wanglab/gogpt-training-data huggingface dataset:
Protein: Alkaline protease 1 (ALP) (EC 3.4.21.63) (Aspergillopeptidase B) (Aspergillus proteinase B) (Elastase) (Elastinolytic serine proteinase) (Oryzin) (allergen Asp f 13) (P28296)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Secreted alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Involved in immune evasion from the human and mice complement systems during infection. Efficiently cleaves important components of the complement cascade such as such as C3, C4, C5, and C1q, as well as IgG, which leads to down-regulation of complement activation at the hyphal surface.
Subcellular location: Secreted {ECO:0000269|PubMed:10677362, ECO:0000269|PubMed:20303595, ECO:0000269|PubMed:20498262, ECO:0000269|PubMed:8500876}.
Interaction partners:
- Alkaline serine protease
- Dipeptidyl-peptidase 5
- Neutral protease 2 homolog AFUB_070680
- Neutral protease 2 homolog AFUA_4G13750
- Neutral protease 2
- Aspergillopepsin-1
Sequence:
MLSIKRTLLLLGAVLPAVFGAPVQETRRAAQKIPGKYIVTFKPGTDTATIESHTLWATDLHKRNLERRDTTSGEPPVGIEKSYKIKDFAAYAGSFDDATIEEIRKSADVAHVEEDQIWYLDALTTQKGAPWGLGSISHKGQASTDYIYDTSAGAGTYAYVVDSGINVNHVEFESRASLAYNAAGGSHVDSIGHGTHVAGTIGGKTYGVAKKTNLLSVKVFQGESSSTSIILDGFNWAVNDIVSKGRTKKAAINMSLGGGYSYAFNNAVENAFDEGVLSVVAAGNENSDASNTSPASAPNALTVAAINKSNARASFSNYGSVVDIFAPGQDILSAWIGSTTATNTISGTSMATPHIVGLSVYLMGLENLSGPAAVTARIKELATNGVVTNVKGSPNKLAYNGNA
Protein: ADP-ribosylation factor-like protein 3 (Arf-like GTPase 3) (Q02804)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the targeting of ARL1 to the Golgi. Can bind and hydrolyze GTP.
Subcellular location: Golgi apparatus.
Interaction partners:
- Protein SYS1
- Golgin IMH1
- Protein PET20, mitochondrial
- GTP-binding protein YPT6
- Conserved oligomeric Golgi complex subunit 8
- ADP-ribosylation factor-like protein 1
- Protein MON2
- Vacuolar protein sorting-associated protein 51
- N-alpha-acetyltransferase 30
- Conserved oligomeric Golgi complex subunit 5
Sequence:
MFHLVKGLYNNWNKKEQYSILILGLDNAGKTTFLETLKKEYSLAFKALEKIQPTVGQNVATIPVDSKQILKFWDVGGQESLRSMWSEYYSLCHGIIFIVDSSDRERLDECSTTLQSVVMDEEIEGVPILMLANKQDRQDRMEVQDIKEVFNKIAEHISARDSRVLPISALTGEGVKDAIEWMIVRLERNKKSRPPIYK
Protein: Cysteine-tryptophan domain-containing zinc finger protein 5 (OsCW-ZF5) (Q0DIQ5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds to histones H3K4me1, H3K4me2 and H3K4me3 in GST pull-down assay. May facilitate the recruitment of effectors to mediate gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28818372}.
