wanglab/gogpt-training-data huggingface dataset:
Protein: DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (DmDNA Lig I) (Q9W1H4)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:17937809}. Note=Does not accumulate at the replication foci (RF).
Interaction partners:
- Flap endonuclease 1
- Exonuclease 1
- Proliferating cell nuclear antigen
- FI04011p
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit 1
- Replication factor C subunit 2
- DNA replication licensing factor Mcm5
- Recombination repair protein 1 endonuclease)
- DNA replication licensing factor Mcm6
Sequence:
MQKSITSFFKKKSDATDSPSPPKKVPKIDAKTELPDEPHIKSESASPETKPKVEPMSVDSEEKTSPVKNVKKEPKEVDDKTTDKKVTTIGLNSTAATKEDVENYDPSADSYHPLKNAYWKDKKVTPYLALARTFQVIEETKGRLKMIDTLSNFFCSVMLVSPEDLVPSVYLSINQLAPAYEGLELGVAETTLMKAICKATGRNLAHIKSQTQLTGDLGIVAEQSRVSQRMMFQPAPLNVRDVFRKLREIAKLSGQSKMDLVYNMFVACRSSEARFFIRSLIGKLRIGIAEQSLLTALAIGLVKKNHIDDCKASKVPDVYKDEIVDTTLLLKTAYCQCPNYDIIIPAILKYDIKELQERCPMHPGMPLRPMLAQPTKGVHEVFERFGGMQITCEWKYDGERAQIHRNEKGEISIFSRNSENNTAKYPDLIARSTALLKGDVKSYIIDSEIVAWDVERKQILPFQVLSTRKRKNVDIEEIKVQVCVYIFDLLYINGTALVTKNLSERRKLLLEHFQEVEGEWKFATALDTNDIDEVQQFLEESIKGNCEGLMVKTLDEEATYEIAKRSRNWLKLKKDYLSNVGDSLDLVVIGGYKGKGRRTGTYGGFLLACYDTENEEYQSICKIGTGFTDEDLQTHSEFLGKHVTSAAKSYYRYDPSLEPDHWFEPVQVWEVKCADLSLSPIHRAAIGIVDGERGISLRFPRFIRIRDDKNSENATDANQVAHMYQSQDQVKNNQKSSTQMEMEDEFY
Protein: Inhibin beta A chain (Activin beta-A chain) (Erythroid differentiation protein) (EDF) (P08476)
Organism: Homo sapiens (Human)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000269|PubMed:11279126}.
Interaction partners:
- Activin receptor type-2A
- Follistatin
- Activin receptor type-2B
- Activin receptor type-1B
- Follistatin-related protein 3
- Inhibin beta B chain
- Activin receptor type-1C
- Inhibin alpha chain
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-1 proprotein
Sequence:
MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
Protein: Transcription factor IIIB 90 kDa subunit (TFIIIB90) (mTFIIIB90) (B-related factor 1) (BRF-1) (Q8CFK2)
Organism: Mus musculus (Mouse)
Function: General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription factor IIIC, polypeptide 3
- Transcription factor TFIIIB component B'' homolog
- TATA-box-binding protein
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MTGRVCRGCGGTDIELDAARGDAVCTGCGSVLEDNIIVSEVQFVENSGGGSSAVGQFVSLDGAGKTPTLGGGFHVNLGKESRAQTLQNGRRHIHHLGSQLQLNQHCLDTAFNFFKMAVSKHLTRGRKMAHVIAACLYLVCRTEGTPHMLLDLSDLLQVNVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTALRLLQRMKRDWMHTGRRPSGLCGAALLVAARMHDFRRTVKEVISVVKVCESTLRKRLTEFEDTPTSQLTIDEFMKIDLEEECDPPSYTAGQRKLRMKQLEQVLSKKLEEVEGEISSYQDAIEIELENSRPKAKGALANLSKDGSGEDATSSPRCEEDTEDEELEAAASHMNKDFYRELLGDDDGSEAAGDPDGGSRPLALESLLGPLPTAASLGISDSIRECISSPSGDPKDSSGDGELDLSGIDDLEIDRYILNESEARVKAELWMRENAEYLREQKEKEARIAKEKELGIYKEHKPKKSCKRREPILASTAGEAIEKMLEQKKISSKINYSVLRDLNSKGGGSPPRDDSQPPERASTKKLSRRKRATTRNSADPGTSTGKRLRPLLSAQPAKKAAVGEALLLSSPALGAEPVKPSAVLVESGPVPYHPEEDADEEDAEDEDGEPCVSALQMMGGNDYGCDGDEDDGY
