wanglab/gogpt-training-data huggingface dataset:
Protein: Structural maintenance of chromosomes protein 3 (DA-box protein SMC3) (P47037)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
Subcellular location: Nucleus. Chromosome. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Interaction partners:
- Meiotic recombination protein REC8
- Sister chromatid cohesion protein 2
- N-acetyltransferase ECO1
- Structural maintenance of chromosomes protein 1
- Cohesin subunit SCC3
- Protein RAD61
- Sister chromatid cohesion protein PDS5
- Sister chromatid cohesion protein 1
- Separin
- Condensin complex subunit 3
Sequence:
MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEKLKISPESVFGTLGELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDVKFPSNTTTQIQFTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLAKKHKLNAITLDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVIEVNREEAIGFIRGSNKFAEV
Protein: Transcription factor Jun (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (Q2L4Q5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSTKMETTFYDDSHNAFSQHQNAGYGYNPKALKHSMTLNLADPTITLKPHLQAKASDILTSPDVQLLKLASPELERLIIQSSNGLITTTPTPTQFLCPRNVTDEQEGFAEGFVRALAELHHQHVLPNAPGVPVTSTGQTRINNSTTLPPVCSVAGSTVYNNVAMRSESPVYENLNTFTPAVTTNSAPGYTTSVPTMSFPSAPPQLPIYGQQSHPHPRLTALKEEPQTVPEMLGETPPLSPIDMENQERIKAERKRMRNRVAASKCRKRKLERISRLEDKVKNLKTQNSDLASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
Protein: Uncharacterized protein C6G10.10c (O14256)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C652.01
Sequence:
MGPSGAGTRGGQAQFQWEEVRNDKQKGRYLGQSIYAASGRWAEGKDLEWWSKGRTTQSAINSENSDKEKYKKEILEIKEREQRMLAEALGLPQPSALALTSSKAANRSSTNTEKDSRSIAHSTSRSRSTSPANRHRRKEKERTRSNHRHGSHRRHEPYRTHLSRHHRHSTTNYHSKRDDRYERRREHSPNDGGS
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (Q9LHL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At1g69250
- Cysteine-rich receptor-like protein kinase 18
- Zinc finger protein CONSTANS-LIKE 13
- Nuclear cap-binding protein subunit 1
- Homeobox protein LUMINIDEPENDENS
- Carbon catabolite repressor protein 4 homolog 4
Sequence:
MGSRSRNDNFQSGDGASPGKIFIGGLHKDTTNTVFNKHFGKYGEITDSVIMRDRHTGQPRGFGFITFADPSVVDKVIEDTHVINGKQVEIKRTIPKGAGGNQSKDIKTKKIFVGGIPSTVTEDELKDFFAKYGNVVEHQVIRDHETNRSRGFGFVIFDSEEVVDELLSKGNMIDMADTQVEIKKAEPKKSLNRSPPSYGSHPRGRSSNDSYASYGGPYGGFDGGYGHPPGPIRSHGGPASRYAGGYGYGRGSVGPEFGGGYNNYGGGSLGGYRNEPPLGYSSRFGPYGSGFGGEGYGRGGEGAYLGYPRGGGEGYGGYGGPGYGGAYESGGPGGSYEGAGGPYGRGYSSSSRYHPYAR
Protein: Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase) (F2Z2Y4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRSRPPGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL
Protein: Aldo-keto reductase family 1 member B7 (EC 1.1.1.21) (Aldehyde reductase) (Aldose reductase-like protein AKR1B14) (Aldose reductase-related protein 1) (Q5RJP0)
Organism: Rattus norvegicus (Rat)
Function: Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. Reduces prostaglandins (By similarity). May play a role in the metabolism of xenobiotic aromatic aldehydes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Sorbitol dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- L-xylulose reductase
- Tyrosine 3-monooxygenase
- Dihydropteridine reductase
Sequence:
MTTFVKLRTKAKMPLVGLGTWKSPPGQVKEAVKAAIDAGYRHFDCAYVYQNESEVGEAIQEKIKEKAVRREDLFIVSKLWSTFFEKSLMKEAFQKTLSDLKLDYLDLYLIHWPQGLQAGKEFLPKDSQGKVLMSKSTFLDAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIAVIAYSPLGSPDRPYAKPEDPVVLEIPKIKEIAAKHKKTIAQVLIRFHVQRNVAVIPKSVTLSHIKENIQVFDFQLSEEDMAAILSLNRNWRACGLFVTSDEEDFPFHEEY
Protein: ATP synthase subunit delta, mitochondrial (F-ATPase delta subunit) (Q12165)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane {ECO:0000269|PubMed:10576729}.