Interaction partners:
Sequence:
MGGGRRGGRREAEEGVAVAGRSRGVAAAAARHEVAGELELASAGGLGGGGGDELVDPDQLTYIHNVFKIDLYSHVLVNLLVTICKDEKLQNILGHFQKEFEGGVSAENLGSQYGGYGSFLPTYQRSPPALSQSGSPAVLPNHGSASRSPYIPLESVQKNHFVKQAIDGRRKNNYCQRTSSENDSNHSQQLLNSGPEQKTAKIRIKVNNKCLERNNAAIYSGLGLDISPSSSIDDSPQWSIEAPESKLFPDESADTIFQIMTCHSVPGGLLLSPLAENVLELRQKSTAVTKKHEAPVYDNDKEELQRNCCHTSSAAPDNNYQLVKKIKLDEQRDHLPEFENSKYRHKNATIMKKGAKPELKDISDEIDSIRAPRCAKTEKHAVGESADFIADTSGRLKEAKNGQFKGKGSTQSSLSIIDVKAANSANDDKHPKGKAKLKVTLVRNAKMESSLDDGFSHKTKSDKCNDQPVTTSSQLQIDPAKKTSLKRDRGKVVCAKDEPSQYKSKELRSLVDAESMGTTTENVAGNSSELLKGKKVSALQASLFGKKLKIKTHKKPNYDTTRKPNGENEGYVLDHRNGSTYLHTEDKSLKTEKESATSGLTDKDFSGGGNDGDHKISPIVVDKSASMPSRCKNETTEASMAVPASEPVDQWVCCDKCETWRLLPYGMNSDTLPKKWRCSMQSWLPGMNNCKLSEGETTNAIRALYVVPIPENNISLDSRCDTATLVRSNDAAIMSDNLGMPEISKSSKKLHAPRNRDGLDCFPKLKEKQKRIESSDKGEKSTVTISSGQTMAKDRMHRKRKTSGADYDNLIASKKLKKVYNEPPKHQPPQFELSKSRPSTKGSLKELPKHTNISPGMGKHALPSSGKQFCDGDNSDRGARASDAGKSDPRDLFIKKNKSKQMQLRQHGPDPRPSDAFAKHVVKEVLSESNAAKEKLGSDLKFLKVDDHEKSAHARGPVTGTNSNAIFSEKEDLIEQHLENIHFQHPLLSESSVRRNICNVQASTAATSSSSKVSSSHKNKPEFQETRTSPVESVSSSPLRTSDKKHLDRHRTNSYAVAEIVHSQESVKTGASCSKEKYGFECGSDHTKPHVSGCSNRVMHQDALEDGDLDKQNILTNGVFNNRSSGLGIRNDQGQPNSLVEQKVNSHVLPIHGSGDFRRPTPDQNGKTLPQYNSNQSDQAKLSSGKHPTQVRPDKGNVEYIDLKTNPSTVAGSKLLPGLNNKVNGNASNKSKQSVVENMKHAAIHVDASTPINASALLKEARDLKHLSDRLKGKGDDLESANICFEACLKFLHVASLKEAAGVDSSKQGDPINTMTLYSDTGNLCGFCAREFERLKKMANAALAYKCVEVAYMKAAFYKHPGAIKDSHALQAASVIAPPAESPSSSASDVDNLNNPSTIAKIVSTRGLCTSQIAKNPISRSNHHLMGLLAYSFSYDPFCLLDKVEDTNYAFEGTRKSQSAFFSYLSGIEKDQADGIALLTEVLNFSFHNVKGLLQLIRHSLECINHERFK
Protein: Bromodomain protein 2, putative (Q8I5S4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Transcription initiation factor TFIID subunit 7, putative
- Histone H4
Sequence:
MNDYNNINNQLLIDTSSGMEHITIENNNNCIINNIDNIDYNNKTTNHIIKNNDSIISYKNNNMSSINNLIDIDNNGTSINNEFQQKNYNNNNIISDNKNMNYFSSFSNENTIDDNGNDTNYMNYDDNMNNSEYTNNHNNNHNNNHNNINSNDHNDDNLKNNNQCNSMNITDEYMSDNNISKNNSTSNILEYHINDNNNNNNINFIKKEEIIKNMDDLFIKNVNDIRSFERGILNLTQEEFIYISNKIHFLGFRFIEIPCVKTKNEKRNTYTAISKRHLNEIKNLSCSLSNSIYDAGKRKSKKTFDPFYSKAEFDSKGTYAQHDQKDTKDTNKKKAQTNNNVNNNNNNDYVNEKDIKNANIKEESHNLNSTKGNNKGTNNTYHNNNSIKSQQESDKLTSTSKGVKRSASNKFDDFDNKHNNKNVHGGSTNLGTNNSTPTHNNSNTGKGKGSKNTNSNNKKINEKESMKKRQKTNSYNEDNLMDEYEQHKKTYKKKIYRTKNPWKNYCFKILHKLKKKEIACWFLKPVNPELDGIPNYFNVIKNPMDFETIENKLINNKYNNPFEWQHDVRQIFFNAFTYHKVKNCVWNDAYKLAKEFDKLIKQGNDVKNILKDCTKNINSVYFNMKQYNDLIEHTNNTNNIINHNNISKTITNTSSDDHSGSLSSSSSSSSSISSSNYDDEAYDNVSSVNYNKRDSQMHKNVHGKKSSMYMTSASTNTLKNNLNSNQIYFPHGKNKKNEKMNKSSKYSINNNNNNNNISNKKNIRDNIKNKKDVNSNTLDDDDFEPPNVGTIPEPPGIQKIGINDKGLNNYQVNLLFKNFKRLAPNQRKAALEIIQDDLGILAENHMFDRFFTFDTDLLSIEKQKRIFLYINHMGRINLEHYKSSLISANKVNNSSFSKGKMGQKIVHNKSFIKHGSNNSNINAHYEKRRTNRYVSSSSNSSDSSTSNSSDSSSFSTSSDDSDSDSDSDMDSDSYDKKRKIKRPFPNDKKKELSNKFLEANRRKTLPQYKPVNENRKSLQIRDDVMGMHADFLGSMDSPRNTKNKHRASVSAWPEWKGQVIQQAILTQHKTNVPINKKELIAEGYDAKI
