wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair protein RAD50 (EC 3.6.-.-) (Q9JIL8)
Organism: Rattus norvegicus (Rat)
Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.
Interaction partners:
- Double-strand break repair protein MRE11
- Nibrin
- Serine-protein kinase ATM
- DNA endonuclease RBBP8
- Serine/threonine-protein kinase ATR
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-associated RING domain protein 1
- X-ray repair cross-complementing protein 6
- DNA repair protein RAD52 homolog
- Flap endonuclease 1
Sequence:
MSRIEKMSTLGVRSFGIEDKDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGEMVLVQRSMLCSQKSKKTEFKTLEGVITRIKHGEKVSLSSKCAEIDREMISCLGVSKSVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQTELKYLRQNKEKACEIRDQITSKEAQLASSREIVKAYENELEPLKNRLKEIEHNLSKIMRLDNEIKALDSRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLSKEARLLNQERAELLVEQGRLQLQADRHQEHIRARDSLIQSLAAHLELDGFERGPFSERQIKNFHELVRERQEREAKTASQLLSDLTDKEALKQRQMDEMRDKKSGLGRMIELKTEILTKKQTELRNVRNELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETLKAEILNLQSEKADLDRNLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDFESDLDRLKEDIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPGCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPMRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTVMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQTVELSTEVQSLNREIKDAKEQINPLEIALEKLQQEKEELIHRKNTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNEVVIQLNECDKHKEKINKEMGTMRQDIDTKKIQERWLQDNLTLRKRREELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALGRQKGYEEEILHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDHAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRVKKNIDQCSEIVKSSINSLGSYVH
Protein: Uncharacterized protein C57A7.05 (P87136)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- SAGA complex subunit Spt3
- SAGA complex subunit Ngg1
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf10
- Uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02
- SAGA complex/NuA4 acetyltransferase complex subunit Tra1
- NuA4 acetyltransferase complex subunit Tra2
- SAGA complex subunit Ada2
Sequence:
MPTSGAPSNLDRANAQLSNTSSTESSSSNNSSTASGSRHVKIESNRVSLPPLKIQKGSFPAIRQPTESSTHFQSSHSVSNAHNQSPLNQSQSSANPVTFEIADEPSPSFNHSFFEKDNARDIPQQPSHSQNPSSSSSSSSSQSSQHSTHLQFQIPSNEKKSLDDPSPRRKPSFFSKSNLKRKYRYLKNPDAWNLPPSLQFIPKNLNRKGLKPVIRAAINSWIAFLLVLARHTNRVLGMSSFFVVITSILVPAMEPIAPMLWKTLFQFLLLFSAYAWTVLAAKLATVARGSPSREASLAQAVSEGFVCPDPSQGFNYCIREAVFQGYFVRPLPSIIWALFEFSAVALFIRLKMKYPPLNFPCVFSIICTAVSANMGPMYPYFYPRIGLFFIVPNCVQTGITIGCTLFILPETCNHAYNTMLCKLTEDTSSFLKRQTEMLSHSPASSHWASFSSLENEIANLKNLLSKMKSTELFLDMEFSYGRLKGEDLVSIQRIFKKTILRLSAFSYFQRLIDHNMQIYDDETIQKAGEATVSSWLNTPALSAASARTSSGRNSSESDRVSYFGLAPVNATTQDSERNGEEIRRLASKQLNVPVNNNFRTVGYASPSNASTASFNDIVQRGRSHVRTGSNNSEAPLAAKTSTTKRNGDLLEPQSPSLRSHKSRLHLPSSLGKFYKKRKKSYKPVGVLEAQQYLALESRLPFNKPQFLDSLLSILKNSSGDLFDQAIYSLDALNAWLVELNHDRIKKIFSKRDQKAAGRDRLKLIKLHYDHLSQALHEYEREKCFDVRKPYESLFQNQDVQQFYMHSLRSLFVVYYYESHLMQAVRGILQILETVIDLEERRPIRRLWWPLRSIRRSLLSQLTGHQGDYDENIHNDVDKDMNQSSTQPRDPDADHPSSLYHICGYRLTKFFKSIFRPMNVFVLKVGTLAVICTIPAFCRSSAGWYYRNRGLWAVILAIMSLQRFTADTVYGYLMRIFGTFFGAILGMVIWYTGSGHGLGNAYGLAAVWGAAIPFIQFIRVHFVILTPMPAVIFCVTAALTVTYSWKSNHEPGVVTLGIGWDVAYRRFLTVAAGITVAFIFSFLPQPRTAKYAVRKNIGNTLIDIGSIHCEISNFARRPVHNHIDPDIQSKVLNLSNTIQSLIGRLNMVNFEPSFKGRWPMEKYQLLCKTQLELVDLLNSLMTTITTLEDRWLFALLYRVGWLDHKFVADQLAVLYMSSNALQTGNPLPQVVPSPLVDRFFTTSGDVFLPPGLNDAPVPIPKAMEYELLNNMQYLNFAVGCTIAYAVVNHIDRIMFITKSLCGEIFEIDKWPFHFDDEYLYTCHPTNSPDQRKSPHDLV
Protein: Cytochrome c550 (Q9I2C5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Is an essential component of the ethanol oxidation system that allows P.aeruginosa to grow on ethanol as the sole carbon and energy source. Is the direct electron acceptor of the quinoprotein ethanol dehydrogenase (QEDH).
