wanglab/gogpt-training-data huggingface dataset:
Protein: Max-like protein X (Class D basic helix-loop-helix protein 13) (bHLHd13) (Max-like bHLHZip protein) (Protein BigMax) (Transcription factor-like protein 4) (Q9UH92)
Organism: Homo sapiens (Human)
Function: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation.
Subcellular location: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the cytoplasm (PubMed:10918583). {ECO:0000269|PubMed:10918583}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the cytoplasm (PubMed:10918583). {ECO:0000269|PubMed:10918583}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the nucleus (PubMed:10918583). {ECO:0000269|PubMed:10918583}.
Interaction partners:
- Carbohydrate-responsive element-binding protein
- MLX-interacting protein
- Max dimerization protein 4
- Max-binding protein MNT
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Bifunctional coenzyme A synthase
- Protein TFG
- NIF3-like protein 1
- ATP-citrate synthase
Sequence:
MTEPGASPEDPWVKASPVGAHAGEGRAGRARARRGAGRRGASLLSPKSPTLSVPRGCREDSSHPACAKVEYAYSDNSLDPGLFVESTRKGSVVSRANSIGSTSASSVPNTDDEDSDYHQEAYKESYKDRRRRAHTQAEQKRRDAIKRGYDDLQTIVPTCQQQDFSIGSQKLSKAIVLQKTIDYIQFLHKEKKKQEEEVSTLRKDVTALKIMKVNYEQIVKAHQDNPHEGEDQVSDQVKFNVFQGIMDSLFQSFNASISVASFQELSACVFSWIEEHCKPQTLREIVIGVLHQLKNQLY
Protein: Pre-B-cell leukemia transcription factor 1 (Q53YC7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGGYPSPCYQPDRRIQ
Protein: Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Asparaginyl-tRNA synthetase 1) (Q8BP47)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells. Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43776}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Glutamyl-tRNA
- Tyrosine--tRNA ligase, cytoplasmic
- Glutamyl-tRNA
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Asparaginyl-tRNA synthetase
- Glutamyl-tRNA
- Leucine--tRNA ligase, cytoplasmic
Sequence:
MSSEVIRGTAEMVLAELYVSDREGNDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWDVISKSQMKNIKKMWHREQMKNDSREKKEAEDNLRREKNLEEAKKIIIKNDPSLPEPACVKISALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLSDDLCQCYNGVVLSTESSVAVYGTLNLTPKGKQAPGGHELSCDFWELVGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMITRCFRDHFFDRGYCEVTTPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEFTHVEAECPFLTFEDLLNRLEDLVCDVVDRVLKSPVASIVYELNPNFKPPKRPFRRMNYSDAIEWLKEHDVKKEDGTFYEFGDDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDPRLTESVDVLMPNVGEIVGGSMRSWDSEEILEGYKREGIDPAPYYWYTDQRKYGTCPHGGYGLGLERFLSWILNRYHIRDVCLYPRFLQRCRP
Protein: Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE) (P07323)
Organism: Rattus norvegicus (Rat)
Function: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase 1
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Phosphoglycerate mutase 2
- Glucose-6-phosphate isomerase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase A
- Fructose-bisphosphate aldolase B
- Glycerate kinase
Sequence:
MSIQKIWAREILDSRGNPTVEVDLHTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAEKDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRCITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGEEARFAGHNFRNPSVL
Protein: Zinc finger protein 773 (Zinc finger protein 419B) (Q6PK81)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 549
Sequence:
MAAATLRDPAQQGYVTFEDVAVYFSQEEWRLLDDAQRLLYRNVMLENFTLLASLGLASSKTHEITQLESWEEPFMPAWEVVTSAILRGSWQGAKAEAAAEQSASVEVPSSNVQQHQKQHCGEKPLKRQEGRVPVLRSCRVHLSEKSLQSREVGKDLLTSSGVLKHQVTHTGEKSHRSSKSREAFHAGKRHYKCSECGKAFGQKYLLVQHQRLHTGEKPYECSECGKLFSHKSNLFIHQIVHTGERPYGCSDCGKSFSRNADLIQHQRVHTGEKPFTCSECGKAFRHNSTLVQHHRIHTGVRPYECSECGKLFSFNSSLMKHQRVHTGERPYKCSECGKFYSHKSSLINHWRVHTGERPYECSECGKFFSQSSSLMQHRKVHTGEKPFKCNECGRFFSENSSLVKHQRVHTGAKPYECRECGKFFRHSSSLVKHRRIHTGEIQ
