wanglab/gogpt-training-data huggingface dataset:
Protein: Actin, alpha cardiac muscle 1 (EC 3.6.4.-) (Alpha-cardiac actin) [Cleaved into: Actin, alpha cardiac muscle 1, intermediate form] (P68033)
Organism: Mus musculus (Mouse)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Troponin I, cardiac muscle
- Myosin-6
- Myosin light chain 3
- Tropomyosin alpha-1 chain
- Myosin-7
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 4
- Tropomyosin beta chain
- Tropomyosin alpha-4 chain
- Tropomyosin alpha-3 chain
Sequence:
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Protein trichome birefringence-like 34 (O80919)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21124849}; Single-pass type II membrane protein {ECO:0000269|PubMed:21124849}.
Interaction partners:
- Protein REDUCED WALL ACETYLATION 2
- Protein REDUCED WALL ACETYLATION 3
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- non-specific serine/threonine protein kinase
- Receptor-like serine/threonine-protein kinase NCRK
Sequence:
MAKRQLLMLGIRTSFHTIAAVLVAGLIFTAVFLSRNSLPKENPQSHGVTDRGGDSGRECNLFEGKWVFDNVSYPLYKEEDCKFMSDQLACEKFGRKDLSYKFWRWQPHTCDLPRFNGTKLLERLRNKRMVYVGDSLNRGQWVSMVCMVSSVITNPKAMYMHNNGSNLITFKALEYNATIDYYWAPLLVESNSDDPTNHRFPDRIVRIQSIEKHARHWTNSDIIVFNSYLWWRMPHIKSLWGSFEKLDGIYKEVEMVRVYEMALQTLSQWLEVHVNPNITKLFFMSMSPTHERAEEWGGILNQNCYGEASLIDKEGYTGRGSDPKMMRVLENVLDGLKNRGLNMQMINITQLSEYRKEGHPSIYRKQWGTVKENEISNPSSNADCIHWCLPGVPDVWNELLYAYILDHHSS
Protein: R2D2 (Q2Q0K7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNKSAVSALQEFCARTQINLPTYSFIPGEDGGYVCKVELLEIEALGNGRSKRDAKHLAASNILRKIQLLPGIHGLMKDSTVGDLDEELTNLNRDMVKELRDYCVRREMPLPCIEVVQQSGTPSAPEFVACCSVASIVRYGKSDKKKDARQRAAIEMLALISSNSDNLRPDQMQVASTSKLKVVDMEESMEELEASRRKKFTTYWELKEAGSVDHTGMRLCDRHNYFKNFYPTLKKEAIEAINSDEYESSKDKAMDVMSSLKITPKISEVESSSLVPLLSVELNCAFDVVLMAKETDIYDHIIDYFRTMLI
Protein: Programmed cell death protein 2 C-terminal domain-containing protein (Q580E6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein uS5
Sequence:
MAKKEVVWLGTPTEADGSELSSPFTSRIGGSAVLFREAPTYSIFNCPKCRSSRWVSLLTQIYAPLDVYDRIVYVLICSSCSEGKGSFCFAVRSQNFNPSYVQSSPAPVVGGGEDEGITFVEDGDWGDDDPKYVDEGPNEVCITNLTCTTMADECKVGSPTQSTDVSSVLVPHGTKVPVEGFCYPCFVLNIFEEPPKPKLCYGTVPDQLLKAQQTYGEDAVETTVVEDEDEPLAEKLLRKYVDRIGRVPSQCVRWGPGQKPLRSSPAPIVIPRCPRCSNERRYELQLTSPIIYFLTKGKEEKDHSLHFGSVLVYTCGGNCNVQPYSLEHCVVEDEV
Protein: Guanine nucleotide-binding protein subunit alpha-12 (G alpha-12) (G-protein subunit alpha-12) (Q63210)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1). GNA12-dependent Rho signaling also regulates protein phosphatese 2A activation causing dephosphorylation of its target proteins (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway and up-regulating pro-inflammatory cytokine production. Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). Together with NAPA promotes CDH5 localization to plasma membrane (By similarity). May play a role in the control of cell migration through the TOR signaling cascade.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12176367}; Lipid-anchor {ECO:0000269|PubMed:12176367}. Lateral cell membrane {ECO:0000250|UniProtKB:Q03113}; Lipid-anchor {ECO:0000269|PubMed:12176367}. Cytoplasm {ECO:0000250|UniProtKB:Q03113}. Note=CDH1 enhances cell membrane localization. {ECO:0000250|UniProtKB:Q03113}.
Interaction partners:
- Rho guanine nucleotide exchange factor 12
- Sphingosine 1-phosphate receptor 2
- Lysophosphatidic acid receptor 1
- Sphingosine-1-phosphate receptor 3
- Sphingosine 1-phosphate receptor 5
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 1
- Guanine nucleotide-binding protein subunit alpha-13
- Lysophosphatidic acid receptor 2
- Transforming protein RhoA
Sequence:
MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPHRLEDVQRYLVQCFDRKRRNRGKPLFHHFTTAIDTENIRFVFHAVKDTILQENLKDIMLQ
Protein: Interleukin 13 (Interleukin 4/13A) (Interleukin-13 precursor) (B3IWZ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Interleukin family protein
- Interleukin 4 receptor, tandem duplicate 1.
- Signal transducer and activator of transcription
- Interleukin-4
- Arginase
- T-box 21 like
- Interleukin 17_5
- Lymphotoxin-alpha
- Interleukin 17_2
- Interleukin 17_1
Sequence:
MMKTLLLLACTVFVSGFTLKGTDAMHKTVLKELVTELEAVLVNPPKETKAKEEIFLVDLGKKGSGLKCEHDYFCQAEEEMVKKVSGLSGVKFDPFRTDKKLMRNLNTYNHQDEKNCKKEIRSHAADEDLEEITLDVFLKDLLKCVKNINSQKSPRPS
Protein: Ionotropic receptor 76a, isoform D (B7Z084)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFVYTKEFEDKKDSYLSGYIFQDQPNILVITSQYLNSSTFEIKTNRFVGPRNFNKNPEPVEFYILQRFDAKGTKATWETQSAMSSKMRNLKGREVVIGIFDYKPFMLLDYLCELGKATIIL
Protein: DNA-directed RNA polymerases IV and V subunit 3B (DNA-directed RNA polymerase II 36 kDa polypeptide B) (DNA-directed RNA polymerase II subunit RPB3-B) (RNA polymerase II subunit 3-B) (RNA polymerase II subunit B3-B) (Q39212)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase V subunit 7
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerase II subunit 4
Sequence:
MDGVTYQRFPTVKIRELKDDYAKFELRETDVSMANALRRVMISEVPTMAIHLVKIEVNSSVLNDEFIAQRLSLIPLTSERAMSMRFCQDCEDCNGDEHCEFCSVEFPLSAKCVTDQTLDVTSRDLYSADPTVTPVDFTSNSSTSDSSEHKGIIIAKLRRGQELKLKALARKGIGKDHAKWSPAATVTYMYEPDIIINEEMMNTLTDEEKIDLIESSPTKVFGIDPVTGQVVVVDPEAYTYDEEVIKKAEAMGKPGLIEIHPKHDSFVFTVESTGALKASQLVLNAIDILKQKLDAIRLSDNTVEADDQFGELGAHMREG
Protein: RING1 and YY1-binding protein (Apoptin-associating protein 1) (APAP-1) (Death effector domain-associated factor) (DED-associated factor) (YY1 and E4TF1-associated factor 1) (Q8N488)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (By similarity). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes. May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis. May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. May bind to DNA (By similarity). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3.
Subcellular location: Nucleus {ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:11953439, ECO:0000269|PubMed:14765135, ECO:0000269|PubMed:27060496}. Cytoplasm {ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:14765135}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8CCI5}. Note=Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies (By similarity). {ECO:0000250|UniProtKB:Q8CCI5}.
Interaction partners:
- Lysine-specific demethylase 2B
- Polycomb group RING finger protein 1
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- Transcriptional repressor protein YY1
- Polycomb group RING finger protein 5
- Polycomb complex protein BMI-1
- Polycomb group RING finger protein 6
- YY1-associated factor 2
- Polycomb group RING finger protein 2
Sequence:
MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKQDKEKPEKDKEISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF
Protein: F-box protein SKIP16 (SKP1-interacting partner 16) (Q9LND7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- F-box/FBD/LRR-repeat protein At3g14710
- Aquaporin TIP4-1
- TIP41-like protein
- non-specific serine/threonine protein kinase
- Protein AUXIN SIGNALING F-BOX 3
- Vacuolar fusion protein MON1 homolog
Sequence:
MGLEDAGDLVLHIVLSKIGPENTARVACVSKRLKVSASEESLWSIFCSNDLNISTPLDPHGDPAPSFKRAYQLWRESFRMYPWNLVKRVRLCWDNLKQWLTLNFPEAKATLRKGVTEDDLQEFETSLKVKLPLPTRLLYRFVDGQELSSPNGLDGSLGLIGGYSAYSHDVNVYLLPLKEVMRETKESFMRDLGFSSRLDLIVMAASVVASLKIFLLDCTTGQLFTGTSNRQLLPCVPDALVRSVHDTNGDQQQDAMLLWLEEHGRRLQTGTINVRQQNNVKSISLFPEIPPLCSVSVTNGVQVRASSVFIPEISNLRDQPPAYWYAYSIRMSLMPEGCILNGTHHSSCQLYWRHWVIRADNEVIDNVNGEAVIGKYPLLQAGEEEFVYESCSSFPTTAGSIDGSFTFVPGSLRDPKGSQFEVKVVEFPLELPDYIF
Protein: Probable protein phosphatase 2C 20 (AtPP2C20) (EC 3.1.3.16) (AtPPC3;1.2) (Q9SIU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in defense signaling.
Interaction partners:
Sequence:
MAGREILHKMKVGLCGSDTGRGKTKVWKNIAHGYDFVKGKAGHPMEDYVVSEFKKVDGHDLGLFAIFDGHLGHDVAKYLQTNLFDNILKEKDFWTDTKNAIRNAYISTDAVILEQSLKLGKGGSTAVTGILIDGKTLVIANVGDSRAVMSKNGVASQLSVDHEPSKEQKEIESRGGFVSNIPGDVPRVDGQLAVARAFGDKSLKIHLSSDPDIRDENIDHETEFILFASDGVWKVMSNQEAVDLIKSIKDPQAAAKELIEEAVSKQSTDDISCIVPCFLRREALSERYCR
Protein: Vacuolar protein sorting-associated protein 20 (Amino acid sensor-independent protein 10) (Charged multivesicular body protein 6) (ESCRT-III complex subunit VPS20) (Vacuolar protein-targeting protein 20) (Q04272)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Required for the oligomerization of SNF7 into a membrane-associated filament. The VPS20-SNF7 subcomplex is responsible for the membrane association of the ESCRT-III complex. Also required for the RIM101 repressor proteolytic activation.
Subcellular location: Endosome membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 4
- Vacuolar protein sorting-associated protein 28
- Vacuolar protein-sorting-associated protein 24
- DOA4-independent degradation protein 4
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein SNF7
- Vacuolar-sorting protein SNF8
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Vacuolar-sorting protein BRO1
Sequence:
MGQKSSKVHITKTDRAILEVKRSKDEIHKFTRRTDNLILVEKSQLKDLIRKNPENYKSNMKVRFLLKRIHYQEHLLQQASDQLINLENMVSTLEFKMVEKQFINGLKNGNEILKKLNKEFSNVDELMDDVQDQIAYQNEINETLSRSLVGTSNYEDDLDKELDALESELNPEKMNNAKVANMPSTEGLPSLPQGEQTEQKEREEFATEERSDTKEPLALLS
Protein: Vacuolar fusion protein MON1 homolog (Q8MRZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEVEQTSVRSDTNSTCEYLDAEGDPESPNLYQEADPDQEAEQQNHSIISELRDGLGTMRDNSALSPEPGQENKGLAASVESLALSTSTSAKTEDSIGGGLEEEYDYQHDSLWQGQKKHIFILSEAGKPIFSLHGNEDKLATLFGVIQALVSFVQMGQDAITSIHAGGIKFAFMQRSSLILVAASRSNMSVQQLQLQLGDVYNQILSILTYSHMTKIFERRKNFDLRRLLSGSERLFYNLLFYDSSSAKVSNNIFTFLTNSIRVFPLPTTIRSQITSAIQSNCSKIKNLVFAVLIANNKLIALVRMKKYSIHPADLRLIFNLVECSESFKSSENWSPICLPKFDMNGYLHAHVSYLADDCQACLLLLSVDRDAFFTLAEAKAKITEKLRKSHCLEAINEELQQPFNAKLYQQVVGIPELRHFLYKPKSTAQLLCPMLRHPYKSLTELERLEAIYCDLLHRIHNSSRPLKLIYEMKEREVVLAWATGTYELYAIFEPVVDKATVIKYVVKLIKWIEKEYDVYFIRNHATF
Protein: LD27185p (Q7K206)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FATNISRLGNYFKIVNKMALPQKHFKRGSPKPEIPEDGVLRYYSMRFCPYSQRAGLVLAAKKIPHHTVYIDLSEKPEWYIDYSPLGKVPAIQLPNLPGQPALVESLVIAEYLDEQYPGEGSLFPKDPLQKALDRILIERLSPAVSAIYPVLFTKNPPADAIKNFETALDVFEQEITKRGTPYFGGNKIGIADYMIWPWFERFPALKYTLDEPYELDKTRYQNLLKWRDLVAQDEAVKATALDARIHAKFMKTRHENKPDYDVAFQPL
Protein: Protein MalY [Includes: Cystathionine beta-lyase MalY (CBL) (EC 4.4.1.13) (Beta-cystathionase MalY) (Cysteine lyase MalY) (Cysteine-S-conjugate beta-lyase MalY); Maltose regulon modulator] (P23256)
Organism: Escherichia coli (strain K12)
Function: Acts as a beta-cystathionase and as a repressor of the maltose regulon.
Interaction partners:
- Cystathionine beta-lyase MetC
- Cysteine synthase A
- PTS system maltose-specific EIICB component
- Cystathionine gamma-synthase
- Acetyl esterase
- Methionine synthase
- 3-mercaptopyruvate sulfurtransferase
- D-cysteine desulfhydrase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Aspartate aminotransferase
Sequence:
MFDFSKVVDRHGTWCTQWDYVADRFGTADLLPFTISDMDFATAPCIIEALNQRLMHGVFGYSRWKNDEFLAAIAHWFSTQHYTAIDSQTVVYGPSVIYMVSELIRQWSETGEGVVIHTPAYDAFYKAIEGNQRTVMPVALEKQADGWFCDMGKLEAVLAKPECKIMLLCSPQNPTGKVWTCDELEIMADLCERHGVRVISDEIHMDMVWGEQPHIPWSNVARGDWALLTSGSKSFNIPALTGAYGIIENSSSRDAYLSALKGRDGLSSPSVLALTAHIAAYQQGAPWLDALRIYLKDNLTYIADKMNAAFPELNWQIPQSTYLAWLDLRPLNIDDNALQKALIEQEKVAIMPGYTYGEEGRGFVRLNAGCPRSKLEKGVAGLINAIRAVR
Protein: Protein disulfide isomerase pTAC5, chloroplastic (EC 5.3.4.1) (Protein PLASTID TRANSCRIPTIONALLY ACTIVE 5) (pTAC5) (A1A6M1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits zinc-dependent disulfide isomerase activity. Required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:23922206}.
Interaction partners:
- Heat shock protein 21, chloroplastic
- Cysteine/Histidine-rich C1 domain family protein
- QWRF motif-containing protein 2
- DnaJ/Hsp40 cysteine-rich domain superfamily protein
- Fructokinase-like 2, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Peptidyl-prolyl cis-trans isomerase FKBP19, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 6, chloroplastic
- UDP-glycosyltransferase 79B7
Sequence:
MASSSLPLSLPFPLRSLTSTTRSLPFQCSPLFFSIPSSIVCFSTQNPDREEVRWLREEQRWIREEQRWIREEQRWIRERESLLQEISDLQLRIQSLESRNSQLGNSIPDTISNIAALLQVLKEKNRISESGLSATPMVLESTREQIVEEVEEEEKRVIIAEEKVRVSEPVKKIKRRILKVGSEGDDVQALQEALLKLGFYSGEEDMEFSSFSSGTASAVKTWQASLGVREDGVMTAELLQRLFMDEDVETDKDEASTMKKEEAGNGAVFTSVTQVPEKKQSIVKDQSDREVDVTQNRVFLLGENRWEDPSRLIGRNKPVDRSESTNTKTRCITCRGEGRLMCLECDGTGEPNIEPQFMEWVGEDTKCPYCEGLGYTVCDVCDGKKNL
Protein: Cornichon related (Q9VQL3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- RH07106p
- Glutamate receptor IB, isoform B
- Glutamate receptor 1
Sequence:
MFLPETATFCITLLVYGAILLLLIYYVLTLADLECDYLNAQECCRRLNFWVIPKFGSHALLCVLLLLGGHWVMFLLNLPMVIWLFYELHRQRRDSLGVYDPVDIHSRGLLKVHLRNCMIYLGYYFVMFFVGLYCLISSLIKGDPIKRYEDDEIVTDF
Protein: Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II) (P21534)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00410}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase polypeptide 5, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MLFFNSILNDAPSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILILVALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTNENEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS
Protein: Ribosomal RNA large subunit methyltransferase E (EC 2.1.1.166) (23S rRNA Um2552 methyltransferase) (Cell division protein FtsJ) (rRNA (uridine-2'-O-)-methyltransferase) (P0C0R7)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- ATP-dependent zinc metalloprotease FtsH
- Ribosomal RNA small subunit methyltransferase A
- GTPase ObgE/CgtA
- Ribosomal RNA small subunit methyltransferase B
- Ribosomal RNA small subunit methyltransferase F
- GTPase Der
- Ribosomal large subunit pseudouridine synthase D synthase)
- tRNA dimethylallyltransferase
- Ribosomal RNA large subunit methyltransferase M
- Signal recognition particle protein
Sequence:
MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGKGRIIACDLLPMDPIVGVDFLQGDFRDELVMKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALEMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP
Protein: Complement C2 (EC 3.4.21.43) (C3/C5 convertase) (A0A096MKF9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAPLLALLALLQLGPASHCPNPGISVGTMRTGSSFDLGDKVSYRCSSTNLVLTGSVERECLSNGVWSGSEPICRQPYSYDFPEDVASALGTSFTHLLGATNPIQKRTENLGRKIQIQRSGHLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYKDHENATGTNTYEALNSVYLMMNNQMDRLGMETSAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREILGISRNRNDYLDIYAIGVGKLDVDWKELNELGSKKDGERHAFILQDAKAVQQVFEHILDVSKLTDTICGVGNMSVNASDQERTPWQVTFKPKSKETCQGSLISDQWVLTAAHCFHDAQMEDRHLWRVIVGDPTSHHGKEFHVEEVLVAPGFNVHAKQSQGISEFYADDIALLKLSQRVKMSSHARPICLPCTVGANMALRRSPGSTCKDHETELLSQQKVPAHFVALNGNRMNINLRTGPERTSCIEAVSQNKGSFPGLTNVSEVVTDQFLCSGMEGDDSPCKGESGGAVFLERRYRFFQVGLVSWGLFDPCHGSSNKNLRRKPPHGVVPRDFHISLFRLQPWLRQHLDGVLDFLPL
Protein: Glutaredoxin-C4 (AtGrxC4) (Q8LFQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Monothiol glutaredoxin-S15, mitochondrial
- Monothiol glutaredoxin-S14, chloroplastic
- Peroxiredoxin-2F, mitochondrial
- Peroxiredoxin-2E, chloroplastic
- Peroxiredoxin-2B
- Peroxiredoxin Q, chloroplastic
- Peptide deformylase 1B, chloroplastic/mitochondrial
Sequence:
MTMFRSISMVMLLVALVTFISMVSSAASSPEADFVKKTISSHKIVIFSKSYCPYCKKAKSVFRELDQVPYVVELDEREDGWSIQTALGEIVGRRTVPQVFINGKHLGGSDDTVDAYESGELAKLLGVSGNKEAEL