wanglab/gogpt-training-data huggingface dataset:
Protein: Elongation factor G-2, mitochondrial (EF-Gmt) (mEF-G 1-2) (Elongation factor G1-2) (F4IW10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:14671022}.
Interaction partners:
- Diphthine--ammonia ligase
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Protein STABILIZED1
- At4g01000
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein bL31c
- Large ribosomal subunit protein uL10c
- At1g43860
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MARFPTSPAPNLLLRLFSSNKRASSPTAALLTGDFHLIRHFSAGTAARAVKDEKEPWWKESMDKLRNIGISAHIDSGKTTLTERVLFYTGRIHEIHEVRGRDGVGAKMDSMDLEREKGITIQSAATYCTWKDYKVNIIDTPGHVDFTIEVERALRVLDGAILVLCSVGGVQSQSITVDRQMRRYEVPRVAFINKLDRMGADPWKVLNQARAKLRHHSAAVQVPIGLEENFQGLIDLIHVKAYFFHGSSGENVVAGDIPADMEGLVGDKRRELIETVSEVDDVLAEKFLNDEPVSAAELEEAIRRATIAQKFVPVFMGSAFKNKGVQPLLDGVVSFLPSPNEVNNYALDQNNNEERVTLTGSPDGPLVALAFKLEEGRFGQLTYLRVYEGVIKKGDFIINVNTGKRIKVPRLVRMHSNDMEDIQEAHAGQIVAVFGIECASGDTFTDGSVKYTMTSMNVPEPVMSLAVQPVSKDSGGQFSKALNRFQKEDPTFRVGLDPESGQTIISGMGELHLDIYVERMRREYKVDATVGKPRVNFRETITQRAEFDYLHKKQSGGAGQYGRVTGYVEPLPPGSKEKFEFENMIVGQAIPSGFIPAIEKGFKEAANSGSLIGHPVENLRIVLTDGASHAVDSSELAFKMAAIYAFRLCYTAARPVILEPVMLVELKVPTEFQGTVAGDINKRKGIIVGNDQEGDDSVITANVPLNNMFGYSTSLRSMTQGKGEFTMEYKEHSAVSNEVQAQLVNAYSASKATE
Protein: Serine/threonine-protein kinase/endoribonuclease IRE1 (Endoplasmic reticulum-to-nucleus signaling 1) (Inositol-requiring protein 1) (Ire1-alpha) (IRE1a) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] (Q9EQY0)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA. The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes. Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11850408}; Single-pass type I membrane protein {ECO:0000269|PubMed:11850408}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- TNF receptor-associated factor 2
- Mitogen-activated protein kinase kinase kinase 5
- X-box-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Tumor necrosis factor
- Presenilin-1
- Presenilin-2
- Bax inhibitor 1
- DNA damage-inducible transcript 3 protein
Sequence:
MPARWLLLLLALLLPPPGPGSFGRTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGGKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQGEVLRKVVHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDLKFDPGLKGKSKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKRSFEEVINIVGQTSDNTPTTVSQDVEEKLARAPAKPEAPVDSMLKDMATIILSTFLLVGWVAFIITYPLSVHQQRQLQHQQFQKELEKIQLLQQQQLPFHPHGDLTQDPEFLDSSGPFSESSGTSSPSPSPRASNHSLHPSSSASRAGTSPSLEQDDEDEETRMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKDNPTYTVDIFSAGCVFYYVISEGNHPFGKSLQRQANILLGACNLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKEALDGPIVRQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPVEVQETLGSIPDDFVRYFTSRFPHLLSHTYQAMELCRHERLFQTYYWHEPTEPQPPVIPYAL
Protein: Cyclic nucleotide-binding domain-containing protein (A8WI01)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cyclic nucleotide-binding domain-containing protein
- Guanine nucleotide-binding protein alpha-17 subunit
- Receptor-type guanylate cyclase daf-11
- Receptor-type guanylate cyclase gcy-10
- Receptor-type guanylate cyclase gcy-28
- Ion transport domain-containing protein
Sequence:
MAENVSTTSSARRETFGGIVFRIYALRGWMQRAQKRLHLFRKNDVDIETNFREALREEQEDDEKSSGFMSFTVDEHSNTFYLWTGLVSLVALHPLVFTALSVFQDVHPFLRNTGPLNLLLDLVNILDLIAHTRIEYVENGVAVKNLSKLMHHRLKSTFFILDVIAVVPAESLHIFGDSFFWSRINRLTKCYRLFDFSTQTDTRTTSPHAFGLFKLIFICVVIFHWNGCLYFYISKVYNYTTARLEHWIFSYDKIINPILATCVTDIPNHRDFCDTDDLLITHLPENEVQFTVTDYMTTWENKTTTIKFANFFRQYALSFYWSALTLVTLGEQPSPCTTFQNAFEIGDTLLGLVIFAVIVGDVGNMVVAINLRKSEFENVLDGCKRFMVYRKVPNLLRKKAVEYFAYVWAHGGAQVDEEEIAEFLPPRLFGEIAVEIHMDTLKKVKLFESCDPRLLYELILKLQLRVYSPMDYICKKGDVGTEMYIVKEGFVEVVSEDGQTIFVTLPAGFVFGELSILNIPGNKNKNLRTASVRSKGYSDLYVLDKEDLWEALHEYPQAKDSLIQKGIQILEKDKMIDPNMVDDEDESFNGPIEDYMEHLEHEILKITKMIDQAEDKIHKSNQKMKTRLFGMEMDLVHEIKELLKENSWKRIARFADGVTVL
Protein: Glutaredoxin-1 (Thioltransferase-1) (TTase-1) (Q9QUH0)
Organism: Mus musculus (Mouse)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Glutathione reductase, mitochondrial
- Thioredoxin
- Mitochondrial peptide methionine sulfoxide reductase
- Thioredoxin, mitochondrial
- Peroxiredoxin-2
- Ribonucleoside-diphosphate reductase subunit M2 B
- Ribonucleoside-diphosphate reductase subunit M2
- Glutathione peroxidase 1
- Glutaredoxin-3
Sequence:
MAQEFVNCKIQSGKVVVFIKPTCPYCRKTQEILSQLPFKQGLLEFVDITATNNTSAIQDYLQQLTGARTVPRVFIGKDCIGGCSDLISMQQTGELMTRLKQIGALQL
Protein: Protein RISC-INTERACTING CLEARING 3'-5' EXORIBONUCLEASE 1 (EC 3.1.13.1) (Q9SF21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3'-to-5' exoribonuclease (RNase) specifically targeting single-stranded RNAs. Triggers miRNA accumulation in RNA-induced silencing complex (RISC), composed of miRNAs and AGO proteins, by degrading uridylated cleavage fragments. Required during plant growth and development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28463111}.
Interaction partners:
- Auxin-responsive protein IAA14
- DELLA protein RGL3
- DELLA protein RGA
- DELLA protein RGL1
- DELLA protein RGL2
- DELLA protein GAI
- Protein HESO1
- F-box protein GID2
- UTP:RNA uridylyltransferase 1
- Protein argonaute 10
Sequence:
MASFDGQGFMMVDNSWVQTKAIDVESTTDISPYLSKILEDSVWNGNRSIVFDVYWDVKSVSTKSEWRLCSVKFSTKNFCLFLRLPNPFCDNLKDLYRFFASKFVTFVGVQIQEDLALLKENHGIVIRSSLEIGKLAAKARGTPIVEFLGTRELAHKILWYDMSRLDSIQSKWDEASSNDRLEAAAIEGWLIFNVYDQLQQ
Protein: dihydropyrimidinase (EC 3.5.2.2) (Q5U187)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTSPKPVKKVPIHLQSAQNRVYIKNGEIVNHDKSFKADVYIEDGIIKFVGPSSEITIPGGVRTIDASGLMIIPGGIDPHTHMQLPFGGAVAVDDFYHGTKAAVAGGTTMIIDFVLPNKHESMIEAYDKWRSWADPKVCCDYGLHVGITWWSKSVSEEIGILCKELGVNSFKTFMAYEGLYQLNDSDLLDVFERIRHLNGVAMVHAENGDIIAKNTQRLLAEGINGPEGHELSRPEEVEAEAVHRACVLAHQVRPLPCRQTVGDGWEEGGRRRRSVSMPVECHCALCRAL
Protein: Methylglyoxal synthase (MGS) (EC 4.2.3.3) (P42980)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Interaction partners:
- N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1
- N-acetyl-alpha-D-glucosaminyl L-malate synthase
- CCA-adding enzyme
- 4-hydroxy-tetrahydrodipicolinate reductase
- Uncharacterized protein YpjD
- Bifunctional ligase/repressor BirA
- Glyoxal reductase
- Uncharacterized oxidoreductase YtbE
- L-lactate dehydrogenase
- Diacylglycerol kinase
Sequence:
MKIALIAHDKKKQDMVQFTTAYRDILKNHDLYATGTTGLKIHEATGLQIERFQSGPLGGDQQIGALIAANALDLVIFLRDPLTAQPHEPDVSALIRLCDVYSIPLATNMGTAEILVRTLDEGVFEFRDLLRGEEPNV
Protein: Iron-sulfur cluster assembly protein (Q389E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTNTVKHSMARLRAKMLGAAKMFPDYNFRHYFVQHVKDQFVAMEKWGVEEQRRFLRQEGAKKLSEMRRMALVNRMYSSQPVFLDERAASKPSVTQEEEE
Protein: Peptide encoded by miPEP319a (P0DKJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory peptide encoded by the primary transcript (pri-miR319a) of the microRNA miR319a that enhances the accumulation of its corresponding mature miRNA. Acts probably as a transcriptional activator of its corresponding pri-miRNA.
