wanglab/gogpt-training-data huggingface dataset:
Protein: Protein PAIR1 (Protein HOMOLOGOUS PAIRING ABERRATION IN RICE MEIOSIS 1) (Q75RY2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in spore formation. Plays an essential role in the establishment of homologous chromosome pairing in early meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15031413}.
Interaction partners:
- Meiotic recombination protein SPO11-1
- Pachytene checkpoint protein 2 homolog
Sequence:
MKLKMNKACDIASISVLPPRRTGGSSGASASGSVAVAVASQPRSQPLSQSQQSFSQGASASLLHSQSQFSQVSLDDNLLTLLPSPTRDQRFGLHDDSSKRMSSLPASSASCAREESQLQLAKLPSNPVHRWNPSIADTRSGQVTNEDVERKFQHLASSVHKMGMVVDSVQSDVMQLNRAMKEASLDSGSIRQKIAVLESSLQQILKGQDDLKALFGSSTKHNPDQTSVLNSLGSKLNEISSTLATLQTQMQARQLQGDQTTVLNSNASKSNEISSTLATLQTQMQADIRQLRCDVFRVFTKEMEGVVRAIRSVNSRPAAMQMMADQSYQVPVSNGWTQINQTPVAAGRSPMNRAPVAAGRSRMNQLPETKVLSAHLVYPAKVTDLKPKVEQGKVKAAPQKPFASSYYRVAPKQEEVAIRKVNIQVPAKKAPVSIIIESDDDSEGRASCVILKTETGSKEWKVTKQGTEEGLEILRRARKRRRREMQSIVLAS
Protein: Mitochondrial RNA binding complex 1 subunit (Q57Y19)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYRLYRRTVGYQTLHQRLSACHVMCRHVSTDNSDGTTPPKPRRSGIRRVVPSDEEMAELHDLEQEVASTTSSRSKQSALSGVMVEPMRFSTSGDSGMEGDGDDLGELEAEGDEEGVGTNSLAEAENVYKRHNDGGALEKRGLAIPPSGKPTDPLLANRDDEGEGGAVPLSQAEEMTVSRSTLERQACVRSLSLEELVEAVTLYLRATKNPRLVSADEEHIFFPVLMERLNEFHVSQLLDVVECHWARSTLVRYGTTFKDMVRDRIALIATAAAKSASKRPAAAGESGNDNRDGGAVEEEADDYDEQGGAVYVHEAEEKTSDLIILRAAEEMSPETVLRCIIVMGMSAGRRKRDLQFFQAMGMFLVHHINHYKDPHELVRVLTAFARAKIVPPKRFLALLGRRFAVLNKRKKLGSLPSYRASVNLYKMGHDQMNTFRFLADCILETIDSNIKAEKKRLRLAQLQGSSNITAATTNENGATNESGCGGSTSSSNPTVTNTTGAGDLKATHTSEGASDVAFIGDLDPHLLQNLRARERFKRLTELKPSMFTKLLLVLARFGAPHQQYLRPTTVPLILPTLRAFPPPSFTRLLRAMSLFRTTDLDLIEPVIDFMADSLGPTNVVPADVLQMVRLVAPPDVPVPRNLVKLISLCEAVYSSSASFSHSDGKSSDSADAAACAMTTLSPIRPGDMCAVAVVLLKIQMKDDVPLEALDPLTRLMEFFAERMYLLMKLHIVSLTHVDVFTDLCRQQQHPDVSGHIERLCAERRRVNDAEGDDEYYSQLDIDVRETLHRILIVNDYNTYGQYRPTPGVLQVDFKQALTEVSAFDVLEAADLFAQAFSNALKPAVERHLSRSIIAKLDGGGEEVITEGNSIVLRPPRELLLTREDLGKFVCLLQRTPLRRVRASPVVWRFVEEKAKKLGMDDVLRVVENKLATAV
Protein: PTS system glucose-specific EIICB component (EIICB-Glc) (EII-Glc) [Includes: Glucose permease IIC component (PTS system glucose-specific EIIC component); Glucose-specific phosphotransferase enzyme IIB component (EC 2.7.1.199) (PTS system glucose-specific EIIB component)] (P69786)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:3129430}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000305|PubMed:15919996}.
