDPLLASGAFISSAGDGTLDSSAKRRPIQGGIGISGSGESVRIGMANGTDQVNHQTESKSRKRAAPGDNWLPPGWRVEDKIRTSGATAGSVDKYYYEPNTGRKFRSRTEVLYYLEHGTSKRGTKKAENTYFNPDHFEGQGSNRVTRTATVPPPPPPPLDFDFKNPPDKVSWSMANAGEEGWIPNIGDVKVQDSVRRDWSTAFTFITSRNPSKVSA
Protein: Cytoplasmic dynein 2 light intermediate chain 1 (mD2LIC) (Q8K0T2)
Organism: Mus musculus (Mouse)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system, facilitating the assembly of these organelles (By similarity). Involved in the regulation of ciliary length (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12802074}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:12802074}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TCX1}. Note=Localizes to the apical cytoplasm. {ECO:0000269|PubMed:12802074}.
Interaction partners:
- Cytoplasmic dynein 2 heavy chain 1
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Dynein light chain 2, cytoplasmic
- Dynein light chain Tctex-type protein 2B
- Dynein light chain roadblock-type 1
- Cytoplasmic dynein 1 intermediate chain 2
- Dynein light chain
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 1 intermediate chain 1
Sequence:
MPSETLWEIAKAEVEKRRSHGSEGDGAEIGEKSVFFIGSKNGGKTTIILRCLDRDESAKPTLALEYTYGRKTKGHNTPKDIAHFWELGGGTSLLDLISIPITVDTLRTFSIVLVLDLSKPNDLWSTMENLLQATKSHVDKVIMKLGKTSSKASAEMRQRMWSVVQKDHPDRELIDPFPIPLVIIGSKYDIFQDFDPEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLAFGIDKSKSICVDQNKPLFITAGLDSLCQIGSPPVPDSDIGKLQAHSPMELWKKVYDKLFPPKSTGTLKAVQDPARDPQYAESEVDEMRVQKDQELEHYKRSSSKTWKQIELDS
Protein: Enterobactin synthase component E (EC 6.3.2.14) (2,3-dihydroxybenzoate-AMP ligase) (DHB-AMP ligase) (2,3-dihydroxybenzoate-AMP synthase) (EC 6.2.1.71) (Dihydroxybenzoic acid-activating enzyme) (Enterochelin synthase E) (P10378)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-trihydroxybenzoate. In the second step, DHB is transferred from 2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB) to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can also transfer adenylated salicylate to holo-EntB.
Subcellular location: Membrane {ECO:0000269|PubMed:10692387}.
Interaction partners:
- Enterobactin synthase component D
- Isochorismate synthase EntC
- Enterobactin synthase component F
- Enterobactin synthase component B
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Ferrienterobactin receptor
- Proofreading thioesterase EntH
- Iron
- Enterobactin biosynthesis protein YbdZ
- Ferric enterobactin-binding periplasmic protein FepB
Sequence:
MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDSIAVIDGERQLSYRELNQAADNLACSLRRQGIKPGETALVQLGNVAELYITFFALLKLGVAPVLALFSHQRSELNAYASQIEPALLIADRQHALFSGDDFLNTFVTEHSSIRVVQLLNDSGEHNLQDAINHPAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSVEICQFTQQTRYLCAIPAAHNYAMSSPGSLGVFLAGGTVVLAADPSATLCFPLIEKHQVNVTALVPPAVSLWLQALIEGESRAQLASLKLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDSAEKIIHTQGYPMCPDDEVWVADAEGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLISIDPEGYITVQGREKDQINRGGEKIAAEEIENLLLRHPAVIYAALVSMEDELMGEKSCAYLVVKEPLRAVQVRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA
Protein: Dimethyladenosine transferase (EC 2.1.1.183) (18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase) (18S rRNA dimethylase) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase) (Q9USU2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
Interaction partners:
- Uncharacterized protein C13G1.09
- Ribosome biogenesis protein tsr1
- Periodic tryptophan protein 2 homolog
- Serine/threonine-protein kinase rio2
- Protein LTV1
- DNA-directed RNA polymerase, mitochondrial
- U3 small nucleolar ribonucleoprotein protein imp4
- rRNA processing protein rcl1
- U3 small nucleolar RNA-associated protein 21 homolog
- Uncharacterized protein C1604.06c
Sequence:
MGKIRVRNNNAASDAEVRNTVFKFNKDFGQHILKNPLVAQGIVDKADLKQSDTVLEVGPGTGNLTVRMLEKARKVIAVEMDPRMAAEITKRVQGTPKEKKLQVVLGDVIKTDLPYFDVCVSNTPYQISSPLVFKLLQQRPAPRAAILMFQREFALRLVARPGDPLYCRLSANVQMWAHVKHIMKVGKNNFRPPPLVESSVVRIEPKNPPPPLAFEEWDGLLRIVFLRKNKTIGACFKTSSIIEMVENNYRTWCSQNERMVEEDFDVKSLIDGVLQQCNLQDARASKCGQTEFLSLLHAFHQVGVHFA
Protein: Phospholipid hydroperoxide glutathione peroxidase GPX4 (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4) (EC 1.11.1.9) (O70325)
Organism: Mus musculus (Mouse)
Function: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation. Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species. The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis. The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures. May be required to protect cells from the toxicity of ingested lipid hydroperoxides. Required for normal sperm development and male fertility. Essential for maturation and survival of photoreceptor cells. Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion. Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity).