Interaction partners:
Sequence:
MNIHTYHHLLFPSLVFHQSSDVPNALSLHIHTYEYIIVVIDPFRITLAFR
Protein: AP-1 complex subunit gamma (Q9W388)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MNSEHGFNPAFNMATIRQAFTEAVERVRMPTPTRLRDLIRQIRAARTAAEERAVVNKECAYIRSTFREEDSVWRCRNIAKLLYIHMLGYPAHFGQLECLKLTASTRFTDKRIGYLGAMLLLDERQDVHLLITNCLKNDLNSSTQFVVGLALCTLGAIASPEMARDLASEVERLMKSPNTYIRKKATLCAFRVIRRVPELMEIFLPATRSLLSEKNHGILITGVTLITEMCENSSDTLMHFKKIVPNLVRILKNLILGGYSPEHDVSGVSDPFLQVKILRLLRILGHNDPDASEAMNDILAQVATNTETSKNVGNTILYETVLSIMDIRSEGGLRVLAVNILGRFLLNSDKNIRYVALNTLLRTVHADTSAVQRHRTTILECLKDPDVSIRRRAMELSFALINAQNIRTMTKELLLFLEKADAEFKAQCSSGMILAAERYSPTTRWHLDTQLSVLIAAGNYVRDDVVSSTIQLVSSSPVPEQTYITNRFWESLQVANHCEDKQPLLQVAVWAIGEYGDLFMYGANEDEFERPTESDLIAVYYKFLTSAQVSTTSKQYALVSLAKLSTRLQQCVEEIQALITSFGSHLNVDLQQRGVEFTQLFGHYKHLRPPLLEKMPAMQISRISSQNGESGGGSFDDNSPDVIENGVEGGGGGGHSLIESNMNTLGDNTNILLDLLGSTDLSAGGAGDLVAATDLSNAVHKKNSRNANDVVAPVSNNQDLLDLLDLDLSAPSSTTTGAPAGGGGGGGIVALVGDNNQSSAANMNNMLGGLDLGGFGSGLDSSASIPTNGNDLASMLGGLGAPPAASPSLAASAPVGNLIDGHAGSLLADLNPTAASNNVVVPPQGPRLTALDKDGLLVQLVSVRGSDCMRIYMTTTNNSDNTLDQYLLQAAVQRSFQLQMLTPSGSVLPPGGVITQEMRVVATSNATLRMRLRIQYVLDGQQQVEQTEVSGFPEQQPAPAAAE
Protein: Tabersonine/lochnericine 19-hydroxylase (EC 1.14.14.-) (Cytochrome P450 71BJ1) (F5BHA2)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications. Cytochrome P450 catalyzing the conversion of (-)-tabersonine to 19-hydroxytabersonine, of lochnericine to horhammericine and of (-)-vincadifformine to (-)-minovincinine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29438577}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLSSLKDFFVLLLPFFIGIAFIYKLWNFTSKKNLPPSPRRLPIIGNLHQLSKFPQRSLRTLSEKYGPVMLLHFGSKPVLVISSAEAAKEVMKINDVSFADRPKWYAAGRVLYEFKDMTFSPYGEYWRQARSICVLQLLSNKRVQSFKGIREEEIRAMLEKINQASNNSSIINGDEIFSTLTNDIIGRSAFGRKFSEEESGSKLRKVLQDLPPLLGSFNVGDFIPWLSWVNYLNGFEKKLNQVSKDCDQYLEQVIDDTRKRDEENGANNNGGNHGNFVSVLLHLQKEDVKGFPSEKGFLKAIILDMIVGGTDTTHLLLHWVITELLKNKHVMTKLQKEVREIVGRKWEITDEDKEKMKYLHAVIKEALRLHPSLPLLVPRVAREDINLMGYRVAKGTEVIINAWAIARDPSYWDEAEEFKPERFLSNNFDFKGLNFEYIPFGSGRRSCPGSSFAIPIVEHTVAHLMHKFNIELPNGVSAEDFDPTDAVGLVSHDQNPLSFVATPVTIF
Protein: Lysozyme C-1 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Lysozyme C type P) (P17897)
Organism: Mus musculus (Mouse)
Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz1 is active against a range of Gram-positive and Gram-negative bacteria. Less effective than Lyz2 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.
