wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (Transmembrane protein 24) (Q80X80)
Organism: Mus musculus (Mouse)
Function: Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (By similarity). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (By similarity). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (By similarity). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (By similarity). Positively regulates insulin secretion in response to glucose. Phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14523}; Single-pass membrane protein {ECO:0000250|UniProtKB:O14523}. Cell membrane {ECO:0000250|UniProtKB:O14523}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14523}. Note=Localizes to sites of contact between the endoplasmic reticulum and the cell membrane. Embedded into the endoplasmic reticulum membrane via its N-terminal transmembrane domain and associates with cell membrane via its C-terminus. In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane and localizes to the reticular endoplasmic reticulum. Reassociates with cell membrane upon dephosphorylation. {ECO:0000250|UniProtKB:O14523}.
Interaction partners:
Sequence:
MDPDWGQRDVGWAALLVLFAASLITVLGWMLQYARGLWLSRADGGRDSRPASAAEPGGSLRELGVWRSLLRLRATRTSTPEEAGVRGLLASLFAFKSFRENWQRAWVRALNEQACRDGSSIQIAFEEIPQLPPRASISHVTCVDQSERTMVLHCQLSAEEVRFPISVTQQSPAAVSMETYHVTLTLPPTQLEVSLEEIPDEGLLVSWAFTDRPELSLKVLPKLQTRERDEEQPELSTVEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPTMSQAQPSIPRPTRLFLRQLRASHLGSELGGTEELCCAAELDNPMQQKWTKPMRAGPEVEWTEDLALDLGPQSRELTLKVLRSSSCGDAELLGQATLPVGSPSRPMSRRQVCPLTPGPGKSLSPAATVTAELHYEQGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTVVTTVTTVQSRPRVDGKLDSPSRSPSKVEVTEKMTTVLSESSGPSNASHSSSRESHLSNGLDPVAETAIRQLTEPSGRAAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASMQDDAGTSGGPSSPPSDPSATSPGPVDALSSPTSVQEADETTRSDISERPSVDDVESETGSTGALETRSLKDHKVSFLRSGTKLIFRRRPRQKEAGLSQSHDDLSNTTATPSVRKKAGSFSRRLIKRFSFKSKPKANGNPSPQL
Protein: Fumigaclavine A dimethylallyltransferase easL (EC 2.5.1.100) (Ergot alkaloid synthesis protein L) (Tryptophan aminopeptidase) (EC 3.4.11.17) (Q4WZ67)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Fumigaclavine A dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. EasL shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Fumigaclavine B O-acetyltransferase easN
Sequence:
MTKTDAQGRHPQETATHAATTDEEVQDQWRAPFEVLSRTLVFQHEDHRLWWERAASKLATYLRLAKYSVGSQYQHLLMFYSVYAPNLGPWPNDKRDNVHWVCGICPGGENLEISMNYQQGAKCTVRIAAETITPAAGTDKDPFNLTAEKKMIEDLKALQPNLNFTWFNHFQREVLVPEEVALNNDEIISKVPFKNQRLHGLDLSEGAFMLKSYFMPAIRSAITGVENTQIMFESIRKLNLKNANFISALSTLEDWMVPTNGRFMEYWDGISYDAVDACKARIKIYTGIRMKSIEHARDVWTLGGRLQGEDIEKGFDLVARLWRRLMDEEPSTCEMKYWMQWVWELRTDVPFPVPKLYFSVAAAEDHYVSDTVVEILDYLGWDDLVQTHRALMDEAWSLGQTTKSYLAFSYISVTFHSIKGPYITTYGNPSGPRPVF
Protein: Putative uncharacterized oxidoreductase C1773.04 (EC 1.1.1.-) (O94563)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL18A
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS14
- Uncharacterized protein C1235.01
- Small ribosomal subunit protein uS15
- Probable nudix hydrolase C6G9.05
Sequence:
MSELVLITGITGFVASHSAEALLSQGYRVRGTYRFQEKLDGLLKNRPEWEKKVEFVQVPDCRAPNAYVEAAKGVDYVIHAATEVHSNLEPPRKDPHELLHIAIQGCENALIAAAQEPKVKRFVYISSEAALKGPVNYFGDGHVFTEKDWNPKTLREAEESDDELLNYTVCKKLGERAMHAFVARNTPRFQAIALNPPLILGPVFHLQSVDNLNFSTWFFWQLIKGRYEVAPESKFFNYVDVRDLAEAQVKALTAKTDKDRFVISGGAFKNDDIVNVALKYFPQFKDKIAKPNGETSPCNYEVDASLSIKELGLTYRPAEETFKDATESLYKLAGLL
Protein: Serpin-Z1 (ArathZ1) (Q9SH52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable serine protease inhibitor.
Interaction partners:
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Gamma-tubulin complex component 2
- ARP protein
- Peroxidase 18
- Molecular chaperone Hsp40/DnaJ family protein
Sequence:
MDVREAMKNQTHVAMILSGHVLSSAPKDSNVIFSPASINSAITMHAAGPGGDLVSGQILSFLRSSSIDELKTVFRELASVVYADRSATGGPKITAANGLWIDKSLPTDPKFKDLFENFFKAVYVPVDFRSEAEEVRKEVNSWVEHHTNNLIKDLLPDGSVTSLTNKIYANALSFKGAWKRPFEKYYTRDNDFYLVNGTSVSVPFMSSYENQYVRAYDGFKVLRLPYQRGSDDTNRKFSMYFYLPDKKDGLDDLLEKMASTPGFLDSHIPTYRDELEKFRIPKFKIEFGFSVTSVLDRLGLRSMSMYHKACVEIDEEGAEAAAATADGDCGCSLDFVEPPKKIDFVADHPFLFLIREEKTGTVLFVGQIFDPSGPCSGSNSDSDDY
Protein: Transcription factor CP2 (A0A0G2JTJ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Zinc finger protein 410
- Gamma-aminobutyric acid receptor subunit beta-3
Sequence:
MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPENENEILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGVIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKIDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVSNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQPQQPQPQQKQEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPQQISQIYKQGPTGIHVLISDEMVQNFQEEACFILDTMEAETSDSYHVILK
Protein: Cell division cycle protein, putative (Q4GYQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MPN domain-containing protein
- Ubiquitin fusion degradation protein, putative
- Ubiquitin thioesterase OTU
- UBX domain-containing protein
- UBX domain-containing protein
- Ubiquitin fusion degradation protein 2, putative
- Guanine nucleotide-binding protein subunit beta-like protein
- Polyubiquitin, putative
Sequence:
MAYSGAGFLILRAQIAWWPPAAELHRHPLDPKRTFFSAITDGGVSIGAGKQFVSLSRLGKSVVLGGRPLMNCSSSPPCLQVYDPFSGMEITVAFKVEGGLTEGSKQCVLDVSTLREFVNDDRVRVTAAPLTAGVPFHQLQEFLQLDEGEEENDATCGEHHGGHRNHDNGFANRPGNYHSLFGDRYLGVALRHITHRLKCSPRPAVCSVLFSGEHGVGKTYAVRRLLELVPPVVDICGCPHLVERREMSIAALLLLSEQEAVATVQAVFTPPLVEAHHDSGNRVNGAEPCGVLLLVTLDRIDLLVSAANSLVALVTHQLCMVLDELQHGVGEGGGRIVVTLATAESTKSIPTALLARLGQRLVNLAHPTLSERLRFIRTTCNDADNLRSYSPCVLERAAEALSGRTAAELQAMKVDEVLQLLEREAALHRKHEPFAKNSVTDVPDEYRGLVGLSDIIREVEELVVWPLQQRKLLSRCGVQPQKGLVVYGPPGSGKTALLTRLARRLKSARVHVLLVDGLSLIEKEVGRTEKNIASLFAAARATSPTALFLDNIDSLAPPRGRETGEVSTTADRSLSTLLTEMDGIGGGHTGSDVPLVFVVAAASNPEALDAAISRPGRLDLHITLPLPTIEALQQHIVRRLVEAVEACDEAEAITADFIANVDAYVMRWLGRSPSATVADANDFVRHILLRVVVEPEGVPGAKDRLLECFTKVLPL
Protein: Amino acid--[acyl-carrier-protein] ligase 1 (EC 6.2.1.n2) (Amino acid:[carrier-protein] ligase [AMP forming] 1) (aa:CP ligase 1) (Aminoacyl-[acyl-carrier-protein] synthetase 1) (L-glycine:[acyl-carrier-protein] ligase 1) (Q89VT8)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: Catalyzes the ATP-dependent activation of L-glycine and its transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein bsr0959 of yet unknown function. May participate in nonribosomal peptide synthesis or related processes. L-alanine is a poor substrate whereas L-serine or D-amino acids are not substrates for ATP-dependent activation. Does not display tRNA aminoacylation activity.
Interaction partners:
- Aminoacyl carrier protein 1
- Acyl-CoA dehydrogenase
- Acyl-CoA dehydrogenase
- Bll7938 protein
- Blr2501 protein
- Valine--tRNA ligase
- Putative membrane protein insertion efficiency factor
Sequence:
MNIAVLPNSPDTAPQIADPLDHLADKLFHSMGSDGVYARTALYESIVERLAALITSHREAGTEALRFPPVMSRAQLEKSGYLKSFPNLLGCVCGLHGTEREINAAVSRFDAGGDWTTSLSPADLVLSPAACYPVYPIAASRGPLPKGGLRFDVAADCFRREPSKHLDRLQSFRMREYVCIGTPDDVSDFRERWMVRAQAIARDLGLTFRVDYASDPFFGRVGQMKAVSQKQQQLKFELLIPLRSEEQPTACMSFNYHREHFGTTWGIQDANGEPAHTGCVAFGMDRLAVAMFHTHGTDLSAWPAKVRDILGLQPHVAAGAHGEGWR
Protein: Regulator of G-protein signaling rgs-10 (O45523)
Organism: Caenorhabditis elegans
Function: Shown to have a role in viability and embryogenesis.
Interaction partners:
- Regulator of G-protein signaling rgs-6
- Regulator of G-protein signaling rgs-3
- RGS domain-containing protein
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Regulator of G-protein signaling egl-10
- Receptor-type guanylate cyclase gcy-17
- Receptor-type guanylate cyclase gcy-25
Sequence:
MSLAVFSPCDVASKLLSEVVGEKYPKVDDDDSIVEPVTSLCLPQLSYEDFHHFSVIPLWNKTFPCRLATEWNPKNKKDAPPKKKNALVILERVASRSNQNAVSRVINILRSKVHLMFSSSNELPSSEDVERWKKSPETLAASEYGCNLFIQFLKEQTSENEVDFWLDCQKFRSSKMSSRQNEARRIFDEYFAMGSPKKIYIERYLWCVVQAYLVNDPGWRHTFDVAQAYVGLKLAKKSHKKFLEDPLYLDLVELVTSGVNYNKFWHDKLE
Protein: Uncharacterized protein YbfE (P0AAU7)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Flavodoxin 1
- Ferric uptake regulation protein
- DNA gyrase inhibitor
- Acetolactate synthase isozyme 2 small subunit
- Uncharacterized protein YebG
- Negative modulator of initiation of replication
- Guanosine-inosine kinase
- UPF0352 protein YejL
Sequence:
MAKEQTDRTTLDLFAHERRPGRPKTNPLSRDEQLRINKRNQLKRDKVRGLKRVELKLNAEAVEALNELAESRNMSRSELIEEMLMQQLAALRSQGIV
Protein: Lipoprotein LpqH (19 kDa lipoprotein antigen) (Putative transporter LpqH) (p19) (P9WK61)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Based on its structure might be involved in ligand transport (Ref.25) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25041568, ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:1906192}. Secreted, cell wall {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:16098710}. Cell surface {ECO:0000269|PubMed:25041568, ECO:0000269|PubMed:25359607}. Secreted {ECO:0000269|PubMed:16098710, ECO:0000305|PubMed:1906192}. Extracellular vesicle, bacterial extracellular vesicle {ECO:0000269|PubMed:21364279}. Host cytoplasm {ECO:0000269|PubMed:11123323}. Note=A soluble cell wall-associated protein (PubMed:10426995). Also found in culture filtrate in increasing quantities during growth (PubMed:16098710, PubMed:1906192). Following infection of mouse macrophage cell line J774A.1 with live (but not heat-killed) bacteria the protein is released in host cytoplasm at 1 hr but decreases dramatically by 3 hrs: release into the host requires protein lipidation and traffics from the immature phagosome through the host class I MHC antigen peptide presentation pathway (PubMed:11123323). Present in bacterial extracytoplasmic vesicles, both in mouse macrophages and in culture media (PubMed:21364279). Immunoelectron microscopy indicates this protein is close to the cell surface (PubMed:25041568). {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:11123323, ECO:0000269|PubMed:16098710, ECO:0000269|PubMed:1906192, ECO:0000269|PubMed:21364279, ECO:0000269|PubMed:25041568}.
Interaction partners:
- Lipoprotein LprA
- Lipoarabinomannan carrier protein LprG
- Phosphate-binding protein PstS 1
- Putative phthiocerol dimycocerosate transporter LppX
- Cell surface glycolipoprotein MPT83
- Putative diacylated glycolipid transporter LprF
Sequence:
MKRGLTVAVAGAAILVAGLSGCSSNKSTTGSGETTTAAGTTASPGAASGPKVVIDGKDQNVTGSVVCTTAAGNVNIAIGGAATGIAAVLTDGNPPEVKSVGLGNVNGVTLGYTSGTGQGNASATKDGSHYKITGTATGVDMANPMSPVNKSFEIEVTCS
Protein: DNA helicase/primase complex-associated protein (HEPA) (Primase-associated factor) (P10192)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04010}.
Interaction partners:
Sequence:
MDTADIVWVEESVSAITLYAVWLPPRAREYFHALVYFVCRNAAGEGRARFAEVSVTATELRDFYGSADVSVQAVVAAARAATTPAASPLEPLENPTLWRALYACVLAALERQTGPVALFAPLRIGSDPRTGLVVKVERASWGPPAAPRAALLVAEANIDIDPMALAARVAEHPDARLAWARLAAIRDTPQCASAASLTVNITTGTALFAREYQTLAFPPIKKEGAFGDLVEVCEVGLRPRGHPQRVTARVLLPRDYDYFVSAGEKFSAPALVALFRQWHTTVHAAPGALAPVFAFLGPEFEVRGGPVPYFAVLGFPGWPTFTVPATAESARDLVRGAAAAYAALLGAWPAVGARVVLPPRAWPGVASAAAGCLLPAVREAVARWHPATKIIQLLDPPAAVGPVWTARFCFPGLRAQLLAALADLGGSGLADPHGRTGLARLDALVVAAPSEPWAGAVLERLVPDTCNACPALRQLLGGVMAAVCLQIEETASSVKFAVCGGDGGAFWGVFNVDPQDADAASGVIEDARRAIETAVGAVLRANAVRLRHPLCLALEGVYTHAVAWSQAGVWFWNSRDNTDHLGGFPLRGPAYTTAAGVVRDTLRRVLGLTTACVPEEDALTARGLMEDACDRLILDAFNKRLDAEYWSVRVSPFEASDPLPPTAFRGGALLDAEHYWRRVVRVCPGGGESVGVPVDLYPRPLVLPPVDCAHHLREILREIELVFTGVLAGVWGEGGKFVYPFDDKMSFLFA
Protein: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic (Protein PnsB4) (NDH DEPENDENT FLOW 6) (NDH-DEPENDENT CYCLIC ELECTRON FLOW 6) (Q8RXS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18535009}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- NAD
- NAD
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
- Photosynthetic NDH subunit of lumenal location 3, chloroplastic
- NAD
- NAD
- Photosystem I chlorophyll a/b-binding protein 6, chloroplastic
Sequence:
MAEAFTSFTFTNLHIPSSYNHSPKQNSGPNHGYWLSKNVNEKRERNLMRGSLCVRKALPHDLPLMAVMVQQIEGMRDIITEKHVWHLSDKAIKNVYMFYIMFTCWGCLYFGSAKDPFYDSEEYRGDGGDGTGYWVYETQEDIEEKARAELWREELIEEIEQKVGGLRELEEAVTK
Protein: Protein cornichon homolog 2 (CNIH-2) (Cornichon family AMPA receptor auxiliary protein 2) (Cornichon-like protein) (Q5BJU5)
Organism: Rattus norvegicus (Rat)
Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein {ECO:0000269|PubMed:19265014}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells).
Interaction partners:
- Glutamate receptor 1
- Voltage-dependent calcium channel gamma-8 subunit
- Glutamate receptor 2
- Glutamate receptor 3
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-2 subunit
- Voltage-dependent calcium channel gamma-7 subunit
- Voltage-dependent calcium channel gamma-5 subunit
- Voltage-dependent calcium channel gamma-4 subunit
- Glutamate receptor ionotropic, kainate 1
Sequence:
MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF
Protein: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 (Q9M9M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13-B
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 8-A
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 9
Sequence:
MALTVAKSALEAIREKGLGGFMRMIREEGFMRCLPDGNLLQTKIHNIGATLVGVDKFGNKYYQKLGDTQYGRHRWVEYASKDRYNASQVPAEWHGWLHFITDHTGDELLSLKPKRYGLEHKENFSGEGDAYIYHSKGHTLNPGQKNWTRYQSWVPTKTQ
Protein: Probable phospholipid-transporting ATPase IM (EC 7.6.2.1) (ATPase class I type 8B member 4) (P4-ATPase flippase complex alpha subunit ATP8B4) (Q8TF62)
Organism: Homo sapiens (Human)
Function: Component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:20947505}; Multi-pass membrane protein {ECO:0000269|PubMed:20947505}. Golgi apparatus {ECO:0000269|PubMed:20947505}.
Interaction partners:
- Cell cycle control protein 50B
- Cell cycle control protein 50A
Sequence:
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYFLCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALSVTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTSWCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWESQTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDRKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDDLDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSEENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNTRKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAYRDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETVTSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNLFGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELACMCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQAVLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQTVYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVLHGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFINHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVMPVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGELITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL
Protein: DEAD-box ATP-dependent RNA helicase 53, mitochondrial (EC 3.6.4.13) (Q9LUW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25732537}.
Interaction partners:
- Nuclear intron maturase 2, mitochondrial
- Nuclear intron maturase 1, mitochondrial
- Nuclear intron maturase 4, mitochondrial
- Nuclear protein-like
- Protein WHAT'S THIS FACTOR 9
- Pentatricopeptide repeat-containing protein At1g74900, mitochondrial
- RNA-binding KH domain-containing protein
- Regulator of nonsense transcripts 1 homolog
- RNA helicase
- Splicing factor-like protein 1
Sequence:
MITTVLRRSLLDASKRNLSASLTSINTVLFHNLAPAATRVSDLALIGSSDVKAGFPFGVEAKGIHFQSGPLDFRASMVSQAGFAISESSERRVGDSESVGGDGLAISELGISPEIVKALSSKGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKYNAKHGRGRNPLCLVLAPTRELARQVEKEFRESAPSLDTICLYGGTPIGQQMRQLDYGVDVAVGTPGRVIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIILEKLPEKRQSMMFSATMPSWIRSLTKKYLNNPLTVDLVGDSDQKLADGITTYSIIADSYGRASIIGPLVTEHAKGGKCIVFTQTKRDADRLSYALARSFKCEALHGDISQSQRERTLAGFRDGHFNILVATDVAARGLDVPNVDLIIHYELPNNTETFVHRTGRTGRAGKKGSAILIYSQDQSRAVKIIEREVGSRFTELPSIAVERGSASMFEGIGSRSGGSFGGGMRDRGSSFGGRSGGGGYGGSSGGYGGGRSGGSSNRYSGDSDRSGFGSFGMRSPEGYGSDRSSQSGGRSSFGGGRSGGSSNNRSSGFGDFGSDRSSQSGGRSSFGGFGSNDGKRSY