wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription regulator (F4HVV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription regulator NOT2/NOT3/NOT5 family protein
- CCR4-NOT transcription complex subunit 11
- AT5g35440/MOK9_2
- Probable NOT transcription complex subunit VIP2
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- NOT2 / NOT3 / NOT5 family
- Carbon catabolite repressor protein 4 homolog 1
- RNA binding
Sequence:
MYSKTIENPDETSPRIMWALKRVSYSRGSTENPRRKSPSPVVPGISDLGFPYLMTPSKVAGHTRFLLHSFHDSDVDSIALQLSQFVDFGVETSIPVLKTCLDCFTARRSHPNSLQLEKVVSLLFKHVLKLSNLATLLPHALNDFELTQESVDDLTTTLNFSISENIGFALALTDFERLDAKTTGRNLLLAQIEQLCANTGQILSSELIHSVLSFLRKSEDLSMHLDSFLQFLSSAQPRDDFSFALTPMLAQQVHEAPVFRSMDFHTDSADNDLDAILAEIDKEVSVGDLMGELGCGFTADAQQCKEILSSFAPLGEATISRIVGNVSRTCADLEDNQTTFSTFTVALGSCIPTELPTPRSWNVDILVDTIKQLQAPGISWRKVIENLDHDGFDIPNMESFSFFMRIYKAACKEPFPLDAVCGSVWKNMDGQLSFLKHAISAPPEVFTFMHSPRKLVYIDNMHSQEQQLGLSNHAWLSLDLLDVLCQLAERGHAVLVSSLLQYPLTQCPRTLLLGMTHIKTAYNLIQREVVSAILPVIITSPQDSGFIHNLWHQNAELVLWGIIDAQHLKADSMLRIIEICHELKILSVVLESVPVSSSIRLAVLASLRGLLDIENWLPNCLYMYKDLFAEECLKFVKNVHFSESDDFRAKIFHPSDPLSDLHLEATTSLLKVLKAHDNAITSSQLVEEIEKVNAAILDCNPKLQNGEAKDSSAPNAYGDDVEAEANAYFHQMFSSHLSVDAMVQMLSRYKESLVPREKLIFECMIANLFEEYRFFPKYPERQLKIASILFGSVIKHQLISSLTLGMALRLVLDSLRKPADSKMFLFGSKALEQFVNRLVELPQYCNHILQISHLRSTHPELVTVIEQALSRISSGNLESDASVSHPGPSQSFPGNGELSGSGIGQPALQLSSPLQLQQKNEVPSVPSNEAKPLLPSLSTTSVDVSVNPKNPGIPTSSSTSTGFVRPARATTSTRFGSALNIETLVAAAERRENAIEAPPSDVQDKVSFIINNISTTNIESKGKEFAEILPQQYYPWFAQYMVMKRASIEPNFHDLYLKFLDKVDSKLLFKEILQNTYENCKVLLGSELIKSSSEERSLLKNLGSWLGRLTIGRNYVLRAREIDPKSLIVEAYEKGLMIAVIPFTSKVLEPCQNSIAYQPPNPWTMAILGLLAEIYSMPNLKMNLKFDIEVLFKNLGVEMKEVVPTSLLKDRKREIDGNPDFSNKDPGVTQISQPQMIPEPKTISPLKQIDLPLDVANSPNTDVPSKLLSQYVAPQRVYTNTLMDEEKVATLGLPEQLPSPQGLFQSTPSPLFSISQLSAALPNIGNHVVINQKLSAFGMHFPFQRVVPLAMDRAIKEIVSGIVQRSVCIACQTTKELVLKDYALEPDESRIYNAAHLMVASLAGSLAHVTCKEPLRTSISGHLRNSLQGLNISNDALEQIVQLVTNDNLDLGCAAIEQAATEKAIQTIDADIAQQLLLRRKHRDGAGSSFFDPNILSQNSVSFIPESLRPKPGHLSLSQQRVYEDFVQHPWQKQSTQTSHGLSAASSSSGDVALGSGYGPVSGKVASEFLSNAGNARMDMVSRPSDISVDGFESSPVSLLSSQVDPAGDSSSLQFTKSLPTSELNLAESSDAATKETGTSLQTLTSAATMERLGASNITQPSLSTRDALDKCQIVTQKMEELVANNAGDDEIQAVISEVPEIILRCISRDEAAFAVAQKAFKALYENASSNLHVSANLAILVAIRDVCKRVVKELTSWVIYSEEDRKLNKDITIGLIQRELLSLAEYNVHMAKHLDGGRNKTATDFAISLLQSLVTEESSVISELHSLVDALAKLASKSGSSESLQQLIDIIRNPVTNTAGLSDSSTGNDNNDRQKDEKVACNTTNTEESTSLDYVESDPAGFQNRVSTLFKNWYQICELPGANETACSQYVLHLHQTGLLKGDDTTESFFRILLELSVAHCISSEDINSGAVQSPQQPQSPSFLIIDMYAKLVFSILKYFPEQESSSRLFLLSEIMADTVRFIQKDAEDKKTSLNSKPYFRLFINWLLDLCSLDPGTDGANFQVLTAFANAFHALQPLKIPAFSFAWLELVSHRSFMPKLLTVNGQKGWPYVQRLLVDLLQFLEPFLRNAELGGPVHFLYKGTLRVLLVLLHDFPEFLCDYHFTFCDVIPSSCIQMRNIILSSFPRNMRLPDPSTPNLKIDLLPEIVEAPCILSEVDAALKAKQMKNDVDEYLTSRQQNSTFLSELKTKLLLSSSEASSAGTRYSVPLINSLVLYTGMQAIQQLQAGETQAQNVVALQMFKYLSMELDTEGRYLFLNAIANQLRYPNNHTHYFSFIMLYLFFESDQEIIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPRYSFWKQAFIRCAPEIEKLFESVARSCGGLKPVDEGMVSGGWVSDNSH
Protein: Antitoxin HipB (P23873)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin HipA. Also neutralizes the toxic effect of non-cognate toxin YjjJ. Binds to operator sites with the consensus sequence 5-'TATCCN(8)GGATA-3' to repress the hipBA operon promoter; binding of HipB(2) to DNA induces a 70 degree bend. This forces HipA dimerization, which blocks HipA's active site and thus its toxic action. May play a role in biofilm formation.
Interaction partners:
- Serine/threonine-protein kinase toxin HipA
- Antitoxin HigA
- mRNA interferase toxin RelE
- Antitoxin MqsA
- Antitoxin YefM
- Antitoxin DinJ
- Endoribonuclease toxin MazF
- mRNA interferase toxin YafQ
- mRNA interferase toxin MqsR
- Toxin YoeB
Sequence:
MMSFQKIYSPTQLANAMKLVRQQNGWTQSELAKKIGIKQATISNFENNPDNTTLTTFFKILQSLELSMTLCDAKNASPESTEQQNLEW
Protein: Mitochondrial-processing protease subunit alpha (A0A1D8PN84)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- mitochondrial processing peptidase
- Cytochrome b-c1 complex reductase subunit, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex catalytic subunit, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- 4Fe-4S ferredoxin-type domain-containing protein
Sequence:
MLSRRTITRKLNKGVSKSLLSFARYNHSITSTTTPASSQPHIELTTFANGLRLITDSTPGHFSAVGAYIDAGSRYEDPKAPGLSYLRDRLSWKSTEDFTGQQMLENLSKLGGNYMSSAQRESMIYQASVFNKDIDRMVGMIGQTIRYPIFSDQEFQEALQTAEYEVAELAYKSDLYLPEELHTVAYKENTLGLPLFIPQERIPLVSKSDVIDYNNKFFQPQNTVIAMVGVPHEYALKLIMENFGDWANTTTTKPNPGIKNYTGGEISLPYTPPLYANLPELYHIQIGFETTGLLNDDLYALATLQKLLGGGSSFSAGGPGKGMFSRLYTKVLNKYPFVENCMSFNHSYIDSGIFGITLSLVPEAAHVSSQIIAHELSQLLVTEESQGGMNAKEVQRAKNQLISSLLMNVESKLARLEDLGRQIQCQGKITTIDEMVDKINRLTIKDLQNVAEKVLTGKVITSNGGTSLGLPSIVMQGERETFGDVEFILRRYGLGNYKGPEITEPRDFSSNQNEKKKKSRWF
Protein: Protein YGP1 (GP38) (P38616)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cellular adaptations prior to stationary phase.
