wanglab/gogpt-training-data huggingface dataset:
Protein: Iron sulfur cluster assembly protein 1, mitochondrial (Iron sulfur cluster scaffold protein 1) (Q9UTC6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein isu1. In a second step, the cluster is released from isu1, transferred to a glutaredoxin, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on isu1 depends on the function of the cysteine desulfurase complex nfs1-isd11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q03020}.
Interaction partners:
- Probable cysteine desulfurase, mitochondrial
- Frataxin homolog, mitochondrial
- Protein isd11
- J-type co-chaperone jac1, mitochondrial
- Iron-sulfur assembly protein 2
- Iron-sulfur assembly protein 1
- NifU-like protein C1709.19c
- Uncharacterized protein C11D3.10
- Uncharacterized aminotransferase C777.03c
- Iron-sulfur cluster assembly factor IBA57
Sequence:
MSVFRRSVQCVGVLPSILAQRSSLLARPANLQFLKTNSSKFVPQVTANVSRRMYHKNVLDHYNNPRNVGTLPKGDPDVGIGLVGAPACGDVMRLAIRVNKDGVIEDVKFKTFGCGSAIASSSYVTTMVKGMTLEEASKIKNTQIAKELCLPPVKLHCSMLAEDAIKSAVKHYRSKQLTPVGTTAGAIESATA
Protein: HMG box domain-containing protein (G8BDQ3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Uncharacterized protein
- Histone H2A
- RuvB-like helicase
- Actin-related protein 5
- BSD domain-containing protein
- rRNA adenine N
- General transcription and DNA repair factor IIH subunit TFB4
- DNA 3'-5' helicase
- DNA-directed RNA polymerase I subunit RPA49
- RNA polymerase II transcription factor B subunit 2
Sequence:
MLRLIVNPSRALATQVICKPLSSASIRHQVVNYSTAKTTRSSKDKEAAYLKKKLQTAKDKKKSIEQDLKDKTREIRELSKERKKKAATQEKTKLKEQKEAEKHKAFLKDTLREPRSLNVHNYFAKATKTPVYELKEKFAELSESEVAKYKEATNKYNHALKSILTPKPVLGPTSAYQNFVSQNYPPDVSGREAMTRLAAKWKALSDEEKKSFDVPDHEVERIKSLQKQWEKTREEEYPKLVKFKQEYKFTI
Protein: Deoxyribonuclease-2-alpha (EC 3.1.22.1) (Acid DNase) (Deoxyribonuclease II alpha) (DNase II alpha) (Lysosomal DNase II) (R31240_2) (O00115)
Organism: Homo sapiens (Human)
Function: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells.
Subcellular location: Lysosome.
Interaction partners:
- Deoxyribonuclease-2-beta
- DNA fragmentation factor subunit beta
- Deoxyribonuclease-1
- DNA fragmentation factor subunit alpha
Sequence:
MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQRGGGTLCAQLPALWKAFQPLVKNYQPCNGMARKPSRAYKI
Protein: Zcf39p (A0A1D8PU45)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Topoisomerase 1-associated factor 1
- non-specific serine/threonine protein kinase
Sequence:
MSTDTTANDEGKNEFSKQWRQSRACTRCRRFKKKCSFENPSFKSCARCFKNGYECSFNEDPAMQPSRKKKRKIQIDDNTHSSIANQLLSTSENTLKLLPEKLNDLSEDSIQHLISNYESIMDKLKSKIKPDTSNEFPYIPYSKNLAKELIYRYNYLTLAEVKTRLDFFLNEILPYYPTIPLSRKLKNFDYMLEKFPLLLIACIFVTVLNDNNLGTTPISKDNLKLCNLLSYYLYSFIAHEVYVKCEQFNIQLIYVCLISSSWCLPPIKLGHFRNQLNSLTASNIALCMGLNELPKNCFEIHLDEESELRNNLRALLSVYCSCGSLELSVRRFKVVTWTQSHQIAMNRLLETSSNQLPTLEDRYICYFAELVFTGHEILDFVDQINLAVNRSRISLSNIKRALRKYEQRLSQILDQSGFTSTKQALALQIQYFHLLVVIYDNLVSGVFNQSDEITPNYADEIPSSNERQFCLKMIIKLITSCESLVDQFVRLNNNIINIPSVLYYRPMHALILLVRLRLILKFQNFKDLEIDVESYFTKVSRVINDNLMKNSLVCSKMKVVLNKIEKWLILSQKYIKSDSVENNGPMNFDVVKIIFQNKDKEIENLDVPKSHNESPIKTNTTIESQDPSPVNSVDNPFTANNEFNGIISLEQIFQGIDSDISHYLNPLESNFDLSTDFNRFS