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:22207760}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:12566075}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:11344099}.
Interaction partners:
- Glutathione synthetase
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Endoplasmic reticulum chaperone BiP
- Glutathione hydrolase 6
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 7
- Glutathione hydrolase 1 proenzyme
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione reductase, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Sequence:
MSWGRLSRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVCLDKYRGFVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAGYNVKFDMYSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
Protein: PRA1 family protein (Q8SXD0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}.
Interaction partners:
Sequence:
MTTPSTSVGDAAAALSGNLQLPPLRTLDDFILGSARFQLPNLKDFEKWGNRVVKNLLYYQTNYFLLFITIYVLMIFFNPSKIITGLLVQALIIGVIWQFFSGKSKKNFIASRLTGGNANAAEQNAQQKWYILAGALLGGYLLLHLLSAVLLTIFTVLLPISLTFIHASLRLRNIKNKLTNSIESLLPPRPWAPCWMP
Protein: 4-chlorobenzoate--CoA ligase (4-CBA:CoA ligase) (EC 6.2.1.33) (P86831)
Organism: Arthrobacter sp
Function: Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoate is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA (By similarity). Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-fluorobenzoate also act as substrates. Inactive towards 4-nitrobenzoate.
Interaction partners:
Sequence:
MRTAFELVAWSAHRQPGAVALLDPESGHRLTYSELLKRIEGVATVLASRGVVRDELVATAMANTLDHAIILLALNRLGAIPVIINPRLKADEMVQLIRRDNIRTVIRTVAEGKSGTPADIDGVEELTLSAEVLSEGLRIDGNATPAFEAPRPEDPAFVFYTSGTTGLPKGVVIPHRAIEPRVLFMSTQAGLRFGGHNNLLGLMPIHHVIGFFGVFLGSLAFNGTWIPVTAFDPAQAVKWVEELDVTCLFASPTHFDALLATSEFAPEKLKSVDSVIFAGAAINQSILKRLEKCLQVPIVDIYGTTETMNSLFNPDATQERGLRPGYHSRVQFASVSESPSVALPAGVEGELVVDASADATFTHYLNNPEATAAKIVDGWYRTGDSGYVDDSGRVILTGRIDDMINTGAENVHAEEVEQIISRHPAVVEAAVVGLPDTRWGEVVTAVVVVSEPLTADLLDQVCLDSELANFKRPRRYFVVNELPRNAAMKVSRRTLREYLGAHAADQPNPETGFIQFTIEESQ
Protein: DNA-directed RNA polymerase III subunit RPC7 (RNA polymerase III subunit C7) (DNA-directed RNA polymerase III subunit G) (RNA polymerase III 32 kDa apha subunit) (RPC32-alpha) (RNA polymerase III 32 kDa subunit) (RPC32) (O15318)
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. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. 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.