Subcellular location: Secreted {ECO:0000269|PubMed:10234784, ECO:0000269|PubMed:18434410}.
Interaction partners:
- Protein YRO2
- Uncharacterized cell wall protein SPI1
- Transcriptional activator HAA1
- 12 kDa heat shock protein
- Polyamine transporter 2
- Covalently-linked cell wall protein 14
- Restriction of telomere capping protein 3
Sequence:
MKFQVVLSALLACSSAVVASPIENLFKYRAVKASHSKNINSTLPAWNGSNSSNVTYANGTNSTTNTTTAESSQLQIIVTGGQVPITNSSLTHTNYTRLFNSSSALNITELYNVARVVNETIQDKSSAGAVVVANAKSLEAVSFFFSIIFDTEKPIVVTEDSAYAIPVANNKNATKRGVLSVTSDKLVYSGVFTPPTACSYGAGLPVAIVDDQDEVKWFFDASKPTLISSDSIIRKEYSNFTTPYGLLENGVPIVPIVYDGGYSSSLIDSLSSAVQGLVVVSSGSTNSTSSTIESTEIPVVYAQANTPLNFIDNKDVPKNAVGAGYLSPIKAQILLSIAAVNGVTSKSALESIFP
Protein: Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial (Q9CR63)
Organism: Mus musculus (Mouse)
Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized MT-CO2/COX and its copper center-forming metallochaperones SCO1, SCO2 and COA6. Probably facilitates MT-CO2/COX2 association with the MITRAC assembly intermediate containing MT-CO1/COX1, thereby participating in merging the MT-CO1/COX1 and MT-CO2/COX2 assembly lines.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9P0S2}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9P0S2}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX18
- Cytochrome c oxidase assembly factor 6 homolog
Sequence:
MIAPAVLRALRKNKTLRYGVPMLLLVVGGSFGLREFSQIRYDAVTIKIDPELEKKLKVNKITLESEYEKIKDSTFENWKNIRGPRPWEDPQLLQGRNPETLKPKTT
Protein: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha (OFOR1) (EC 1.2.7.11) (Q96Y66)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta
- 2-oxoacid oxidoreductase
- 2-oxoacid oxidoreductase
- ADP-forming acetyl-CoA synthetase
- Succinyl-CoA synthetase beta subunit
- Succinate--CoA ligase subunit alpha
- Succinate-semialdehyde dehydrogenase
- Pyruvate kinase
- isocitrate dehydrogenase
Sequence:
MRLSWVIGGAQGTGIDTAANIFGNAVASAGYYIYGNREYYSNIKGRHSYFSLTISDKRVRSNTQKIDILVSFDAETVFQHFYDVKDILIYNKAVETTKIDAVQSMEPELAERIKDFLTKQGYETTVKGALEYASKNNVTLIPVNYDEIAKKVADEMKVPLSVTERVKNIVGITISYKLLGLDVNYLIEAINSTFKQDLYRKMNELAVKDSYDIVESRYNLKPSSKERRRFWLDGNTAVAIGKIYGGVRFQSYYPITPASDESVYIEAHQDVLMEDPITGDKKKGTIVVVQAEDELAAINMAIGAALTGVRAATATSGPGFSLMVEGLGWAGMNEVPVVITYYIRGGPSTGLPTRTAQSDLIFPIFAGHGEFPKIVLASGDHAEAFKDAIWALNLAEKYQTPVIHLVEKTLANSYSTIPYEELELDKLKAERGKIVESGDISYKRFKFTEDGISPRAFLGKATMYYTGDEHNEEGHISEDVVNRTMMYEKRMKKLEVADKEIPEESRVKIYGDLNSRNLIITWGSPTGVLRDILEESNFDFTLLQIRMFSPFPKNLVSKLMEGRDKIITVEGNYLAQTSLLVKMYTGKDVTNSILKWNGRPFLRDELEEALIKVIKDGEKRVVLNGGI
Protein: Hapless 2 (HAP2) (Generative cell specific-1) (A4GRC6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes. Required for membrane fusion, but not for the initial adhesion between gametes. Inserts (via its extracellular domain) into lipid membranes (in vitro). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20335357, ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}; Single-pass type I membrane protein {ECO:0000269|PubMed:28235200, ECO:0000305|PubMed:20335357, ECO:0000305|PubMed:25655701}. Cell projection {ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25655701}. Note=In male gametes, detected both in cytoplasmic vesicles and on cell projections called mating structures at the cell membrane. {ECO:0000269|PubMed:25655701}.