Interaction partners:
- PTS system glucose-specific EIIA component
- DNA-binding transcriptional repressor Mlc
- Phosphocarrier protein HPr
- Glucokinase
- Glucose-6-phosphate isomerase
- Phosphoenolpyruvate-protein phosphotransferase
- PTS system beta-glucoside-specific EIIBCA component
- Glucose-6-phosphate 1-dehydrogenase
- PTS system maltose-specific EIICB component
- PTS system fructose-specific EIIB'BC component
Sequence:
MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMPLIFAIGVALGFTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIASKHLADTGVLGGIISGAIAAYMFNRFYRIKLPEYLGFFAGKRFVPIISGLAAIFTGVVLSFIWPPIGSAIQTFSQWAAYQNPVVAFGIYGFIERCLVPFGLHHIWNVPFQMQIGEYTNAAGQVFHGDIPRYMAGDPTAGKLSGGFLFKMYGLPAAAIAIWHSAKPENRAKVGGIMISAALTSFLTGITEPIEFSFMFVAPILYIIHAILAGLAFPICILLGMRDGTSFSHGLIDFIVLSGNSSKLWLFPIVGIGYAIVYYTIFRVLIKALDLKTPGREDATEDAKATGTSEMAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNH
Protein: Phospholipase A1-Ialpha2, chloroplastic (EC 3.1.1.-) (DAD1-like lipase 5) (Q9SIN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Has a strong galactolipase activity toward monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG). Low triacylglycerol (TAG) lipase activity. Plays a role in plant growth and in leaf senescence.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:17259290, ECO:0000269|PubMed:19527719}.
Interaction partners:
Sequence:
MALIQNPNMKHAPFLRNRSPQQTLFIPYTLSLPISYQNPKRLKTANSSSSSSLLAPVILNSPVASSSPPPIYCAPKFPCSSGAATVPLSRVWREIQGCNNWKDLIEPLNPLLQQEITRYGNLVSTCYKAFDLDPNSKRYLNCKYGKQTLLKETEIDQPEDYQVTKYIYATPDININISPIQNEMNRRARWVGYVAASSDDSVKRLGRRDIVVTFRGTVTNPEWLANFMSSLTPARFHPHNPRLDVKVESGFLSLYTSDESESKFGLESCRQQLLSEISRLMNKYKGEEMSITLAGHSMGSSLAQLLAYDIAELGLNRRIGKGDIPVTVFSFAGPRVGNLEFKKRCEELGVKVLRITNVNDPVTKLPGVLFNENFRVLGGFYELPWSCSCYVHVGVELTLDFFDVQNISCVHDLQTYIDLLNQRRTNSRSVDSDEDEDSDNVALEFLKTNGEKMMFLKRQRMMYWSNAVDLLFSFSNHMSYCNIF
Protein: Glucan endo-1,3-beta-glucosidase 4 (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase 4) ((1->3)-beta-glucanase 4) (Beta-1,3-endoglucanase 4) (Beta-1,3-glucanase 4) (Q94CD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- alpha-D-xyloside xylohydrolase
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase MMS21
- Beta-glucosidase 31
- Non-structural maintenance of chromosomes element 4 homolog B
- Non-structural maintenance of chromosomes element 4 homolog A
- Structural maintenance of chromosomes protein 6A
- Structural maintenance of chromosomes protein 6B
- Probable pectate lyase 12
Sequence:
MLLPRWFAEALLLLLSILACSNAAFIGVNIGTDLTNMPPPSDIVTLLKSQQITHVRLYDANSHMLKAFANTSIEVMVGVTNEEILKIGRFPSAAAAWVNKNVAAYIPSTNITAIAVGSEVLTTIPHVAPILASALNNIHKALVASNLNFKVKVSSPMSMDIMPKPFPPSTSTFSPSWNTTVYQLLQFLKNTGSFFMLNAYPYYGYTTANGIFPLDYALFKQLSPVKQIVDPNTLLHYNSMFDAMVDAAYYSMEALNFSKIPVVVTETGWPSSGGSDEAAATVANAETFNTNLIKRVLNNSGPPSQPDIPINTYIYELYNEDKRSGPVSERNWGILFPNGTSVYPLSLSGGSSSAALNGSSMFCVAKADADDDKLVDGLNWACGQGRANCAAIQPGQPCYLPNDVKSHASFAFNDYYQKMKSAGGTCDFDGTAITTTRDPSYRTCAYTGSLNANATNGNFPPDALGPASPLGGNANARIIFSYHLPILAPLALTLLQLLLQHDRLL
Protein: Lipoprotein-releasing system ATP-binding protein LolD (EC 7.6.2.-) (Q9HZL7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01708}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01708}.
