wanglab/gogpt-training-data huggingface dataset:
Protein: Nicotinic acetylcholine receptor Dalpha 4 subunit (Q9NFR5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MKFLFEILRLFIKKPSSGGTLRAWILSALMVHGAVAGNPDAKRLYDDLLSNYNKLVRPVVNTTDVLKVCIKLKLSQLIDVNLKNQIMTTNLWVEQSWYDYKLRWEPKEYGGVHMLHVPSDHIWRPDIVLYNNADGNFEVTLATKATIYSEGLVEWKPPAIYKSSCEIDVEYFPFDEQTCVLKFGSWTYDGFKVDLRHMDEQQGSNVVAVGVDLSEFYMSVEWDILEVPAVRNEKFYTCCDEPYLDITFNITMRRKTLFYTVNIIIPCMGISFLTVLTFYLPSDSGEKVTLSISILISLHVFFLLVVEIIPPTSLVVPLLGKYLIFAMILVSISICVTVVVLNVHFRSPQTHKMAPWVKRVFIDFLPAFLFIKRPTYNFETSKLLLKDTHACFYPYYSATNIDRLVSSGYNNSLPKEDLSQSITANGPFGGSCQVHGPVPPLTHCSSDEIAAVPDMDIGPLGMKSPILNNPAFSHSKCLPKIHKSCFCVRFIAEHTKMQEDSTKVKEDWKYVAMVLDRLFLWIFTLAVVVGTAGIILQAPTLYDDRIPIIEQKDLDFSGTSAGRCRPPQ
Protein: N-carbamoyl-L-amino acid hydrolase (EC 3.5.1.87) (L-carbamoylase) (Q53389)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Interaction partners:
Sequence:
MIQGERLWQRLMELGEVGKQPSGGVTRLSFTAEERRAKDLVASYMREAGLFVYEDAAGNLIGRKEGTNPDATVVLVGSHLDSVYNGGCFDGPLGVLAGVEVVQTMNEHGVVTHHPIEVVAFTDEEGARFRFGMIGSRAMAGTLPPEALECRDAEGISLAEAMKQAGLDPDRLPQAARKPGTVKAYVELHIEQGRVLEETGLPVGIVTGIAGLIWVKFTIEGKAEHAGATPMSLRRDPMAAAAQIIIVIEEEARRTGTTVGTVGQLHVYPGGINVIPERVEFVLDLRDLKAEVRDQVWKAIAVRAETIAKERNVRVTTERLQEMPPVLCSDEVKRAAEAACQKLGYPSFWLPSGAAHDSVQLAPICPIGMIFVRSQDGVSHSPAEWSTKEDCAAGAEVLYHTVWQLAQGE
Protein: Cytochrome c oxidase subunit 7A2-like, mitochondrial (Cytochrome c oxidase subunit 7A-related protein) (COX7a-related protein) (Cytochrome c oxidase subunit VIIa-related protein) (EB1) (Supercomplex assembly factor 1) (O14548)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of oxidative phosphorylation and energy metabolism (By similarity). Necessary for the assembly of mitochondrial respiratory supercomplex (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:27545886}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99KD6}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Sequence:
MYYKFSGFTQKLAGAWASEAYSPQGLKPVVSTEAPPIIFATPTKLTSDSTVYDYAGKNKVPELQKFFQKADGVPVYLKRGLPDQMLYRTTMALTVGGTIYCLIALYMASQPKNK
Protein: SNARE protein Ykt6 (cDNA, FLJ93006, Homo sapiens SNARE protein Ykt6 (YKT6), mRNA) (A4D2J0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00025701}; Lipid-anchor {ECO:0000256|ARBA:ARBA00025701}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00025701}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004444}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004444}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004444}.
Interaction partners:
Sequence:
MKLYSLSVLYKGEAKVVLLKAAYDVSSFSFFQRSSVQEFMTFTSQLIVERSSKGTRASVKEQDYLCHVYVRNDSLAGVVIADNEYPSRVAFTLLEKVLDEFSKQVDRIDWPVGSPATIHYPALDGHLSRYQNPREADPMTKVQAELDETKIILHNTMESLLERGEKLDDLVSKSEVLGTQSKAFYKTARKQNSCCAIM
Protein: Protein IRS1 (Q6SW04)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Acts as a transactivator along with IE2, and is required for oriLyt-dependent DNA replication in the transient transfection replication assay using native promoters.