Interaction partners:
Sequence:
MCRAIAVALIVYLAQHYILAHAEVIASGRLEKCVVDGVTEELDCQEKVVVTLTVGNGQSLQTEALEFSLSCLNSPDGRCPCSCSAADPTCACRDLAAPLRVSLTKSPLWASYPLQYLSSFNWKPLEVILRPSNKVCKDGDWEDSPTCGWFSQGGVRVADSQGFCCECSSSQVWDDTFGSSKERTRANLDCDFWSDPLDILIGRKPVSAHCLTFDPQWYSGYELGAASLQFEIAITVEVPTAPSPTTATTSATPRTNNSSSANSTNSTNSPAPQFLSPPAPSTREVLHLGPSVPLASSASRLLSAKLLGDLAMYTQLPAISNQVLMVPQPPAAAAATGSPLDATLATNRSAWMLLDKTMLSMDGLACDKVGTGFSAFRYQPSGCGRAPQACLSGQLKDLWEADLARIADGRVPLYMITRFTGGSDTTLQSFSGGPLSFALPVTSHSQSLVTLSVAADGVRLVTNRSPGKITGAAVCRFAGTSCGGFEAVAARGYIYVNITNTGRLDSDYTLTVSNCSSNVRPIEARTLAVRAGSAASLDPPMELYVEDQAAAAARTCTVSLYDSVGAVTDSLTLSFYTNATQLVVKPSGGYNGTGDGAGVKRNGTDCSTACTNPIDVLCFVTKKCWSKFGRLLGIIGGALVGLGLLAVALKFGWLASLAASCCGGGGGAAAGGAGGGMGLGTGGGGGCFGGGQQQQQLPPAASHAMSPPQQQQRSHAEVAAGAAVAGAGAAGAAAAVLGAKHGGGGGGARGKQQHADTRHLQDRDSRAIDGGASIGSSSAGGSSSLSSYSQPREAGGRLLQPPAAAVFVPEGGGGGAAGDEGARAQSSDWDARGRSPRVADEHGSPRQRYDGVRQSPYMVSANPYDGWYDGGSGGGGGGGGGGYGREAPPPQGPPPHPVGAPPPPPRRRSLWERMWLQRPGGGGGGGGGGGGGGGGGSGGGVDQHGGRSCADAARRGGGGPGGMRGVEGLMSNGGRPNGPHPHAPPPPPPPQQQQQQQRQRRSFLESLTAMMTLPWGGGREEEAGGDRRGGGRGGAAAAHGGRGAGGGRGHPPSIGSPPPGPLQPPEYGPQGGQARRWGAGGGRGGVGGDGGGGGVGAAAYVQLSTGGRGGGGGGGRGRGGGREGPTWHNPVYDWQAPPK
Protein: Adenosine deaminase 2 (EC 3.5.4.4) (Cat eye syndrome critical region protein 1) (Q9NZK5)
Organism: Homo sapiens (Human)
Function: Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity.
Subcellular location: Secreted {ECO:0000269|PubMed:15926889, ECO:0000269|PubMed:20147294, ECO:0000269|PubMed:20453107}.