Protein: Slr1196 protein (P73344)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Slr1169 protein
- Slr0872 protein
- Slr2027 protein
- Slr0420 protein
- Sll0611 protein
- Ssr0349 protein
- Slr1724 protein
- Sll1698 protein
- Sll0350 protein
- Slr1799 protein
Sequence:
MYPSSSPGHRQYFLGVKSSLPLLWLMVFPALIGGVLNINPVQAQGTPYIPPPITPPPLSPSENPFDPSLFPTDPLIPSGETLTPLQRRRLIEALDALEAEALVLDQAGQGDQAFEVRYRSLRGRQRLGDLAEVEALGRIGAIAWEQGRNQDVMAIGQRLEDLQLSLTKDKAMSPELLTAFAKAYGQLHSLDSAIAVYQQMRREAQQQGDYRRENQALSMLGELYLAKFNYPAAAEVYETLLARATNARNSYYEGIYLQKLGEIYQQSAQPDNAIRIKEQLVQRRLQDGKPELVPDIQIAIGDHYLELEQPENASQAYQKAYTLAWSIKQLSTAAIALDKLGDLYLFSEQPNYALQIYKQLLQVQQQSYNYYGMMITYEKIAQLYIDAQQTSAALTAYQQALSLARSLKYSTKENNILNQIQTISGGTGS
Protein: Putative serine/threonine-protein kinase PRKY (EC 2.7.11.1) (O43930)
Organism: Homo sapiens (Human)
Interaction partners:
- F-box-like/WD repeat-containing protein TBL1Y
- Amelogenin, Y isoform
- Amelogenin, X isoform
- Eukaryotic translation initiation factor 1A, Y-chromosomal
- Lysine-specific demethylase 5D
- Protocadherin 11 Y-linked
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Testis-specific Y-encoded protein 1
- Zinc finger Y-chromosomal protein
- Small ribosomal subunit protein eS4, Y isoform 1
Sequence:
MEAPGPAQAAAAESNSREVTEDAADWAPALCPSPEARSPEAPAYRLQDCDALVTMGTGTFGRVHLVKEKTAKHFFALKVMSIPDVIRRKQEQHVHNEKSVLKEVSHPFLIRLFWTWHEERFLYMLMEYVPGGELFSYLRNRGHFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILLDRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSGFPPFFDDNPFGIYQKILAGKLYFPRHLDFHVKTGRMM
Protein: Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Embryo-derived protein kinase) (Edpk) (Myristoylated and palmitoylated serine/threonine-protein kinase) (MPSK) (Protein kinase Krct) (Protein kinase PKL12) (TGF-beta-stimulated factor 1) (TSF-1) (Tyrosine-protein kinase STK16) (EC 2.7.10.2) (O88697)
Organism: Mus musculus (Mouse)
Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9712705}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles.
Interaction partners:
Sequence:
MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREAEMHRLFQHPNILRLMAYSLKERGAKHEAWLLLPFFKKGTLWNEIERLKDQGSFLTEDQILPLLLGISRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNELSIPQSPRHSSALRQLLSSMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
Protein: diphosphoinositol-polyphosphate diphosphatase (EC 3.6.1.52) (Q59MU0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Putative tyrosine-protein phosphatase OCA1
- Uncharacterized protein
Sequence:
MSDYMDDPFQMDEEIPSKKDPIPSKERSLPIPENATIDRDITPSYPTPPNIHYDNNKIIRSKLDQLKLEENTGGTNTTTEEEGEKYEEDIDDKLDMSLQAKLRLEYENCLDYDKPLTPPENFAPVINKIYRSSFPQPNNFAFLKKLKLKSILCLIPEDYPHLQQEFIKNENIKLFQLGMSGNKEPFVKISADLITEAVKIVLNPENQPILIHCNRGKHRTGCLVGVIRKLQNWSLTLIFDEYRKFACPKERPMDQQFIELYDDTEILEYCYEYDLLPLKWD
Protein: GPI mannosyltransferase 2 (EC 2.4.1.-) (Q388T1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363112}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363112}.