Subcellular location: Virion {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Note=Isoform IRS1-263 is predominantly nuclear. {ECO:0000250}.
Interaction partners:
Sequence:
MAQRNGMSPRPPPLGRGRGAGGPSGVGSSPPSSCVPMGATSTAGTGASAAPTATPGHGVHRVEPRGPPGAPPSSGNNSNFWHGPERLLLSQIPVERQALTELEYQAMGAVWRAAFLANSTGRAMRKWSQRDAGTLLPLGRPYGFYARVTPRSQMNGVGATDLRQLSPRDAWIVLVATVVHEVDPAADPTVGDKAGHPEGLCAQDGLYLALGAGFRVFVYDLANNTLILAARDADEWFRHGAGEVVRLYRCNRLGVGTPRATLLPQPALRQTLLRAEEATALGRELRRRWAGTTVALQTPGRRLQPMVLLGAWQELAQYEPFASAPHPASLLTAVRRHLNQRLCCGWLALGAVLPARWLGCAAGPATGTTSPPAASGTETEAAGGDAPCAMAGAVGSAVTIPPQPYGGAGGSAICVPNADAHAVVGADATAAAAAAAAAPTVMVGPTAMAGPAASGTVPRAMLVVVLDELGAVFGYCPLDGHVYPLAAELSHFLRAGVLGALALGRESAPAAEAARRLLPELDREQWERPRWDALHLHPRAALWAREPHGQWEFMFREQRGDPIHDPVAFRLSDARTLGLDLTTVMTERQSQLPEKYIGFYQIRKPPWLMEQPPPPSRQTKPDAATMPPPLSAQASVSYALRYDDESWRPLSTVDDHKAWLDLDESHWVLGDSRPDDIKQRRLLKATQRRGAEIDRPMPVVPEECYDQRFTTEGHQVIPLCASEPEDDDEDPTYDELPSRPPQKHKPPDKPPRLCKTGPGPPPLPPKQRHGSTDGKVSAPRQSEHHKRQTRPPRPPPPKFGDRTAAHLSQNMRDMYLDMCTSSGHRPRPPAPPRPKKCQTHAPHHVHH
Protein: Dimethyladenosine transferase 2, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 2) (Mitochondrial transcription factor B2) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2) (d-mtTFB2) (Q9VH38)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA. Also regulates mitochondrial DNA copy number. Stimulates transcription independently of the methyltransferase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15060065}.
Interaction partners:
- DNA-directed RNA polymerase
- Mitochondrial transcription factor A, isoform B
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
- Transcription termination factor, mitochondrial
Sequence:
MLPLRCSWSFARANYSTKKELVTRYSGDFPEKLLNRKQKVPTHMYIANSEAAARINQYLEPHFQSSGCDTVMELNSGAGYFTRHLLDRESQFRRIILLESMDHFMPKIQELHTLYPERVKVRQGDFVNLWKLVYMDKMDGGSRVADLLSDVPQKAFTDDINMLVFGAVGSYPFFKHLINSLIFQTSLFNLGRCEMILAMPPPIYIHLTCNNEIGYLIYRSTSVLFQILFEHKFIAKVPREDFLPQQMAYSPTKSSKLGKVQSINPEYLYLVKFTPRRNLHELCQSQDLPALWFFIKQNYVSRRNRIIPNLEKWVPGCGPRLIINPKSSESVTPIYPDELPKKLPQYSCQSTTMSTRNYYPGINIYTQFGDLLPSQILTLFSQFRQWPEYGESSFLASLENALLKLETANDEPNLEDGVTLPEEDDAEADEIIEEESPVPATTPVKRRRKASS
Protein: Eukaryotic translation elongation factor 1 delta (E9PJV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWVNKSSFDQAERAFVE
Protein: Phospholipid-transporting ATPase 1 (AtALA1) (EC 7.6.2.1) (Aminophospholipid flippase 1) (P98204)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Has activity with phosphatidylserine and with a much lower efficiency with phosphatidylethanolamine, but not with phosphatidylcholine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22514601}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22514601}; Multi-pass membrane protein {ECO:0000255}. Note=Requires the presence of an ALIS protein to exit the endoplasmic reticulum to the cell membrane. {ECO:0000269|PubMed:22514601}.