Interaction partners:
- Lipoprotein-releasing ABC transporter permease subunit
- Lipoprotein-releasing ABC transporter permease subunit
- Outer-membrane lipoprotein carrier protein
- Outer-membrane lipoprotein LolB
- Probable permease of ABC transporter
- Outer membrane lipoprotein Blc
- Small ribosomal subunit protein uS11
Sequence:
MNDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIAA
Protein: Long-chain N-acyl amino acid synthase (Q8KNZ7)
Organism: uncultured bacterium CSLC2
Interaction partners:
Sequence:
MTPRKVARILVAPNERDAARRIVRTTYEAQGYAIDESFATFLEGPSATTFGLFNGEVLYGTISIINDGAQGLPMDSIYAVELAAWRGEGKKLAEVVQFAMDHTLYEAVAGAKPSPFEAASLFTMVLTYALETHIDYLCISINPKHDTFYSLLGFTQIGALKHYGTVNAPAIARALYVPEWRSQTLLAQFMDAERSH
Protein: Ribosomal protein S4 (Q2F8W8)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MPALRFKTCRLLPGNVRNRELSLIQRRILRRLRNKRRSIKRNLSQRENLNSNIKSQTTRKLSLYYGDLPIREMHRGRERTSYIPFLLNQETRSDVIPVRLHFCDTLPQARQPISHRRVCLNNGLVTITHLKVSHGDLISFQENDARTRGEEIRRSFYIDISVGKIIGKLLPVRIWRKTKTEWFRLLTTQRVCRLLLKSWFLQELRSYMQEEDLERTKKFGSAKVCLGSSFAEHNRMKRNLFHFKYFFLLKRRKEEEELIRTIGEAENRKRAISPFVYKSSLYRNSTYCSGSPFTRKIRIKRIELPTHYSEVNHRTLKAVVSYGPNIGHIPHDIRLKDPNLPLRSGNGRGQNI
Protein: Telomeric repeat-binding factor 2 (TTAGGG repeat-binding factor 2) (Telomeric DNA-binding protein) (Q15554)
Organism: Homo sapiens (Human)
Function: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20655466}. Chromosome, telomere {ECO:0000269|PubMed:20655466}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. {ECO:0000269|PubMed:20655466}.
Interaction partners:
- Protection of telomeres protein 1
- Telomeric repeat-binding factor 2-interacting protein 1
- Adrenocortical dysplasia protein homolog
- 5' exonuclease Apollo
- TERF1-interacting nuclear factor 2
- Telomeric repeat-binding factor 1
- Structure-specific endonuclease subunit SLX4
- Nibrin
- X-ray repair cross-complementing protein 6
- Double-strand break repair protein MRE11
Sequence:
MAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLNSSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDEDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLGMN
Protein: Rab11 family-interacting protein 4 (FIP4-Rab11) (Rab11-FIP4) (Arfophilin-2) (Q86YS3)
Organism: Homo sapiens (Human)
Function: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. In case of infection by HCMV (human cytomegalovirus), may participate in egress of the virus out of nucleus; this function is independent of ARF6.
Subcellular location: Endosome {ECO:0000269|PubMed:20682791}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12857874}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12857874}. Recycling endosome membrane {ECO:0000269|PubMed:15601896}; Peripheral membrane protein. Cleavage furrow {ECO:0000269|PubMed:15601896}. Midbody {ECO:0000269|PubMed:12857874, ECO:0000269|PubMed:15601896}. Cytoplasmic vesicle {ECO:0000269|PubMed:15601896}. Note=Recruited to the cleavage furrow and the midbody during cytokinesis. {ECO:0000269|PubMed:15601896}.