Subcellular location: Periplasm {ECO:0000269|PubMed:10075429}.
Interaction partners:
- Quinoprotein ethanol dehydrogenase
- Coenzyme PQQ synthesis protein B
- Glycerol metabolism activator
- Pyrroloquinoline-quinone synthase
- PqqA peptide cyclase
- GfdT protein
- NAD+ dependent aldehyde dehydrogenase ExaC
- histidine kinase
- Pentapeptide repeat-containing protein
- PqqA binding protein
Sequence:
MNKNNVLRGLLVLAGLSLSSLALAHGDVTPQAVDTKGLEPLGKEWRDTNPYRKPYAKHDLAVEIGASAYNQNCARCHGLEAKSGGIAPDLRLLETGAEGDEWFKERVINGAVRDGAVYMPKMADFISQEGLWAIRSYLESVHVDE
Protein: Calponin-homology (CH) domain-containing protein (Q8BJG0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MESISESSQQQRRKPVTHGLEDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQQQQQPEKQPLSSSPLPPAGSQVAGAPSQCQAGTPQHQGLATPQAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMSENVPAPLENSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEK
Protein: Aspartate-beta-hydroxylase (A0A0G2K2B5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
Sequence:
MAEDKEAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLEGPGGLAKRKTKAKGLKERSTSERTFPPEEAETQAELEEQAPEGAEAQNVEDEVKEQIQSLLQESVHTDHDLEADGPAGEPQSEVEDFLTATDSDDRFEALEPGTVHEDTEDSYHVEETASQNHPNDAEEVMSEQESSDHGEAVTDDGLQQHAEEVRHEDYDEPVYEPSENERIEISDNAIDDSNIISEEINVASVEEQQDTPPVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPRETGYTELVKSLERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCTLLEKFSETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Protein: N(2)-(2-carboxyethyl)arginine synthase (CEA synthetase) (CEAS) (EC 2.5.1.66) (Q9LCV9)
Organism: Streptomyces clavuligerus
Function: Involved in the biosynthesis of the beta-lactamase inhibitor, clavulanic acid. Catalyzes the thiamine diphosphate (ThDP) dependent condensation of D-glyceraldehyde-3-phosphate (D-G3P) with L-arginine to yield the beta-amino acid, N2-(2-carboxyethyl)arginine (CEA) via a beta-elimination resulting in the formation of an enol which undergoes a second elimination to generate the alpha,beta-unsaturated acryloyl-ThDP.