Subcellular location: Secreted.
Interaction partners:
- Lysozyme C-2
Sequence:
MKALLTLGLLLLSVTAQAKVYNRCELARILKRNGMDGYRGVKLADWVCLAQHESNYNTRATNYNRGDRSTDYGIFQINSRYWCNDGKTPRSKNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRTQCQNRDLSQYIRNCGV
Protein: Homocitrate synthase AksA (EC 2.3.3.14) ((R)-homo(2)citrate synthase) (EC 2.3.3.-) ((R)-homo(3)citrate synthase) (EC 2.3.3.-) (Q57926)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.
Interaction partners:
- Homoisocitrate dehydrogenase
- Methanogen homoaconitase large subunit
- Methanogen homoaconitase small subunit
- Acetyl-CoA acetyltransferase
- 2-oxoglutarate synthase subunit KorA
- Pyruvate synthase subunit PorA
- 2-oxoglutarate synthase subunit KorB
- Pyruvate synthase subunit PorB
- Pyruvate synthase subunit PorC
- Acetate--CoA ligase
Sequence:
MTKVLVMFMDFLFENSWKAVCPYNPKLDLKDIYIYDTTLRDGEQTPGVCFTKEQKLEIARKLDELGLKQIEAGFPIVSEREADIVKTIANEGLNADILALCRALKKDIDKAIECDVDGIITFIATSPLHLKYKFNNKSLDEILEMGVEAVEYAKEHGLFVAFSAEDATRTPIEDLIKVHKAAEEAGADRVHIADTTGCATPQSMEFICKTLKENLKKAHIGVHCHNDFGFAVINSIYGLIGGAKAVSTTVNGIGERAGNAALEELIMALTVLYDVDLGLNLEVLPELCRMVEEYSGIKMPKNKPIVGELVFAHESGIHVDAVIENPLTYEPFLPEKIGLKRNILLGKHSGCRAVAYKLKLMGIDYDREMLCEIVKKVKEIREEGKFITDEVFKEIVEEVLRKRNKN
Protein: Tetraspanin (Q9V3X2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MGLNGCCSCVKYLMVLINILFWLIGLTIVVTSVWMLTDPTFMLSMTQNYNHYHIALYVFLAIGILITLGAFFGCCGVCRESQCLLVSFFCVILIVMVAQIAAGAWAFHNKDKLDDIVRAAVKSSVQEEYGQSTMSSRTVTFDTLQKNLKCCGADGPGDWATSRFNNVDRTNIVEIAVSSMNVFYNIPESCCKDNLKDNECELSRRLKFGGPLNNAIYQQGCVDKLIEIIYENWVTIFAVTAAVILLELLSLTFALSLCCAVRNQHYKA
Protein: CMRF35-like molecule 6 (CLM-6) (CD300 antigen-like family member C) (CMRF35-A1) (CMRF-35) (Immunoglobulin superfamily member 16) (IgSF16) (CD antigen CD300c) (Q08708)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Sequestosome-1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA type A receptor associated protein like 1
- Microtubule-associated protein 1 light chain 3 beta
- Leukocyte immunoglobulin-like receptor subfamily A member 2
- Leukocyte immunoglobulin-like receptor subfamily B member 1
- CMRF35-like molecule 7