Interaction partners:
- Dolichol phosphate-mannose biosynthesis regulatory protein
Sequence:
MSPTRAQRLEGLERIAYCSDVKLFFLVSGSRMFLLLLMLFLRVALPHIYGTELLWDSGTLLYDDMNSTWSLLNFPRSWDGVHFFHVAKHGYSHENVCAFFPLVPFIVRTVSWLNDVLLPEFLTAVPVTFQVALLNVAMGGAAAVCLRRITILTLLSGSHGVDYTNKKDKAMSMTSGTWLDSLPLPPPYYRHEVTVKEHLNARLWKEVGATVLMWMLSPTAVFSVVLYTESVFSFATFLGVYMLIVSPQGKWRTAAAEAGAVLCFAVAGCARSNATTYIGFVLYPVFLQVFFFDTYRKRYAKRYGVTSPIRRWPSLARCVIVLIEVVIIITPYLGLNYLCYSRFVPLWDDMSRAAIGGRFWAFYGWMQKRYWNVGFLQSYRWGNAPNVLISAPIMFFTVRGFVLFIVQPALARSMETESNISKEYQEPRSDCREDRCGNKKQRLFSIYKLMENLVQSSNIICLLVILAFGATMAHVNVVNRLVMSSPALYWLWGRQFVCDPWGGNTVVMVRIFLLWNCIGALFVPNGLPWT
Protein: Large ribosomal subunit protein bL27m (54S ribosomal protein L2, mitochondrial) (YMR6) (YmL2) (P12687)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS2m
- Large ribosomal subunit protein uL5m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS15m
Sequence:
MWNPILLDTSSFSFQKHVSGVFLQVRNATKRAAGSRTSMKDSAGRRLGPKKYEGQDVSTGEIIMRQRGTKFYPGENVGIGKDHSIFALEPGVVRYYLDPFHPKRKFIGVALRRDLKLPSPHFEPTVRRFGRFELTNKRAAYKEENSISRKDYLAKPNILKQLEVRESKRKELQDKLSKVLRDELKLDIKDIELATSYLIRVRASLKNGYPIEDARFNSRYYLKEEERLKARRESWTNEKLSESLSKIDECSDLLNSSTSFNNKLELHQYISEQEKQALKAKLLEDLEKSQHLETKKDKNYIKALFKDACNFLTLSEEVHLRRKYLKSVFPETDSTVETKSGKKSIVSRRFDYTKNKVEVIARSRRAFLSKL
Protein: Polymerase delta-interacting protein 3 (46 kDa DNA polymerase delta interaction protein) (p46) (S6K1 Aly/REF-like target) (SKAR) (Q9BY77)
Organism: Homo sapiens (Human)
Function: Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by association with the TREX complex.
Subcellular location: Nucleus. Nucleus speckle. Cytoplasm. Note=Nucleocytoplasmic shuttling protein.
Interaction partners:
- SAP domain-containing ribonucleoprotein
- Spliceosome RNA helicase DDX39B
- Eukaryotic initiation factor 4A-III
- Chromatin target of PRMT1 protein
- UAP56-interacting factor
- Nuclear cap-binding protein subunit 1
- THO complex subunit 4
- ATP-dependent RNA helicase DDX39A
- Ribosomal protein S6 kinase beta-1
- THO complex subunit 1
Sequence:
MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQVPQQKAMAPLHPHPAGMRINVVNNHQAKQNLYDLDEDDDGIASVPTKQMKFAASGGFLHHMAGLSSSKLSMSKALPLTKVVQNDAYTAPALPSSIRTKALTNMSRTLVNKEEPPKELPAAEPVLSPLEGTKMTVNNLHPRVTEEDIVELFCVCGALKRARLVHPGVAEVVFVKKDDAITAYKKYNNRCLDGQPMKCNLHMNGNVITSDQPILLRLSDSPSMKKESELPRRVNSASSSNPPAEVDPDTILKALFKSSGASVTTQPTEFKIKL
Protein: Antifungal protein 2 large subunit (CW-2) (P83143)
Organism: Malva parviflora (Little mallow) (Cheeseweed mallow)
Function: Possesses antifungal activity against P.infestans but not F.graminearum.