Interaction partners:
- Acetolactate synthase small subunit
- Carboxyethyl-arginine beta-lactam-synthase
- Ketol-acid reductoisomerase
- Dihydroxy-acid dehydratase
- Dihydroxy-acid dehydratase
- Proclavaminate amidinohydrolase
- Putative dehydrogenase
- 3-isopropylmalate dehydratase large subunit
Sequence:
MSRVSTAPSGKPTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTAGVAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSESHDIFPNDTHQCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEPVGPSFISLPVDLLGSSEGIDTTVPNPPANTPAKPVGVVADGWQKAADQAAALLAEAKHPVLVVGAAAIRSGAVPAIRALAERLNIPVITTYIAKGVLPVGHELNYGAVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAEDLRPSMWQKGIEKKTVRISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHDIEPLRARIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDIGFFRHYGVLFARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLIAGDGGFHSNSSDLETIARLNLPIVTVVVNNDTNGLIELYQNIGHHRSHDPAVKFGGVDFVALAEANGVDATRATNREELLAALRKGAELGRPFLIEVPVNYDFQPGGFGALSI
Protein: Tetraspanin-13 (Q9SI56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of cell differentiation.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- AP-5 complex subunit beta-like protein
- Peroxidase 6
- Protein TORNADO 1
- Tubby-like F-box protein 1
- GDSL esterase/lipase At2g19050
- Geranylgeranyl transferase type-2 subunit alpha 1
- Proline transporter 3
- B3 domain-containing transcription factor NGA3
- Alkylated DNA repair protein ALKBH8 homolog
- Tetraspanin-14
Sequence:
MARDKEDQNNENPSIVQNMSFPFNTIFLISSAIFLVTAAFWFVAVMTLHYRTDECNRFVTTPGIFISFSLLAMSLTGFYAAYFKSDCLFRIHFFIFFLWMFVVVSKAIFVIFLHKETNPRLFPGTKIYEFRYEDYSGWVSRLVIKDDEWYRTRRCLVKDNVCNRLNHKMPASEFYQMNLTPIQSGCCKPPLSCGLNYEKPNNWTVSRYYNNLEVDCKRWNNSADTLCFDCDSCKAVIIADVHNTSFSITVNIIHIIFSLCIGMTGWFAWLRILRESQK
Protein: D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein) (A0JPF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cytidylyltransferase required for protein O-linked mannosylation. Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively (By similarity). Not involved in dolichol production (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A4D126}.
Interaction partners:
- Fukutin.
- Transcription and mRNA export factor ENY2
- SFI1 centrin-binding protein.
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Beta-1,4-glucuronyltransferase 1
- Protein O-mannosyl-transferase 2
- DNA repair protein complementing XP-C cells
- Protein O-mannosyl-transferase 1
- Ribitol-5-phosphate transferase
- Protein O-mannose kinase
Sequence:
MGTVTIQLSCLRHIRKLCFSCPWEGRRLFKMLLQFHHETQRPLDPGCLLPQDAERSADQPGRAVVDFPVAAVLPAGGSGERMGLTTPKQFCSIFNRPLISYTIQAFERLPWIVMVVVVVAKDNHDLMLNIVRKFNHTKVKVVHGGTTRHRSIYNGLQAFSDSTDSSTPKPKVVIIHDAVRPFVEEDLLLKITLAAKEQGASGAIRPLVSTVIATTSESYLDHSLERAKYRASEMPQGFLYDIIFQAYQRCSEFDLEFGTECLHLALQYCGTNARLIEGPPTLWKVTYKRDLAAAEAIIKETLSVSACIIAEAEEEAVELAKTLQKNLNMMETDVIPCGKESNVQYLSKTRNFIHISASASSSLWVLEMVKCFEDIDHARLYPVVIVWVQLSMTKQSADSQETDEFMALASEVKQRNVLLYGIKIDHSKELEQWQRSLERLGQITLVLIRDRNMALTGQMLHV
Protein: Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Protein A1S9) (Ubiquitin-activating enzyme E1) (P22314)
Organism: Homo sapiens (Human)
Function: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1376922}. Mitochondrion {ECO:0000269|PubMed:1376922}. Nucleus {ECO:0000269|PubMed:1376922, ECO:0000269|PubMed:22456334}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:33108101, ECO:0000269|PubMed:7528747, ECO:0000269|PubMed:9099746}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:33108101, ECO:0000269|PubMed:7528747}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-conjugating enzyme E2 D2
- Polyubiquitin-C
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 D1
- Polyubiquitin-B
- Ubiquitin-conjugating enzyme E2 K
- Ubiquitin-conjugating enzyme E2 S
- Ubiquitin-conjugating enzyme E2 R1
Sequence:
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
Protein: Augurin (Esophageal cancer-related gene 4 protein homolog) (D4A540)
Organism: Rattus norvegicus (Rat)
Function: Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system. ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9H1Z8}. Cytoplasm {ECO:0000269|PubMed:21349154}. Apical cell membrane {ECO:0000250|UniProtKB:Q9H1Z8}.