- Next to BRCA1 gene 1 protein
- Microtubule-associated protein 1A
Sequence:
MTARAWASWRSSALLLLLVPGYFPLSHPMTVAGPVGGSLSVQCRYEKEHRTLNKFWCRPPQILRCDKIVETKGSAGKRNGRVSIRDSPANLSFTVTLENLTEEDAGTYWCGVDTPWLRDFHDPIVEVEVSVFPAGTTTASSPQSSMGTSGPPTKLPVHTWPSVTRKDSPEPSPHPGSLFSNVRFLLLVLLELPLLLSMLGAVLWVNRPQRSSRSRQNWPKGENQ
Protein: Transcriptional regulatory protein DOT6 (Disrupter of telomere silencing protein 6) (PAC-binding factor 2) (P40059)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RPD3 histone deacetylase complex RPD3C(L) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. DOT6 binds to sequences containing the core CGATG, which resembles the PAC (Polymerase A and C) motif.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein STB3
- Transcriptional regulatory protein RXT3
- Histone deacetylase RPD3
- Histone deacetylase complex subunit CTI6
- Transcriptional regulatory protein TOD6
- Serine/threonine-protein kinase SCH9
- Transcription factor SFP1
- Transcriptional regulatory protein UME6
- Transcriptional regulatory protein SIN3
- Transcriptional regulatory protein SDS3
Sequence:
MSISTSLNSASIHLSSMDTHPQLHSLTRQPHSSSTAMSKNEAQESSPSLPASSSSSTSASASASSKNSSKNPSSWDPQDDLLLRHLKEVKKMGWKDISQYFPNRTPNACQFRWRRLKSGNLKSNKTALIDINTYTGPLKITHGDETANAQQKPSKKVEENVLTEDTAEFTTTSSIPIPSRKTSLPSFHASMSFSQSPSNVTPTTIVSNAASSMPFAPPTLPAALPHHPHQHLHHHPHHKTLKPRSNSHSFTNSLNQDPIVRSNDEEKYGFIPKVFVRSRRSSFAYPQQVAITTTPSSPNSSHVLLSSKSRRGSLANWSRRSSFNVSSNNTSRRSSMILAPNSVSNIFNVNNSGSNTASTSNTNSRRESVIKKEFQQRLNNLSNSGGPTSNNGPIFPNSYTFMDLPHSSSVSSSSTLHKSKRGSFSGHSMKSSCNPTNLWSKDEDALLMENKKRNLSVMELSILLPQRTEVEIQWRLNALSSDADMLSPTHSPQKTLSKKTCPRMFKSGSTTDDDKGSDKEDVMGDGSNDDDEDNVDPLHRAKQSSNKTVFSSSSSNISSKDVSPDPIFSPDPADDSSNTSDAGSRCTITSDTSSSAATMNRTPNSKNPQDIALLNNFRSEAITPRPKPSSTTTSITTETTNNMINHSSSTTTTTNNSPLPSINTIFKDML
Protein: Nucleolar protein 6 (Nucleolar RNA-associated protein) (Nrap) (Q8R5K4)
Organism: Mus musculus (Mouse)
Function: Probably associated with rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11895476}. Chromosome {ECO:0000269|PubMed:11895476}. Note=Localizes to condensed chromosomes in mitosis. {ECO:0000269|PubMed:11895476}.
