wanglab/gogpt-training-data huggingface dataset:
Protein: K(+)/H(+) antiporter NhaP2 (Potassium/proton antiporter NhaP2) (P76007)
Organism: Escherichia coli (strain K12)
Function: K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels (By similarity). Participates in control of cell volume in low-osmolarity conditions.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01075}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01075}.
Interaction partners:
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Sequence:
MDATTIISLFILGSILVTSSILLSSFSSRLGIPILVIFLAIGMLAGVDGVGGIPFDNYPFAYMVSNLALAIILLDGGMRTQASSFRVALGPALSLATLGVLITSGLTGMMAAWLFNLDLIEGLLIGAIVGSTDAAAVFSLLGGKGLNERVGSTLEIESGSNDPMAVFLTITLIAMIQHHESNISWMFIVDILQQFGLGIVIGLGGGYLLLQMINRIALPAGLYPLLALSGGILIFSLTTALEGSGILAVYLCGFLLGNRPIRNRYGILQNFDGLAWLAQIAMFLVLGLLVNPSDLLPIAIPALILSAWMIFFARPLSVFAGLLPFRGFNLRERVFISWVGLRGAVPIILAVFPMMAGLENARLFFNVAFFVVLVSLLLQGTSLSWAAKKAKVVVPPVGRPVSRVGLDIHPENPWEQFVYQLSADKWCVGAALRDLHMPKETRIAALFRDNQLLHPTGSTRLREGDVLCVIGRERDLPALGKLFSQSPPVALDQRFFGDFILEASAKYADVALIYGLEDGREYRDKQQTLGEIVQQLLGAAPVVGDQVEFAGMIWTVAEKEDNEVLKIGVRVAEEEAES
Protein: UPF0654 protein C22G7.11c (Q09802)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Pre-mRNA polyadenylation factor fip1
Sequence:
MPDPNRVLAGKKATLHNPNVSQQAKERAEDYIESHSSGQETGDYSAQAGGRDLDYEDLGDYDEDADFDNEEGLNVLGDESGFVDDPMKTGDLVEEDQLEGKNIENVRGGYKATMHNPNVSKQAKTRAQRALEEIDDETQA
Protein: Nucleoplasmin-like protein ANO39 (39 kDa oocyte-expressed nucleolar protein) (Nucleic acid-associated protein 36) (Nucleic acid-binding nuclear protein) (NAAP) (NAAP1) (NAAP2) (Q9NLA3)
Organism: Patiria pectinifera (Starfish) (Asterina pectinifera)
Function: Binds double-stranded RNA and both single-stranded and double-stranded DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10632699, ECO:0000269|PubMed:10828953}. Cytoplasm {ECO:0000269|PubMed:10632699, ECO:0000269|PubMed:10828953}. Note=In oocytes, expression is limited to the germinal vesicle with highest levels in the nucleolus although a considerable portion is present in other regions of the germinal vesicle. In oocytes that progress to the first meiotic metaphase, diffuse expression is observed throughout the egg cytoplasm. {ECO:0000269|PubMed:10632699, ECO:0000269|PubMed:10828953}.