Interaction partners:
- S-protein homolog 15
- ALA-interacting subunit 1
- ALA-interacting subunit 3
- ALA-interacting subunit 5
- At3g14430
- Defensin-like protein 90
- Probable methyltransferase PMT18
Sequence:
MDPRKSIDKPPHHDPILGVSSRWSVSSKDNKEVTFGDLGSKRIRHGSAGADSEMLSMSQKEIKDEDARLIYINDPDRTNERFEFTGNSIKTAKYSVFTFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASIMPLAFVLLVSAIKDAYEDFRRHRSDRVENNRLALVFEDHQFREKKWKHIRVGEVIKVQSNQTLPCDMVLLATSDPTGVVYVQTTNLDGESNLKTRYAKQETLLKAADMESFNGFIKCEKPNRNIYGFQANMEIDGRRLSLGPSNIILRGCELKNTAWALGVVVYAGGETKAMLNNSGAPSKRSRLETRMNLEIILLSLFLIVLCTIAAATAAVWLRTHRDDLDTILFYRRKDYSERPGGKNYKYYGWGWEIFFTFFMAVIVYQIMIPISLYISMELVRIGQAYFMTNDDQMYDESSDSSFQCRALNINEDLGQIKYLFSDKTGTLTDNKMEFQCACIEGVDYSDREPADSEHPGYSIEVDGIILKPKMRVRVDPVLLQLTKTGKATEEAKRANEFFLSLAACNTIVPIVSNTSDPNVKLVDYQGESPDEQALVYAAAAYGFLLIERTSGHIVINVRGETQRFNVLGLHEFDSDRKRMSVILGCPDMSVKLFVKGADSSMFGVMDESYGGVIHETKIQLHAYSSDGLRTLVVGMRELNDSEFEQWHSSFEAASTALIGRAGLLRKVAGNIETNLRIVGATAIEDKLQRGVPEAIESLRIAGIKVWVLTGDKQETAISIGFSSRLLTRNMRQIVINSNSLDSCRRSLEEANASIASNDESDNVALIIDGTSLIYVLDNDLEDVLFQVACKCSAILCCRVAPFQKAGIVALVKNRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGRQAVMASDFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLILFWYVLFTCYTLTTAITEWSSVLYSVIYTAIPTIIIGILDKDLGRQTLLDHPQLYGVGQRAEGYSTTLFWYTMIDTIWQSAAIFFIPMFAYWGSTIDTSSLGDLWTIAAVVVVNLHLAMDVIRWNWITHAAIWGSIVAACICVIVIDVIPTLPGYWAIFQVGKTWMFWFCLLAIVVTSLLPRFAIKFLVEYYRPSDVRIAREAEKLGTFRESQPVGVEMNLIQDPPRR
Protein: U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) (Q9VE17)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region (By similarity). Regulates alternative splicing of a distinct group of target genes.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D3
- Probable small nuclear ribonucleoprotein Sm D2
- U1 small nuclear ribonucleoprotein A
- U1 small nuclear ribonucleoprotein 70 kDa
- Probable small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein G
- Probable U2 small nuclear ribonucleoprotein A'
- BcDNA.LD23634
Sequence:
MPKYYCDYCDTYLTHDSPSVRKTHCTGRKHRDNVKFYYQKWMEEQAQHLIDATTAAFKAGKITNNPFAGGPGGAPPKPAGVSIPPPNMGAPPRPGMPGMPYMPPLMNPMMGMRPPPIMNPMAMMGPPPPLGTIPGVRPGIMNGPK
Protein: 5-hydroxytryptamine receptor 1A (5-HT-1A) (5-HT1A) (G-21) (Serotonin receptor 1A) (P08908)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:26365466, ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}; Multi-pass membrane protein {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}. Cell projection, dendrite {ECO:0000250|UniProtKB:P19327}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Sodium-dependent serotonin transporter
- Fibroblast growth factor receptor 1
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2A
- 5-hydroxytryptamine receptor 1B
- Galanin receptor type 1
- Amine oxidase [flavin-containing] A
- Oxytocin-neurophysin 1
Sequence:
MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCAVLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAALISLTWLIGFLISIPPMLGWRTPEDRSDPDACTISKDHGYTIYSTFGAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPKKSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNSKEHLPLPSEAGPTPCAPASFERKNERNAEAKRKMALARERKTVKTLGIIMGTFILCWLPFFIVALVLPFCESSCHMPTLLGAIINWLGYSNSLLNPVIYAYFNKDFQNAFKKIIKCKFCRQ