Protein: Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3) (O43525)
Organism: Homo sapiens (Human)
Function: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10788442}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 5
- Calmodulin-1
- Potassium voltage-gated channel subfamily KQT member 4
- Inward rectifier potassium channel 4
- Ankyrin-3
- Potassium voltage-gated channel subfamily KQT member 1
- ATP-sensitive inward rectifier potassium channel 12
- Inward rectifier potassium channel 2
- Inward rectifier potassium channel 18
Sequence:
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
Protein: Oxidoreductase NAD-binding domain-containing protein 1 (EC 1.-.-.-) (Q8VE38)
Organism: Mus musculus (Mouse)
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Dihydroorotate dehydrogenase
- Diphthamide biosynthesis protein 3
- Uridine 5'-monophosphate synthase
Sequence:
MAHVALIPGLSRGSVGAVCTQAASWGLKASTLRHLTLASIIKSRRKTDHLERTASVLRREVMAAAKVCEITHESPSVKSLRLLVADKDFSFKAGQWVDFFIPGVSVVGGFSICSSPQRLERDRIIELAVKYADHPPAVWVHNKCTLDSEVALRVGGEFFFDPQPTDAPRNLILIAGGVGINPLLSILRHSADLHRDHADKGRSYEIGTVKLFYSAKNTSELLFKKDILDLVHEFPEKISCSFHVTKQTAQISAELKPYVTDGRITEKEIRDHISAETLFYVCGPPPMTDFFSKHLESCHVPKEHICFEKWW
Protein: Cytochrome b-c1 complex subunit 7, mitochondrial (Complex III subunit 7) (Complex III subunit VII) (Ubiquinol-cytochrome c oxidoreductase subunit 7) (Ubiquinol-cytochrome c reductase 14 kDa protein) (P00128)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 10, mitochondrial
Sequence:
MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDNIEVSK
Protein: EF-hand domain-containing protein D1 (EF-hand domain-containing protein 1) (Mitocalcin) (Swiprosin-2) (Q9D4J1)
Organism: Mus musculus (Mouse)
Function: Acts as a calcium sensor for mitochondrial flash (mitoflash) activation, an event characterized by stochastic bursts of superoxide production (By similarity). May play a role in neuronal differentiation.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16336229}.
Interaction partners:
Sequence:
MSSEELACKLQRRLRLEVRAETDQGDPQPAPCDAPAGHPEPEPPARAPTASADSELNLKLSRRLDIHQGTARPGRSKVFNPYTEFPEFSRRLLKDLEKMFKTYDAGRDGFIDLMELKLMMEKLGAPQTHLGLKSMIKEVDEDFDGKLSFREFLLIFHKAAAGELQEDSGLLALAKFSEIDVALEGVRGAKNFFEAKAQALSCSSKFEAELKAEQEERKREEEARRLRQAAFRELKAAFSA
Protein: F-box/WD repeat-containing protein A (F-box protein A) (Protein cheater A) (Q9Y0T2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May target the cAMP phosphodiesterase regA for degradation leading to an increase in cAMP and PKA activity. Promotes development of prestalk cells as opposed to prespores within the developing fruiting body. Required for culmination and fruiting body development.