Interaction partners:
- ATP synthase subunit J, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit H
Sequence:
MLRSIIGKSASRSLNFVAKRSYAEAAAASSGLKLQFALPHETLYSGSEVTQVNLPAKSGRIGVLANHVPTVEQLLPGVVEVMEGSNSKKFFISGGFATVQPDSQLCVTAIEAFPLESFSQENIKNLLAEAKKNVSSSDAREAAEAAIQVEVLENLQSVLK
Protein: Eukaryotic translation initiation factor 3 subunit F (eIF3f) (eIF-3-epsilon) (eIF3 p32 subunit) (O04202)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Involved in cell growth and differentiation, especially during embryogenesis and male gametophyte germination. Regulates sensitivity to sugars (e.g. sucrose).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:20444226}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit G
Sequence:
MAATSEHTILQFVSPSSTASATTSVLTARIHPLVIFNVCDCFVRRPDSAERVIGTLLGSILPDGTVDIRNSYAVPHNESSDQVAVDIDYHHNMLASHLKVNSKETIVGWYSTGAGVNGGSSLIHDFYAREVPNPIHLTVDTGFTNGEGTIKAFVSSNLSLGDRQLVAHFQEIPVDLRMVDAERVGFDVLKATSVDKLPNDLEGMELTMERLLTLINDVYKYVDSVVGGQIAPDNNIGRFIADAVASLPKLPPQVFDNLVNDSLQDQLLLLYLSSITRTQLSLAEKLNTAAQML
Protein: Transmembrane protein 98 (Q91X86)
Organism: Mus musculus (Mouse)
Function: Functions as a negative regulator of MYRF in oligodendrocyte differentiation and myelination. Interacts with the C-terminal of MYRF inhibiting MYRF self-cleavage and N-fragment nuclear translocation. The secreted form promotes differentiation of T helper 1 cells (Th1).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:30249802}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y2Y6}. Cell membrane {ECO:0000250|UniProtKB:Q9Y2Y6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y2Y6}. Secreted {ECO:0000269|PubMed:25946230}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9Y2Y6}. Note=Secreted by exosomes through a non-classical pathway. {ECO:0000250|UniProtKB:Q9Y2Y6}.
Interaction partners:
- Serine protease 56
- Myelin regulatory factor
- Membrane frizzled-related protein
Sequence:
METVVIVAIGVLATIFLASFAALVVVCRQRYCRPRDLLQRYDSKPIVDLIGAMETQSEPSELELDDVVITNPHIEAILENEDWIEDASGLMSHCIAILKICHTLTEKLVAMTMGSGAKMKTSASVSDIIVVAKRISPRVDDVVKSMYPPLDPKLLDARTTALLLSVSHLVLVTRNACHLTGGLDWIDQSLSAAEEHLEVLREAALASEPDKSLPNPEGFLQEQSAI
Protein: Acid-sensing ion channel 2 (ASIC2) (ZASIC2) (Q708S5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probable cation channel with high affinity for sodium. In vitro, has no proton-gated channel activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16515}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16515}.