Interaction partners:
Sequence:
PEDPQRRYQEXQREXRXQQE
Protein: Protein ABA AND ROS SENSITIVE 1 (Q9M8S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for breaking seed dormancy before seed germination. Prevents reactive oxygen species (ROS) accumulation in response to abscisic acid (ABA) and oxidative stress, probably by repressing the accumulation of ABA-induced ROS-scavenging enzymes (e.g. CSD3).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26583028}. Cytoplasm {ECO:0000269|PubMed:26583028}. Note=Translocates from the nucleus to the cytoplasm in response to abscisic acid (ABA) and oxidative stress (e.g. hydrogen peroxide H(2)O(2) and methyl viologen (MV)). {ECO:0000269|PubMed:26583028}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- ATPase E1
- Tetratricopeptide repeat
- At2g19270
- AT3G18790 protein
- rhamnogalacturonan endolyase
- SNW/SKI-interacting protein
- Pliceosome associated protein-like protein
- Pre-mRNA-processing-splicing factor 8A
- Proline-rich spliceosome-associated
Sequence:
MDAQAKKKAMFRSKLNAKKKDTRIDSPLVRYNESDQPVCRVCNVVLKSESLWDVHQASRKHHEAIDSLKASAAGVQRGSKPAETRPTKIEALAKSSNSQTSSGLPPNFFENREPARAEVEPAKSKNLEQSKHTIGSETNKSKGPLPAGFFDNQKTDSSNTKTTSEPKQSQTQTTGPETKPMVNGNLPTGFFDNKEADLLAHGIKLVKPDIKDEYKEFEKLIQDDLQVVDSRMEEEEVDAAETIEEEEQREQRSYKEKVEILKRKKMELKAARLAKRSKTSEGSVKKPKKTEEESPSDEEDDEDSAVDWRAQHL
Protein: Dephospho-CoA kinase (EC 2.7.1.24) (AtCoaE) (Dephosphocoenzyme A kinase) (Q9ZQH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19329564}.
Interaction partners:
- Phosphopantetheine adenylyltransferase
- Phosphopantothenate--cysteine ligase 1
- Phosphopantothenoylcysteine decarboxylase
- Formamidopyrimidine-DNA glycosylase
- holo-[acyl-carrier-protein] synthase
- Alkaline-phosphatase-like family protein
- Pantothenate kinase 2
- Pantothenate kinase 1
- Probable UMP-CMP kinase 1
- Probable UMP-CMP kinase 2
Sequence:
MRIVGLTGGIASGKSTVSNLFKASGIPVVDADVVARDVLKKGSGGWKRVVAAFGEEILLPSGEVDRPKLGQIVFSSDSKRQLLNKLMAPYISSGIFWEILKQWASGAKVIVVDIPLLFEVKMDKWTKPIVVVWVSQETQLKRLMERDGLSEEDARNRVMAQMPLDSKRSKADVVIDNNGSLDDLHQQFEKVLIEIRRPLTWIEFWRSRQGAFSVLGSVILGLSVCKQLKIGS
Protein: Glycerol-3-phosphate acyltransferase (Q9TJS7)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
EPFDYYMFGQNYIRPLVDYRNSYVGNISIFQDMEQKLQQGHKVVLMSNHQTEADPAIIALLLERSNPWISENIVYVAGDRVVTDPLCKPFSMGRNLICVYSKKHM
Protein: Myosin-J heavy chain (Myosin-5b) (P54697)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Processive motor protein that can move over long distances along F-actin without disassociating; processiveness depends on high physiological Mg(2+) concentrations. Presents a high actin affinity in the presence of ADP, fast ATP hydrolysis, and a high steady-state ATPase activity in the presence of actin that is rate limited by ADP release. Physiological decrease of free Mg(2+) ions leads to an increased rate of ADP release and shortening of the fraction of time it spends in the strong acting binding states.