Interaction partners:
Sequence:
MSKEFFWGDSLTGTKKEVKWNPSLDDEDDFDNLDSDGIQHFLFLKQAVLGANAKEGERNVVEIETENFDGDNVKQPLFSLKLGLNESSPLDIGIQPPVTFILTAGSGPVFLSGQHMIEISADDEEELEEDDEEEEEEDEVEVNASPDLPVAKSKKRPLSTSDGTAKKTKMAKLDKDADKKEDDDEEEDDEEEDEVMAMMDDDEDDEDDEDFEGGEDDEEEDEEESDEDEDDEDDNEEEEEEDEDEESPEKPLKTTAKGKKGQMNGTTTAKGDNKPKAKAKTDTKLVKGKAKKKVLALDEIKGKLQESSNVPKKEEKFKNYVRSAFHISEAKKLQDLWGWFRASLQK
Protein: U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (E7EVX8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLADELLADLEEAAEEEEGGSYGEEEEEPAIEDVQEETQLDLSGDSVKTIAKLWDSKMFAEIMMKIEEYISKQAKASEVMGPVEAAPEYRVIVDANNLTVEIENELNIIHKFIRDKYSKRFPELESLVPNALDYIRTVKELGNSLDKCKNNENLQQILTNATIMVVSVTASTTQGQQLSEEELERLEEACDMALELNASKHRIYEYVESRMSFIAPNLSIIIGASTAAKIMGVAGGLTNLSKMPACNIMLLGAQRKTLSGFSSTSVLPHTGYIYHSDIVQSLPPDLRRKAARLVAAKCTLAARVDSFHESTEGKDEIERKFDKWQEPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKERLGLTEIRKQANRMSFGEIEEDAYQEDLGFSLGHLGKSGSGRVRQTQVNEATKARISKTLQRTLQKQSVVYGGKSTIRDRSSGTASSVAFTPLQGLEIVNPQAAEKKVAEANQKYFSSMAEFLKVKGEKSGLMST
Protein: Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N) (Q9EQX9)
Organism: Rattus norvegicus (Rat)
Function: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway.
Interaction partners:
- Ubiquitin conjugating enzyme E2 V1 like 1
- Ubiquitin-conjugating enzyme E2 variant 2
- TNF receptor-associated factor 6
- Mitogen-activated protein kinase kinase kinase 7
- E3 ubiquitin-protein ligase RNF8
- Polyubiquitin-C
- Toll-like receptor 4
- Ubiquitin thioesterase OTUB1
- Ubiquitin-ribosomal protein eL40 fusion protein
- STIP1 homology and U-Box containing protein 1, isoform CRA_b.
Sequence:
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKSNEAQAIETARAWTRLYAMNNI
Protein: Cell surface glycolipoprotein MPT83 (Lipoprotein p23) (P9WNF3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Recombinant, non-modified protein stimulates secretion of cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines in a TLR2-dependent fashion, which leads to increased host innate immunity responses against the bacterium. Serves as a strong human and mouse antigen T cell antigen during M.tuberculosis infection, inducing strong IFN-gamma expression.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:22567094, ECO:0000305|PubMed:8633206}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Secreted, cell wall {ECO:0000305|PubMed:22567094}. Secreted {ECO:0000250|UniProtKB:P0CAX7}.
Interaction partners:
- ECF RNA polymerase sigma factor SigK
- NADH-quinone oxidoreductase subunit D
- Protein DipZ
- 6 kDa early secretory antigenic target
- Lipoprotein LpqH
- Anti-sigma-K factor RskA
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
Sequence:
MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVTTAAMADPAADLIGRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGGEYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADLTVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ
Protein: Autophagy-related protein 9 (Q2XY38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}.
Interaction partners:
Sequence:
YRSLAEEAASPFLEHHPSTGQGPSKTQDAKANAAAAHLDPLGEHGLEQPLDEHDTEHEGEDTPRNSGVMIHMVPETGRARWNHIEDLDSFFSRMYQYQQKHGFTVIVVDEMLQVLEFGFVVWLLAFVMHCVRFDVLFGDTPPGGLNPNKTTLSDVMYPTGECLANFTWVTYLVVFIAAIYLGIRLLKMVYHITQYADIKRFYNSALHIEDSDLDNFTWHEVQQRIRRVQAEQHMCIDKESLTELDIYHRVLRFKNYLVALMNKQLLPVRFHIPLYGEVVSLSRGMLFNIDFILFRGPGSPFQNNWQLRDEFAVRSNQTELAQRLSKLILGVALLNLVLAPVIFVWQLIYFSFSYANILRKEPGALGLRTWSNYGRLYLRHFNELDHELDARLNRAYDYADRYLNSFSSPLAAVIAKNLLFISGGLLLLILALGIYEEHVFQVEHLLAILAGLGAIGVVCRTLIPDENLVWCPEQLMTAILAHVHYLPSEWRQQAHTTKVRQEFSNFFQFKAGYLLSEIFSPFVTPFVLIFVFRPKAIELVRFFRTFTVSVRGVGNVCSFAQMDVRKHGNPDWQLTSELEEMTRATPQQPQQEPQQQSLAGGKTEMSLLRFTLNNPEWQMPKEAKQFLRGVREHAVGELVQAKTSIVQENPLTNSLISFGTMGADYCSIANSVLTAQVTPQQLEISQSLRPGLGPVSGGFPVAASDFRQMLQQNLSASVGPLDSMRRLRLSRAEGRLEGPTDTLLYGLCGVDPRVGSTPLNVGVADMCLSALYLHELNQQKRQARQSRIDEAEDERPGTSHWPPRPPAAPSADTGFGSRHTVITSKAAESTPL
Protein: Glycine betaine transporter BetL (Glycine betaine-Na(+) symporter) (Q9X4A5)
Organism: Listeria monocytogenes
Function: High-affinity uptake of glycine betaine, driven by a sodium-motive force. Involved, with GbuABC and OpuC, in osmoprotection and cryoprotection of Listeria. Does not mediate either carnitine or choline uptake.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKKLTNVFWGSGFLVLLAVLFGAFLPEQFETFTNHIQKFLTSNFGWYYLIVVAIIIIFCLFLVLSPIGSIRLGKPGEEPGYSNKSWFAMLFSAGMGIGLVFWGAAEPLSHYAVQAPGGEVGTQAAMKDALRYSFFHWGISAWSIYAIVALALAYFKFRKNAPGLISATLYPILGKHAKGPIGQLIDIIAVFATVIGVATTLGLGAQQINGGLTYLFGVPNNFTVQFTIIVIVTILFMLSAMSGLDKGIQLLSNVNIYVAGVLLVLTLILGPTLFIMNNFTNSFGDYLQNIIQMSFQTAPDAPDARKWIDSWTIFYWAWWLSWSPFVGIFIARISRGRTIRQFLLGVIVLPALVSVFWFAVFGGSAIFVEQHGNSGLSSLATEQVLFGVFNEFPGGMMLSIVAMILIAVFFITSADSATFVLGMQTTGGSLNPPNSVKVTWGLLQAGIASVLLYAGGLTALQNASIIAAFPFSIVIILMIVSLFVSLTREQEKLGLYVRPKKSQRSQL
Protein: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase (EC 1.14.15.34) (Cytochrome P-450 monooxygenase TylH1) (Q9ZHQ1)
Organism: Streptomyces fradiae (Streptomyces roseoflavus)
Function: Involved in the biosynthesis of the complex macrolide antibiotic tylosin. Catalyzes the hydroxylation of 20-oxo-5-O-beta-mycaminosyltylactone at the C-23 position to yield 5-O-beta-mycaminosyltylonolide.
Interaction partners:
- DNA polymerase I
- 50S ribosomal protein L6
Sequence:
MSSSGDARPSQKGILLPAARANDTDEAAGRRSIAWPVARTCPFSPPEQYAALRAEEPIARAELWDGAPVWLISRQDHVRALLADPRVSIHPAKLPRLSPSDGEAEASRSLLTLDPPDHGALRGHFIPEFGLRRVRELRPSVEQIVTGLLDDLTARGDEADLLADFALPMATQVICRLLDIPYEDRDYFQERTEQATRPAAGEEALEALLELRDYLDRLISGKTGRESGDGMLGSMVAQARGGGLSHADVLDNAVLLLAAGHETTASMVTMSVLVLLQHPTAWRELTVNPGLLPGAVDELLRYLSIADGLRRSATADIEIDGHTIRAGDGLVFLLAAANRDEAVFSEPEAFDIHRSARRHVAFGYGPHQCLGQNLARMELEVALGAVLERLPALRPTTDVAGLRLKSDSAVFGVYELPVAW
Protein: Transcription factor atf-4 homolog (cAMP-dependent transcription factor family member 4) (Q22156)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Involved in positively modulating longevity and stress tolerance, probably acting by positively regulating expression of transsulfuration enzyme cth-2, leading to increased hydrogen sulfide production and therefore increased protein persulfidation, a protective modification of redox-reactive cysteines. May mediate longevity and increased stress resistance induced by mTORC1 suppression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000305|PubMed:35181679}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2-alpha kinase pek-1
- Homeobox protein dve-1
- BZIP domain-containing protein.