Interaction partners:
- Adenosine deaminase
- Adenosine kinase
- Purine nucleoside phosphorylase
- 5'-nucleotidase
- 5'
- 5'
- Cytosolic 5'-nucleotidase 3A
- Cytosolic purine 5'-nucleotidase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Deoxycytidine kinase
Sequence:
MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK
Protein: Terminase small subunit (EC 3.6.4.-) (DNA-packaging protein Nu1) (Gene product Nu1) (gpNu1) (P03707)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: The small subunit is responsible for the binding to multiple recognition elements within the packaging initiation site cos. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (binding to packaging sequence cos), and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging) (Probable). The terminase binds, cooperatively with the host factor IHFA/IHFB, to the cos site at the junction of adjacent viral genomes in the concatemeric DNA. The endonuclease and helicase activities of the large subunit cleave the viral DNA generating 5'overhangs of 12 bp in length (Probable). The terminase remains bound to the left end of the genome to be packaged, forming a stable DNA-terminase complex (Probable). In a reaction facilitated by the viral assembly catalyst gpFI, the DNA-terminase complex binds to the portal of the procapsid and the terminase packages the viral DNA into the procapsid until the next cos site on the concatemer reaches the complex (Probable). The downstream cos site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome (Probable).
Subcellular location: Host cytoplasm {ECO:0000305}. Note=The terminase lies at a unique vertex of the procapsid during viral DNA packaging. {ECO:0000305}.
Interaction partners:
Sequence:
MEVNKKQLADIFGASIRTIQNWQEQGMPVLRGGGKGNEVLYDSAAVIKWYAERDAEIENEKLRREVEELRQASEADLQPGTIEYERHRLTRAQADAQELKNARDSAEVVETAFCTFVLSRIAGEIASILDGLPLSVQRRFPELENRHVDFLKRDIIKAMNKAAALDELIPGLLSEYIEQSG
Protein: L-ascorbate peroxidase T, chloroplastic (EC 1.11.1.11) (Thylakoid-bound ascorbate peroxidase) (AtAPx06) (tAPX) (Q42593)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in hydrogen peroxide removal.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR2
- Monodehydroascorbate reductase 3
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione reductase, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- Monodehydroascorbate reductase, chloroplastic/mitochondrial
- NADPH-dependent thioredoxin reductase 3
Sequence:
MSVSLSAASHLLCSSTRVSLSPAVTSSSSSPVVALSSSTSPHSLGSVASSSLFPHSSFVLQKKHPINGTSTRMISPKCAASDAAQLISAKEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEEWPLRGGANGSLRFEAELKHAANAGLLNALKLIQPLKDKYPNISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEGRLPDAGPPSPADHLRDVFYRMGLDDKEIVALSGAHTLGRARPDRSGWGKPETKYTKTGPGEAGGQSWTVKWLKFDNSYFKDIKEKRDDDLLVLPTDAALFEDPSFKNYAEKYAEDVAAFFKDYAEAHAKLSNLGAKFDPPEGIVIENVPEKFVAAKYSTGKKELSDSMKKKIRAEYEAIGGSPDKPLPTNYFLNIIIAIGVLVLLSTLFGGNNNSDFSGF
Protein: Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Pentose-5-phosphate 3-epimerase) (PPE) (RPE) (P46969)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate (By similarity). Involved in the protective response to oxidative stress.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribose-5-phosphate isomerase
- Transketolase 1
- Transketolase 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- Xylulose kinase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Transaldolase
- Transaldolase NQM1
