wanglab/gogpt-training-data huggingface dataset:
Protein: PTS system galactitol-specific EIIB component (EIIB-Gat) (Galactitol-specific phosphotransferase enzyme IIB component) (EC 2.7.1.200) (P37188)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in galactitol transport. It can also use D-glucitol.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8955298}.
Interaction partners:
- Galactitol 1-phosphate 5-dehydrogenase
- PTS system galactitol-specific EIIA component
- D-tagatose-1,6-bisphosphate aldolase subunit GatZ
- Putative permease IIC component
- Putative phosphotransferase IIA component SgcA
- D-tagatose-1,6-bisphosphate aldolase subunit GatY
- Phosphocarrier protein HPr
- Putative phosphotransferase enzyme IIB component SgcB
- PTS system glucitol/sorbitol-specific EIIB component
- PTS system glucitol/sorbitol-specific EIIC component
Sequence:
MKRKIIVACGGAVATSTMAAEEIKELCQNHNIPVELIQCRVNEIETYMDGVHLICTTAKVDRSFGDIPLVHGMPFISGIGIEALQNKILTILQG
Protein: Tektin-4 (Testicular microtubules-related protein 4) (Q149S1)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). Contributes to normal sperm motility.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q2TA38}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:16596631, ECO:0000269|PubMed:17244819, ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}. Note=Found in the abaxial (convex) surface of outer dense fibers in sperm flagella. {ECO:0000269|PubMed:16596631}.
Interaction partners:
- Tektin-1
- Protein Flattop
- Tektin-2
- Cilia- and flagella-associated protein 52
- EF-hand domain-containing family member C2
- EF-hand domain-containing protein 1
- Piercer of microtubule wall 1 protein
- Cilia- and flagella-associated protein 276
- RIB43A-like with coiled-coils protein 2
- Tektin-3
Sequence:
MAQTGVLLTKEPAPQSIDVCELPRKEYEVACNTGAYTSSGLATAGFRTAKYLRDEWFQNSYARYHQAFADRDYSERQRHESGQLVAETGALAQRTQLDSTRKVGERLEDMHCWKSELQREIDELSSETDLMMAQKLRLQRALDATSVPYSIATDNLQCRERRQHPDLVRDYVEVELLKETELIRNIQELLKRTIGQAVDQIRLNREHKESCEMNWSDKVEVYNIDDTCSRYTNESTQVQFYPHSSKFEESASTPETWAKFNHDNLLRAERERLASVNLRKLIDCILRDTAEDLRLQCDAVNSAFSSRCQELDDSLQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEAPLRVAQTRLYQRSHRPNVELCRDNAQFRLLSEVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDIAVKTNSLFIDRQKCMTHRNRYPSVLQLAGYQ
Protein: Anaerobic nitric oxide reductase transcription regulator NorR (P37013)
Organism: Escherichia coli (strain K12)
Function: Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54. Not required for induction of the aerobic NO-detoxifying enzyme NO dioxygenase. Binds to the promoter region of norVW, to a consensus target sequence, GT-(N7)-AC, which is highly conserved among proteobacteria.
Interaction partners:
- Anaerobic nitric oxide reductase flavorubredoxin
- Flavohemoprotein
- HTH-type transcriptional repressor NsrR
- RNA polymerase sigma-54 factor
- Redox-sensitive transcriptional activator SoxR
- Nitric oxide reductase FlRd-NAD
Sequence:
MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSDEELRLIAALAAGALSNALLIEQLESQNMLPGDATPFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRCLRVDVRVLAATNRDLREEVLAGRFRADLFHRLSVFPLSVPPLRERGDDVILLAGYFCEQCRLRQGLSRVVLSAGARNLLQHYSFPGNVRELEHAIHRAVVLARATRSGDEVILEAQHFAFPEVTLPTPEVAAVPVVKQNLREATEAFQRETIRQALAQNHHNWAACARMLETDVANLHRLAKRLGLKD
Protein: Cyclin-dependent kinase 11.1 (EC 2.7.11.22) (Q09437)
Organism: Caenorhabditis elegans
Function: Probable cyclin-dependent kinase whose activity is most likely regulated by the cyclin cyl-1/Cylin-L. Important for normal oocyte and sperm development; probably required during multiple stages of gametogenesis. Plays a role in the activation of RAS-ERK signaling in the germ line. Also acts partially redundantly with cdk-11.2 to ensure embryonic viability.