Protein: Hyaluronoglucuronidase (LHyal) (EC 3.2.1.36) (Hyaluronate 3-glycanohydrolase) (X4Y2L4)
Organism: Hirudo nipponia (Korean blood-sucking leech)
Function: Hyaluronidase that mediates hydrolysis of (1->3)-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate. Very specific to hyaluronate: not able to hydrolyze chitin, heparin or chondroitin sulfate.
Interaction partners:
Sequence:
MKEIAVTIDDKNVIASVSESFHGVAFDASLFSPKGLWSFVDITSPKLFKLLEGLSPGYFRVGGTFANWLFFDLDENNKWKDYWAFKDKTPETATITRRWLFRKQNNLKKETFDDLVKLTKGSKMRLLFDLNAEVRTGYEIGKKMTSTWDSSEAEKLFKYCVSKGYGDNIDWELGNEPDHTSAHNLTEKQVGEDFKALHKVLEKYPTLNKGSLVGPDVGWMGVSYVKGLADGAGDHVTAFTLHQYYFDGNTSDVSTYLDATYFKKLQQLFDKVKDVLKNSPHKDKPLWLGETSSGYNSGTKDVSDRYVSGFLTLDKLGLSAANNVKVVIRQTIYNGYYGLLDKNTLEPNPDYWLMHVHNSLVGNTVFKVDVSDPTNKARVYAQCTKTNSKHTQSRYYKGSLTIFALNVGDEDVTLKIDQYSGKKIYSYILTPEGGQLTSQKVLLNGKELKLVSDQLPELNADESKTSFTLSPKTFGFFVVSDANVEACKK
Protein: Kinesin-like protein KIF2A (Kinesin-2) (hK2) (O00139)
Organism: Homo sapiens (Human)
Function: Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, spindle. Note=Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1.
Interaction partners:
- Centrosomal protein of 170 kDa
- Tubulin beta-2B chain
- Tubulin alpha-1B chain
- Serine/threonine-protein kinase PLK1
- Centromere-associated protein E
- Kinesin-like protein KIF18A
- Cell division cycle protein 20 homolog
- Kinesin-like protein KIF2C
- Dynactin subunit 1
- Ninein
Sequence:
MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL
Protein: Transcription factor Jun (AH119) (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (Jun A) (P05627)
Organism: Mus musculus (Mouse)
Function: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity. Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 (By similarity). Binds to the USP28 promoter (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P05412}.
Interaction partners:
- Estrogen receptor
- Protein c-Fos
- Cyclic AMP-dependent transcription factor ATF-3
- Fos-related antigen 2
- Cyclic AMP-dependent transcription factor ATF-2
- Fos-related antigen 1
- Protein FosB
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 9
- Transcription factor JunD
Sequence:
MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
Protein: CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) (P26051)
Organism: Rattus norvegicus (Rat)
Function: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P15379}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15379}. Cell projection, microvillus {ECO:0000250|UniProtKB:P15379}. Secreted {ECO:0000250|UniProtKB:P16070}. Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000250|UniProtKB:P15379}.
Interaction partners:
Sequence:
MDKVWWHTAWGLLCLLQLSLAQQQIDLNITCRYAGVFHVEKNGRYSISRTEAADLCEAFNTTLPTMAQMELALRKGFETCRYGFIEGHVVIPRIHPNAICAANNTGVYILLASNTSHYDTYCFNASAPLEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDEDVSSGSTIEKSTPEGYILHTDLPTSQPTGDRDDAFFIGSTLATIATTPWVSAHTKQNQERTQWNPIHSNPEVLLQTTTRMTDIDRNSTSAHGENWTQEPQPPFNNHEYQDEEETPHATSTTWADPNSTTEEAATQKEKWFENEWQGKNPPTPSEDSHVTEGTTASAHNNHPSQRMTTQSQEDVSWTDFFDPISHPMGQGHQTESKGHSSGNQDSGVTTTSGPARRPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGTVEDRKPSELNGEASKSQEMVHLVNKEPTETPDQFMTADETRNLQSVDMKIGV
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 (SERCA3) (SR Ca(2+)-ATPase 3) (EC 7.2.2.10) (Calcium pump 3) (Q64518)
Organism: Mus musculus (Mouse)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q93084}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q93084}.
Interaction partners:
- Phospholamban
- Histidine rich calcium binding protein
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Nuclear receptor ROR-alpha
- Histone acetyltransferase KAT5
- Sarcolipin
- Stromal interaction molecule 1
Sequence:
MEEAHLLSAADVLRRFSVTAEGGLSLEQVTDARERYGPNELPTEEGKSLWELVVEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSILTGESVSVTKHTDAIPDPRAVNQDKKNMLFSGTNIASGKALGVAVATGLQTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEAEAGTCRLHEFTISGTTYTPEGEVRQGEQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLKGLSRVERAGACNSVIKQLMRKEFTLEFSRDRKSMSVYCTPTRADPKVQGSKMFVKGAPESVIERCSSVRVGSRTAPLSTTSREHILAKIRDWGSGSDTLRCLALATRDTPPRKEDMHLDDCSRFVQYETDLTFVGCVGMLDPPRPEVAACITRCSRAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVLGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKPPRNPREALISGWLFFRYLAIGVYVGLATVAAATWWFLYDTEGPQVTFYQLRNFLKCSEDNPLFAGIDCKVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWLNPWLLGAVVMSMALHFLILLVPPLPLIFQVTPLSGRQWGVVLQMSLPVILLDEALKYLSRNHMDEKKDLK
Protein: Putative tail-fiber/lysozyme protein (H9C1A7)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MAENSGTIDSLLVSLGLETDAKSFQKGADAIKGVTDGMMQLAAAAGVGLGFKALTQGVASSYSELKRLSDITGFTIQQIRGLEFAMRRIGSANPVASGQKLAQLIPDIVRRFGQGQLNQDAYYSDKFKPSELVKISTTQGNDAATEYFLNAYGSMNATERAYMRSGVGISENDDIARLGEYGGKFFRESMNMSNAMTPEIDPKLAKVAQDFNDEMAKLARNFENLAYSMGSQLLPIVNKFLELVNGFIHENPEIASAMIGAAGVAGTVGALGFGKRILGLGGGGGSAAGGSGGMSWLSRLLVNPITAGAVSAFTPGNFFTSSEDARMMESPDAFLRKKWERENPGVPYNGQYGGVTPYQAYLKQKAGNIGDALNNPNARSYLDAISRAEGTSGYMNSGYHTMFGGGQIASLADHPRQLKDFQQTDGTWNKTSAAGRYQFTQKSWDEAAAALGLNDFSPQSQDMAALWLIQRAGQLDNVLNGDFMTATNNLGGVWASLPSSPYAQPKRSQAEMESYYTPDYVQRRSQAPYNSSVNRSESSKPVSITLNNTQNISGLGLNEQQVQDTVASALTTAGENLERSFNNNRW
Protein: CRIB domain-containing protein (Q19275)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Uncharacterized protein T23G5.3
- DUF4149 domain-containing protein
- Nuclear hormone receptor family member nhr-54
- Serpentine Receptor, class H
- G-protein coupled receptors family 1 profile domain-containing protein
- C-type lectin domain-containing protein
- Nuclear Hormone Receptor family
- Serpentine receptor class r-10
- Serpentine receptor class r-10
- Serine/threonine-protein kinase dyf-5
Sequence:
MPNDLPLLPPKNQHKHLDKTMISLPSDFRHLAHVGPMGSSEIENLRTSDNVIDTVNESSYYIRPSSSNSTLRSQRKEKDRVGLDDAFPSASKSEEEVEVVRGYENQPTSHQYINIAPPRPSKKNYKAPAPPTPPPQNSKPNLIFNAQDDEEETSEISEQPVVFRSISHTSNISTHIAPPPKIQTADRIVAPKPNSLVIERPGDLGGAFSFGLDDCIPIVKSTPPLNTLSPLHRPLAIPKNQEETPILSPASPPDDSNYMSTIRSTSVQGRKILDELDDWLDDLDDLDRDQLSTISTDESGYPTLALEKDRAFMKHLVEKYELGVAPETIRLRKKKGPAPKAPSLPPDLSSPTFQAPGFIPAFSARPVSMPPNRPPPSYEAPSFDAPEAPGTVLINGRALTKQNALDLRSSDESGVPPAIARFLYDKRIKSATMPMSIGRMTSSSGNTDVSTTSSRSNADTVSSILSTVGEDDDVEVLKRDREVEEEFVPPVPKPRSRKTVSTEPLKEEEEENVEEEIKGENVIGEEFQVVGDTKINDEQEDRVEATKDKINDAFIMLPPPSAAAMIPSDSESEDDDNFIITRF
Protein: 26S rRNA (cytosine-C(5))-methyltransferase nsun-5 (EC 2.1.1.-) (5-methylcytosine rRNA methyltransferase nsun-5) (NOL1/NOP2/Sun domain family member 5) (RNA cytosine C(5)-methyltransferase nsun-5) (rRNA cytosine C(5)-methyltransferase nsun-5) (Q9NAA7)
Organism: Caenorhabditis elegans
Function: S-adenosyl-L-methionine-dependent methyltransferase which methylates the carbon-5 position of cytosine 2381 to 5-methylcytosine (m5C2381) in 26S rRNA. Plays a role in the production of mature 5S, 5.8S, 18S and 26S rRNAs and promotes the processing of the internally transcribed spacer 2 (ITS2), which separates the 5.8S and 26S rRNAs on large pre-rRNA precursors. May play a role in the translation of leucine and proline codons (Probable). May play a role in maintaining ribosomal frameshifting in response to osmotic stress. Not required for global translation.
Interaction partners:
- tRNA N
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar complex protein 2 homolog
- Ribosome biogenesis protein BOP1 homolog
- Probable rRNA-processing protein EBP2 homolog
- 5-cytosine rRNA methyltransferase nsun-4
- RRM domain-containing protein
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
- tRNA
- Nucleolar GTP-binding protein 1
Sequence:
MATDALYNEVAEIIRCVLAKEKSVRNAVYGSSYKNKKALLRLSCESLKFRPVFDEILQDKELKSMKRDANIGGSVELLYVLMYETLVGSGLTRCSQELKSVISRRIQRIKEVEHAMQDEGRGIKAMKEADDGMKKIQIPRYARINTLKWTADEAMKTLETEKWKILGTLKPENFAEMVTKMKDDEVYVDPHVENLIIFAPNIQNFYEYWMVEQRYLILQDKASCLPAFLLNPRPGSQVFDTCAAPGMKTSHAAAIMENQGKVWAMDRAADRVATMKQLLDASKVAIASSFCGDFLKTDVTDKKFSKVKFAIVDPPCSGSGIVKRMDEITGGNAEKERLEKLKNLQAMILKHALKLPGLKRAVYSTCSVHEEENEQVVDEVLLDTYVRQNYVLKKNVLPEWTYRGLKTYEVGEHCLRANPKVTLTNGFFVAVFERVKSSE
Protein: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC 1.2.4.1) (Pyruvate dehydrogenase complex component E1 beta) (PDHE1-B) (P32473)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Pyruvate dehydrogenase complex protein X component, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- NAD-dependent malic enzyme, mitochondrial