Subcellular location: Contractile vacuole {ECO:0000269|PubMed:18650439}.
Interaction partners:
Sequence:
MTTSTIENGASSPIIVSSSTPKLYQEGAGVWIPDQELGWIGADVIEHSETSADQVLVRTEDDREVKIPLSKVFQKNPDILEGVDDLSFLSHLHEPAILHNLHHRYNLNQIYTYIGKILIAINPYTSLPLYGKEMISAYYGKQLGTLAPHVYAVAEDAFKDMRYDGTSQSILVSGESGAGKTETTKFLLQYFAAMGNMIKESTSSSSINGINTSSDGIPVTPPPSPMKKSPVDKSVEERVLESTPLLEAFGNAKTLRNDNSSRFGKFIEIHFNEMGSIIGAKILTYLLEKSRIVRQVYNERNYHIFYQLLSGASEELKEKLNLKTIEEYSYLNKSGCFEIEGVSDEEHFNKTCHAMQVAGITLVEQENVFRILSAILLIGNFEFENIAGSNDDSCQLIDRDPLEKVSVLLGCAQPDELLNSMLTRKVVTGKESYISHNTKERAENARDSLSMFLYGMMFDWLVVKINSSMSISTQQKSKSFIGVLDIYGFESFEVNGFEQFCINYANEKLQQLFNQHVFKEEQQEYIKEKIDWSYIDFNDNQDTLDLIEKKPICILTLLDEETMFPKATPQTLATKLYSKMTSHSKFEKPRFSSTAFTINHYAGKVTYETDQFLDKNKDFIIPEQISILQRSNFSFIKVLMSHSDKFTQSPGGHPQGNGGPTSSNTKGTSGSSSMKFLSVGSQFSTSLATLMKTISTTTPHYVRCIKPNPEKLPQTFNKQDVIHQLRCGGVMESVRICCAGFPTRRLLSEFYQRYKILYVKDINTGSGGGKKGSNNNKIKDPKILVQNLLTGIELSDDKYKIGLTKVFLRAGQLASLEDMRLEQLDRSATVIQKRWKGYLYRKRYKQLRDASLIIQTKLRSVHAKQQLSALQRTHSAILIQKVWRAHRDRVQYQKIRDASLQLQTVMRRHLFSEQVHRERCENAAIILQTKIRQILSKREVDKKLRGIILIQARWRMKLAKRVYIQLRAEARSLRTVQEQKNKLQEKLEELQWRLTSEAKRKQQLEDQKVKSDTTISELSSNNDHLELQLSEIQLKYQELDKSNQSSQLQLSECLSKLEEQTQQLDHSSKLNKKLEKDLSDQHDSIEKLQSQFNETEQQLQQFKQQSEELSSKLSKTTQQLDFNKQEFDRLSQERDTDNTNNQLEIQQLKKANSTLEEDYFSLSGIRDNLERQVLELRDENQLIKERLDSLGQQSSQFQSGAALEKQQLEQLVQEQSEQLIKLSSEKLGSEEEAKKQINQLELELTDHKSKLQIQLQLTEQSNEKIKKLKGKLEEYQDEKKQLQQELERIKQSKQSVEDEKNSLITQLTTVKFESTQVSTNVSHQKEKITTLKSTIEELNKSIGKLQAEQKNKDDEIRKIQFELNDQKQQFTRQTKEFSDLQSQQSIDRQKSEITIHSLERTNETLKSDFERVQQSLKQQERDCQQYKDTINRLENEVKQLTQLKERFENEFFVAKEQNSNQTQESVYLKEVTTQMQQNQSRIERELEEKKQHITRIDDERDELKKQLTQLQQQHEQSSTQLLLAQNELERLRKKELKYKERGHETSKQQDQFNMEIQSLRITNNDQLKSLQDYEQEKKKLKDKLSSSKQEAQQQRESIIKMDAELSAIKQHSQWVENSFTDMKQRNQELIESSALYKQQLLQQTSTIDSTIKEKENEISKLQQQLETSNQQLHQLKEELNSMKQSNQLESTEQSKQLNQLIQENQQLKSVTNEISKQLDDAVFENQKINNTIKEQEIKSKRMSVELQQHIDEGKQQEIQQLQSTIAQLKQQQQSETDRLEKEIQQMKRERETQMKLVESTKLNYHMLEDRMELYRNVMEIIDYKETEWEKLARLAGCKELDTKLLSDFLLSCKLEHTSLGSQMWFHQIDYWCPYERDSSKGIFYGIIRSIVDFTIKNFDDVDLLSYLLACCSLTLFLYKKNLVKHLNGANSIMPIIPTLGDLEELNERLSHQSLTTSGKFSGGGGGGGIDFIDQLQQSTGITFGLIFKATTLKLSPLVDGAILNENYNKKLTSISASSFGSGSFGLGSNGVGSVLSIELITTYLSSIITIFQHRMVHFTLSQRFFNQVFCWIGALIMKGFMLRQTFCTETFATFVKTKIDFLTRWADDIGNVWVGDVANAFQQVREVINVLNIKDKEKIIDDKIRKQYCPTLNSNQLKQVLSLFSPGEFGGKRVSAKVIASICPPNKSSAGQSFVQDENKLNTIPIDSLHYLEIQDIKTLSLPLSIRQTIETEIINLKQQIACKK