Subcellular location: Nucleus {ECO:0000269|PubMed:29886128}.
Interaction partners:
- Cyclin L homolog cyl-1
- Uncharacterized protein.
- Protein kinase domain-containing protein
Sequence:
MSDHLGSSHDEGELSDESHKKSQRASSSDEPNPAKSNKGLESKMRESILSRLSKRKNSESDDDTTEQRFSIQPKNAQKAKEDRYRDKERDKKREKDKRDDRRDVRGPDARQKDRDFKGRQERSGRDQKVHEHRHHHHHRKHETDGHRTNRSNRDRSSERDSEKHKRHIDRHKKSSTTSPDNDKSPHKKSKHTDVPADAKLFDRILDPNYKKKDDDVLVIEDVEMSPIEILEEKEEKEIVEFTIDSPAGPKKYSKFESDPESDHDDTKPKSPGKAEDDDDVIEVLDDALHSDDDADSDEDKYLKTPEDREWEEMTETEQRLHKEAMKKRASMKQKTLIAQLPVFYPGLMGCRNIDEYECVNRVDEGTFGVVYRGKDKRTDEIVALKRLKMEKEKEGFPITALREINMLLKAGNHPNIVNVKEILLGSNMDKIYMAMEFVEHDMKSLLDTMSRRNKRFSIGEQKTLLQQLLSGIEHMHKLWILHRDLKTSNLLMSHKGILKIADFGLAREYGDPLKKFTSIVVTLWYRSPELLLGTRLYSTPVDMWSVGCIMAEFILLKPLFPGRGELEQIKKIFMEMGTPTESIWPGVTELDGWKALTFEKYPYNQLRKRFLAGRLLNDTGFKLLNGLLTLDPKNRFSATQALDHEWFTEEPYPVPPEEFPTFPAKSEQNKAPPPAKQKQQENRISHVDPETAKLLKQFEVRPEQVKPGGFSLKFDPTRF
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (EC 7.1.1.2) (Complex I-20kD) (CI-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) (PSST subunit) (P42026)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH-ubiquinone oxidoreductase chain 2
Sequence:
MAALAALRLLHPILAVRSGVGAALQVRGVHSSMAADSPSSTQPAVSQARAVVPKPAALPSSRGEYVVAKLDDLINWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQKKIKREKRLRIWYRR
Protein: Fimbrin-1 (AtFIM1) (Fimbrin1) (Q7G188)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cross-links actin filaments (F-actin) in a calcium independent manner. Induces the formation of actin aggregates. Stabilizes and prevents F-actin depolymerization mediated by profilin. Key regulator of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11506361}.