- Glucose-6-phosphate 1-dehydrogenase
- NADPH-dependent aldose reductase GRE3
Sequence:
MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCHMMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
Protein: 1,4-alpha-glucan branching enzyme GlgB (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Glycogen branching enzyme) (BE) (P07762)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Interaction partners:
- Glycogen phosphorylase
- Glycogen synthase
- Glucose-1-phosphate adenylyltransferase
- Glycogen debranching enzyme
- 4-alpha-glucanotransferase
- Maltodextrin phosphorylase
- Phosphoglucomutase
- Cytoplasmic alpha-amylase
- Periplasmic alpha-amylase
- ATP synthase subunit beta
Sequence:
MSDRIDRDVINALIAGHFADPFSVLGMHKTTAGLEVRALLPDATDVWVIEPKTGRKLAKLECLDSRGFFSGVIPRRKNFFRYQLAVVWHGQQNLIDDPYRFGPLIQEMDAWLLSEGTHLRPYETLGAHADTMDGVTGTRFSVWAPNARRVSVVGQFNYWDGRRHPMRLRKESGIWELFIPGAHNGQLYKYEMIDANGNLRLKSDPYAFEAQMRPETASLICGLPEKVVQTEERKKANQFDAPISIYEVHLGSWRRHTDNNFWLSYRELADQLVPYAKWMGFTHLELLPINEHPFDGSWGYQPTGLYAPTRRFGTRDDFRYFIDAAHAAGLNVILDWVPGHFPTDDFALAEFDGTNLYEHSDPREGYHQDWNTLIYNYGRREVSNFLVGNALYWIERFGIDALRVDAVASMIYRDYSRKEGEWIPNEFGGRENLEAIEFLRNTNRILGEQVSGAVTMAEESTDFPGVSRPQDMGGLGFWYKWNLGWMHDTLDYMKLDPVYRQYHHDKLTFGILYNYTENFVLPLSHDEVVHGKKSILDRMPGDAWQKFANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASLDWHLLEGGDNWHHGVQRLVRDLNLTYRHHKAMHELDFDPYGFEWLVVDDKERSVLIFVRRDKEGNEIIVASNFTPVPRHDYRFGINQPGKWREILNTDSMHYHGSNAGNGGTVHSDEIASHGRQHSLSLTLPPLATIWLVREAE
Protein: RNP domain-containing protein (J9VJ75)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Interaction partners:
Sequence:
MEDDREMRGDEPMAPEAGDRYRRDDRDRSRSRERHSSRRDEDRYRSRRRSYSRSRSRSRTRSPHRHRHRSPSRSRSRSRDRRDRDRSRSRDRGERRSYREDRHGGDHRGSGRPRSPRRGSGRYGAPRQDWEKSVGGPMNAPASEAEAHAKVSKRENRLYVGNLAYDCNYKDLANFMERGGGKVVFSEVLTTPAGQSKGCGIVEFASQEEAQRAKAELSDKPFFGRSVFIREDREETARFGAPPIPGKIGIALGEARHFLGNQQPHGFHGHGPAIPNRNLFVGNLPLQASWQDLKDLMRQAGEVIRADIGFRPDGTPKGNGTVVFLNADDAKAAIEMFNGFDWFGNVLEVREDRFAHGGAFRGRGGFRGAFFPRGGFGFRGGFRGGFRGGFMGGGMGMGHMGMNAVAGGVGAGGAAAAAGGRNFSNDLYADYNGPEGGEGMAVDQVAPSGLEPIPAEPNQQILVRNLPWSTSNEDLVELFETIGTVTLAEILYSGGQSKGEGIVQFAETADAANASEKFMGWPYGGRALDVQFNPRWHEFSASAIKVPQA
Protein: Beta-adaptin-like protein (F4JXV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MAPPAASQRYPSPSQPSGKSEVSDLKTQLRQLAGSRAPGVDDSKRDLYKKVISYMTIGIDVSSVFGEMVMCSATSDIVLKKMCYLYVGNYAKGNPDLSLLTINFLQRDCKDEDPMIRGLALRSLCSLRVPNLVEYLVGPLGSGLKDNNSYVRTIAVTGVLKLYHISPSTCIDADFPATLKSLMLHDSDAQVVANCLSALQEIWSLEASHSEEACREKESLLSKPVIYYFLNRIKEFNEWAQCLILELAVKYVPSDSNDIFDIMNLLEDRLQHANGAVVLATVKVFLQLTLSMTDVHQQVYERIKSPLLTLVSSGSPEQSYAILSHLHLLVVRAPFIFAADYKHFYCQYNEPSYVKKLKLEMLTAVANESNTYEIVTELCEYAANVDIAIARESIRAVGKIALQQYDVNAIVDRLLQFLEMEKDYVTAETLVLVKDLLRKYPQWSHDCISVVGGISSKNIQEPKAKAALIWMLGEYAQDMSDAPYVLENLIENWEEEHSAEVRLHLLTAAMKCFFKRAPETQKALGTALAAGIADFHQDVHDRALFYYRVLQYDVHVAERVVSPPKQAVSVFADTQSSEIKDRVFDEFNSLSVIYQKPSYMFTDKEHRGPFEFSDEVGNISITPEASSDIVPAQQYEANDKDLLLGIDEKDENKGVSNNNGSAYTAPSLESSSNITSQMQELAISGPATSATTPQSFGFDDLFGLGLSTAPAPTPSPPLLKLNARAALDPGAFQQKWRQLPISLTQECSVNPQGIAALTVPQSLIKHMQSHSIHCIASGGQSPNFKFFFFAQKESEPSNYLTECIINTSSAKAQIKVKADEQSTCQAFTTVFETALSKFVSLTFDFVSLCY
Protein: N-glycosylation protein EOS1 (ER-localized and oxidants sensitive protein 1) (P53938)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in oxidative stress resistance and N-glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10649453, ECO:0000269|PubMed:17187761}; Multi-pass membrane protein {ECO:0000269|PubMed:10649453, ECO:0000269|PubMed:17187761}.