Protein: DNA oxidative demethylase ALKBH2 (EC 1.14.11.33) (Alkylated DNA repair protein alkB homolog 2) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2) (Oxy DC1) (Q6NS38)
Organism: Homo sapiens (Human)
Function: Dioxygenase that repairs alkylated nucleic acid bases by direct reversal oxidative dealkylation. Can process both double-stranded (ds) and single-stranded (ss) DNA substrates, with a strong preference for dsDNA. Uses molecular oxygen, 2-oxoglutarate and iron as cofactors to oxidize the alkyl groups that are subsequently released as aldehydes, regenerating the undamaged bases. Probes the base pair stability, locates a weakened base pair and flips the damaged base to accommodate the lesion in its active site for efficient catalysis. Repairs monoalkylated bases, specifically N1-methyladenine and N3-methylcytosine, as well as higher order alkyl adducts such as bases modified with exocyclic bridged adducts known as etheno adducts including 1,N6-ethenoadenine, 3,N4-ethenocytosine and 1,N2-ethenoguanine. Acts as a gatekeeper of genomic integrity under alkylation stress. Efficiently repairs alkylated lesions in ribosomal DNA (rDNA). These lesions can cause ss- and dsDNA strand breaks that severely impair rDNA transcription. In a response mechanism to DNA damage, associates with PCNA at replication forks to repair alkylated adducts prior to replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:19736315}. Nucleus, nucleolus {ECO:0000269|PubMed:23972994}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23972994}. Note=Relocates to the replication foci during S-phase. {ECO:0000269|PubMed:12594517}.
Interaction partners:
- Nucleic acid dioxygenase ALKBH1
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
- Probable RNA/DNA demethylase ALKBH6
- tRNA
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
Sequence:
MDRFLVKGAQGGLLRKQEEQEPTGEEPAVLGGDKESTRKRPRREAPGNGGHSAGPSWRHIRAEGLDCSYTVLFGKAEADEIFQELEKEVEYFTGALARVQVFGKWHSVPRKQATYGDAGLTYTFSGLTLSPKPWIPVLERIRDHVSGVTGQTFNFVLINRYKDGCDHIGEHRDDERELAPGSPIASVSFGACRDFVFRHKDSRGKSPSRRVAVVRLPLAHGSLLMMNHPTNTHWYHSLPVRKKVLAPRVNLTFRKILLTKK
Protein: Diterpene cyclase DtcycB (Cembrene A synthase) (EC 4.2.3.150) (Nephthenol synthase) (EC 4.2.3.149) (Pentamethylcyclopentadecatrienol synthase) (EC 4.2.3.151) (M1VDX3)
Organism: Streptomyces sp
Function: Diterpene cyclases that can form multiple diterpene products.