Interaction partners:
- Cullin-1
- FNIP repeat-containing protein DDB_G0290617
- RING-box protein 1
- Cation efflux protein cytoplasmic domain-containing protein
Sequence:
MQYVNGNDISSQSIHEVLELAFSTKIPWTKLEYESSEKHIIHSYSSHERGIYLSKGVAEFNISPENMYELLLDISSRSKWDFHCREAHIIEEYDHLNHIIHLNFTNPLISNLDMNLYRSCKYDPQERLFVIAMRSIELEDGDVDQFECLPNGWVIQGLRGQKDKCKMTFVQQCDLRDIELQRIPGYKSFNSKERLEDFQFLTLFPATVSGRLAKIFESIELYISNNVKDIETKDIRISIMEKAEKEVNEMFGTTNPDYGWKIYLKKLDMEILIKKTTSGYYMIGKGSFSSRYSPELLADVLYQKNPFEWDTFYDKTKLVESINSSIREVEVHYRMWRNTITMRLLQSVKKGPGNFSSVHWRSICSPNYQVADGIEVHYLPTALLNYGLGDGSFTSFLAAIEVKGYPTPWEEEMVTKMFAARIISNQNSIINHVNKLTGGSEMIRELPVIPSVQHHCGDVGSHIGTPQVYNAMVENFADILLDEGNKDGNVVSSKNKRKRNKNNENKNNNNDNIIDEEIEQEEENIEKDQQQTQQQQTQKQQQQQQQQQKTQQQPQQQQQQPQEQQQNHSQLKKEIKPTRPSIRFTYLLSNSSSGQRPIAWYESKKQPFLFLVSDSSERKGKIQRKTYYFSNSGFDNLPEEVVQIIFSNLSAINIVNLSLVCKRFKMATDSPILWKNLYKSNPLFHKKTPKRKQIIHSNLSNDENKVNSNSGDSADGSSSQEEEEQQQQNQQQNQQQNQQQQQQQTFDLSNINLNDPISLLMVFTNGIIPQNLSPTEIINVGGIVSQIDLNDLSNVETLIQQLPHQVLSLIQMNTLDAKIQHLSMISGMPATIGQESPINKNSSDNPKPNAYNKRDNNSYIPDEEFINWKSHYTEKHKQSKRWVNMEPIRITPLKGHNRAIKAVKSEGNSAITVSTEKKIKFWNLNTGQCIGDYEGESGVLSVEYDHTQKSSCIWPLSDYTKVHIGHKNGTVTMVDFIEQPIEVIHTSRPTNLADGFDFTFPGKYLIWEHTIIHYWDVETSTLLWNELNAHTKKITQSKIVAQHELSNKGIVFTTSSDKSAKVWDLTNGTCINTLVGHSYAVNCIEPIGDYMALTGSTDKTLKLWDLRQASTFISSYSTKHTGPIRCISYQEKNGIVLSGSDDGSIIAFNLDNWNLSNISVVKKPIFNNVIGNIGTTTTTTTTTTTTTTTTTSTTNNTNVPEIPKINLGTFKDSKRLHNHESAVTCIESDEAGFISGSQNGLVLRWDF
Protein: Paired box 2 (D4ACZ2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- T-cell leukemia, homeobox 1
- Eyes absent homolog
- PAX-interacting protein 1
- Protein C-ets-1
- LIM/homeobox protein Lhx1
- SIX homeobox 2.
- SIX homeobox 1
- LIM homeobox transcription factor 1-beta
- Homeobox A11
- Wilms tumor protein homolog
Sequence:
MDMHCKADPFSAMHRHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIAEYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGAGTGVTAPGHTIVPSTASPPVSSASNDPVGSYSINGILGIPRSNGEKRKREEVEVYTDPAHIRGGGGLHLVWTLRDVSEGSVPNGDSQSGVDSLRKHLRADTFTQQQLEALDRVFERPSYPDVFQASEHIKSEQGNEYSLPALTPGLDEVKSSLSASTNPELGSNVSGTQTYPVVTGRDMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRGSAPAAAAAAYDRH
Protein: GTP-binding protein REM 2 (EC 3.6.5.2) (RAS (RAD and GEM)-like GTP-binding 2) (Rem2) (B0R168)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Spermatogenesis-associated 13.