Interaction partners:
Sequence:
MGTSSARPAVLALAGLALLLLLCLGPGDVSGNKLKKMLQKREGPVPSKTNVAVSEHTAKEFLGGLKRAKRQLWDRTRPEVQQWYQQFLYMGFDEAKFEDDVNYWLNRNQNGHDYYGDYYQRHYDEDAAIGPRSREGFRHGASVNYDDY
Protein: Tudor domain-containing protein 1 (Q99MV1)
Organism: Mus musculus (Mouse)
Function: Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14550528, ECO:0000269|PubMed:17038506, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20439430}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20439430). DDX4 is required for meiotic nuage localization. Also present in chromatoid body. {ECO:0000269|PubMed:20439430}.
Interaction partners:
- Piwi-like protein 2
- ATP-dependent RNA helicase DDX4
- RNA helicase Mov10l1
- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
- Putative ATP-dependent RNA helicase TDRD12
- Piwi-like protein 4
- Protein maelstrom homolog
- Piwi-like protein 1
- ATP-dependent RNA helicase TDRD9
- Small RNA 2'-O-methyltransferase
Sequence:
MMPRNNLEASTCKMAEPFNFEKKESKPPPQDPLRSPVAQHNHPTFRLKSPENGNTKNNFLLCEQNKQYLASQEDSSVVSSNPAVVNGEVGGSKGDRKPPPTGNPVSPLSLGNSSPPNQVKTKPSSNVTPEKSKKSHKLFENALSVNNPALFNSLGPPLRSTTCHRCGLFGSLRCSQCKQTYYCSTACQRRDWSSHSTICRPVQQSLNKLEDNKSPFETKAIEVKSEVDCPPGVTKEITAGAERVMFSDLRSLQLKKTMEIKGTVTEFKHPSNFYIQLYSSEVLENMNQLSTSLKETYANVVPEDGYLPVKGEVCVAKYTVDQTWNRAIVQAVDVLQRKAHVLYIDYGNEEMIPIDSVHPLSRGLDLFPPSAIKCCVSGVIPTAGEWSEGCVAAVKALLFEQFCSVKVMDILEEEVLTCAVDLVLQSSGKQLDHVLVEMGYGVKPGEQSSTEQSVDHSALEDVGRVTVESKIVTDRNALIPKVLTLNVGDEFCGVVAHIQTPEDFFCQQLQSGHKLAELQESLSEYCGHVIPRSDFYPTIGDVCCAQFSEDDQWYRASVLAYASEESVLVGYVDYGNFEILSLKRLCPIIPKLLDLPMQALNCVLAGVKPSLGIWTPEAVCVMKEMVQNRMVTVRVVGMLGTRALVELIDKSVAPHVSASKALIDSGFAIKEKDVADKGSSMHTASVPLAIEGPAEALEWTWVEFTVDETVDVVVCMMYSPGEFYCHFLKDDALEKLDDLNQSLADYCAQKPPNGFKAEIGRPCCAFFSGDGNWYRALVKEILPSGNVKVHFVDYGNVEEVTTDQLQAILPQFLLLPFQGMQCWLVDIQPPNKHWTKEATARFQACVVGLKLQARVVEITANGVGVELTDLSTPYPKIISDVLIREQLVLRCGSPQDSLMSRPANQHKQIDSHRVQASPSAEQWKTMELPVNKTIAANVLEIISPALFYAIPSEMSENQEKLCVLAAELLEHCNAQKGQPAYRPRTGDACCAKYTNDDFWYRAIVLETSESDVKVLYADYGNIETLPLSRVQPIPASHLELPFQIIRCSLEGPMELNGSCSQLVMELLRNAMLNQSVVLSVKAISKNVHAVSVEKCSENGMINIAENLVMCGLAENLTSKRKSASTKEIPHSRDCCCTELQKQIEKHEQILLFLLNNPTNQSKFTEMKKLLRS
Protein: HORMA domain-containing protein (Q8T870)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTDVKTQNAISLKGSAQLVKEFFHFGLNSILYQRALYPSDSFKREKKYGLTLWVAHEKKLQAFMDPLLQQVEYWLAKRQLKRLVMVISEVKTKEVVERWQFDIHTENLAEEGYEIV