Subcellular location: Nucleus {ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:33335104}. Cytoplasm {ECO:0000250|UniProtKB:Q6NXY9}. Note=Excluded from nucleoli (PubMed:21898682). In zygotes and the 2-cell stage embryos, mainly in the cytoplasm. Starts to localize to the nucleus in the 8-16 cell stage embryo and early blastocysts (By similarity). {ECO:0000250|UniProtKB:Q6NXY9, ECO:0000269|PubMed:21898682}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAGPKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDDDAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Protein: 60S ribosomal protein L36 (B4UN40)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL39
- L1c
- YL17
- Candida glabrata strain CBS138 chromosome M complete sequence
- 40S ribosomal protein S24
- 60S ribosomal protein L13
- Candida glabrata strain CBS138 chromosome G complete sequence
- 40S ribosomal protein S26
Sequence:
MAVKTGIAVGLNKGTKVTQMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNAGEKRARKVAKKRLGSFTRAKAKVEEMNSIIAASRRH
Protein: Transcription factor AS1 (Myb-related protein 91) (AtMYB91) (Protein ASYMMETRIC LEAVES 1) (Protein PHANTASTICA) (AtPHAN) (O80931)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor required for normal cell differentiation. Positively regulates LATERAL ORGAN BOUNDARIES (LOB) within the shoot apex, and the class III HD-ZIP genes REV, PHB, and PHV. Interacts directly with ASYMMETRIC LEAVES 2 (LBD6/AS2) to repress the knox homeobox genes BP/KNAT1, KNAT2, and KNAT6 and the abaxial determinants ARF3/ETT, KAN2 and YAB5. May act in parallel with the RDR6-SGS3-AGO7 pathway, an endogenous RNA silencing pathway, to regulate the leaf morphogenesis. Binds directly to KNAT1, KNAT2, and KNATM chromatin, regulating leaf development. LBD6 is required for this binding. Positive regulator of flowering that binds to the promoter of FT. Regulates FT expression by forming a functional complex with CO. Involved in leaf polarity establishment by functioning cooperatively with NUCL1 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures.
Subcellular location: Nucleus {ECO:0000269|PubMed:23271976}.
Interaction partners:
- Protein ASYMMETRIC LEAVES 2
- Homeobox protein knotted-1-like 2
- Auxin response factor 3
- Probable galactinol--sucrose galactosyltransferase 2
- Histone deacetylase 6
- Homeobox protein knotted-1-like 1
- Axial regulator YABBY 1
- Homeobox protein knotted-1-like 6
- Probable transcription factor KAN2
- Axial regulator YABBY 5
Sequence:
MKERQRWSGEEDALLRAYVRQFGPREWHLVSERMNKPLNRDAKSCLERWKNYLKPGIKKGSLTEEEQRLVIRLQEKHGNKWKKIAAEVPGRTAKRLGKWWEVFKEKQQREEKESNKRVEPIDESKYDRILESFAEKLVKERSNVVPAAAAAATVVMANSNGGFLHSEQQVQPPNPVIPPWLATSNNGNNVVARPPSVTLTLSPSTVAAAAPQPPIPWLQQQQPERAENGPGGLVLGSMMPSCSGSSESVFLSELVECCRELEEGHRAWADHKKEAAWRLRRLELQLESEKTCRQREKMEEIEAKMKALREEQKNAMEKIEGEYREQLVGLRRDAEAKDQKLADQWTSRHIRLTKFLEQQMGCRLDRP
Protein: Mitochondrial import protein 1 (Q9C1W7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the mitochondrial outer import machinery (MIM) complex that mediates transport of proteins into mitochondrial compartments. Promotes the insertion of tom70 into the outer mitochondrial membrane. Promotes the insertion of atg43 into the outer mitochondrial membrane. The MIM complex cooperates with the receptor tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane (By similarity). Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments (By similarity). Required for the assembly of the TOM (translocase of outer membrane) receptor complex, which is responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q08176}.
Interaction partners:
- Mitochondrial import protein 2
- Mitophagy receptor atg43
- Probable mitochondrial import receptor subunit tom70
- SAM50-like protein SPAC17C9.06
- Metaxin-like protein C409.19c
- Probable mitochondrial import receptor subunit tom40
- Mitochondrial distribution and morphology protein 10
- Mitochondrial import receptor subunit tom22
- Mitochondrial import receptor subunit tom20
- Mitochondrial distribution and morphology protein 12
Sequence:
MEKNTVTVPKTLFSQVIHIFKYAAINLGLPFLNGVMLGFGEIFAHAFIHSLGWAPGHTRIYSIQRHQYIQA