- Potassium channel subfamily K member 17
- Rap guanine nucleotide exchange factor
Sequence:
MSDQGYGLTLSAAPPLRRGSTPLPIKHQLRREEAVSEEYDWTPGLNESATPQISVTNIQDSPSLKPPQQKYHGPLRIVLLGQNGVGKSSLALCLAGLSDRSLSIDSETQAADEGYPRRVTVDDEDSSILVYDNWKQELSTLQCEVCILVFSLTDRRSFHRIAQLRLLLRESLPHTPIILVGNKSDLVRSREISTEEAHSSAMMFGCLYLELSVSLDHRTNDLLEAAVRAARGHSLGPGWTEGSPSAARRESLTSRAKRFLSGLVPRSHLGRERDREPGRDRDLSRHRGSRMLRQKSRSCHDLSALM
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial (Complex I-AGGG) (CI-AGGG) (NADH-ubiquinone oxidoreductase AGGG subunit) (O95178)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MSALTRLASFARVGGRLFRSGCARTAGDGGVRHAGGGVHIEPRYRQFPQLTRSQVFQSEFFSGLMWFWILWRFWHDSEEVLGHFPYPDPSQWTDEELGIPPDDED
Protein: Hyaluronan and proteoglycan link protein 2 (Brain link protein 1) (Q9GZV7)
Organism: Homo sapiens (Human)
Function: Mediates a firm binding of versican V2 to hyaluronic acid. May play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS) which facilitates neuronal conduction and general structural stabilization. Binds to hyaluronic acid (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9ESM3}.
Interaction partners:
- Neuronal cell adhesion molecule
- Receptor-type tyrosine-protein phosphatase zeta
- Ermin
Sequence:
MPGWLTLPTLCRFLLWAFTIFHKAQGDPASHPGPHYLLPPIHEVIHSHRGATATLPCVLGTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPLGGRARMRRGHRLDASLVIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGRPGIRSYGPRDRMRDRYDAFCFTSALAGQVFFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPDPGVRSFGFPRPQQAAYGTYCYAEN
Protein: Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.-) (SET domain-containing protein 7) (A0A8I6A0F7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037249}. Chromosome {ECO:0000256|PIRNR:PIRNR037249}.
Interaction partners:
Sequence:
FQESTITPTISLSPGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGKPHFELTSGSSVFHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDMFVHPRFGPIKCIRTLRAVEAEEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
Protein: D12 (Q9VLL1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
- Ada2a-containing complex component 2
- Protein Dr1
- SAGA-associated factor 29kDa
- Transcriptional adaptor 3, isoform C
- histone acetyltransferase
- Transcriptional adapter 2A
- Ada2a-containing complex component 1
- Molybdopterin synthase catalytic subunit
- Protein will die slowly
- DNA polymerase epsilon subunit 3
Sequence:
MDQQQATPPKKRRHSEYHDPDYQQTEVSSQDEEETCAEAESPGQRKWTKTEQSDGMLPLSDKFQRIRELLRLEFQREISQKVEQLAEIDRRLLQGRQLLDRLRYQVVSEYYRKQQVPLTGADIAKVRGDSLFGDDIAAPQLPLHPAIKKIVGKRPVVIQNHLPERTAATLAKETIRLRNPAHRRAERRRQQKIKEQGIVTDHSKDKKDQPEQEPPISVKLEDEQPCTSRQAHERQVELNASRLNNKNKFNFVVGNTSKYIGEDSRENGTGGNALTYKWLVYVQGKDLPEPLEKYIKKVRFHLHPSYRPNDIVDVHRSPFQLNRHGWGEFPMRIQLFFQEHLQQKPVQLMHTVVLDKTMCGLHTMGAETTVEIWLRAKQAITKQKSGKPHPPHEQETAVPAPPLAAPNVLEPSVFAFPGESCKPRTISITQNKEELDDNLFAGINKIELSDDIEKIEPTVLVSEPLKLNYSPRKQPPTPSSPPRTQLRLNAAQVTASKPSVVYLPVNGRSPRQESLPERQRQEFSPVKHYPPASPQRAWKESSSDRPPIKPVPNGHHQGKKNVVFQRAGKLYIIDPLQRKLKQAAKQQSLLKPQLSLLKPPSETRWHMLQCMQHDHGYANMSGEMEEKPMLLPPIVDTTIQSRPRRLEHIFRSAQFRNMRSAVEFLLSRLPLASIDQQKEYPFTCITLEEFHNHTALKQRCFEYLRARMLRRCLMQHHELHKLDISGKEHYWSLREIVAFARVHGYTPALKDVLPVVHEKRKQKLSDEEQLARRVQAQLKGEPQPQLSAYSSLSSGNRLEAWITKQSDRLLGHDQQMRDKEFIDVLGVDKPHPLASRLTNSADVSFQMVNHRQLLYLPPPKHLDSTLQLVQEMCKDINITLEPEESPPGVSQPLALSMLGQVLRTFIEKLVRRSLAAKLQQETLEQLPPAAANAPLCLQPQDIGRVISLCSELDFLGNSHLGVAPIEPQI
Protein: Putative pre-16S rRNA nuclease (EC 3.1.-.-) (P0A8I1)
Organism: Escherichia coli (strain K12)
Function: Involved in the processing of the 5'-end of pre-16S rRNA during 70S ribosome maturation (processing does not occur on total cellular RNA off the ribosome); may be a nuclease. A temperature-sensitive yqgF mutant no longer grows when Rho or NusA are overproduced, and has reduced transcription of genes encoded downstream of Rho terminators; transcription increases again in the presence of the Rho inhibitor bicylomycin.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}.