- Stress activated transcription factor atfs-1
- Transcription factor atf-6 homolog
- Eukaryotic translation initiation factor 2-alpha kinase gcn-2
- Lon protease homolog, mitochondrial
- Putative ribosomal protein S6 kinase alpha-1
- Putative ribosomal protein S6 kinase alpha-2
Sequence:
MAYVNEQNPQFLLYNGMHNQTHSTPQYHNHHHHHHQSPTYPQSYFNPYSHQSYQQHHLNSDVNFQMVPQSTSVPPDPFCSIEPMETNVQAKEQILEEIVRECEEIERRSNSSASPASNWSSDEHDSQSEKSYHPYKTPEKKERKKAQNRLAATRYREKKRREKEEAMTCIEGLSVTNGKLKDQVSELEREIRYFKKFMTEMGMKTVTD
Protein: SWIM-type domain-containing protein (Q583Y0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDGNPGEDAIRKVIVSASPHCDLLHFVGHVPHPYGVITPQTMMEKNAECVKFSLTPLEREPSVTVSGNHPLFAPVVIPRVKATSSAPAAASEAGMSPYFPHSGVGLAQSAFRSNFETFSWGVVSSDEQRQQNYQSQRHKVTERGDHQVQQQPAHNEAETPNPDAVGEQAFIPTVTDSSSRLVNTSRIGGEIRYEVNFLAVRRSLLQVFLILHMPERSPAVAFRFCSHDPLPGGTTCLSVLPRCAERLPTLAHPAEVTFTDVQATAHWKYSLRCDCRIIQEGEEASVAEGKSQRFISMRWTTGGTPERTLELSALLTEVMTPMLFAVPAKLLKSTEERGKTTPQITGFFQRRSFHLMALIAHGVWCEKVARYIINESNRSGLVALCAETCSAKLKLRDDVSLDANEKWETELTFHRTESCDCTTTERSVQKPKPSKCLHVLVRGCEDVMGWGWGTASTRSGLQDLAEAVTR
Protein: Cytosolic phospholipase A2 gamma (cPLA2-gamma) (EC 3.1.1.4) (Cytosolic lysophospholipase) (EC 3.1.1.5) (Cytosolic lysophospholipid O-acyltransferase) (EC 2.3.1.-) (Phospholipase A2 group IVC) (Q9UP65)
Organism: Homo sapiens (Human)
Function: Calcium-independent phospholipase, lysophospholipase and O-acyltransferase involved in phospholipid remodeling with implications in endoplasmic reticulum membrane homeostasis and lipid droplet biogenesis. Preferentially hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids with choline and ethanolamine head groups, producing lysophospholipids that are used in deacylation-reacylation cycles. Transfers the sn-1 fatty acyl from one lysophospholipid molecule to the sn-2 position of another lysophospholipid to form diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl ether bonds at sn-1 position of lysophospholipids. Catalyzes sn-2 fatty acyl transfer from phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with lower efficiency. In response to dietary fatty acids, may play a role in the formation of nascent lipid droplets from the endoplasmic reticulum likely by regulating the phospholipid composition of these organelles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332}; Lipid-anchor {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:14529291, ECO:0000269|PubMed:9705332}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189, ECO:0000269|PubMed:28336330}; Lipid-anchor. Mitochondrion membrane {ECO:0000269|PubMed:15944408, ECO:0000269|PubMed:19501189}; Lipid-anchor. Lipid droplet {ECO:0000269|PubMed:28336330}. Note=Translocates from endoplasmic reticulum to lipid droplets in response to oleate. {ECO:0000269|PubMed:28336330}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Phospholipase A2, membrane associated
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Guanine nucleotide-binding protein G
- Platelet-activating factor acetylhydrolase
- Patatin-like phospholipase domain-containing protein 6
- Lysosomal phospholipase A and acyltransferase
Sequence:
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPEDEGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTTHNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIEAWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCLA
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha-2) (SCS-alpha-2) (Q8LAD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
Sequence:
MSRQVTRLLGSLRHSGGGCSGSSKVCSLTSLVQSRSFGTTPPPPAAVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVAGVTPKKGGTEHLGLPVFNTVAEAKAETKANASVIYVPAPFAAAAIMEGLAAELDLIVCITEGIPQHDMVRVKAALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKENGTDKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKSLRDAGVKVVESPAKIGAAMFELFQERGLLK
Protein: Aspartate--tRNA ligase, mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Q6PI48)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:15779907, ECO:0000269|PubMed:30006346}. Mitochondrion membrane {ECO:0000269|PubMed:30006346}.