Protein: tRNA(Met) cytidine acetyltransferase TmcA (EC 2.3.1.193) (Lysine 2-hydroxyisobutyryltransferase) (EC 2.3.1.-) (P76562)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2). Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA (Probable).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
Interaction partners:
- Small ribosomal subunit protein bS1
- Uncharacterized protein YpfJ
- RNA 3'-terminal phosphate cyclase
- tRNA pseudouridine synthase B
- Esterase YpfH
- DNA-directed RNA polymerase subunit beta'
- Acetyltransferase YpeA
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS11
Sequence:
MAELTALHTLTAQMKREGIRRLLVLSGEEGWCFEHTLKLRDALPGDWLWISPRPDAENHCSPSALQTLLGREFRHAVFDARHGFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTADNEAILWRQNQPFSLAHFTPRTDWYPATGAPQPEQQQLLKQLMTMPPGVAAVTAARGRGKSALAGQLISRIAGRAIVTAPAKASTDVLAQFAGEKFRFIAPDALLASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRGFLLKFCARFPHLHRFELQQPIRWAQGCPLEKMVSEALVFDDENFTHTPQGNIVISAFEQTLWQSDPETPLKVYQLLSGAHYRTSPLDLRRMMDAPGQHFLQAAGENEIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAAHGNNPLAATLRGRRVSRIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTAMALLPMSDAGKQLAEREHYRLRRDAQALAQWNGETLPVDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGCLLRLLQTSELALPALRGRLQKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFALNDVRTERLRDRITQWQLFH
Protein: DEMETER-like protein 3 (EC 3.2.2.-) (O49498)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential transcriptional activator that may act by nicking the target promoter. Catalyzes the release of 5-methylcytosine (5-meC) from DNA by a glycosylase/lyase mechanism (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA
- DNA
- DNA
- DNA
- Protein REPRESSOR OF SILENCING 3
- Increased DNA methylation 1
- Increased DNA methylation 2
- Polynucleotide 3'-phosphatase ZDP
- DNA-directed RNA polymerase V subunit 1
- Methyl-CpG-binding domain-containing protein 7
Sequence:
MLTDGSQHTYQNGETKNSKEHERKCDESAHLQDNSQTTHKKKEKKNSKEKHGIKHSESEHLQDDISQRVTGKGRRRNSKGTPKKLRFNRPRILEDGKKPRNPATTRLRTISNKRRKKDIDSEDEVIPELATPTKESFPKRRKNEKIKRSVARTLNFKQEIVLSCLEFDKICGPIFPRGKKRTTTRRRYDFLCFLLPMPVWKKQSRRSKRRKNMVRWARIASSSKLLEETLPLIVSHPTINGQADASLHIDDTLVRHVVSKQTKKSANNVIEHLNRQITYQKDHGLSSLADVPLHIEDTLIKSASSVLSERPIKKTKDIAKLIKDMGRLKINKKVTTMIKADKKLVTAKVNLDPETIKEWDVLMVNDSPSRSYDDKETEAKWKKEREIFQTRIDLFINRMHRLQGNRKFKQWKGSVVDSVVGVFLTQNTTDYLSSNAFMSVAAKFPVDAREGLSYYIEEPQDAKSSECIILSDESISKVEDHENTAKRKNEKTGIIEDEIVDWNNLRRMYTKEGSRPEMHMDSVNWSDVRLSGQNVLETTIKKRGQFRILSERILKFLNDEVNQNGNIDLEWLRNAPSHLVKRYLLEIEGIGLKSAECVRLLGLKHHAFPVDTNVGRIAVRLGLVPLEPLPNGVQMHQLFEYPSMDSIQKYLWPRLCKLPQETLYELHYQMITFGKVFCTKTIPNCNACPMKSECKYFASAYVSSKVLLESPEEKMHEPNTFMNAHSQDVAVDMTSNINLVEECVSSGCSDQAICYKPLVEFPSSPRAEIPESTDIEDVPFMNLYQSYASVPKIDFDLDALKKSVEDALVISGRMSSSDEEISKALVIPTPENACIPIKPPRKMKYYNRLRTEHVVYVLPDNHELLHDFERRKLDDPSPYLLAIWQPGETSSSFVPPKKKCSSDGSKLCKIKNCSYCWTIREQNSNIFRGTILIPCRTAMRGAFPLNGTYFQTNEVFADHETSLNPIVFRRELCKGLEKRALYCGSTVTSIFKLLDTRRIELCFWTGFLCLRAFDRKQRDPKELVRRLHTPPDERGPKFMSDDDI
Protein: Amidase family protein (Q8MMR8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, mitochondrial
- Endonuclease 4 homolog
- Multifunctional protein pyr1-3
- asparaginase
- glutamate--tRNA ligase
- GMP synthase
- Acetyl-CoA carboxylase
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
Sequence:
MTSSSLSKSSSTSSTSSKNEEKGEKKIYDLISLEVPRLQGLLLRSTLFLCENHYLKNSFLSSLYTKNKMPLISQFNLNLSPTFYPIVDISNHQQQQQNKSEFTFKKYLATDMLHDKDLIKYLQSKNLEINSQSSSSSSSNNQSLINNIPENSIINYYNLYMTGKITPNEIANFFIECKNHSDEQSPPLKAFIKILEDDIKSQAMASAERWKSGSPLSLIDGVPISLKDEIDQIGYHTTCGTTFLEKVFPNVKTEDSGVAKMLRQQGAILVGKNNMHEIGISTLGYNTHFGFTRNPYNLNHYPGGSSSGSASSVSAGLNPLSIGCDGGGSIRVPASLCGVVGLKPTFARVSHGGIFDLCWSVGHVGPIGSSVIDTAIGYACIAGSDSADHQSVLAEQYGGKPTVPMFTEIPLIQPLKGLKIGVFYDWINDCNIEFKDSTYKCIEILKEQGAEIIEIEISNLLVTRLSQGAIILSEMNSSMKRFKNYSNELQYDSRISLSIGNILPTSDYLQANKVRTFCIEQFTEIFKGVDLIVTPTNAIAAPEIEKSVLSMGESNFGSVGELMKYVFIGNITGIPGITVPVGLTKDKNLPIGFQIMAKWWQEDLLLYTSYVLEKNIDFKGKPQYYNCPLTNCTNPNN
Protein: Spastic paraplegia 20 isoform 1 (Spastic paraplegia 20, spartin (Troyer syndrome), isoform CRA_a) (A0A024RDV9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEQEPQNGEPAEIKIIREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSKESEHTGPGWESARQMQQKMKETLQNVRTRLEILEKGLATSLQNDLQEVPKLYPEFPPKDMCEKLPEPQSFSSAPQHAEVNGNTSTPSAGAVAAPASLSLPSQSCPAEAPPAYTPQAAEGHYTVSYGTDSGEFSSVGEEFYRNHSQPPPLETLGLDADELILIPNGVQIFFVNPAGEVSAPSYPGYLRIVRFLDNSLDTVLNRPPGFLQVCDWLYPLVPDRSPVLKCTAGAYMFPDTMLQAAGCFVGVVLSSELPEDDRELFEDLLRQMSDLRLQANWNRAEEENEFQIPGRTRPSSDQLKEASGTDVKQLDQGNKDVRHKGKRGKRAKDTSSEEVNLSHIVPCEPVPEEKPKELPEWSEKVAHNILSGASWVSWGLVKGAEITGKAIQKGASKLRERIQPEEKPVEVSPAVTKGLYIAKQATGGAAKVSQFLVDGVCTVANCVGKELAPHVKKHGSKLVPESLKKDKDGKSPLDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGYNAGEATHHAVDSAVNVGVTAYNINNIGIKAMVKKTATQTGHTLLEDYQIVDNSQRENQEGAANVNVRGEKDEQTKEVKEAKKKDK