Protein: (thale cress) hypothetical protein (A0A178VN99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAQILSPVCTDLLKFQNSALSSRSGASPRFSAKTTGASSSWYLPRYAGKRRTDSIGRLRVATEDASSLSTGDVADDYYAVLGLLPDATQEEIKKAYYNCMKSCHPDLSGNDPETTNFCMFINDIYEILSDPVQRMVYDEIHGYTVTAINPFLDDSTPRDHVFVDEFACIGCKNCANVAPDIFQIEEDFGRARACNQRGNPDLVQQAVETCPVDCIHQTSAAQLSLLEDEMRRVERVNVALMLSGMGSGAVDVFRMARSRWEKRQAKVLNQARSRMMKRKNTDETPSYWDNLWGKQNEYQKSEEEVQERAQRAAAAARRWREYSRRGVDKRPTFKLPDSASRGDN
Protein: Molybdenum cofactor sulfurase (MCS) (MOS) (MoCo sulfurase) (hMCS) (EC 2.8.1.9) (Molybdenum cofactor sulfurtransferase) (Q96EN8)
Organism: Homo sapiens (Human)
Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- Aldehyde oxidase
- Cysteine desulfurase
- Selenocysteine lyase
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Cystathionine gamma-lyase
- Frataxin, mitochondrial
- Thiosulfate:glutathione sulfurtransferase
- Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3
- 3-mercaptopyruvate sulfurtransferase
Sequence:
MAGAAAESGRELWTFAGSRDPSAPRLAYGYGPGSLRELRAREFSRLAGTVYLDHAGATLFSQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDYTVIFTAGSTAALKLVAEAFPWVSQGPESSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEDLWSAEERSASASNPDCQLPHLFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLAGEDFYIPRQSVAQRFEDGTISFLDVIALKHGFDTLERLTGGMENIKQHTFTLAQYTYVALSSLQYPNGAPVVRIYSDSEFSSPEVQGPIINFNVLDDKGNIIGYSQVDKMASLYNIHLRTGCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQAFLRFIIDTRLHSSGDWPVPQAHADTGETGAPSADSQADVIPAVMGRRSLSPQEDALTGSRVWNNSSTVNAVPVAPPVCDVARTQPTPSEKAAGVLEGALGPHVVTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRIMVIKAKGMEPIEVPLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHGKDQLPGTMATLSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFSLKDLSLRFRANIIINGKRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQHVFQKLSESRETKVNFGMYLMHASLDLSSPCFLSVGSQVLPVLKENVEGHDLPASEKHQDVTS
Protein: Jumonji C domain-containing protein 5 (EC 1.14.11.73) (EC 3.4.-.-) (Lysine-specific demethylase 8) (Q9W0M3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:28701701, ECO:0000269|PubMed:29339751}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28701701}. Cytoplasm {ECO:0000269|PubMed:28701701}.
Interaction partners:
- 2-oxoglutarate and iron-dependent oxygenase JMJD4 homolog
- Small ribosomal subunit protein eS6
- JmjC domain-containing histone demethylation protein 1
- Lysine-specific demethylase 3
- LD39062p
- Probable lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
Sequence:
MDSEFLELTQLLPRWVDLENVVRGEVEARYILKRAADHLANLRSGGDSGAEETGYLVGALVDRNWERIHTGHFSQVPLVTRKIYAIACCFKIFFLLLESTSPAQKDACSEILDEAQLLGCMEDWSELKVALMDYLDKDGAVALNSAPLPTLEPLTRVTSNCDIPQLDAPSLEEFQTKCFEAGQPTLLLNTIQHWPALHKWLDLNYLLQVAGNRTVPIEIGSNYASDEWSQQLVKIRDFLSRQFGKEPSKAGQNIEYLAQHELFAQIPALKEDISIPDYCTISNEDTPGAVDIKAWLGPAGTVSPMHYDPKHNLLCQVFGSKRIILAAPADTDNLYPHDSEFLANTARIDAAQLDPETYPLVAKVKFYQLLLQPGDCLYMPPKWWHYVRSEAPSFSVSFWWE
Protein: 2-octaprenylphenol hydroxylase (EC 1.14.13.240) (2-polyprenylphenol 6-hydroxylase) (P25535)
Organism: Escherichia coli (strain K12)