Interaction partners:
Sequence:
MDLKEACGSEASRETESGGMGSLGGHSSWQSFAHRSTLHGLRFIFPYSSSSSSSSSYRSTSRRLLWSAALLASLVLLVLESTERLAYFLSYPHVTSVDAVVSGSLVFPAVTVCNLNAYRFTRLTQNDLYHAGELLALLDVHLQIPEPHLAEPHVLAFLTEKSNFTNYRPKPFSMREFTERVGHDLKEMMLYCRFQGQECSHQDFKTVFTRYGKCYMFNAAEEGKTLRTTMKGGTGNGLEIMLDIQQDEYLPVWGETEETAFEAGVRVQIHSQAEPPFVHELGFGVAPGFQTFVATQEQRLTYLPPPWGECVSRALDSGLFQVYSVSACRIECETRYIVENCNCRMVYMPGDSPYCTPEQYKDCAEPALAALSAVEGTNCICRSPCNMTRYNKELSMVKIPSKTSARYLEKKFNRSEKYITDNILVLDVFFEALNYETIEQKKAYEVAGLLGDIGGQMGLFIGASILTLLELFDYAYEVVKERLLDLLNREEEEESHGEDVSTCDPVVNHSESISHTVSVPLQTTLGTLEEIAC
Protein: Fascin-3 (Testis fascin) (Q9QXW4)
Organism: Mus musculus (Mouse)
Function: Acts as an actin bundling protein.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Transmembrane protein 225
Sequence:
MAEVDWIHRHPKAEDLRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCFLLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWTPRPALHVHVILYSPIYHSYARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPRGLVALCDGEGGTLYPQGSHLLLGMGSAPMKGEEWFVLQHFPTWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNCGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFANRPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLLTVLAPNGFYLRADRSGTLLADSEEITKECIWEF
Protein: Acetylcholine receptor-like protein cup-4 (Coelomocyte uptake defective protein 4) (P34271)
Organism: Caenorhabditis elegans
Function: Thought to regulate endocytosis in coelomocytes through modulation of phospholipase C activity. Possible acetylcholine receptor.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15936276}; Multi-pass membrane protein {ECO:0000269|PubMed:15936276}.
Interaction partners:
- Neuropeptide-like protein 7
Sequence:
MKIIIFVCFILIFYLPIQKKHVNSQQQGIDSDDGDAESFFNKSYSEHQSALEQKIFRGYNPKNRPMKNASFPTIVDVHWHIIHVSINQREQTMTVHGHIYMRWFDEFLVWDPKDFNNIQYARVKKWQVWQPKIKVSNSASGLGSAFDFSTSAHVIIQMMGKDRAKVEMYPTFSIKVGCAFDFTDYPYDLNKCAINLFSTSTMADVQLQNLYAIPPTLSFGWEEQKMKRIISDFKIQNVSSSALYYTNGNITSSAPITGFDLGSTWSMLAVTVSFVRHSPLFEAAVVTPCIVVASLISMTFFIDSLSSTFLLMMLHFYVQLIFLHDLVEKLPLSVSEIPFCIKLIGILMYTNGLTLVLHSSLLCGSYYKCPVPQQLNKIFVIEEYIPNTFKEKVQIKKEESNKSWRDLMKLIRPIIGFVLIILLICMFFVCLLL
Protein: Palmitoyl-acyl carrier protein thioesterase, chloroplastic (EC 3.1.2.-) (16:0-acyl-carrier protein thioesterase) (16:0-ACP thioesterase) (Acyl-[acyl-carrier-protein] hydrolase) (Acyl-acyl carrier protein thioesterase B1) (AtFATB1) (Q9SJE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an essential role in chain termination during de novo fatty acid synthesis. Possesses high thioesterase activity for palmitoyl-ACP versus other acyl-ACPs. Substrate preference is 16:0 > 18:1 > 18:0 > 16:1. Plays an essential role in the supply of saturated fatty acids necessary for plant growth and seed development. Contributes to 16:0 production particularly in flowers. May be involved in the synthesis of long chain fatty acid.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Long chain acyl-CoA synthetase 9, chloroplastic