Interaction partners:
- Ras-related protein Rab-11A
- Rab11 family-interacting protein 3
- Rab11 family-interacting protein 2
- Rab11 family-interacting protein 1
- ADP-ribosylation factor 6
- Rab11 family-interacting protein 5
- Ras-related protein Rab-25
- ADP-ribosylation factor 5
- Homeobox protein goosecoid
- Unconventional myosin-Id
Sequence:
MAGGAGWSGAPAALLRSVRRLREVFEVCGRDPDGFLRVERVAALGLRFGQGEEVEKLVKYLDPNDLGRINFKDFCRGVFAMKGCEELLKDVLSVESAGTLPCAPEIPDCVEQGSEVTGPTFADGELIPREPGFFPEDEEEAMTLAPPEGPQELYTDSPMESTQSLEGSVGSPAEKDGGLGGLFLPEDKSLVHTPSMTTSDLSTHSTTSLISNEEQFEDYGEGDDVDCAPSSPCPDDETRTNVYSDLGSSVSSSAGQTPRKMRHVYNSELLDVYCSQCCKKINLLNDLEARLKNLKANSPNRKISSTAFGRQLMHSSNFSSSNGSTEDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIKH
Protein: Geraniol synthase, chloroplastic (PcTps-C) (EC 3.1.7.11) (Q4JHG3)
Organism: Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into geraniol.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSISQKVVIGLNKAAANNNLQNLDRRGFKTRCVSSSKAASCLRASCSLQLDVKPVQEGRRSGNYQPSIWDFNYVQSLNTPYKEERYLTRHAELIVQVKPLLEKKMEPAQQLELIDDLNNLGLSYFFQDRIKQILSFIYDENQCFHSNINDQAEKRDLYFTALGFRLLRQHGFDVSQEVFDCFKNDNGSDFKASLSDNTKGLLQLYEASFLVREGEDTLEQARQFATKFLRRKLDEIDDNHLLSCIHHSLEIPLHWRIQRLEARWFLDAYATRHDMNPVILELAKLDFNIIQATHQEELKDVSRWWQNTRLAEKLPFVRDRLVESYFWAIALFEPHQYGYQRRVAAKIITLATSIDDVYDIYGTLDELQLFTDNFRRWDTESLGRLPYSMQLFYMVIHNFVSELAYEILKEKGFIVIPYLQRSWVDLAESFLKEANWYYSGYTPSLEEYIDNGSISIGAVAVLSQVYFTLANSIEKPKIESMYKYHHILRLSGLLVRLHDDLGTSLFEKKRGDVPKAVEICMKERNVTEEEAEEHVKYLIREAWKEMNTATTAAGCPFMDELNVAAANLGRAAQFVYLDGDGHGVQHSKIHQQMGGLMFEPYV
Protein: E3 ubiquitin-protein ligase RNF114 (EC 2.3.2.27) (RING finger protein 114) (RING-type E3 ubiquitin transferase RNF114) (Zinc finger protein 228) (Zinc finger protein 313) (Q9Y508)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates. In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity. Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3. May promote the ubiquitination of TRAF6 as well. Acts also as a negative regulator of T-cell activation. Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C. This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23645206}. Nucleus {ECO:0000269|PubMed:23645206}.