Function: FAD-dependent monooxygenase required for the aerobic hydroxylation of 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol, the first hydroxylation step in coenzyme Q (ubiquinone) biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30686758}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase
- 2-octaprenyl-6-methoxyphenol hydroxylase
- Ubiquinone biosynthesis accessory factor UbiJ
- Ubiquinone biosynthesis accessory factor UbiK
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- 3-octaprenyl-4-hydroxybenzoate carboxy-lyase
- Flavin prenyltransferase UbiX
- 3-demethoxyubiquinol 3-hydroxylase
- 4-hydroxybenzoate octaprenyltransferase
- UPF0149 protein YgfB
Sequence:
MQSVDVAIVGGGMVGLAVACGLQGSGLRVAVLEQRVQEPLAANAPPQLRVSAINAASEKLLTRLGVWQDILSRRASCYHGMEVWDKDSFGHISFDDQSMGYSHLGHIVENSVIHYALWNKAHQSSDITLLAPAELQQVAWGENETFLTLKDGSMLTARLVIGADGANSWLRNKADIPLTFWDYQHHALVATIRTEEPHDAVARQVFHGEGILAFLPLSDPHLCSIVWSLSPEEAQRMQQASEDEFNRALNIAFDNRLGLCKVESARQVFPLTGRYARQFASHRLALVGDAAHTIHPLAGQGVNLGFMDAAELIAELKRLHRQGKDIGQYIYLRRYERSRKHSAALMLAGMQGFRDLFSGTNPAKKLLRDIGLKLADTLPGVKPQLIRQAMGLNDLPEWLR
Protein: Nuclear factor related to kappa-B-binding protein (DNA-binding protein R kappa-B) (Q6PIJ4)
Organism: Mus musculus (Mouse)
Function: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Actin-related protein 5
- INO80 complex subunit E
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- Chromatin-remodeling ATPase INO80
- Actin-related protein 8
- RuvB-like 1
- TCF3 fusion partner homolog
- Microspherule protein 1
- INO80 complex subunit C
- Transcriptional repressor protein YY1
Sequence:
MDSLDHMLTDPLELGPCGDGHSTGIMEDCLLGGTRVSLPEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPRFPADSVEQQRELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSDLLEMARRSGPALPFPHKHHSPSRSPEEREWRTQQRYLKVLREVKEECGDTALSSDEEDLSSWLPSSPARSPSPAVPLRVVPTLSTTDMKTADKIELGDSDLKLMLKKHHEKRKHQPDHPDLLTGDLTLSDIMTRVNAGRKGSLAALYDLAVLKKKVKEKEEKKKKKIKLIKSEAEDLAEPLSSTEGVPTLSQAPSPLAISSIKEEPLEDIKPCLGINEISSSFFSLLLEILLLESQASLPMLEDRVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFHLWLETKDQAFCKENEDSSDAMTPVPRVRTDYVVRPSTGEEKRVFQEQERYRYSQPHKAFTFRMHGFESVVGPVKGVFDKETSLNKAREHSLLRSDRPAYVTILSLVRDAAARLPNGEGTRAEICELLKDSQFLAPDVTSTQVNTVVSGALDRLHYEKDPCVKYDIGRKLWIYLHRDRSEEEFERIHQAQAAAAKARKALQQKPKPPSKVKSSNKEGSTKGLSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPTPISPPPVSAVNRSGSSTVSEPAQSSSGVLLVSSPTMPQLGTMLSPASIQTPPSSQATARVVSHSSSAGLPQVRVVAQPSLPAVSQQSVGPAQPLPQMPAGPQIRVPVTATQTKVVPQAVMATVPVKGQTAAASVQRPGPGQTGLTVTNLPAAVSPVSKTAMSSPGNSAPSASTTAVIQNVTGQNIIKQVSITGQLGVKPQTGSSIPLTATNFRIQGKDVLRLPPSSITTDAKGQTVLRITPDMMATLAKSQVTTVKLTQDLFGAGSGTAGKGISATLHVTSNPVHAADSPAKAPSASVPSSAPAGTTVVKVTPDLKPTETANSAFRLMPALGVSVADQKGKNTVASSEAKPAATIRIVQGLGVMPPKAGQTITVAAHAKQGASVAGGSGTVHSSTVSLPSINAAVSKTVAVASGATSTPISIGTGAPTVRQVPVNTTVVSTSQSGKLPTRITVPLSVISQPMKGKSVVTAPIIKGNLGANLSGLGRNIILTTMPAGTKLIAGNKPVSFLTAQQLQQLQQQGQATQVRIQTVPASHLQQGTASGSSKAVSTVVVTTAPSPKQAPEQQ
Protein: Pectinesterase inhibitor 3 (Pectin methylesterase inhibitor 3) (AtPMEI3) (Q84WE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pectin methylesterase (PME) inhibitor that regulates de-methylesterification of pectins in the apical meristem and affects primordia formation and phyllotactic patterning.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q9STY5}.