Interaction partners:
- F-actin-capping protein subunit beta
- Actin cross-linking protein
- Actin cross-linking protein
- L-type lectin-domain containing receptor kinase VIII.2
- Protein DMP1
- Tubulin alpha-6 chain
- Remorin 1.4
- Derlin-1
- Two-pore potassium channel 1
- Myosin-12
Sequence:
MSGYVGVVVSDPWLQSQFTQVELRTLNSKYVSVKNQNGKVTIEDLPPLFAKLKALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKIYLNLLSKAAEKSGGHHKNSSSFLKACTTTLLHTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNLKKTPQLVELLEDSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFHERNGLNKDGKYAFAEMMTEDVETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLLKSLRSRTLGKEMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSVFLLPEDIVEVNQKMILILTASIMYWSLQRHSRESSDSSSTQSTTTTCTSTASSPAPSVTEEEEVSSLSGEVTSLAVGDAVSEITTVSEEASIE
Protein: Uncharacterized protein (Q586B1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPVVKRPLWSYFTPATFASTLHRTAYHTPKLMFGVAAAAILAKQSYYRGSLADEEENTCDRIERRAYVALPDGRMALVYPIIDTQLTPTRALLSLFDMMNPLP
Protein: Aryl hydrocarbon receptor (Q9I9E2)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNPNVTYASRKRRKPVQKIVKPSPAEGVKSNPSKRHRDRLNAELDRLASLLPFPQDVIAKLDKLSVLRLSVSYLRAKSFFDVALKSSNSTRLERNGIQESRTAKLGEGMQILEGELLLQALNGFVLVVTADALVFYVSSTIQDYLGFQQSDIIHQSVFELIHTEDRPEFQRQLHWALNPTQSADSGPSVQGDNGFSQPANYYNPDQLPPENSSFMERNFICRLRCLLDNSSGFLAMNFQGRLKFLHGQNKKGKDGAALSPQLALFAVATPLQPPSILEIRTKNFIFRTKHKLDFTPTGCDAKGKIVLGYTEAELCMRGTGYQFIHAADMLYCAENHVRMMKTGESGMTVFRLLTKENRWAWVQANARLVYKNGRPDYIISTQRPLTDEEGAEHLRKRNMKLPFMFATGEAVLYELTFPMSSLSDTSQPRSKTTTGKGGKTTLHGDSVDPNSLLGAMLRQDESVYLCPPASHKLSFERNFFADSRDELSGVVSSDWTDSLLPAGSHNILKQELMECSQDSSVPLPEDSAALFQDNKTNDLYSIMKNLGIDFEDLKCIQQDEEFFKTELSGMDDIGDIDITDEILTYVQDSLNKSDFLYSGCNQQQPLVQNAGCLVQQELDQHQIHQHQKQLMEQQQQQQQQLCQKMKHMQVNGMFTNWSSGTSMPLCSPQQPQQYTFPGMQATAAEFSYKSEVNASPYACRQEFVPYKQPTAMMPQLSNFSQMDFPVAGLDRSAYSASSNLEDFLGCLQQVPENLDCGINSESVMLTPQTCYAGAVSMYQCTQEAQPNCMDQMQYDPMMANQQTLLNKFQNGFNGGNVNEAYPSQLDVISNSQTATHLQPVHHPTEPRSFPDLASSGFM
Protein: Kinesin (Q57Y53)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLCDGIAVLLLLLCTDWKHLSLSNRTTGNQTREGLLWVAACVSLCSVFSTGSAVRLYVRCLFPLFFLHSLLCASFPVCLVFHLGPRLSLSSLHLAAPVGGWTMYQSGGRSNHRVTVALSLSQGSNQTQEKSEAGGVHVLHRDGERGIPGGLGMPLQDAWASVCCSDIPQQRGNQKCKPPTVLGVRTSFVTAGDGEGCTLSYTAYVEALANCVASTLLDCNGVELLTLAHGPSGSGKTTQLFGSSLSSRPNVSTSAVGLFPLVLQQLFAVPHDPAEYHSPVAAVSVVEWRLVAPTSGTATAEPLGRPNHGNMKRGPVPNSTGCCGSSRGDDVLPQSEAVDLLARAPDASSPTRCFMEDYADIPAARYVLCSSVHEVQVTLHEAFSSSLAWRPVDRSPEQPSETTLRSQGCVIGDFDLGSPDAVLSPVVGSNSHVLVTLLIRSRGASGCDAVSIWRLWDLCGPPPFSYDRNSTHFCLARSVHMSLLRTAQLMIWSGGLHTGLMSIIAESMADEAETVRTLPRHISDVVPLTSTAQQSLFQCRGQNNQNLLFSGLDSVSAMIEACVQHSCSSVLWMGALRRGTSFDVINKEVLRAAAAVSECGDAENADLVEELRRQRRQENLRAAERVINIFAVPFKQRGVLQFSVVRGLSNYNVDCCSPKVTTPNDISRCGDPASSRLRSRLISPVLASEAPAGSSCADRIATAPRQHLPSLPRANCGAFLQANVVDVQSTPNSRSQRPQGQAEDLAHPVGSPHGLKGHSPVTVSHPDAVCASTPSSKGTEHPNPMLVSSTYATDCPDISRVPVSGDPSFVSQHELEGVAHVLQRLLEHPLAQLQEVSQHYREQLRQQRRAISNLSALFHSGGLMLSEVRQHEHQQEKLLAAAERNSFLEQRLQRLERENNELRTQLNLLRGQNDTTATPPAGSAPASGSALAGTPRHIVRASGTNADPVVATRSVEKQSVGVQTLEHRGEITLSDLAAETKEPQHRAAGRGDPTAGSLLAGTCTSAGDTVTVNPKCYNEIITTNGAGMVRWASQEGHSTAASDDSSASAHLLDVLARATKVAPSSADVVREKKVTPTQLRESCASSKWPEGVNIGTRTHLCRWGELSITSNESGDICADLRAFREAVTAARDGALRALYVAKEAVRDSCVQSLSSCAVSVCNGDTCQSVNRDSEILCNSSIEGRALRNVWEELGQQETKVSKALDALQREALALEQNTLGALSREKQLLSRAIFAE
Protein: COP9 constitutive photomorphogenic-like subunit 5 (A7TX80)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MAASGSGMAQKTWELANNKQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS
Protein: BTB/POZ domain-containing protein 8 (AP2-interacting clathrin-endocytosis) (APache) (Q5XKL5)
Organism: Homo sapiens (Human)
Function: Involved in clathrin-mediated endocytosis at the synapse. Plays a role in neuronal development and in synaptic vesicle recycling in mature neurons, a process required for normal synaptic transmission.
Subcellular location: Cell projection, axon {ECO:0000250|UniProtKB:Q80TK0}. Presynapse {ECO:0000250|UniProtKB:Q80TK0}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:D4A0X3}. Nucleus {ECO:0000269|PubMed:14654994}. Note=In primary cultures, mainly present at axonal and presynaptic terminal levels of mature neurons. In immature neurons, localizes to the cell body and growing processes, including axons (By similarity). Localized to nucleus in fetal cells (PubMed:14654994). {ECO:0000250|UniProtKB:Q80TK0, ECO:0000269|PubMed:14654994}.
Interaction partners:
Sequence:
MARCGEGSAAPMVLLGSAGVCSKGLQRKGPCERRRLKATVSEQLSQDLLRLLREEFHTDVTFSVGCTLFKAHKAVLLARVPDFYFHTIGQTSNSLTNQEPIAVENVEALEFRTFLQIIYSSNRNIKNYEEEILRKKIMEIGISQKQLDISFPKCENSSDCSLQKHEIPEDISDRDDDFISNDNYDLEPASELGEDLLKLYVKPCCPDIDIFVDGKRFKAHRAILSARSSYFAAMLSGCWAESSQEYVTLQGISHVELNVMMHFIYGGTLDIPDKTNVGQILNMADMYGLEGLKEVAIYILRRDYCNFFQKPVPRTLTSILECLIIAHSVGVESLFADCMKWIVKHFARFWSERSFANIPPEIQKSCLNMLIQSLNDKNAAFLLMESDRLIISLPRVKWTEAALTMASQLQEKCIAFIVDNFSKIIQSENFALLLQSQAMSSTADLLDTILKAIEENITTENSCSLLMALDTLLNSDSTKEMGFTCKIQALRDKLWIFLVQSFYAVRHTESWKLMSTDDQQKIQAAAFDKGDDRRLGKKPIFSSSQQRKQVSDSGDIKIKSWRGNNKKECWSYLSTNKKMKSDGLGASGHSSSTNRNSINKTLKQDDVKEKDGTKIASKITKELKTGGKNVSGKPKTVTKSKTENGDKARLENMSPRQVVERSATAAAAATGQKNLLNGKGVRNQEGQISGARPKVLTGNLNVQAKAKPLKKATGKDSPCLSIAGPSSRSTDSSMEFSISTECLDEPKENGSTEEEKPSGHKLSFCDSPGQMMKNSVDSVKNSTVAIKSRPVSRVTNGTSNKKSIHEQDTNVNNSVLKKVSGKGCSEPVPQAILKKRGTSNGCTAAQQRTKSTPSNLTKTQGSQGESPNSVKSSVSSRQSDENVAKLDHNTTTEKQAPKRKMVKQVHTALPKVNAKIVAMPKNLNQSKKGETLNNKDSKQKMPPGQVISKTQPSSQRPLKHETSTVQKSMFHDVRDNNNKDSVSEQKPHKPLINLASEISDAEALQSSCRPDPQKPLNDQEKEKLALECQNISKLDKSLKHELESKQICLDKSETKFPNHKETDDCDAANICCHSVGSDNVNSKFYSTTALKYMVSNPNENSLNSNPVCDLDSTSAGQIHLISDRENQVGRKDTNKQSSIKCVEDVSLCNPERTNGTLNSAQEDKKSKVPVEGLTIPSKLSDESAMDEDKHATADSDVSSKCFSGQLSEKNSPKNMETSESPESHETPETPFVGHWNLSTGVLHQRESPESDTGSATTSSDDIKPRSEDYDAGGSQDDDGSNDRGISKCGTMLCHDFLGRSSSDTSTPEELKIYDSNLRIEVKMKKQSNNDLFQVNSTSDDEIPRKRPEIWSRSAIVHSRERENIPRGSVQFAQEIDQVSSSADETEDERSEAENVAENFSISNPAPQQFQGIINLAFEDATENECREFSATKKFKRSVLLSVDECEELGSDEGEVHTPFQASVDSFSPSDVFDGISHEHHGRTCYSRFSRESEDNILECKQNKGNSVCKNESTVLDLSSIDSSRKNKQSVSATEKKNTIDVLSSRSRQLLREDKKVNNGSNVENDIQQRSKFLDSDVKSQERPCHLDLHQREPNSDIPKNSSTKSLDSFRSQVLPQEGPVKESHSTTTEKANIALSAGDIDDCDTLAQTRMYDHRPSKTLSPIYEMDVIEAFEQKVESETHVTDMDFEDDQHFAKQDWTLLKQLLSEQDSNLDVTNSVPEDLSLAQYLINQTLLLARDSSKPQGITHIDTLNRWSELTSPLDSSASITMASFSSEDCSPQGEWTILELETQH
Protein: Aldehyde dehydrogenase X, mitochondrial (EC 1.2.1.3) (Aldehyde dehydrogenase family 1 member B1) (Q9CZS1)
Organism: Mus musculus (Mouse)
Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldo-keto reductase family 1 member A1
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde oxidase 3
- Acetyl-coenzyme A synthetase, cytoplasmic
- Aldehyde oxidase 4
- Aldehyde oxidase 1
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MLTARLLLPRLLCLQGRTTSYSTAAALPNPIPNPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKVPEKNS
Protein: tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82 (Transfer RNA methyltransferase 82) (Q03774)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- Multifunctional methyltransferase subunit TRM112
- tRNA pseudouridine synthase 1
- tRNA
- tRNA
- tRNA
Sequence:
MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGLGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYNSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEMSEKQKGDLALKQIITFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS
Protein: Endo-1,4-beta-xylanase F3 (Xylanase F3) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase F3) (Q96VB6)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000269|PubMed:11999400, ECO:0000269|PubMed:16672490}.