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme A) (E1JIE7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTIKPVSAPPSAKRVAGNVDPDNKEAQVVVVEQSVVSQTHNHAHNHRNVVIDGQSPQRRGEVYDELARTHRCSPHKSTRSKRREHHEAHAHLYKRDRLEREKLVHPTAAAGSGAPGVSGSKCNSPPSTSTSGSSSPSAVGRNSPEHLGLGCTTVPTAQVQMSTSTAAANLLKTVEETFSGYNSGDEHHQPKERLIPVEEWQRRDLEFAKCMEQRGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQAISEIYSRTVEVYCYQSNPINIFNSEQSQAGYPPLRLSYQRGSHYNAILDPYNATVGVGLGLAGYKPEIQTKEAVRLSEQLEIEQTMFEDKLKTTDWEATNEAIEEQIARESYLQWCRENTQRSRNSNTAAGSATSSTVTSAEALTDSDASPSKYSACGGTGSSGNPPVALTSGSGGDGAGPAFSLSPKTLNQFSHKLPQEVNELGGYDSDATDMSSTSSVGHSGGSSSPSTAASQRSGKGSKSQRRATALRKKRRHETRETTLASKRLVFVATCGAAY
Protein: Ubiquitin-conjugating enzyme E2 W (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme W) (N-terminal E2 ubiquitin-conjugating enzyme) (EC 2.3.2.25) (N-terminus-conjugating E2) (Ubiquitin carrier protein W) (Ubiquitin-conjugating enzyme 16) (Ubiquitin-protein ligase W) (Q9XWF6)
Organism: Caenorhabditis elegans
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (By similarity). Together with ubc-18, required for the ubiquitination of membranous organelles, and the removal of paternal mitochondria from early embryos.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 variant 1
- E2 ubiquitin-conjugating enzyme
- E2 ubiquitin-conjugating enzyme
- UBC core domain-containing protein
- E1 ubiquitin-activating enzyme
- UBiquitin Conjugating enzyme
- Ubiquitin-conjugating enzyme E2 J2
- UBC core domain-containing protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Allophagy receptor allo-1
Sequence:
MSDAATRRLMKELAQLKSEAPEGLLVDNTSTSNDLKQWKIGVVGAEGTLYAGEVFMLQFTFGPQYPFNSPEVMFVGETIPAHPHIYSNGHICLSILSDDWTPALSVQSVCLSILSMLSSSKEKKHPIDDAIYVRTCSKNPSKTRWWFHDDSV
Protein: Polyglutamylase complex subunit TTLL1 (EC 6.3.2.-) (Tubulin polyglutamylase TTLL1) (Tubulin polyglutamylase complex subunit 3) (PGs3) (Tubulin--tyrosine ligase-like protein 1) (p49) (Q91V51)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of a polyglutamylase complex which modifies tubulin, generating side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Probably involved in the side-chain elongation step of the polyglutamylation reaction rather than the initiation step (Probable). Modifies both alpha- and beta-tubulins with a preference for the alpha-tail. Unlike most polyglutamylases of the tubulin--tyrosine ligase family, only displays a catalytic activity when in complex with other proteins as it is most likely lacking domains important for autonomous activity. Part of the neuronal tubulin polyglutamylase complex. Mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility. Involved in respiratory motile cilia function through the regulation of beating asymmetry. Essential for sperm flagella biogenesis, motility and male fertility. Also mediates glutamylation of non-tubulin proteins. Involved in KLF4 glutamylation which impedes its ubiquitination, thereby leading to somatic cell reprogramming, pluripotency maintenance and embryogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20498047}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:20498047}. Cell projection, cilium, flagellum {ECO:0000305|PubMed:20442420}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- Leucine-rich repeat-containing protein 49
- Cytosolic carboxypeptidase 1
- Tubulin polyglutamylase complex subunit 1
Sequence:
MAGRVKWVTDIEKSVLINNFEKRGWIQVTENEDWNFYWMSVQTIRNVFSVETGYRLSDDQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGSPLAEKDENGKYLYLDFVPVTYMLPADYNLFVEEFRKSPSSTWIMKPCGKAQGKGIFLINKLSQIKKWSRDSKTSSFVSQSTKEAYVISVYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGFCRFCTVKYTPSTSELDNMFVHLTNVAIQKHGEDYNHIHGGKWTVNNLRLYLESTRGREVTSKLFDEIHWIIVQSLKAVAPVMNNDKHCFECYGYDIIIDDKLKPWLIEVNASPSLTSSTANDRILKYNLINDTLNIAVPNGEIPDCKWNKSPPKEVLGNYEILYDEELAQGDGAERELRNRPGQPVGPRAGRSRDSGRSVLTTWK
Protein: Calmodulin (CaM) (P04464)
Organism: Triticum aestivum (Wheat)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Interaction partners:
- Two pore calcium channel protein 1
- BRCT domain-containing protein
- BRCT domain-containing protein
- Rad4 beta-hairpin domain-containing protein
- Rad4 beta-hairpin domain-containing protein
- Rad4 beta-hairpin domain-containing protein
- Ribosomal protein L37
- Ribosomal protein L37