Interaction partners:
Sequence:
MTWILSTGMGPHEDKYAKHERATFKKTYSSMKTLSLNHLTAKQHMLMALCRDISLLPPLTYIFTSLRKAWRVSMRTSITLYEPQSLRDAFTYFWQKLNSAYDNNSSFEGASQKAVNGDGKDSLLLSALTTARASEYLLCSLWCLVSLYLSYAILDSLMVRWIVKYSTVAAILRMFSMSLIIVTLELLLLSSLSPELDYFLHTWILISCVLTAVYIWQSYLTSDLRYIRNQEGEVQEDTNVPEETEDYEDGEDDADEDSHVVVADESTVDVPSNDSLSDNSDGGLFPVNRPSVSHSQSPKRPKKYPKKAFNFTTKRTIDLYKITVLCVVPVGLASFITMLGLLRNLFIQRLDVEQLERILHEMHPPA
Protein: UPF0616 protein C1687.04 (O94450)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm7
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm10
- Cell division control protein 45 homolog
- N-acetyltransferase eso1
Sequence:
MVIALSDSFIENPRSFLQRFQDALFAGSKPDLQGTLGIDEEVSNIFATEERIRKIPNYLDCKWSELKTGQLLRLQGMVQDTNFGHEFFAGAVEVNENIWRGCRYILDFSEDEMHLDESKIVLDERYSLFLTNVPGERTLPVIEALGNWGSESLKERSLKYSNRLQASNDTGVCVKCYGGMETKVQVCQAIDVIGIYEEPSEYSDGLPILHMLCFKDYTQSATQAPSPQQAEIIRPKILKYFEKVLGENIAAESLMLALLSNVVHKTTGLVIGGFTLNLTNCTSELVSQLVSVLRPLIKRMVIQKVNVAELNRKPLYPLSDGETLDTSHLQVAPGTLIVLDETELSSGTLNDVGCRNVQFLSSLISQQDLTFFYPFSSFTVHSNVRIIILSHGRSILPADVGCRCRGDSPDTIEFPTDSDELQEFCNFFHMWNMRANIPENMLDYIQSTYVSSRQYNKEINEKTLSLQINCSRLYAKSFGRQLVSRIDFEAARSLINHWTVN
Protein: Tousled-like kinase, isoform G (EC 2.7.11.1) (B7Z126)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histone chaperone asf1
- Sarcolemmal membrane-associated protein
- FGFR1 oncogene partner 2 homolog
- Cell cycle checkpoint control protein Rad9
Sequence:
MSCTPSPLCGSFALAMLQQQQQQLEIREAQQRQQQKSRLQLNNYYKDIPRNQHHMQNCQDFLQVQQTVEINKLHFVQKTQQQECYMQQIHHHQQQQQKQIVDYQRVNERAHMQPTQILQSQQKISELQQIQRSARKPELLQIPEILQKQQFQTAQQKQTKKQGANTATITSFNSNSNSNNSSSSCKNYNTTSNSNKNNIDNNSSNSSGQIMLASASASASARKRSRSTSNGSKSNNKTASGRIFTKSMSPGAHLQMSPQNTSSLSQHHPHQQQQLQPPQQQQQHFPNHHSAQQQSQQQQQQEQQNPQQQAQQQQQILPHQHLQHLHKHPHQLQLHQQQQQQLHQQQQQHFHQQSLQGLHQGSSNPDSNMSTGSSHSEKDVNDMLSGGAATPGAAAAAIQQQHPAFAPTLGMQQPPPPPPQHSNNGGEMGYLSAGTTTTTSVLTVGKPRTPAERKRKRKMPPCATSADEAGSGGGSGGAGATVVNNSSLKGKSLAFRDMPKVNMSLNLGDRLGGSAGSGVGAGGAGSGGGGAGSGSGSGGGKSARLMLPVSDNKKINDYFNKQQTGVGVGVPGGAGGNTAGLRGSHTGGGSKSPSSAQQQQTAAQQQGSGVATGGSAGGSAGNQVQVQTSSAYALYPPASPQTQTSQQQQQQQPGSDFHYVNSSKAQQQQQRQQQQTSNQMVPPHVVVGLGGHPLSLASIQQQTPLSQQQQQQQQQQQQQQLGPPTTSTASVVPTHPHQLGSLGVVGMVGVGVGVGVGVNVGVGPPLPPPPPMAMPAAIITYSKATQTEVSLHELQEREAEHESGKVKLDEMTRLSDEQKSQIVGNQKTIDQHKCHIAKCIDVVKKLLKEKSSIEKKEARQKCMQNRLRLGQFVTQRVGATFQENWTDGYAFQELSRRQEEITAEREEIDRQKKQLMKKRPAESGRKRNNNSNQNNQQQQQQQHQQQQQQQNSNSNDSTQLTSGVVTGPGSDRVSVSVDSGLGGNNAGAIGGGTVGGGVGGGGVGGGGVGGGGGRGLSRSNSTQANQAQLLHNGGGGSGGNVGNSGGVGDRLSDRGGGGGGIGGNDSGSCSDSGTFLKPDPVSGAYTAQEYYEYDEILKLRQNALKKEDADLQLEMEKLERERNLHIRELKRILNEDQSRFNNHPVLNDRYLLLMLLGKGGFSEVHKAFDLKEQRYVACKVHQLNKDWKEDKKANYIKHALREYNIHKALDHPRVVKLYDVFEIDANSFCTVLEYCDGHDLDFYLKQHKTIPEREARSIIMQVVSALKYLNEIKPPVIHYDLKPGNILLTEGNVCGEIKITDFGLSKVMDDENYNPDHGMDLTSQGAGTYWYLPPECFVVGKNPPKISSKVDVWSVGVIFYQCLYGKKPFGHNQSQATILEENTILKATEVQFSNKPTVSNEAKSFIRGCLAYRKEDRMDVFALARHEYIQPPIPKHGRGSLNQQQQAQQQQQQQQQQQQQQSSTSQANSTGQTSFSAHMFGNMNQSSSS
Protein: BZIP domain-containing protein (O16393)
Organism: Caenorhabditis elegans
Interaction partners:
- AF4/FMR2 family member lilli
- F-box domain-containing protein
- Coiled-coil domain-containing protein 69
- Uncharacterized protein C03B8.2
- C2H2-type domain-containing protein
- Major facilitator superfamily
- Major facilitator superfamily
- Double-Strand Break factor
- General transcription factor IIH subunit 4
Sequence:
MAGLFRTIFKGKKSRKENENDDDYTVFNPCVRSMSLKRQPTARFADDCMLPPTAAYHTTSAPKLRKGPQSCPGGRDDFNAAAYSRSNKLPRTFPLGASSSSRQDFQIDDFERGSRNHKIRESSSMEFAKRDQKEGDDEDNEAMLERKSRYYMQKWENSEKQRREERRKQERYEQERESIQSVMSNMAYCMASAQQLEQLKKERDQYKKEMRRYKAKCEQLESKCEQLQTMSPSYGAFQSMQNLQNPMLPSPFQTPQFPAPRSFAYPNPPLPFHRSMDFLNSGPPSYLYNENLSSLCSSSMSHTPTTNGSDGAGESLVNPSDVSFLKNFSNGPTNSYDNDDEDEVKNYRQEQDYFVSSPQASNTN