Interaction partners:
Sequence:
MDLPPALLSFYCPIASEVSPEHEAVAQEMYAWIHAMSLTSDNRQAKMLAQAGAGFNSYFTPRARGELARALSKYNVCAWIANGMVQEIRDPGTFGAMAARWARIMEEPATCPADGIPMDFALADAFSHIRRTLSPVKWQHFSAAQSHWMHGLAWENCLHQVKGLTVHDYLSFRYVMSGCFAAAAFAYAVPERHPSAEEWAHPKVRAAADAAMMVDALDNDRYSYLKESLTEADKKTIFAALRHENPALGREEVIVRGVQLRDRILTLYLTLRGELLCDASEGLRSYLTGLDLIIAGNLVFCADMGLRYGLPEGSVRTDAEPLDRTVAPPGIGAIDHWWAQAGA
Protein: Piwi-like protein Siwi (EC 3.1.26.-) (A8D8P8)
Organism: Bombyx mori (Silk moth)
Function: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. 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 govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Recognizes piRNAs containing a phosphate at the 5'-end and a 2'-O-methylation modification at the 3'-end. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias) and a complementary adenosine in the target (t1A bias). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle: antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally cleave complementary transcripts, to couple the amplification of piRNAs with the repression of transposable elements. In this process Siwi acts as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto Ago3. In this process, Siwi requires the RNA unwinding activity of the RNA helicase Vasa for the release of the cleavage products.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25558067}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:25558067). {ECO:0000269|PubMed:25558067}.
Interaction partners:
- Putative ATP-dependent RNA helicase TDRD12
- Piwi-like protein Ago3
- piRNA biogenesis protein EXD1
- Uncharacterized protein
- Tudor and KH domain-containing protein homolog
- Pre-piRNA 3'-exonuclease trimmer
- Uncharacterized protein.
Sequence:
MSEPRGRGRARGRAGRGGDGGGPAPRRPGEQAGPSQQSMPPGPRPQPPSGWGPQSSVPPVRAGVPTPTAQAGRASHRVTPTTHEHPGDIDVQQRMQKLELGPHSSGGGDASSVVGRGSRRGGGRVLPETISILRTRPEAVTSKKGTSGTPLDLLANYFTVETTPKWGLYQYHVDISPEEDSTGVRKALMRVHSKTLGGYLFDGTVLYTVNRLHPDPMELYSDRKTDNERMRILIKLTCEVSPGDYHYIQIFNIIIRKCFNLLKLQLMGRDYFDPEAKIDIPEFKLQIWPGYKTTINQYEDRLLLVTEIAHKVLRMDTVLQMLSEYAATKGNNYKKIFLEDVVGKIVMTDYNKRTYRVDDVAWNVSPKSTFKMRDENITYIEYYYKKYNLRIQDPGQPLLISRSKPREIRAGLPELIYLVPELCRQTGLSDEMRANFKLMRSLDVHTKIGPDKRIEKLNNFNRRFTSTPEVVEELATWSLKLSKELVKIKGRQLPPENIIQANNVKYPAGDTTEGWTRDMRSKHLLAIAQLNSWVVITPERQRRDTESFIDLIIKTGGGVGFRMRSPDLVVIRHDGPIEYANMCEEVIARKNPALILCVLARNYADRYEAIKKKCTVDRAVPTQVVCARNMSSKSAMSIATKVAIQINCKLGGSPWTVDIPLPSLMVVGYDVCHDTRSKEKSFGAFVATLDKQMTQYYSIVNAHTSGEELSSHMGFNIASAVKKFREKNGTYPARIFIYRDGVGDGQIPYVHSHEVAEIKKKLAEIYAGVEIKLAFIIVSKRINTRIFVQRGRSGENPRPGTVIDDVVTLPERYDFYLVSQNVREGTIAPTSYNVIEDTTGLNPDRIQRLTYKLTHLYFNCSSQVRVPSVCQYAHKLAFLAANSLHNQPHYSLNETLYFL