Interaction partners:
- Glutamyl-tRNA
- Bifunctional glutamate/proline--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Glutamyl-tRNA
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- Valine--tRNA ligase, mitochondrial
- GMP synthase
- Alanine--tRNA ligase, cytoplasmic
Sequence:
MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALSKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLETRGVVLRDPTLFSFLWVVDFPLFLPKEENPRELESAHHPFTAPHPSDIHLLYTEPKKARSQHYDLVLNGNEIGGGSIRIHNAELQRYILATLLKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKPTDSKAERAH
Protein: RWD domain-containing protein 4 (Protein FAM28A) (Q6NW29)
Organism: Homo sapiens (Human)
Interaction partners:
- Developmentally-regulated GTP-binding protein 2
- Developmentally-regulated GTP-binding protein 1
Sequence:
MSANEDQEMELEALRSIYEGDESFRELSPVSFQYRIGENGDPKAFLIEISWTETYPQTPPILSMNAFFNNTISSAVKQSILAKLQEAVEANLGTAMTYTLFEYAKDNKEQFMENHNPINSATSISNIISIETPNTAPSSKKKDKKEQLSKAQKRKLADKTDHKGELPRGWNWVDVVKHLSKTGSKDDE
Protein: Zinc finger protein 1 (AtZFP1) (Q42485)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in the regulation of shoot development, downstream of photomorphogenic activation (Probable). Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q39261}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 17
- F-box protein SKIP14
- Zinc finger CCCH domain-containing protein 47
- Zinc finger protein 5
Sequence:
MEPSIKGDQEMLKIKKQGHQDLELGLTLLSRGTATSSELNLIDSFKTSSSSTSHHQHQQEQLADPRVFSCNYCQRKFYSSQALGGHQNAHKRERTLAKRGQYYKMTLSSLPSSAFAFGHGSVSRFASMASLPLHGSVNNRSTLGIQAHSTIHKPSFLGRQTTSLSHVFKQSIHQKPTIGKMLPEKFHLEVAGNNNSNMVAAKLERIGHFKSNQEDHNQFKKIDLTLKL
Protein: Heat stress transcription factor A-9 (AtHsfA9) (AtHsf-21) (Q9LVW2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seed-specific transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Seems to be specialized for the developmental expression of heat shock protein (HSP) genes during seed maturation. Activated by ABI3.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- B3 domain-containing transcription factor ABI3
- Probable protein phosphatase 2C 28
- 17.4 kDa class I heat shock protein
- Chaperone protein ClpB1
- Oil body-associated protein 2A
- Dehydration-responsive element-binding protein 2A
- Heat shock 70 kDa protein 4
- Protein DOG1-like 4
Sequence:
MTAIPNVVDIESSSSSLCQETATETVTVERGSSDSSSKPDDVVLLIKEEEDDAVNLSLGFWKLHEIGLITPFLRKTFEIVDDKVTDPVVSWSPTRKSFIIWDSYEFSENLLPKYFKHKNFSSFIRQLNSYGFKKVDSDRWEFANEGFQGGKKHLLKNIKRRSKNTKCCNKEASTTTTETEVESLKEEQSPMRLEMLKLKQQQEESQHQMVTVQEKIHGVDTEQQHMLSFFAKLAKDQRFVERLVKKRKMKIQRELEAAEFVKKLKLLQDQETQKNLLDVEREFMAMAATEHNPEPDILVNNQSGNTRCQLNSEDLLVDGGSMDVNGRIEIE
Protein: Homeobox protein homothorax (Homeobox protein dorsotonals) (O46339)
Organism: Drosophila melanogaster (Fruit fly)
Function: All isoforms are required for patterning of the embryonic cuticle. Acts with exd to delimit the eye field and prevent inappropriate eye development. Isoforms that carry the homeodomain are required for proper localization of chordotonal organs within the peripheral nervous system and antennal identity; required to activate antennal-specific genes, such as sal and to repress the leg-like expression of dac. Necessary for the nuclear localization of the essential HOX cofactor, extradenticle (exd). Both necessary and sufficient for inner photoreceptors to adopt the polarization-sensitive 'dorsal rim area' (DRA) of the eye fate instead of the color-sensitive default state. This occurs by increasing rhabdomere size and uncoupling R7-R8 communication to allow both cells to express the same opsin rather than different ones as required for color vision.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936, ECO:0000269|PubMed:9463350}.