Interaction partners:
- Nucleolar protein 10
- U3 small nucleolar RNA-associated protein 6 homolog
- Ribosomal RNA-processing protein 7 homolog A
- WD repeat domain 36
- U3 small nucleolar RNA-associated protein 4 homolog
- Periodic tryptophan protein 2 homolog
- HEAT repeat-containing protein 1
- Nucleolar protein 14
- Transducin beta-like protein 3
- U3 small nucleolar ribonucleoprotein protein MPP10
Sequence:
MPSAGERPAVKMGPAPAGEQHRRATEDPEVMELAFEGMDKEKAPSRKRARTEPPAEGLLQPVNLSREELYKEPTNEELNRLRETEILFHSTLLRLQVEELLKEVRLSEKKKERIDNFLKEVTKRIQKVPPVPEAELTDQSWLPAGVRVPLHQVPYAVKGSFRFRPPSQITVVGSYLLDTCMRPDINVDVAVTMPREILQDKDGLNQRYFRKRALYLAHLAYHLAQDPLFSSVRFSYMSGCHLKPSLLLRPHGKDERLVTVRLLPCPPLDFFRPCRLLPTKNNVRSAWYRGQSCPDYEPPTPHYNTWILQDVALETHMHLLASVLGSAQGLKDGVALLKVWLRQRELDKGLGGFNGFIISMLVAFLVSKRKIHTTMSGYQVLRSVLQFLATTDLTINGISFSLSSDPSLPTLAEFHQLFAVVFVDPSGRLNLCADVTASTYNQVQYEAELSMALLDSKADDGFQLLLMTPKPMIQAFDHVVHLHPLSRLQASCHQLKLWPELQDNGGDYVSAALGPLTNILVQGLGCRLHLLAHSRPPVPEWSINQDPPKHKDAGTLTLGFLFRPEGLTSVIDLGPEADKPEAADFRQFWGTRSELRRFQDGAIREAVVWEAESLFEKRLIPHQVVTHLLALHADIPDTCIQYVGGFLDALIQNPKEISSTGEEALALAVRCYDDLSRLLWGLEGLPLTVSAVQGAHPVLRYTEVFPPAPVRPAYSFYNRLQELASLLPRPDKPCPAYVEPMTVVCHLEGSGQWPQDAEAVQRVRAAFQLRLAEVLTQEHRLQCCATATHTDVLKDGFVFRIRVAYQREPQILKEVRSPEGMVSLRDTPASLRLERDTKLLPLLTSALHGLQQQYPAYSGVARLAKRWVRAQLLGEGFTDESLDLLAASLFLHPEPFTPPSVPQVGFLRFLYLVSTFDWKNNPLIVNLNGELTAEEQVGIRSSFLAARTQLPVMVIITPQDRRSSVWTQDGPSAQILQQLVSLAAEALPILEKQLMDPRGPGDIRTVFRPPFDMYDVLIHLTPRHIPRHRQAVDPPVASFCRGLLAEPGPSSLMPVLGYDPPQLYLAQLREAFEDLALFFYDQHGGEVIGVLWKPSSFQPQPFKASSIKGRMVVSQGGELVMLPNIEAILEDFAVLGEGLVQAVEARSERWTV
Protein: Nucleic acid binding protein 2 (C9JT95)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAAS
Protein: KH domain-containing protein At2g38610 (Quaking-like protein 3) (Q9ZVI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At2g30880/F7F1.9
Sequence:
MSGLYNNSSYFSPARAASPQIRSTPEIDSSQYLTELLAEHQKLTPFMQVLPICSRLLNQEMFRVSGMMSNQGFGDFDRLRHRSPSPMASSNLMSNVSNTGLGGWNGLSQERLSGTPGMTMDWQGAPGSPSSYTVKRILRLEIPVDNYPNFNFVGRLLGPRGNSLKRVEATTGCRVFIRGKGSIKDPEKEDKLRGRPGYEHLNEQLHILIEADLPASIVEIRLRQAQEIIEELLKPVDESQDFIKRQQLRELALLNSNNLREESPGPSGGGSVSPFNSSGKRPKTGC
Protein: Thrombospondin type I repeat-containing single pass transmembrane protein (M5FK96)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MIVMVLFNIFVFVNFSYSLANLNDSSILYSQVVSNKCASNNGIFCECSKQGGEIKIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW
Protein: Putative Polycomb group protein ASXL3 (Additional sex combs-like protein 3) (Q9C0F0)
Organism: Homo sapiens (Human)