Interaction partners:
- Pectinesterase 5
- Pectinesterase inhibitor 5
- Pectinesterase inhibitor 2
- Probable pectinesterase 68
- Pectinesterase inhibitor 1
- FAD/NAD
- At1g63840/T12P18_14
- Probable pectinesterase/pectinesterase inhibitor 19
- CAP superfamily protein
- Probable pectinesterase/pectinesterase inhibitor 41
Sequence:
MAPTQNLFLVAIAFAVIFTASTVHGRHNGAEDIVHSSCEHASYPSLCVRTLSSYSGPTITNRRDLAQAAIKISLSHAQSAAKKLAVVRDSVGKKKQEKAALVDCVEMIGDSVDELSRTLGVLKHLRVSGGSAKEFRWQMSNAQTWASAALTDDDTCLDGFQGMDDGEIKTEVKQWMTKVARVTSNALYMVNQLDETRGKPHDVHL
Protein: Regulator of nonsense transcripts 3B (Nonsense mRNA reducing factor 3B) (Up-frameshift suppressor 3 homolog B) (hUpf3B) (Up-frameshift suppressor 3 homolog on chromosome X) (hUpf3p-X) (Q9BZI7)
Organism: Homo sapiens (Human)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core.
Subcellular location: Nucleus {ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187}. Cytoplasm {ECO:0000269|PubMed:11163187}. Note=Shuttling between the nucleus and the cytoplasm. {ECO:0000269|PubMed:11163187}.
Interaction partners:
- RNA-binding protein with serine-rich domain 1
- Nuclear RNA export factor 1
- Regulator of nonsense transcripts 1
- Regulator of nonsense transcripts 2
- Eukaryotic initiation factor 4A-III
- Nonsense-mediated mRNA decay factor SMG5
- RNA-binding protein 8A
- Protein mago nashi homolog
- Protein CASC3
- Protein mago nashi homolog 2
Sequence:
MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKVHRFLLQAVNQKNLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNRLCPPDDSTKSGDSAAERKQESGISHRKEGGEE
Protein: Protein-ADP-ribose hydrolase (SpyMacroD) (EC 3.2.1.-) (P0DN70)
Organism: Streptococcus pyogenes serotype M5 (strain Manfredo)
Function: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds. Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L (SpyM50867), by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress.
Interaction partners:
Sequence:
MPSSFDLLGEMIDLLQTEQLTSYWACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDTYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFIPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGRHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTIIFNTFTSEDKALYDTYLQKENNCE
Protein: Melanocortin receptor 3 (MC3-R) (P41968)
Organism: Homo sapiens (Human)
Function: Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-opiomelanocortin
- Agouti-related protein
- Copper-transporting ATPase 1
- Growth hormone secretagogue receptor type 1
- Cathepsin Z
- Appetite-regulating hormone
- Melanocortin-2 receptor accessory protein 2
- Pro-neuropeptide Y
- Leptin
- Agouti-signaling protein
Sequence:
MNASCCLPSVQPTLPNGSEHLQAPFFSNQSSSAFCEQVFIKPEVFLSLGIVSLLENILVILAVVRNGNLHSPMYFFLCSLAVADMLVSVSNALETIMIAIVHSDYLTFEDQFIQHMDNIFDSMICISLVASICNLLAIAVDRYVTIFYALRYHSIMTVRKALTLIVAIWVCCGVCGVVFIVYSESKMVIVCLITMFFAMMLLMGTLYVHMFLFARLHVKRIAALPPADGVAPQQHSCMKGAVTITILLGVFIFCWAPFFLHLVLIITCPTNPYCICYTAHFNTYLVLIMCNSVIDPLIYAFRSLELRNTFREILCGCNGMNLG