Interaction partners:
- UPF0301 protein YqgE
- Crossover junction endodeoxyribonuclease RuvC
- Glutathione synthetase
- Ribosomal RNA small subunit methyltransferase E
Sequence:
MSGTLLAFDFGTKSIGVAVGQRITGTARPLPAIKAQDGTPDWNIIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVEVKLHDERLSTVEARSGLFEQGGYRALNKGKVDSASAVIILESYFEQGY
Protein: Ribosome production factor 2 homolog (Brix domain-containing protein 1 homolog) (Ribosome biogenesis protein RPF2 homolog) (Q9UUG1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Ribosome biogenesis regulatory protein homolog
- Probable rRNA-processing protein ebp2
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein rlp24
- Ribosome biogenesis protein erb1
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein brx1
- Probable nucleolar GTP-binding protein 1
- Ribosome biogenesis protein nsa2
Sequence:
MLRQVKPKNARTKRALEKREPKLVEGAKTAIFLRGNATSQISLDVLGDIHALKKPFSVNFQKKNNILPFEDASSLEFFSEKNDAALAVMATHNKKRPHNLTWVRFFNYRVLDMIELGIVNYKSIQSFSATPIVPGTKPMILFQGPVFDAHPTYRHIKSLFLDFFRGEPIQKLDSAGLSYVIVVSAAEAQEDETKPLPLVHFRVYGTKLLKTKTNLPRVELEEMGPRIDFNIRRVQPAESDVLEEALKKPKTQEPKPKKNVDVDIIGNKVGRIHVDQQDLGNLQTRKMKGLKRSVEEREDSENEEVEIEEDVISDASE
Protein: Histone deacetylase 14, chloroplastic (EC 3.5.1.-) (N-acetylserotonin deacetylase) (Q941D6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates lysine acetylation levels of plastid proteins related to photosynthesis. Involved in the regulation of the activation state of RuBisCO, which is controlled by lysine acetylation of RuBisCO activase under low-light conditions. Associates with alpha- and beta-tubulins and deacetylate alpha-tubulin. Does not seem to be required for the cellular patterning in the root epidermis. Involved in the regulation of melatonin biosynthesis by catalyzing the deacetylation of N-acetylserotonin to produce serotonin. N-acetylserotonin is methylated by acetylserotonin O-methyltransferase (ASMT) to produce melatonin (N-acetyl-5-methoxytryptamine) (Probable). Deacetylates melatonin to produce 5-methoxytryptamine. In vitro, deacetylates N-acetyltyramine and N-acetyltryptamine to produce tyramine and tryptamine, respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:22404109}. Cytoplasm {ECO:0000269|PubMed:22363501, ECO:0000269|PubMed:22404109}. Plastid, chloroplast stroma {ECO:0000269|PubMed:29061669, ECO:0000269|PubMed:29247559}. Mitochondrion {ECO:0000269|PubMed:29061669}.