- Long chain acyl-CoA synthetase 8
- Long chain acyl-CoA synthetase 1
- Long chain acyl-CoA synthetase 6, peroxisomal
- Long chain acyl-CoA synthetase 4
- Long-chain-fatty-acid--[acyl-carrier-protein] ligase AEE15, chloroplastic
- Probable acyl-activating enzyme 16, chloroplastic
- Long chain acyl-CoA synthetase 2
- Long chain acyl-CoA synthetase 5
Sequence:
MVATSATSSFFPVPSSSLDPNGKGNKIGSTNLAGLNSAPNSGRMKVKPNAQAPPKINGKKVGLPGSVDIVRTDTETSSHPAPRTFINQLPDWSMLLAAITTIFLAAEKQWMMLDWKPRRSDMLVDPFGIGRIVQDGLVFRQNFSIRSYEIGADRSASIETVMNHLQETALNHVKTAGLLGDGFGSTPEMFKKNLIWVVTRMQVVVDKYPTWGDVVEVDTWVSQSGKNGMRRDWLVRDCNTGETLTRASSVWVMMNKLTRRLSKIPEEVRGEIEPYFVNSDPVLAEDSRKLTKIDDKTADYVRSGLTPRWSDLDVNQHVNNVKYIGWILESAPVGIMERQKLKSMTLEYRRECGRDSVLQSLTAVTGCDIGNLATAGDVECQHLLRLQDGAEVVRGRTEWSSKTPTTTWGTAP
Protein: Proline-rich basic protein 1 (E7EW31)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLTALAPPALPGIPRQLPTAPARRQDSSGSSGSYYTAPGSPEPPDVGPDAKGPANWPWVAPGRGAGAQPRLSVSAQNSRQRHGPGSGFPRGPGSGPRPPQPQLRTLPSGEMEVIFGVGPLFGCSGADDREAQQQFTEPAFISPLPPGPASPAAVPRQSQVPDGGSRWATYLELRPRGPSPAAPAQFECVEVALEEGAAPARPRTVPKRQIELRPRPQSPPRAAGAPRPRLLLRTGSLDESLGPLQAAAGFVQTALARKLSPEAPAPSSATFGSTGRSEPETRETARSTHVVLEKAKSRPLRVRDNSAPAKAPRPWPSLRERAIRRDKPAPGTEPLGPVSSSIFLQSEEKIQEARKTRFPREAPDRTVQRARSPPFECRIPSEVPSRAVRPRSPSPPRQTPNGAVRGPRCPSPQNLSPWDRTTRRVSSPLFPEASSEWENQNPAVEETVSRRSPSPPILSQWNQCVAGERSPSLEAPSLWEIPHSAVADAVEPRSSPSPPAFFPWEAPDRPIGTWGPSPQETWDPMGPGSSIAFTQEAQNGLTQEELAPPTPSAPGTPEPTEMQSPSTREISDLAFGGSQQSPEVAAPEPPGSHPVGTLDADKCPEVLGPGEAASGRPRMAIPRPRDVRKLVKTTYAPGFPAGAQGSGLPAPPADPCGEEGGESKTQEPPALGPPAPAHYTSVFIKDFLPVVPHPYEPPEPSFDTVARDASQPNGVLRRRAENSTAKPFKRTEIRLPGALALGRRPEVTSRVRARGPGGENRDVEAQRLVPDGDGRTSPLGGARSSSQRSPVGPAGVRSPRPGSPQMQASPSPGIAPKPKTPPTAPEPAAAVQAPLPREPLALAGRTAPAQPRAASAPPTDRSPQSPSQGARRQPGAAPLGKVLVDPESGRYYFVEAPRQPRLRVLFDPESGQYVEVLLPPSSPGPPHRVYTPLALGLGLYPPAYGPIPSLSLPPSPGPQALGSPQLPWVSEAGPLDGTYYLPVSGTPNPAPPLLLCAPPSSSGPTQPGKGSLFPL
Protein: Extracellular protease inhibitor 1 (Secreted effector EPI1) (D0MVC9)
Organism: Phytophthora infestans (strain T30-4) (Potato late blight agent)
Function: Secreted effector that interacts with and inhibits the pathogenesis-related P69B subtilisin-like serine protease of host tomato. Inhibition of host proteases by a pathogen extracellular protease inhibitor forms a specific type of defense-counterdefense mechanism between plants and microbial pathogens.
Subcellular location: Secreted {ECO:0000305|PubMed:15096512}. Note=Localizes to host apoplast where it targets defense proteases for inhibition. {ECO:0000269|PubMed:15096512}.