- Kinesin-like calmodulin-binding protein
- Kinesin-like calmodulin-binding protein
Sequence:
MADQLTDEQIAEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQDGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKVMMAK
Protein: Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) (P35408)
Organism: Homo sapiens (Human)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Prostaglandin E2 receptor EP1 subtype
- Prostaglandin E2 receptor EP2 subtype
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Prostaglandin G/H synthase 2
- Beta-arrestin-1
- Prostaglandin E synthase
- Guanine nucleotide-binding protein G
Sequence:
MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLAINHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTAHAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRGHPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQPSLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSGQHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPGMGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSETLNLSEKCI
Protein: Transmembrane emp24 domain-containing protein 5 (p24 family protein gamma-2) (p24gamma2) (p28) (Q9Y3A6)
Organism: Homo sapiens (Human)
Function: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Note=Probably cycles between compartments of the early secretatory pathway.
Interaction partners:
- Transmembrane emp24 domain-containing protein 9
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 4
Sequence:
MGDKIWLPFPVLLLAALPPVLLPGAAGFTPSLDSDFTFTLPAGQKECFYQPMPLKASLEIEYQVLDGAGLDIDFHLASPEGKTLVFEQRKSDGVHTVETEVGDYMFCFDNTFSTISEKVIFFELILDNMGEQAQEQEDWKKYITGTDILDMKLEDILESINSIKSRLSKSGHIQTLLRAFEARDRNIQESNFDRVNFWSMVNLVVMVVVSAIQVYMLKSLFEDKRKSRT
Protein: Bergaptol O-methyltransferase (PpBMT) (EC 2.1.1.69) (A0A166U5H3)
Organism: Kitagawia praeruptora (Peucedanum praeruptorum)
Function: O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses. Catalyzes specifically the methylation of bergaptol. Not active on xanthotol, isoscopoletin, scopoletin and esculetin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27252733}.
Interaction partners:
Sequence:
MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYVPGGKERTEKEFEALATSAGFKSFRKVCCAFNTWIMEFSK
Protein: Mitochondrial ATP-dependent zinc metallopeptidase, putative (Q38AK2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Stomatin-like protein, putative
- Prohibitin
- Prohibitin
Sequence:
MHRRCPIIPAFPSGRTTPLPLLPSCGGTGALTVFPGGFTQKRHSSVYPQPPVNPLPPYPPYASGYQSFYHPHAHQGVSQVPPPFNSGMGASGYVGVGVPELGTKERPVVVVSAPQKTTWTTRLWLLLLFGIGASCTLSLIEELMSRMQDGNSVTKIGGISRGQQIGMFGSPDVKPVDLTGLDVTFDTIRGCDEAKKELKEIVEFLKEPEKFHKLGGRLPKGALLVGPPGCGKTMLAKAIAKEADVSFFYSAGSEFDEMFVGVGSRRVRELFAAAKARAPSLIFIDEIDALGGKRSGTDHAYSRMTLNQLLAEMDGFDSKDSVIVIAATNTPDSLDKALTRPGRFDVVVSVDPPDMKGREEVLQIYLSKIKAESSVSAAAIARGTTGFTGAELSNLVNIAAIRAATLNNQVVTMNDIEYAKDRVMMGAESAKVIPEDERKVTAYHEGGHALAALLLEKEGAEPVHKATIVPRGNGIMGLVQQLPEKDKYSQSKRQCLARLKVCLAGRVGEEILLGSDDVTTGASSDFHQATKIARNMVRRFGFSGDLGFVDYESSDTPEGAYMSDETKGKIEKEVSTLLQNSYTEIKQMLLSHREELESIAKHLMQHETLSGDELKRIVNGETIPARKEKVSIHHHCSKMPPAGTESMKGKQRPVSIT
Protein: Transcription regulator LexA (LexA-related repressor) (P73722)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: A probable transcription regulator, probably involved in carbon metabolism. Binds and probably regulates expression of bidirectional hydrogenase (hoxEFUHY), probably activates its transcription. A possible regulator of redox-responsive genes. Binds 2 direct repeats of the DNA with sequence 5'-CTA-N(9)-CTA-3' in the upstream region of both its own gene (includes the transcription start site) and crhR (includes the initiation codon) in a sequence-specific manner; does not bind crhR RNA. Binds to the crhR gene, represses its transcription.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21642463}. Note=Localized in the innermost region of the cytoplasm, associated with DNA in an evenly distributed pattern no changes are seen when cells are grown in the dark. {ECO:0000269|PubMed:21642463}.