Interaction partners:
- Homeobox protein extradenticle
- Protein teashirt
- Transcriptional coactivator yorkie
- Homeobox protein abdominal-A
- Homeobox protein abdominal-B
- Homeotic protein antennapedia
- Homeotic protein distal-less
- Protein decapentaplegic
- Protein phosphatase eya
- FI23031p1
Sequence:
MAQPRYDDGLHGYGMDSGAAAAAMYDPHAGHRPPGLQGLPSHHSPHMTHAAAAAATVGMHGYHSGAGGHGTPSHVSPVGNHLMGAIPEVHKRDKDAIYEHPLFPLLALIFEKCELATCTPREPGVQGGDVCSSESFNEDIAMFSKQIRSQKPYYTADPEVDSLMVQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDTTKPPELGSANGEGRSNADSTSHTDGASTPDVRPPSSSLSYGGAMNDDARSPGAGSTPGPLSQQPPALDTSDPDGKFLSSLNPSELTYDGRWCRREWSSPADARNADASRRLYSSVFLGSPDNFGTSASGDASNASIGSGEGTGEEDDDASGKKNQKKRGIFPKVATNILRAWLFQHLTHPYPSEDQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVYTPHPGPSGYGHDAMGYMMDSQAHMMHRPPGDPGFHQGYPHYPPAEYYGQHL
Protein: Uncharacterized protein (Q9BL91)
Organism: Caenorhabditis elegans
Interaction partners:
- X chromosome NonDisjunction factor
- RecQ-mediated genome instability protein 1 homolog
Sequence:
MPGNDDIVMLSDEIVADLRRFIASRPVIQFDRRPGYVPTPWRNCWKEIIEIWSDDDSEDDDGDVITGSQEAQLKRLNNEEAGSSSCRKSPETAKSTPKVRKPVEIPKISSEKLPETANSTENQDAPATEQTILNNRAAGSSPSPKSPRFAEKPSEIAKSTPKIRKLVKISKICSEKLPKTANSTENQDAPATEQTMLNNRAAGSSPSRKSPGFAEKPSEFAKSTPKIRKLVEISKICSEKLPETANSTEKIALDFKKLVEISKIALKAEIPEPERKRLRKSPRLAGSTKIPLIRPEKQSETAKSTPKNFKESKSLNAQCKLEMQLARFKALRLSKPSKNHRSSRQCAAISEKKSKIMMNSWAEDSIFEK
Protein: Toxin To3 (PT-alpha' NaTx14.2) (Toxin Tc48b/Tc49a) (Toxin To48b/To49a) (P60213)
Organism: Tityus obscurus (Amazonian scorpion) (Tityus cambridgei)
Function: Affects sodium-permeability in pituitary GH3 cells in culture. Inhibits the inactivation of sodium activated channels (Nav). Slightly delays the activation time course, and consequently the time to peak. Shifts the voltage dependence of the activation to more negative potentials. Does not reduce the peak sodium-current amplitude.
Subcellular location: Secreted {ECO:0000269|PubMed:11821128, ECO:0000269|PubMed:15025998}.
Interaction partners:
Sequence:
MTRFVLFISCFFVIGMVVECKDGYLVGNDGCKYNCLTRPGHYCANECSRVKGKDGYCYAWMACYCYSMPDWVKTWSRSTNRCGRGK