Interaction partners:
- Cystatin-like cysteine protease inhibitor EPIC2B
- Cystatin-like cysteine protease inhibitor EPIC1
- Kazal-like protease inhibitor
- Kazal-like protease inhibitor
- Kazal-like protease inhibitor
- Kazal-like protease inhibitor
- Kazal-like protease inhibitor
Sequence:
MKSALLFTLVVAAVHAQSPQVISPAPRRESNEIDCPEYCLDVYDPVGDGEGNTYSNECYMKRAKCHNETTPPAWKDLVLITGSSTGEQPPSKKCSTVCPDVELPVCGSNRVRYGNPCELRIAACEHPELNIVEDSGKACVGSKVTPQEG
Protein: DNA-directed RNA polymerase, mitochondrial (MtRPOL) (EC 2.7.7.6) (Q8BKF1)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Has DNA primase activity. Catalyzes the synthesis of short RNA primers that are necessary for the initiation of lagging-strand DNA synthesis from the origin of light-strand DNA replication (OriL).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23283301}.
Interaction partners:
- Dimethyladenosine transferase 2, mitochondrial
- Transcription factor A, mitochondrial
- Transcription elongation factor
- Dimethyladenosine transferase 1, mitochondrial
- Large ribosomal subunit protein bL12m
- DNA polymerase subunit gamma-1
- Single-stranded DNA-binding protein, mitochondrial
- Twinkle mtDNA helicase
- Serum response factor-binding protein 1
- DNA-directed RNA polymerase I subunit RPA2
Sequence:
MSALRWTRSAAGLGRVLRSPGPHRPPSEEGTFGGFCSSRRSSAASPREQHVLREWGHAELLEVLEARVRQLRAEGTPEMRVKKVQVDRPPQGHSSRWAQKLEAEKRVKQRRQKEVDQQKQALTQEFWTLHKEPKIWNKKLAGYLQPSKKGTPTNSEEKQLAQALQAALGRLSSREAEALARKKAKAVEAQILVLQQKFLAFFECCVCTGQVPLAHHVLVTHHNNGDRQQVLTLHMYNTVMLGWARKGSFRELVYVFLMLKDAGLSPDLCSYAAALQCMGRRDQDVRTIQRCLKQMMEEGFQPQLLFTDLVLEEEDRAALLRAVVKAEPAFRPPPQAPSPVNTSTLLKDIYSKEGPVSYPKLHLPLDTLQDLFYQQLHVELSSSVCVQSVEKAPVMSKEVIEARKTLQALREQWEVELLRVLRETKATMGRQAYEGQPTLYPFLCLLSEGEFVSILMQVLKVLPAQGEPLIQLAHNLGLRVLNRHLVKQKQVTNHVQKLGQRYSQYLQLLASDTQVAPCLPREYWESLGPLEAPAQQPWSVPVLLQLGKQLAELLVQAVQMPRSLAARQGAQRSIPVLYHVYSFRSYRQVGILKPHPAFTHLLETAAEPTLTFETTEVPMLCPPLPWTSLHSGAYLLSSTKLMRATEGTTQHQRLLEQCPPAQLHGPLDALTQLGNCAWRVNGHLLDLVLQIFRDKGCMPLGVPPPRSEAPRPARYQLPPGSTPVHKSELRKELARCLKVAREMHSLRSEALYRLSLAQHLRHRVFWLPHNMDFRGRTYPCPPHFNHLGSDLARALLEFAEGRPLGPRGLDWLKIHLINLTGLKKGDSLRMRLAFADEVMEEILDSADNPLTGRKWWMEADEPWQTLACCMEVAHAVRSPDPAAYISHLPVHQDGSCNGLQHYAALGRDSVGAASVNLTPSDLPQDVYREVATQVEEFRQQDAKEGLRVAQVLEGFISRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFTSTRAIQHWLTESANLISHAGWPVEWVTPLGIPIIQPYHRESKVQVKGGLQSITLTSSVDESQKPNTLKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLIFVSVHDCFWTHAADIPTMNEVCREQFVRLHSQPILEDLAKFLKKRFCSVSSIKSLKSSERALVTKLQETLQSLPKTGTFDLGQVIRSTYFFS
Protein: Argininosuccinate lyase, chloroplastic (EC 4.3.2.1) (Arginosuccinase) (Q9LEU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Argininosuccinate synthase, chloroplastic
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Arginine biosynthesis bifunctional protein ArgJ
- Acetylglutamate kinase, chloroplastic
- Arginase 1, mitochondrial
- Arginase 2, chloroplastic/mitochondrial
- Probable amino-acid acetyltransferase NAGS1, chloroplastic
- Ornithine aminotransferase, mitochondrial
- Acetylornithine aminotransferase, chloroplastic/mitochondrial
Sequence:
MGAIDLSFSQSLLFSSSRSNLSSSTHRSVSFLPPGSKSRCLPPLRSMSHDDDTASKEVKLWGGRFEESVTEKVEKFTESISFDKVLYKQDIMGSKAHASMLAHQGLITDSDKDSILRGLDDIERQIEANKFEWRTDREDVHMNIEAALTDLIGEPAKKLHTARSRNDQVATDFRLWCRDAIDTIIVKIRNLQRALVELALKNEALIVPGYTHLQRAQPVLLPHVLLTFVEQLERDAGRYVDCRARLNFSPLGACALAGTGLPIDRFMTANALGFTEPMRNSIDAVSDRDFVLEFLYTNANTGIHLSRLGEEWVLWASEEFGFMTPSDSVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLTLCKGLPLAYNRDFQEDKEPMFDSTKTIMGMIDVSAEFAQNVTFNEDRIKKSLPAGHLDATTLADYLVKKGMPFRSSHDIVGKLVGVCVSKGCELQNLSLEEMKKLSPVFEEDVFGFLGVENSVNKFSSYGSTGSNCVAEQLGYWVNKLNITST
Protein: Ubiquinol-cytochrome c reductase complex assembly factor 6 (Protein BRAWNIN) (Q69YU5)
Organism: Homo sapiens (Human)
Function: Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation. Mediates early complex III biogenesis (By similarity). Participates in regulating the levels of electron transport chain proteins, and therefore energy supply, in response to changes in energy demand (By similarity). Also required for cytochrome c oxidase complex (complex IV) assembly.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:32161263, ECO:0000269|PubMed:34969438}; Single-pass type II membrane protein {ECO:0000305|PubMed:32161263}.
Interaction partners:
Sequence:
MPAGVPMSTYLKMFAASLLAMCAGAEVVHRYYRPDLTIPEIPPKRGELKTELLGLKERKHKPQVSQQEELK
Protein: Patatin-like phospholipase domain-containing protein 7 (EC 3.1.1.-) (EC 3.1.1.5) (Liver NTE-related protein 1) (NTE-related esterase) (Q5BK26)
Organism: Rattus norvegicus (Rat)
Function: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Also can deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A2AJ88}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:A2AJ88}. Lipid droplet {ECO:0000250|UniProtKB:A2AJ88}.
Interaction partners:
- Lysosomal phospholipase A and acyltransferase
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phosphatidylcholine-sterol acyltransferase
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase A and acyltransferase 3
- Phospholipase B1, membrane-associated
- lysophospholipase
- Membrane bound O-acyltransferase domain containing 1
- Lysophosphatidylcholine acyltransferase 4
- Acyl-protein thioesterase 2
Sequence:
MQKEEDVCPEAGYCLGTALSSWGLHFMEEHSQSTMLMGIGIGVLLTLAFVGLAAFFVYRKVSRFRRAEPIPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTAAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVASTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSPRLSEFNSSDQRSVAVSGPLLKRSCSVPLPPIHGEIDELRQAQGSGSNTSAFQESQEGATSDLGMAYNRARILPHSEEQLGSSLASKSKKSVVAETSAVFHYSEKPRDEPGPSGRTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTIVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVRRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVEMLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSGTGHQLGFNTASSKWDLGNPPGNLSTVAAMPVSEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADSTLTPWTQRCIRQADCILIVGLGDQEPALGELEQMLESTAVRAQKQLILLHKEEGPAPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRIFQRPPDRHSDFSRLARILTGNAIALVLGGGGARGCAQVGILRALAECGIPVDIIGGTSIGAFMGALFAEERSYSQIRIRAKQWAEDMTSMVKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGALWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGPAGFDIWVRSGVLEKMLQDQQGTSKRMDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSECEPSMSQGPHSLTSPKQSQDSFPWLPNQDDQGPRLYRPS