Interaction partners:
- Histone deacetylase 17
- Putative histone deacetylase 10
- NAD-dependent protein deacylase SRT2
- High mobility group B protein 9
- NAD-dependent protein deacetylase SRT1
- Histone-lysine N-methyltransferase SUVR3
- High mobility group B protein 10
- Putative high mobility group B protein 11
- High mobility group B protein 15
- Histone deacetylase HDT4
Sequence:
MSMALIVRPFFVPGSAGISGSRNICKKNQWRKYLLKPSGSSINCSFSTEKNPLLPSIQQLADARLIYSVSAALGHNKESHPECSARVPAIVNALEMNELTPKFRGSQILELANFKTATVEDIANVHDKAYVFGLEKAMDEASDSGLIFIEGSGPTYATSTTFQDSLIAAGAGMALVDSVIAASRNSVDPPIGFALIRPPGHHAVPKGPMGFCVFGNVAIAARHAQRTHGLKRIFIIDFDVHHGNGTNDAFTEDPDIFFLSTHQDGSYPGTGKISDIGKGKGEGTTLNLPLPGGSGDIAMRTVFEEIIVPCAQRFKPDIILVSAGYDAHVLDPLANLQFTTATYYSLAKDIKRLAKEVCGGRCVFFLEGGYNLESLSSSVADSFRALLGEDSLASEFDNPAYLYDEPMRKVRDAIQRAKSIHCL
Protein: Retinol-binding protein 4-B (Plasma retinol-binding protein 2) (PRBP-2) (Plasma retinol-binding protein II) (PRBP-II) (P24775)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: RBP delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.
Subcellular location: Secreted {ECO:0000269|PubMed:1740159}.
Interaction partners:
Sequence:
SDCQVSNIQVMQNFDRSRYTGRWYAVAKKDPVGLFLLDNVVAQFSVDGSGKVTATAQGRVIILNNWEMCANMFGTFEDTPDPAKFKMRYWGAAAYLQSGNDDHWVIDTDYDNYAIHYSCREVDLDGTCLDGYSFIFSRHPTGLRPEDQKIVTDKKKELCFLGKYRRVSHTGFCESS
Protein: Acetyl-CoA hydrolase (EC 3.1.2.1) (Acetyl-CoA deacylase) (Q5BD33)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Malate synthase, glyoxysomal
- Acetyl-coenzyme A synthetase
- homocitrate synthase
- Aldehyde dehydrogenase family
- aldehyde dehydrogenase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase ALDH
- aldehyde dehydrogenase
- acetyl-CoA C-acetyltransferase
- Aldehyde dehydrogenase
Sequence:
MSASALLRSRVRRPSYLNKIAKAEDLIDLFPNGSYIGWSGFTGVGYPKKVPTALADHVEKNGLEGKLKYTLFVGASSGAETENRWARLNMIDRRSPHQVGKEIAKGINNGQIKFFDKHLSMFPSDLTYGWYTLNKPKNRIDVAVIEASAITEDGGIIPGASVGASPELVQMADKVIIEVNTASPSFEGLHDITMSELPPNRKPYLILQPEDRIGTPHIPVDPEKVVAIVESDYPDQTQPNSPEDANSQAIASNLIEFLKHEVKHGRLPPNLLPIQSGIGNIANAVIGGLSKGGADFTNLKVWTEVLQDSFLDLFDSGNLDFATATSIRFSPDGFKRFYDNWERYAGKLLLRSQQVSNSPEIIRRLGCIGMNTPVEVDIYAHANSTCVMGSRMLNGLGGSADFLRSSKYSIMHTPSVRPSKTDPTGVSCIVPFATHIDQTEHDLDVIVTEQGLADVRGLSPRERARVIIKKCSHPDYTPILTDYLDRAEFECLKKGMAHEPHLLFNAFKMHKNLQENGTMKISNWD
Protein: Uncharacterized protein TP_0004 (O83050)
Organism: Treponema pallidum (strain Nichols)
Interaction partners:
- DNA replication and repair protein RecF
- Beta sliding clamp
- DNA gyrase subunit A
- DNA gyrase subunit B
Sequence:
MNNGVNKLSDLLVLTTEYIQASYETEAFDAHREWVCIVGNPVALHSTLVDIRNGKVVVKVTHPGWAQYLLLKKDEIVHALRRRYPSLGVTGMSTYVDSTSRTPSAKKDMQGLSVSEKQTRPVPELAEVFEQLRTLFQVKTEEPSH