Function: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Histone-lysine N-methyltransferase EZH2
- Putative Polycomb group protein ASXL2
- Bromodomain-containing protein 4
- Polycomb group protein ASXL1
- E3 ubiquitin-protein ligase RING2
Sequence:
MKDKRKKKDRTWAEAARLALEKHPNSPMTAKQILEVIQKEGLKETSGTSPLACLNAMLHTNTRIGDGTFFKIPGKSGLYALKKEESSCPADGTLDLVCESELDGTDMAEANAHGEENGVCSKQVTDEASSTRDSSLTNTAVQSKLVSSFQQHTKKALKQALRQQQKRRNGVSMMVNKTVPRVVLTPLKVSDEQSDSPSGSESKNGEADSSDKEMKHGQKSPTGKQTSQHLKRLKKSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDGILRLSTSALNNEFFAYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEKKTEPWKEKFFERFYGEKLGMSREESVKLTTGPNNAGAQSSSSCGTSGLPVSAQTALAEQQPKSMKSPASPEPGFCATLCPMVEIPPKDIMAELESEDILIPEESVIQEEIAEEVETSICECQDENHKTIPEFSEEAESLTNSHEEPQIAPPEDNLESCVMMNDVLETLPHIEVKIEGKSESPQEEMTVVIDQLEVCDSLIPSTSSMTHVSDTEHKESETAVETSTPKIKTGSSSLEGQFPNEGIAIDMELQSDPEEQLSENACISETSFSSESPEGACTSLPSPGGETQSTSEESCTPASLETTFCSEVSSTENTDKYNQRNSTDENFHASLMSEISPISTSPEISEASLMSNLPLTSEASPVSNLPLTSETSPMSDLPLTSETSSVSSMLLTSETTFVSSLPLPSETSPISNSSINERMAHQQRKSPSVSEEPLSPQKDESSATAKPLGENLTSQQKNLSNTPEPIIMSSSSIAPEAFPSEDLHNKTLSQQTCKSHVDTEKPYPASIPELASTEMIKVKNHSVLQRTEKKVLPSPLELSVFSEGTDNKGNELPSAKLQDKQYISSVDKAPFSEGSRNKTHKQGSTQSRLETSHTSKSSEPSKSPDGIRNESRDSEISKRKTAEQHSFGICKEKRARIEDDQSTRNISSSSPPEKEQPPREEPRVPPLKIQLSKIGPPFIIKSQPVSKPESRASTSTSVSGGRNTGARTLADIKARAQQARAQREAAAAAAVAAAASIVSGAMGSPGEGGKTRTLAHIKEQTKAKLFAKHQARAHLFQTSKETRLPPPLSSKEGPPNLEVSSTPETKMEGSTGVIIVNPNCRSPSNKSAHLRETTTVLQQSLNPSKLPETATDLSVHSSDENIPVSHLSEKIVSSTSSENSSVPMLFNKNSVPVSVCSTAISGAIKEHPFVSSVDKSSVLMSVDSANTTISACNISMLKTIQGTDTPCIAIIPKCIESTPISATTEGSSISSSMDDKQLLISSSSASNLVSTQYTSVPTPSIGNNLPNLSTSSVLIPPMGINNRFPSEKIAIPGSEEQATVSMGTTVRAALSCSDSVAVTDSLVAHPTVAMFTGNMLTINSYDSPPKLSAESLDKNSGPRNRADNSGKPQQPPGGFAPAAINRSIPCKVIVDHSTTLTSSLSLTVSVESSEASLDLQGRPVRTEASVQPVACPQVSVISRPEPVANEGIDHSSTFIAASAAKQDSKTLPATCTSLRELPLVPDKLNEPTAPSHNFAEQARGPAPFKSEADTTCSNQYNPSNRICWNDDGMRSTGQPLVTHSGSSKQKEYLEQSCPKAIKTEHANYLNVSELHPRNLVTNVALPVKSELHEADKGFRMDTEDFPGPELPPPAAEGASSVQQTQNMKASTSSPMEEAISLATDALKRVPGAGSSGCRLSSVEANNPLVTQLLQGNLPLEKVLPQPRLGAKLEINRLPLPLQTTSVGKTAPERNVEIPPSSPNPDGKGYLAGTLAPLQMRKRENHPKKRVARTVGEHTQVKCEPGKLLVEPDVKGVPCVISSGISQLGHSQPFKQEWLNKHSMQNRIVHSPEVKQQKRLLPSCSFQQNLFHVDKNGGFHTDAGTSHRQQFYQMPVAARGPIPTAALLQASSKTPVGCNAFAFNRHLEQKGLGEVSLSSAPHQLRLANMLSPNMPMKEGDEVGGTAHTMPNKALVHPPPPPPPPPPPPLALPPPPPPPPPLPPPLPNAEVPSDQKQPPVTMETTKRLSWPQSTGICSNIKSEPLSFEEGLSSSCELGMKQVSYDQNEMKEQLKAFALKSADFSSYLLSEPQKPFTQLAAQKMQVQQQQQLCGNYPTIHFGSTSFKRAASAIEKSIGILGSGSNPATGLSGQNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLVVR