wanglab/gogpt-training-data huggingface dataset:
Protein: RNA helicase (EC 3.6.4.13) (F4HYJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQLYSAIFRGHIRPNAVVGAASMFIQHNSIQLHRSPKLLLRPSSVVRSLHCRRSGGLVTHSQRSRVLCVKAARGDASSSTLGIEWRAANLPYFQRQNSGYGRIAYNDYESSDESDRDVGSSQSQQMAGSTLDNIDQWRFKLTMLLRNKEDQEVVSRERKDRRDFDHISALATRMGLHSRQYSKIVVISKAPLPNYRPDLDDKRPQREVVLPFGLQSEVDAHLHSFLDQKKTLIPEMPRQNSSESLANGYGNYETPETVMQNSLARERILRPRSLQLKSKQQQWVDSPEGQKMVGFRKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMHIPGFTYPVRAHFLEDYLETSGYRLTTYNQIDDYGEEKTWKMQKQAQFKKRKSLISSAVEDALEAADFKGYNFRTRDSLSCWSPDSIGFNLIENVLCHIVKGERPGAVLVFMTGWDDINSLKNQLEAHSLLGDPNKVLLLACHGSMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVMPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFLSRALQPPEALSVQNAVEYLKIIGALDDDENLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFLMPFDKKDLAETARSKFSGRDYSDHLTLVRAYNGWKDAERTHSGYDYCWKNFLSSQTLKAMDSMRKQFFNLLKEASLIDNIEGCSKLSHDEHLVRAIICAGMFPGVCSVVNKEKSITLKTMEDGQVLLYSSSVNGNVPMIPFPWLVFNDKVKVNSVFLRDSTAVSDSVLLLFGDKISSGGFDGHLKMLGGYLEFFMKPTLAYTYLSLKRELDELIQNKLVNPKLDIQLYDKLMTAIRLLVSEDQCEGRFVYGRKALSPTPAKKLKDVGAQLQNSGGENNKNQLQTLLARAGHGSPVYKTRQLKNNQFRSMVTFNGLDFMGKPCGSKKNAEKDAAHEALLWLQGESKSSLNDLNHMSMLLKKNKKRVGRLHKKKSREVLTDEILS
Protein: Probable complex I intermediate-associated protein 30, mitochondrial (NADH ubiquinone oxidoreductase assembly factor 1) (Q18726)
Organism: Caenorhabditis elegans
Function: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Required for normal growth and reproduction.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- Evolutionarily conserved signaling intermediate in Toll pathway
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- NADH-ubiquinone oxidoreductase chain 3
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
Sequence:
MITSFPVRNFLPRVTITSCAFFSKESTSAAGTVAEKKESELQKFAGKSNLLEKKKVGIFGTSTVPINTNFPNPKGVVDYDPDFSIKELVAELPNTRKTQGAKLSEEIKNAFNSVSIEKTELLEDIGFVRHNEARVDYRFDTQEKLDLWKIGCDSDWKEGFSTCSLVNSDRGTAVFSGNISTKVLKDGRVERAGWASMKLEDRKAFNRKKFLSKWRNFSHLLLKVRGDGRSYKIMLHSPLSMDFTWGDSFSHPLHTHGGPYWQYEKIPFSKFFHTVAGRIQDRQYRVNLEDTSSIGIVLMDRIDGDFRLEIDYIGVYNDTTHVEDFAYETYTLPVFNTHGF
Protein: Uncharacterized protein (Q382X6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDIGNFDSRPASILEYIKRNPSSALSTRWVFDLPEAEQEECLVKMIENAAFPETWMVYFDYAERNRITVTDDIALEAIHSVGLDPHSAPLWLKVIDICCGEGKKRELFHMALQVPLYQQNMVYKVYRTFESDAAKRSGEKVGNHLALSDINHFSEMLKTEPRWPDRFVDSSACSSYQRNVLCSQWNILLQTLLGRCDQDSMRELHLRRAELAFRQMCSQFPNEDVCWYTYACFMAVKMNDHVQAMEILKRGRASSSEVSVALWLAEPLLNRDFQLEQPLTKDKVNAQLFIQRLYANTARNFLQNKKCLRDIGKRAVAENVSDWKLYHQWASAERSVLRDQSMTSKIYERGISCVSKSPKDAILFSNEAMKYHLWRQDERQVVGYSELQIELLSTSQHDGWVRAGWNYLVNAESMIGLPSLPKTLNRRAERNNDLPYKSIIERYRVGSYIPCADRDLDWIEFVNDITRIRREEQEHIFQAVTPIKNSSISVPAPRKFVGASPDTSLWCPIEMAPRHEGVSIKDPDEIVGPRYLRGRLVYKLTLDDKTAARLRREEYMRGKREGMDEKHTPAGAAQSALQLLVERLGAKRWNETQLRLCRLVSAEWLMNTLAMGDLDLAKKKA
Protein: P-type phospholipid transporter (EC 7.6.2.1) (Q6PSM0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MELEEDLNGRADKNFSKMGKKSKKEKKEKKPAVSVLTMFRYAGWLDRFYMLLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNNRSMSFYNATDIYAKLKDEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIELGNEACESKDGIDNVDMSSKDSGSSLIRRRSTRKSIRGPHDQDGELSTKEALDDDVPPASFWRILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEGNVKFNGVMFNYPTRPNIPVLQGLSLEGKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS
Protein: Ribonucleoside-diphosphate reductase small chain (EC 1.17.4.1) (Ribonucleotide reductase small subunit) (P36603)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Nucleus {ECO:0000269|PubMed:12695334}. Cytoplasm {ECO:0000269|PubMed:12695334}. Note=Localization to the cytoplasm is CSN- and checkpoint-dependent and is required for an efficient DNA damage response.
Interaction partners:
- Ribonucleoside-diphosphate reductase large chain
- Adenylate kinase
- Nucleoside diphosphate kinase
- Guanylate kinase
- Uridylate kinase
- Thymidylate kinase
- Golgi apyrase
- Pyruvate kinase
- Adenylate kinase isoenzyme 6 homolog
- DNA replication licensing factor mcm2
Sequence:
MGLEHLEEFSYPKEHGEEVEYDSEQGVRKIYVKSIKETFNFDNVSEEEKQEGGDYYLGKKEDELDEVVLRPNPHRFVLFPIKYHEIWQFYKKAEASFWTAEEIDLSKDLVDWDNKLNADERYFISTVLAYFAASDGIVNENLLERFSSEVQIPEARCVYGFQIMIENIHSETYSLLLDTYIREPKEKQRHFDAILTMGSIKAKAKWALRWINDEDSTYAIRLVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELICRDEGLHTDFACLMFSHLKHRPGRKVVEAIIVEAVDIEKEYFTDALPVSLLGMNKDLMCQYIEFVADRLLVALGNDKYYNVTNPFDFMENISLAGKTNFFEKKVSDYQIAGVMSGTKRAEKDDHTFTIDEDF
Protein: Neuroligin-2 (Q62888)
Organism: Rattus norvegicus (Rat)
Function: Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Promotes clustering of postsynaptic LHFPL4 (By similarity). Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane {ECO:0000269|PubMed:29742426}. Presynaptic cell membrane. Note=Detected at presynaptic membranes in retina, and at postsynaptic membranes in brain. Detected at dendritic spines in cultured neurons. Colocalizes with GPHN and ARHGEF9 at neuronal cell membranes.
Interaction partners:
- Neurexin-1
- Neurexin-3
- Neurexin-2
- MAM domain-containing glycosylphosphatidylinositol anchor protein 1
- Disks large homolog 4
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Gephyrin
- SH3 and multiple ankyrin repeat domains protein 3
- Neuroligin-1
- Neuroligin-3
Sequence:
MWLLALCLVGLAGAQRGGGGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDGPLTKKRDEATLNPPDTDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVATLNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALFTDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAFAALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRV
Protein: Nipped-B protein (SCC2 homolog) (Q7PLI2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a structural role in chromatin. Involved in sister chromatid cohesion, probably via an interaction with the cohesin complex. Participates in the transcriptional activation mediated by remote enhancers on genes such as cut and Ubx, possibly by alleviating the cohesin-mediated blocking of enhancer-promoter communication.
Subcellular location: Nucleus {ECO:0000269|PubMed:15060134}.
Interaction partners:
- Structural maintenance of chromosomes protein
- FI11703p
- MAU2 chromatid cohesion factor homolog
- Structural maintenance of chromosomes protein
- LD34181p
- Precocious dissociation of sisters 5, isoform A
- Protein wings apart-like
- Stromalin-2
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein
Sequence:
MGERDNPTVPVTTLAGLTSTSDLLSELPVADSLQSAASLNKSLLFHALVANESSNLLSMRNENLVRQLVTAIERTNSDNIELIHCPVQDTATNCSTYPELLQGIYHFRPAVFNTSIKIHSPDQHTANARLEAKKMQIDSYSIPECYASPTNLSISNEHQLQDAQACFNQLTSMTSKEILEEFSQINFKENATEKDKIDVIENSDLNVTKILSQNTLKKKSNTPERSTVQSIQEQFFIQQQEANYNLKHDLNQVSTNVGQIQNISDTFPQEPSNFNLNSVNIPNMLYVQSPPFTESEPTQAHHSSIEYLKKKKSQILDVSILNRQQVLENTSLHIINKSSTYQTNQNVSTTTSTSTSSSGKSQVRVCINRLSIEDSRLMQQSIKKFVQKSPELARSMGLLQETCQQQHENLNIIPTSAEECVLESRASSTNNTVKIPIDTFSTIKADEKRSAKRKLAISIGDIPPEQIFSKPKMRRVERITPLSNTKCVKEEVTRSQTYQQFIRNMDHIIEILDDSESPNFDSEDVDETIECISSKLLNSMSTDVAKLKAKQALDSIPKNKLTLLINYAMRNVYLARNYFAGTEDEDEFVDDEVIEKLLNAMDACLLICNIYSTVSDLQFLQEDNVSHIIKFTQFQLRETIFPLHDPVYTAKSIKRTTHRKKIKSHQAQNRSMQLFYLKTVELLKVFVTLFDKCVFVDTIVLPLSTLAIEPFFVDNIETLQFVCLELVTTIFRKERYDKIRNSILGDILTSIDRLPSSKKNLRPYKLTNNGGNIQMVTALVLQLIQCATILPDSLCDNGKFSNKPQEGNTFDEEGKKLLQPSQDLLVLQKYDVAVSIGGNFLTTFLNKCKSRSNETDFRPLFENFIHDLLATVNKPEWPASELLLSLLGTMLVRYVSDKGIEQSIRLVSLDYLGIVAARLRKDTVESRCRVNIIDSMIQSIKLEQEKEGDVTSNNDQFDLEPEEQRTDFLQKILLDFLAVNAQEENLIWDYARHFYLAQWYRDVIYQRRRINDGKKGLAFRKSKIRNNRRTNGDYLDTSDSGSCDESDTDTNKKRIHCVDSNDFELNINIYKALEARKQYFINKIKPFSVFGEQNHSSNQHIKTYIDYNNAQLIAQYLATKRPFSQSFDGCLKKIILVVNEPSIAVRTRAMKCLANIVEVDPLVLKRKDMQMGVNQKFLDTAISVREAAVDLVGKFVLSNQDLIDQYYDMLSTRILDTGVSVRKRVIKILRDICLEYPDFSKIPEICVKMIRRVHDEEGIQKLVTEVFMKMWFTPCTKNDKIGIQRKINHIIDVVNTAHDTGTTWLEGLLMSIFKPRDNMLRSEGCVQEFIKKNSEPPMDIVIACQQLADGLVDRLIELEDTDNSRMLGCITTLHLLAKVRPQLLVKHAITIEPYLNIKCHSATAAKFICAVADILEKVVPLVNNASESFLASLEEHLMLLVVSRNQAEVTSCVSCLGALVNKITHNFKLIRDCFQKFYRVLDVSRSQVIQGNNSVDNIYTPSFRRSLFTIGILMRYFDFKSPIALGETNDGLPVSICEDVFHCLMFFCRCTNQEIRKQALISLGSFCVLNDGYLTRSELKNLYCEILSSIANDAGFKIICMRNIWIYLTESEMFMHNKEKEWEKQSKHEDLKEMNDVSSGMASRIIQLYLEEILECFLNRDDTVRLWAVKVIQIVLRQGLVHPVRMVPYLICLSTDHRIESAHRADALLKDIDKTYSGFVNMKVQFGLQLCFKLQKILQINNRGKLEIIRGYASRGPDNTTTALNDFLYTLLRTTKPQRRALVQTVTKQFDDQKTSLQQMLYIADNLAYFPYVVQDEPLYLIHQIDLLISMAGTHLLATFKEHIKPSDKEGDVLEDDDDVEDPEVLFNRLPEDLTEIIKCITSAQACMLLLILKDHLKEMYAITDSKISRYSPSEQKLYEKAVTRKSVNDFNPKTTIDVIKKQMSQEKLSTDINFTLTKEEKLDLVVKYLDFKQLMLKLDPDDGDSDADESRDKTMLNISASSDGVAFSSSAKNSHSACDGYSLTVTDVVDVPMSHIAKASMLTSKPSGRKTNPVRTKKKRRKIDSTDDETSDAEYA
Protein: SWI/SNF complex subunit SWI3B (AtSWI3B) (Transcription regulatory protein SWI3B) (Q84JG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. May play an essential role in the transition from the vegetative to the reproductive phase of development. May be a positive regulator of ABA signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:16055636, ECO:0000269|PubMed:19033529}.
Interaction partners:
- Chromatin structure-remodeling complex protein BSH
- Actin-related protein 4
- At3g01890
- SWI/SNF complex component SNF12 homolog
- Armadillo repeat-containing protein LFR
- SWI/SNF complex subunit SWI3C
- Chromatin structure-remodeling complex protein SYD
- Protein phosphatase 2C 16
- SWI/SNF complex subunit SWI3A
- Probable ATP-dependent DNA helicase CHR23
Sequence:
MAMKAPDPGGSGEILPSTPSLSETTSGGAAAASKSAQLPSSSSDIDNIHVPSYSSWFSWTDINDCEVRSLPEFFDSRSSSKNPKFYLYLRNSIIKQYRDDHPRKISFTDVRRTLVSDVVSIRRVFDFLDSWGLINYNSSASAKPLKWEEKEAGKSAGDAASEPATTVKETAKRNCNGCKAICSIACFACDKYDLTLCARCYVRSNYRVGINSSEFKRVEISEESKPEWSDKEILLLLEAVMHYGDDWKKVASHVIGRTEKDCVSQFVKLPFGEQFVKESDSEDGLEMFDQIKDSDIPESEGIDKDGSSPNKRIKLTPLADASNPIMAQAAFLSALAGTNVAEAAARAAVRALSDVDYEADKNASRDPNRQDANAASSGETTRNESERAWADAKSLIEKEEHEVEGAIKETVEVEMKKIRDRIVHFEKLDLEMERSRKQLEEVRNLLFVDQLNIFFHTRKARKTEDRIEC
Protein: Histone H2A.v (H2A.F/Z) (H2A.Z) (P08985)
Organism: Drosophila melanogaster (Fruit fly)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Acts as a Polycomb group (PcG) protein required to maintain the transcriptionally repressive state of homeotic genes of the animal throughout development. Required for histone H3 'Lys-9' methylation and histone H4 'Lys-12' acetylation, two modifications that are essential for heterochromatin formation. Also involved in DNA double strand break (DSB) repair. Essential for early development.
Subcellular location: Nucleus {ECO:0000269|PubMed:10801889}. Chromosome {ECO:0000269|PubMed:10801889}. Note=Widely distributed in the genome, irrespective of the transcriptional status or coding capacity of the sequence.
Interaction partners:
- TBP-associated factor 3
- Vacuolar protein sorting-associated protein 72 homolog
- YEATS domain-containing protein 4
- RuvB-like helicase 1
- Uncharacterized protein, isoform B
- Actin-related protein 6
- Histone H3.3A
- DNA methyltransferase 1-associated protein 1
- Histone acetyltransferase Tip60
- Brahma associated protein 55kD
Sequence:
MAGGKAGKDSGKAKAKAVSRSARAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKEETVQDPQRKGNVILSQAY
Protein: WD repeat-containing protein LWD1 (Protein ANTHOCYANIN 11-A) (AtAN11-A) (Protein LIGHT-REGULATED WD1) (WD repeat-containing protein AN11-A) (Q9LPV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Clock protein essential for the proper expression phase and period length of both the oscillator and output genes known to participate in photoperiod sensing. Required for the expression of APRR9, APRR7, and APRR5. Regulated by APRR9 and APRR7 at the transcriptional level, indicating the existence of a positive feedback loop within the circadian clock. May function to delay the expression of the morning genes until dawn approaches.
Subcellular location: Nucleus {ECO:0000269|PubMed:21357491}.
Interaction partners:
- Transcription factor TCP22
- Dual specificity protein kinase YAK1 homolog
- Protein REVEILLE 8
- Transducin/WD40 repeat-like superfamily protein
- Two-component response regulator-like APRR9
- Transcription factor TCP20
- Protein CCA1
- Protein LHY
- Protein REVEILLE 6
- Protein LNK1
Sequence:
MGTSSDPIQDGSDEQQKRSEIYTYEAPWHIYAMNWSVRRDKKYRLAITSLLEQYPNRVEIVQLDESNGEIRSDPNLSFEHPYPPTKTIFIPDKECQRPDLLATSSDFLRLWRIADDHSRVELKSCLNSNKNSEFCGPLTSFDWNEAEPRRIGTSSTDTTCTIWDIEREAVDTQLIAHDKEVFDIAWGGVGVFASVSADGSVRVFDLRDKEHSTIIYESSEPDTPLVRLGWNKQDPRYMATIIMDSAKVVVLDIRFPALPVVELQRHQASVNAIAWAPHSSCHICTAGDDSQALIWDISSMGQHVEGGLDPILAYTAGAEIEQLQWSSSQPDWVAIAFSTKLQILRV
Protein: Reticulophagy regulator 3 (Q86VR2)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress. When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins. Promotes ER membrane curvature and ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes. Required for collagen quality control in a LIR motif-dependent manner (By similarity). Mediates NRF1-enhanced neurite outgrowth.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33826365, ECO:0000269|PubMed:34338405}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes preferentially to endoplasmic reticulum tubules and sheet edges. {ECO:0000269|PubMed:33826365}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- 60S ribosomal export protein NMD3
Sequence:
MAEAEGVPTTPGPASGSTFRGRRDVSGSWERDQQVEAAQRALVEVLGPYEPLLSRVQAALVWERPARSALWCLGLNAAFWFFALTSLRLVFLLAFGLMIIVCIDQWKNKIWPEIKVPRPDALDNESWGFVHPRLLSVPELCHHVAEVWVSGTIFIRNVLLFKKQNPGKFCLLSCGILTFLAVLGRYVPGLLLSYLMLVTVMMWPLAVYHRLWDRAYVRLKPALQRLDFSVRGYMMSKQRERQLRRRALHPERAMDNHSDSEEELAAFCPQLDDSTVARELAITDSEHSDAEVSCTDNGTFNLSRGQTPLTEGSEDLDGHSDPEESFARDLPDFPSINMDPAGLDDEDDTSIGMPSLMYRSPPGAEEPQAPPASRDEAALPELLLGALPVGSNLTSNLASLVSQGMIQLALSGASQPGPSGAPAQRATRGFLRSPSSDLDTDAEGDDFELLDQSELSQLDPASSRSH
Protein: L-gulonolactone oxidase (LGO) (EC 1.1.3.8) (L-gulono-gamma-lactone oxidase) (GLO) (P10867)
Organism: Rattus norvegicus (Rat)
Function: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
Subcellular location: Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Interaction partners:
- Regucalcin
- Lactoylglutathione lyase
- Hydroxyacylglutathione hydrolase, mitochondrial
- 3-ketodihydrosphingosine reductase
Sequence:
MVHGYKGVQFQNWAKTYGCSPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQITVEAGILLADLHPQLDEHGLAMSNLGAVSDVTVAGVIGSGTHNTGIKHGILATQVVALTLMTADGEVLECSESRNADVFQAARVHLGCLGIILTVTLQCVPQFHLQETSFPSTLKEVLDNLDSHLKRSEYFRFLWFPHTENVSIIYQDHTNKAPSSASNWFWDYAIGFYLLEFLLWTSTYLPCLVGWINRFFFWMLFNCKKESSNLSHKIFTYECRFKQHVQDWAIPREKTKEALLELKAMLEAHPKVVAHYPVEVRFTRGDDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHWAKAHNCTQKDFEEMYPTFHKFCDIREKLDPTGMFLNSYLEKVFY
Protein: AT1G19000 protein (F14D16.15) (Homeodomain-like superfamily protein) (Putative Myb-related transcription activator protein) (Q9LMC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At1g26580
- Zinc finger CCCH domain-containing protein 22
- Receptor-like protein 31
- Telomere repeat-binding factor 4
Sequence:
MAAVSSSSETGDCGVTGKRDEIMLFGVRVVVDPMRKCVSLNNLSDYEKSSPEDEIPKIVTAGAGDGEDKNETDATVIVADGYASANDAVQISSSSGGRKRGVPWTENEHKRFLIGLQKVGKGDWKGISRNFVKSRTPTQVASHAQKYFLRRTNLNRRRRRSSLFDITTETVTEMAMEQDPTQENSPLPETNISSGQQAMQVFTDVPTKTENAPETFHLNDPYLVPVTFQAKPTFNLNTDAAPLSLNLCLASSFNLNEQPNSRHSAFTMMPSFSDGDSNSSIIRVA
Protein: Proton/glutamate-aspartate symporter (Glutamate-aspartate carrier protein) (Proton-glutamate-aspartate transport protein) (P21345)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the proton-dependent, binding-protein-independent transport of glutamate and aspartate.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02063, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1971622, ECO:0000269|PubMed:2537813}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02063}.
Interaction partners:
- Sodium/glutamate symporter
- Sel1-repeat-containing protein YjcO
Sequence:
MKNIKFSLAWQILFAMVLGILLGSYLHYHSDSRDWLVVNLLSPAGDIFIHLIKMIVVPIVISTLVVGIAGVGDAKQLGRIGAKTIIYFEVITTVAIILGITLANVFQPGAGVDMSQLATVDISKYQSTTEAVQSSSHGIMGTILSLVPTNIVASMAKGEMLPIIFFSVLFGLGLSSLPATHREPLVTVFRSISETMFKVTHMVMRYAPVGVFALIAVTVANFGFSSLWPLAKLVLLVHFAILFFALVVLGIVARLCGLSVWILIRILKDELILAYSTASSESVLPRIIEKMEAYGAPVSITSFVVPTGYSFNLDGSTLYQSIAAIFIAQLYGIDLSIWQEIILVLTLMVTSKGIAGVPGVSFVVLLATLGSVGIPLEGLAFIAGVDRILDMARTALNVVGNALAVLVIAKWEHKFDRKKALAYEREVLGKFDKTADQ
Protein: Wings apart-like protein homolog 1 (H2L0H5)
Organism: Caenorhabditis elegans
Function: Regulator of meiotic chromosome structure and function, playing a role in sister chromatid cohesion, possibly via antagonizing the coh-3/-4 association with axial elements in nuclei during late prophase, cohesin association with chromatin, DNA double strand break repair and polar body positioning following meiotic divisions during oogenesis. Regulates the morphogenesis and temporal assembly of axial elements to control the organization of meiotic chromosomes in pachytene nuclei and is also involved in meiotic chromosomal remodeling in late pachytene nuclei. Required for the removal of the cohesin component scc-1 from mitotic chromosomes.
Subcellular location: Nucleus {ECO:0000269|PubMed:26841696}. Note=Expressed in mitotic and meiotic nuclei, with low expression in nuclei during the early meiotic prophase stages leptotene and zygotene, and increased expression in late pachytene nuclei which then continues to remain high in diplotene and diakinesis oocytes. {ECO:0000269|PubMed:26841696}.
Interaction partners:
- Cnd1 domain-containing protein
- Structural maintenance of chromosomes protein 3
- Nipped-B-like protein scc-2
- Maternal uncoordinated protein 2
- Cohesin subunit scc-3
- Rad21_Rec8 domain-containing protein
- Rad21/Rec8-like protein C-terminal eukaryotic domain-containing protein
- Rad21/Rec8-like protein C-terminal eukaryotic domain-containing protein
- N-acetyltransferase ESCO2
- Structural maintenance of chromosomes protein 1
Sequence:
MSSDANSDDPFSKPIVRKRFQATLAQQGIEDDQLPSVRSSDSPDVPDTPDVPVNQLSSPPLSLPETLSEGNAETLQNLSDDSEPEMLSQSSTSSLNRRMEDSAIDPSRGTRKSQSRGFDYDPAGERTTAPVQKKKKDEIDMGGAKFFPKQEKKHVYTHKWTTEEDDEDEKTISSSSNRYSSRPNQPAVSARPRQPVYATTSTYSKPLASGYGSRVRHIKEANELRESGEYDDFKQDLVYILSSLQSSDASMKVKCLSAISLAKKCVSPDFRQFIKSENMTKSIVKALMDSPEDDLFALAASTVLYLLTRDFNSIKIDFPSLRLVSQLLRIEKFEQRPEDKDKVVNMVWEVFNSYIEKQEVGGQKVSFDMRKESLTPSSLIIEALVFICSRSVNDDNLKSELLNLGILQFVVAKIETNVNLIADNADDTYSILILNRCFRILESSSVFHKKNQAFLISHRSNILISSLAKFLQVILDRVHQLAEEEVKKYISCLALMCRLLINISHDNELCCSKLGQIEGFLPNAITTFTYLAPKFGKENSYDINVMMTSLLTNLVERCNANRKVLIAQTVKMVIPGHDVEEVPALEAITRLFVYHESQAQIVDADLDRELAFDEGGCGDEEEEEEGGDESSDEDGVRKDGRLDRNKMDRMDQVDVVHALQQVMNKASAHMEGSVIASYHALLVGFVLQQNEDHLDEVRKHLPGKNFQNMISQLKRLYDFTKATMAKRVESNSGFRAIERVIEYLERLE