Interaction partners:
- Ubiquilin-4
- Protein mono-ADP-ribosyltransferase PARP11
- DDB1- and CUL4-associated factor 16
- XIAP-associated factor 1
- Ubiquitin-conjugating enzyme E2 D1
- Tumor necrosis factor alpha-induced protein 3
- Ubiquitin-conjugating enzyme E2 D2
- E3 ubiquitin-protein ligase RNF4
Sequence:
MAAQQRDCGGAAQLAGPAAEADPLGRFTCPVCLEVYEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSALAPGVRAVELERQIESTETSCHGCRKNFFLSKIRSHVATCSKYQNYIMEGVKATIKDASLQPRNVPNRYTFPCPYCPEKNFDQEGLVEHCKLFHSTDTKSVVCPICASMPWGDPNYRSANFREHIQRRHRFSYDTFVDYDVDEEDMMNQVLQRSIIDQ
Protein: Cysteine-rich receptor-like protein kinase 5 (Cysteine-rich RLK5) (EC 2.7.11.-) (Receptor-like protein kinase 6) (Q9C5S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in multiple distinct defense responses. May function as a disease resistance (R) protein.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSAYTSLNFLFLLTFFIGSLRVSAQLQDPTYVGHVCTNRISRNSIYFSNLQTLLTSLSSNNAYFSLGSHSLTKGQNSDMVFGLYLCKGDLSPESCRECVIFAAKDTRSRCPGGKEFLIQYDECMLGYSDRNIFMDTVTTTTIITWNTQKVTADQSDRFNDAVLSLMKKSAEEAANSTSKKFAVKKSDFSSSQSLYASVQCIPDLTSEDCVMCLQQSIKELYFNKVGGRFLVPSCNSRYEVYPFYKETIEGTVLPPPVSAPPLPLVSTPSFPPGKGKNSTVIIIAIVVPVAISVLICVAVFSFHASKRAKKTYDTPEEDDITTAGSLQFDFKVIEAATDKFSMCNKLGQGGFGQVYKGTLPNGVQVAVKRLSKTSGQGEKEFKNEVVVVAKLQHRNLVKLLGFCLEREEKILVYEFVSNKSLDYFLFDSRMQSQLDWTTRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLDADMNPKVADFGMARIFEIDQTEAHTRRVVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGRKNSSLYQMDASFGNLVTYTWRLWSDGSPLDLVDSSFRDSYQRNEIIRCIHIALLCVQEDTENRPTMSAIVQMLTTSSIALAVPQPPGFFFRSNHEQAGPSMDKSSLCSIDAASITILAPR
Protein: Histone H1.3 (H1 VAR.4) (H1d) (P43277)
Organism: Mus musculus (Mouse)
Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
Subcellular location: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}.
Interaction partners:
Sequence:
MSETAPAAPAAPAPVEKTPVKKKAKKTGAAAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKTAKKTPKKAKKPAAAAGAKKVSKSPKKVKAAKPKKAAKSPAKAKAPKAKASKPKASKPKATKAKKAAPRKK
Protein: Probable acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (Q86AD9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- 3-hydroxybutyryl-CoA dehydrogenase
- Hydroxymethylglutaryl-CoA synthase B
- Hydroxymethylglutaryl-CoA synthase A
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase, mitochondrial
- malate synthase
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-CoA carboxylase
- Probable short/branched chain specific acyl-CoA dehydrogenase
- Mevalonate kinase
- Citrate synthase, mitochondrial
Sequence:
MISNLSKVLNSNVKRMYTTAKNLESVVIVSAVRTPIGSIGGSLSTIPGTKLSSITIEEAVKRAGIKPSDVDEAIIGNVISANLGQAPARQCALGAGLEQKTITTTINKVCSSGMKAIVFGAQSIALGHSKTVVAGGFESMSQVPYYADKMRFGAKYGNQTFIDGLVRDGLADAYNGSAMGVCGDDCADKYKITREQQDKFAVDSYLRALEAQKNGFFNDEIVQVPIVGRGGKVTYVVEDEEPKKVLFDKIPNLKPAFTPNGTVTPANASKLNDGASSVILMSESHAKELGLKPLARIIGYADAEQAPIEFPTAPALAIPKALKNAGINMSQVDLFEINEAFAVVGLANAKILDIDHNKLNVNGGAVALGHPIGSSGCRIVVTLTHLLQNKNLKYGVAAICNGGGGSTALVLEKL
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (eIF-3 p48) (H0YBP5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus, PML body {ECO:0000256|HAMAP-Rule:MF_03004}.