Interaction partners:
- Endo-1,4-beta-xylanase A
- Probable endo-1,4-beta-xylanase B
- Probable alpha-L-arabinofuranosidase axhA
- Exo-1,4-beta-xylosidase xlnD
- Xylanolytic transcriptional activator xlnR
Sequence:
MVHLKSLAGILLYTSLCIASSQQAPASINNAFVAKGKKYFGTCADQGTLSDGTNSGIIKADFGQLTPENSMKWDATEPSQGKFSFSGADYLVNYAATNNKLIRGHTLVWHSQLPSWVQGITDKNTLTSVLKNHITTVMNRYKGKVYAWDVVNEIFNEDGTLRSSVFYNVLGEDFVRIAFETARAADPQAKLYINDYNLDSANYGKTTGLANHVKKWIAQGIPIDGIGSQTHLSAGGSSGVKGALNTLAASGVSEVAITELDIAGASSNDYVNVVEACLEVSKCVGITVWGVSDKNSWRSAESPLLFDGNYQPKSAYNAILNAL
Protein: Serine/threonine-protein kinase (EC 2.7.11.13) (X1WHC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR000552}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSVPPVIRPPSPLPGSQGISFQIQIGLSREPVLLDSGEFSLAQVREMACSIVDQKFPECGFYGMYDKILLFRHDPNSENILQLVRSAAEIMEGDLVEVVLSASATVEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGIRKRRLSNVSLTGLTNTRSISAEPSPSTSDEALLSPVSPSMEQKTPSDIFPGRGRSNSQSYIGRPIELDKILLSKVKVPHTFVIHSYTRPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKRCAPKVPNNCLGEVSRNGDLLSPGAESDVVMEEGCDDHDGDRHSPLIDDMEESLVGDSAAYLEAGHGELGDFQDLDPDESNRIISPSTSNNIPLMRVVQSVKHTKRKSSNVMKEGWLVHFTSKDTLRKRHYWRLDSKCITLFQNDTGSKYYKEIPLSEVLSLEPAKTFNLLPEGANPHCFEIATTSLVYYVGENLSRADGGSSGYGSSMLVSGVGQDVAHMWEMVIQHALMPVIAKGISQGGHHNYHKEVSISISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGIVNLECMFETPERVFVVMEKLHGDMLEMILSSEKGRLPERITKFLVSQILVALRHLHFKNIVHCDLKPENVLLASADSFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKTVTPEAIDLINNLLQVKMRKRYSVDKSLSHPWLQDYQMWLDLRTLECKMLERYITHESDDLRWEHFAEQNGLQYPAHLMNPHADVRELEEPDELVMGRLSDRVSVL
Protein: Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2) (Q80TH2)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may contribute to stabilize this unphosphorylated state (By similarity). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion.
Subcellular location: Cell junction, hemidesmosome {ECO:0000250|UniProtKB:Q96RT1}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane (By similarity). Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q96RT1}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-2
- Nucleotide-binding oligomerization domain-containing protein 2
- Plakophilin-4
- Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog
- Receptor tyrosine-protein kinase erbB-3
- Mothers against decapentaplegic homolog 2
- Epidermal growth factor receptor
- GTPase KRas
- Mothers against decapentaplegic homolog 3
- Caveolin-1
Sequence:
MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNMRTFAADHNYLQQLPPEIGNWKNITVLFLHCNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDTETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKCVKTSESTTTKSKLDEREKYMNSVQKMSEPEAETNGGNLPVTASMKLSGNLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIESSINQPKVVALSNNKKDDAKDADSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTPVDSNSKVRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDIDSKATSDDSRQLDHINMNINKLVTNNIFQPEVMERSKMQDIVLGTGFLSIHPKNEAEHIENGAKFPNLESINKVNGLCEDTAPSPGRVEPQKASSSADVGISKSTEDLSPQRSGPTGAVVKSHSITNMETGGLKIYDILGDDGPQPPSAAVKIASAVDGKNIVRSKSATLLYDQPLQVFTAASSSSELLSGTKAVFKFDSNHNPEEPDIIRAATVSGPQSTPHLYGPPQYNVQYSGSATVKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYAKHSANMNFSNHNNVRANTGYHLQQRLAPARHGEMWAISPNDRLVPAVTRTTIQRQSSVSSTASVNLGDPTRRTEGDYLSYRELHSMGRTPVMSGSQRPLSARAYSIDGPNTSRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNTRVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKHPQTSSPGECCQDDRFMSEEQNHPSGALSHRGLPDSLMKMPLSNGQMGQPLRPQAHYSQTHHPPQASVARHPSREQLIDYLMLKVAHQPPYTHPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFHNAVDLIIVREVSS
Protein: Sin3A, isoform D (A1Z928)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MMKRTRVDEVQFGTRPVPQTSGGVGVGVVGVTGGGPTSGGGGTATVGVNTTGVTIGTVVPSAHNATISGIGSIHHRILTPQHGGAQTIAYLPSTTPTATNLKTTTSIVDSTTAGGPVGAGAQVAVGVGSAAGGGGVVVSTGSTGTQTLQYTTSYSVASIQAGGTLKANTADGANTVQIHVTGGGAANNPASAQTVSSSSQTGTIRQRTISGTQTVATAVGNLATISQQQPVQQSPLGKAQTPPSSVVANSIPVGGTTPPQGQSGNATPRLKVEDALSYLDQVKYQYADQPQIYNNFLDIMKEFKSHCIDTPGVIERVSTLFKGHTELIYGFNMFLPPGYKIEIHSDALGCSVPVVSMPSPPGAPTSTGTVHMLTGNSSMSGAGHIAIKTTNAATLTPAAGAGAAAAAAAVAQIQSAGAVNLMTHGGASLTQTTIHALQQATPPQSQSPGGGHVHVSVTNSTAANAVVPGQPGISVSAHNVPQNYSRDRERATITPTGQVAGAAANVNASASIVVGGPPTPNSLSELSPHGGAGGGPGAGAAQHNLHHIQQAHQSILLGETGQQNQPVEFNHAITYVNKIKNRFQNQPAKYKKFLEILHDYQREQKVMKEGSLNQGKMLTEQEVYTQVAKLFGQDEDLLREFGQFLPDATNHQSGQYMSKSASVHNDHGKRPTATLSGGAHITMSSASPAPSGSPLHLGATTLPQIDKSAHAAAIGNLSAVNTSVSIKTYNNNQQQQNHVIGSGLNATRNDILFEKDYHAGLQQQAHQRGAGVGGHHHLAGTAAGANIGRPGVGASVMVSYDKEHRNNHHVQKYVGHAPNQNLTHGHNAKKSPSYGIPSVIGSMPHISDNSLDRSSPGISYATPPLPSGPHGQHNSGSATRRPGDDSLVGHYASGAPPAKRPKPYCRDVSFSEASSKCTISDAAFFDKVRKALRSPEVYDNFLRCLTLFNQEIVSKTELLGLVSPFLMKFPDLLRWFTDFLGPPSGQPAGGLIDGMPLAATQRQGGGSSNSSHDRGTSHQSAAEYVQDVDLSSCKRLGASYCALPQSTVPKKCSGRTALCREVLNDKWVSFPTWASEDSTFVTSRKTQFEETIYRTEDERFELDLVIEVNSATIRVLENLQKKMSRMSTEELSKFHLDDHLGGTSQTIHQRAIHRIYGDKSGEIITGMKKNPFVAVPIVLKRLKVKEEEWREAQKTFNKQWREQNEKYYLKSLDHQAINFKPNDMKALRSKSLFNEIETLYDERHDQEDDAMEPFGPHLVLPYKDKTILDDAANLLIHHVKRQTGIQKQEKQKIKQIIRQFVPDLFFAPRQPLSDDERDDAFPFLVDDNTKMDVDSPLGRTESSTRNAKSTPSESASPARSNASTSSVTPAGIKKETDDSKATTGSFAPASSATASSATPVDDATPSTSSAAAAASAASSSTVSGTEGKPKDDPLSSHKEEGAGSTSSGVATSPRQAQDTAGAGVDVEIKLEHPADFSNPKLLPPHAHGQREDESYTLFFANNNWYLFLRLHAILCDRLHVMYERARLLAIEEERCRVNRRESTATALRLKPKPEIQVEDYYPTFLDMLKNVLDGNMDSNTFEDTMREMFGIYAYISFTLDKVVSNAVRQLQYCVTERAALDCVELFATEQRRGCTGGFCRDAHKTFDREMSYQRKAESILNEENCFKVYIYKIDCRVTIELLDSEPEEVDKPAALKAQKFSKYVERLANPALGGGGNTGRSDSALGNDSVVDGSDIKTEADEDTAEVNTKA
Protein: DNA-directed DNA/RNA polymerase mu (EC 2.7.7.7) (Q6PIY2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR000817}.
Interaction partners:
Sequence:
MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKVRRAGLGPTPGMSCPGNDNTVHTMHGEANRGS