Interaction partners:
- Protein RecA
- UmuC protein
- DNA repair protein RecN
- UvrABC system protein A
- Holliday junction branch migration complex subunit RuvB
- Holliday junction branch migration complex subunit RuvA
- RNA helicase CrhR
- Crossover junction endodeoxyribonuclease RuvC
- Hydrogenase large subunit
- Glucosylglycerol-phosphate synthase
Sequence:
MEPLTRAQKELFDWLVSYIDETQHAPSIRQMMRAMNLRSPAPIQSRLERLRNKGYVDWTDGKARTLRILHQKPKGVSVIGELKGGELVEADAEEVEKIDFAPLMKKSSVFALRVMSNDLVDDFIVEGDMLILRSVTGEEEIEDGELVAASIKGGKIAIKRYYQDGTKVVLKASNNKGPGQELKASDVEIQGILMGVWRNFQGV
Protein: Serine/arginine-rich splicing factor 12 (Q8I468)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Serine/arginine-rich splicing factor 4
- Alternative splicing factor ASF-1, putative
- Serine/arginine-rich splicing factor 1
- Small ribosomal subunit protein eS30
Sequence:
MGPYINQKNQPMSLLIRKLKFDTSPSIVREKFKRFGAIKDVYLPIDYYTKEPRGFGFVEFYDAKDAEQALKEMNGSEIDGSRIEVFVAQKGRSDPRHMRYKEKGGYAYRKNPDNKIRRRYISKSNSRYGSYSRDKIRRRERSKERFRYRSSYDRKMSSYRDRKNYHMKSYDKYRDRNHDRSLSRRSREYRNNTSRYRDKRRYDKYYRSTSRRASRHEKRNENYKSKYNHSNDDYSDETRNSSKHSRKEHVSRSISFNSEKDDAKKKNDNTSERDNSNDWKGSEQRKEEEDEEVEKEKENEEEEEAIYD
Protein: Thioredoxin peroxidase (Q5A5A0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutathione reductase
- glutathione transferase
- Gtt13p
- Gst3p
- glutathione transferase
- Gtt1p
- Gst2p
- Protein URE2
- Gst1p
- Ecm38p
Sequence:
MRDKKQTKKKKSFFFATHTTMSQQPHLRLGSTAPDFKADTTNGPISFHEYIGDSWAILFSHPAAHTSVCSTELSAFARLEPEFTKRGVKLLAISADPVEANSDWIDDMEDFSGSRVKFPIIADPERKVATLYDMIDHQDATNLDDKGLQLTIRAVFIIDPSKKIRLIMTYPASTGRNTAEVLRVLDSLQLVDKQKVITPINWVPGDDVLVHMGVPDDEARVLFPKYRAIKPYIRLTPLEKEDK
Protein: T. brucei spp.-specific protein (Q38CD9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYETGRVATGGKRQREERRRVPLFWVSVPSCVIMVSLRCDFLNIPVGGCDSDLALRDCCSAALLGSFIPSAFALGAIRGNRRRVSGTSVSFKCGFLPPPPNFLAECPSQVPCQPSIPEKVLGKHRISAAPRPSFLSLLRCGPSVFCRPKPHSPCLPTLLRKQGP
Protein: TSC complex subunit 2 (H3BMQ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGFSGASWSTMAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTDSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESQSFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV
Protein: Anterior gradient 3, protein disulphide isomerase family member (B5MC62)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMLHSALGLCLLLVTVSSNLAIAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFYAQKSKKPLMVIHHLEDCQYSQALKKVFAQNEEIQEMAQNKFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADIAGRYSNRLYTYEPRDLPLCKYSQMISNSGHS
Protein: Pectin lyase-like superfamily protein (Polygalacturonase) (Putative polygalacturonase) (Q38958)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 46
- Proline-rich extensin-like family protein
- Polygalacturonase 1 beta-like protein 2
- Glucuronoxylan 4-O-methyltransferase 2
- Polygalacturonase QRT3
Sequence:
MKTVKSLPILAMLLGVIIVAAAISTVSVEGRKHHVKKIKPKHRRHSKNTPTGSPAPAPYPSTNEGVFNIFSYGAKGDGVSDDSKALVGAWKAACKVVGGKVEIPAGTQFLVKAVTLQGPCKEETVVQIEGILVAPEKIGSWPNSSLFQWLNFKWVSHLTIQGSGTLNGRGYNWWNLDTYQTQTRNKYIPPMKPTALRFYSSNNVTVRDISIVNSPLCHLKFDDSDGVKVNNITISSPENSPNTDGIHLQNTRNVEIQHSNIACGDDCVSIQTGSSNVHIHHINCGPGHGISIGGLGKDKSVACVSDIIVEDISIQNTLAGVRIKTWQGGLGVVKNLTFSNIQVKDVKVPIVIDQYYCDKSKCKNQTRAVSISGVKYNNIVGSFTVQPVRIACSNNVPCMDVDLMDIRLRPSGGIRGLQTHQQQQALCWNSYGKTQGPLVPSSIGYCLRKSNIGGYYSQKVSRSYDKICPS
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (F8W3B7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- B cell linker.
- Lymphocyte cytosolic protein 2a.
- G-protein alpha 12 alpha 12) alpha 12a)
Sequence:
MADRVLEEVFIKRSQQKKKTSPLNFKERLFVLTHDKISYYDYDAEKAKRKSLKGYVDIEKIRCVEVVLPEDSAPPDRHYPFQIVYDEGPLYVFAKSDQIRKHWIHELKNVVRFNKDLMQKYHPCFWEDGVWKCCLQEVKQAMGCRVLETKNGGVFKRGSKNRDSRKPLPPTPEEEKPARPLPPEPPMPPAFSIGMTVIAEYEYAPMTTNDLELRKDEEYTLLEISDPNWFKAKDKYGKEGYIPSNYIVQALNGLEKYDWYCKNINRSQAENLLKTENKDGGFLVRDSGKFTGKYTVSVFTKAGGETSGSCRHYNILLTADGQFYLAEKHNFTNIPELINYHQHNAAGLVSRLKYIVSNRAQNAPCTAGLGYGSWEIDPRQLTFIRELGNGQFGVVKYGKWQGRHDVAIKMVKEGSMSEDDFIEEAKVMMKLCHGNLVQLYGVCTKQRPIYIVTEYLANGCLLNYLQEGLLNPTSIALLEMCKDVSEGMKYLEANQFIHRDLAARNCLVDSNGTIKVTDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLLYCKFSSKSDIWAFGVLMWEIYTQGRMPYDRWNNTEIVEKISAGHRLYRPQMANENVFAIMNSCWHERPDERPTFQELVGVIKDLLFSMQEI
Protein: DNA-binding protein (Arginine-rich protein 6.9 kDa) (Basic viral core protein) (Nucleocapsid protein) (P06545)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays a role in viral DNA packaging and nucleocapsid assembly. Promotes viral gene transcription during the late stage of infection while it is non-essential for the basal level of viral gene transcription.
Subcellular location: Virion {ECO:0000269|PubMed:22951830}. Host cytoplasm {ECO:0000269|PubMed:22951830}. Note=Within the host cell, the majority of P6.9 is distributed near the inner nuclear membrane. Present in both the budded virus (BV) and the occluded virus (OV). The occluded form allows the virus to be transmitted from insect to insect through ingestion of contaminated food while the budded form is responsible for the dissemination of infection throughout the insect host. {ECO:0000269|PubMed:22951830}.
Interaction partners:
Sequence:
MVYRRRRRSSTGTTYGSTRRRRSSGYRRRPGRPRTYRRSRSRSSTGRRSYRTRYY
Protein: Protein CADMIUM TOLERANCE 5 (Cd tolerant 5) (OsCDT5) (B9FMS2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Confers resistance to heavy metal ions (e.g. cadmium (CdCl(2)) and copper (CuCl(2))) by chelating them at the plasma membrane of root cells, thus stopping their entry and reducing their accumulation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5VSB5}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000250|UniProtKB:Q5VSB5}.
Interaction partners:
Sequence:
MYNPPSAQEMTYKDHVQRRHEEKGCLYACLFTLCCCFCCYETCECCLETLCCCC