Interaction partners:
Sequence:
MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPHMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Protein: Gap junction protein (A7VKB2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
Sequence:
MTEWTLLKRLLDAVHQHSTMIGRLWLTIMVIFRLLIVAVATEDVYTDEQEMFVCNTLQPGCPNVCYDAFAPISQPRFWVFQIITVSTPSLCFIIYTWHNLSKQPEGEQIKEALERSCDSESCSIKSHKHINPSLEGVTNQKPSQASKTSSGVLSKYYIFHVCFRTILEVAFVVAQWLLFGFRVPAHFVCTSSPCMQSVDCYVSRPTEKTVFLIFMFCVGVFCIFLNFLELNHLAWKMIKRSVLVKDGSWNGYGAINQDSQSIASLTFRDVTSTTSLPTLDLVVDHQPDWTCAANCSTKKDNRGTQSKPKTNRKAKQRSTEVWI
Protein: C4-dicarboxylic acid transporter DauA (Dicarboxylic acid uptake system A) (P0AFR2)
Organism: Escherichia coli (strain K12)
Function: Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH. Can transport other C4-dicarboxylic acids such as aspartate and fumarate. May also play a role in the regulation of C4-dicarboxylic acid metabolism at pH 7, via regulation of expression and/or activity of DctA. May act as a co-sensor of DcuS.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23278959}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Carbonic anhydrase 1
- Acyl carrier protein
- Carbonic anhydrase 2
- Putative ankyrin repeat protein YahD
Sequence:
MNKIFSSHVMPFRALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIGSGVAPQYGLYTAAVAGIVIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLLSGIFLILMGLARFGRLIEYIPVSVTLGFTSGIGITIGTMQIKDFLGLQMAHVPEHYLQKVGALFMALPTINVGDAAIGIVTLGILVFWPRLGIRLPGHLPALLAGCAVMGIVNLLGGHVATIGSQFHYVLADGSQGNGIPQLLPQLVLPWDLPNSEFTLTWDSIRTLLPAAFSMAMLGAIESLLCAVVLDGMTGTKHKANSELVGQGLGNIIAPFFGGITATAAIARSAANVRAGATSPISAVIHSILVILALLVLAPLLSWLPLSAMAALLLMVAWNMSEAHKVVDLLRHAPKDDIIVMLLCMSLTVLFDMVIAISVGIVLASLLFMRRIARMTRLAPVVVDVPDDVLVLRVIGPLFFAAAEGLFTDLESRLEGKRIVILKWDAVPVLDAGGLDAFQRFVKRLPEGCELRVCNVEFQPLRTMARAGIQPIPGRLAFFPNRRAAMADL
Protein: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (Q9W4N2)
Organism: Drosophila melanogaster (Fruit fly)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Positively regulates the Ago2-dependent small RNA pathway, with roles in both siRNA biogenesis and RISC assembly. Involved in facilitating conversion of pre-RISC into holo-RISC, possibly by promoting the unwinding of Ago2-bound siRNA duplexes and thus the retention of the guide strand in holo-RISC.
Subcellular location: Nucleus {ECO:0000269|PubMed:32504809}. Cytoplasm {ECO:0000269|PubMed:32504809}.
Interaction partners:
Sequence:
MDEPSDDENSEPTPKKIKREWVKSYSNKAMEMMKKMGYENDKGLGKSNQGRLEPIIAVQQDGRRGFGLKLDTVQSSAGQWDPACEELEIPEPVLWLHNPGSRADAYSLDQLMGHLVTGEKKLTLDGETRYCDPAILHHILNAKTVFDDLNDNEKRRARSRCNPFETIRSSIFLNRAAVKMANIDSMCNFMFTNPRDPAGQTLVAPDELLYFTDMCAGPGGFSEYVLYRKSWEAKGFGFTLRGANDFKLEKFFAASPESFDTFYGVKEDGNIFDESNQDSLNEYIRMHTPQGVHFAMADGGFSVEGQKNIQEILSKQLYLCQFLTALKILRPNGSFVCKVFDLFTPFSVGLVYLMYKCFQQIAIIKPNSSRPANSERYLVCKYKRSDAETAGIVAYLNTVNLMLSDESQLDENDVLEIFNANELAEDEDFLRYIIDSNNAIGKKQIVGLRKIAAFAQNLELKETKQSEVRQECLKRWGLPDKLRQAPENKPTDRLLDELLADWANERSWLSLPATEMKGVASLNATIKNVADWYFVPVGREETNINACSLFLCKSRGNLLRYTEHKKWELVETAFEVQPRSIFFGQIVYEFYGEGRTIQRMAALHIIDGICLGGVDIRRRPYRERVSMCDKFARSLNKPYRKDRTFGALRSKPLFRLQDMGSFFANMRHYVLKDNSQRLGFALDDNKFFVPGGIMMFCELTNNYVSAHSRSRGQLYYFNVRNKESYYKDQIPRNKADEIFASFRFSFSCRLLWKWTDLRQVEELATEDNPKILFRSDFVKFIADKLGHS