- Pyruvate kinase 1
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Increased recombination centers protein 15
Sequence:
MFSRLPTSLARNVARRAPTSFVRPSAAAAALRFSSTKTMTVREALNSAMAEELDRDDDVFLIGEEVAQYNGAYKVSKGLLDRFGERRVVDTPITEYGFTGLAVGAALKGLKPIVEFMSFNFSMQAIDHVVNSAAKTHYMSGGTQKCQMVFRGPNGAAVGVGAQHSQDFSPWYGSIPGLKVLVPYSAEDARGLLKAAIRDPNPVVFLENELLYGESFEISEEALSPEFTLPYKAKIEREGTDISIVTYTRNVQFSLEAAEILQKKYGVSAEVINLRSIRPLDTEAIIKTVKKTNHLITVESTFPSFGVGAEIVAQVMESEAFDYLDAPIQRVTGADVPTPYAKELEDFAFPDTPTIVKAVKEVLSIE
Protein: LOC100006122 protein (A8KC58)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGPSGDEIYPELRDLVEDTREISEDKFNDVLSKLKELLDLKSLGDQRDLEVCKLRLYTHGVLQYCSSSLRFSPARIQGGYAALTQMADLLSTCCVGLAAFRDIEVFSHEFLPSVVESLLFLAERLMNRALRDKAPSEMIRLFRKVFDSIGWLLRAHRHLIHHVLRCKHYESVQICEDDDVSIVTVTLWNDIFRKNSAVLAEMGNRALTDIMDDIVYKMSSSSNPVIGRAAVKTLVLILDHSSSTQQLIQRRYRGLSDLAEKDWRGKGFDSALDQLIDHLQLDVPWKNLRSRLRSV
Protein: Endoplasmic reticulum to nucleus signaling 1 (A0A8I5ZPE4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPARWLLLLLALLLLPPGPGSFGRASTVTLPEALLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGGKNNEGLTVRIFNSLVLTCF
Protein: Uncharacterized protein C594.04c (O74507)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTLASTMPIIYSASDAAKWKVAVSPYLYQLSNLKLLFTGKLNFADFYYNTNPFVVGLLLSFILGNVLWGVSVWTKNTSQVDRLWPILPTAFSLHFLFYGLGYNIASRRLMIMAFLQTLWSARLTYNYYRKGGYNRGAEDYRWVRVRQIMPKWIYPLFHYFYIHIFQVLHLYLLASPTYIAMLAGNERAFGAWDWIALELFMFMFVLEMLADQQQWDYYEARNHYNVDKTVPPRFKYDLLSLGRGFNATGLFRWSRHPNFLAEQLIWLSFYLFGAIASESLLNWTIFAWLGLVGVFQGSTRLTEKMSCEKYPLYRVYQDKVGRFFPRLDGSHWDIVDDDASLKED
Protein: Transcription initiation factor TFIID subunit 12 (TAFII-61) (TAFII61) (TAFII-68) (TAFII68) (TBP-associated factor 12) (TBP-associated factor 61 kDa) (Q03761)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SAGA complex subunit ADA2
- Transcription initiation factor TFIID subunit 11
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- Histone acetyltransferase GCN5
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 3
- SAGA complex subunit SPT20
- SAGA complex subunit NGG1
- SAGA complex subunit SPT7
- SAGA complex subunit SPT3
Sequence:
MSSNPENSGVNANNNTGTGNADAITGAQQNMVLQPRQLQEMAAKFRTLLTEARNVGETTPRGKELMFQAAKIKQVYDALTLNRRRQQAAQAYNNTSNSNSSNPASIPTENVPNSSQQQQQQQQQTRNNSNKFSNMIKQVLTPEENQEYEKLWQNFQVRHTSIKEKETYLKQNIDRLEQEINKQTDEGPKQQLQEKKIELLNDWKVLKIEYTKLFNNYQNSKKTFYVECARHNPALHKFLQESTQQQRVQQQRVQQQQQQQQQQQQQQQQQQQQQQQRQGQNQRKISSSNSTEIPSVTGPDALKSQQQQQNTITATNNPRGNVNTSQTEQSKAKVTNVNATASMLNNISSSKSAIFKQTEPAIPISENISTKTPAPVAYRSNRPTITGGSAMNASALNTPATTKLPPYEMDTQRVMSKRKLRELVKTVGIDEGDGETVIDGDVEELLLDLADDFVTNVTAFSCRLAKHRKSDNLEARDIQLHLERNWNIRIPGYSADEIRSTRKWNPSQNYNQKLQSITSDKVAAAKNNGNNVASLNTKK