wanglab/gogpt-training-data huggingface dataset:
Protein: Expressed protein (Lung seven transmembrane receptor family protein) (Membrane protein PTM1 isolog; 58165-60455) (O04088)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTNLFLGFLVISFCLLGNLIHAADGSIHDYNNSGGFTKIANARYFVGGSEGIYGSEFLDVHHASSDTPLLKGNSFIRFDDITFVRTKESASKQNSTLAAAGLVEAILFEVKQRDRVGGSFFKSEDMCCTPKLADAGSCNLGEVMISADPNDPEWPKRIPTFFKRGEEEVKMSPEAVIIKKTGLYTVYFMTCDPELDGATIRGRTVWKNRGGYLQGEKAPLKKFYASMLLAYVVLGLVWFPQVAQYWKDGIQLHSHINFVIAFTMGELAFLYLDFVYLDSAGTSPMEVTVWAITLSSMRKALSRLLLLVISSGFGIVRPTLGGITLKMLLIGVLCFVISESLGLAMQFGNISENGMNYLMLSWAILETCFIQWIFRSLSKTLKKLKLNKRNITKLQLYKMFATVLVIMVVLSFAWIYVEVYLYSSLSQFWKVKWIVPTLWYILSYAMLVLICLFWPPSEKPMRYLYVADMEEETEEEDDLSTAETGMNATKAEYERSERKTLLEAFILLLGNIPGEK
Protein: Glycogenin-1 (GN-1) (GN1) (EC 2.4.1.186) (Q9R062)
Organism: Mus musculus (Mouse)
Function: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13280}. Nucleus {ECO:0000250|UniProtKB:P13280}. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm (By similarity). Cytosolic localization is dependent on the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:C4R941, ECO:0000250|UniProtKB:P13280}.
Interaction partners:
- Glycogen [starch] synthase, muscle
- Glycogen [starch] synthase, liver
- 1,4-alpha-glucan-branching enzyme
- E3 ubiquitin-protein ligase TRIM7
- Glycogen debranching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- Protein phosphatase 1 regulatory subunit 3C
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Lysosomal alpha-glucosidase
Sequence:
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDSAHLTLMKRPELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSGWATTDITKHLPFVYNLSSISIYSYLPAFKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVNCDSQDPTVSHPEFLNLWWDTFTTNVLPLLQHHGLVKDASSYLMMEHVSGALSDLSFGEAPAAPQPSMSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
Protein: Aminopeptidase RNPEPL1 (EC 3.4.11.-) (Arginyl aminopeptidase-like 1) (Methionyl aminopeptidase) (EC 3.4.11.18) (Q9HAU8)
Organism: Homo sapiens (Human)
Function: Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine.
Interaction partners:
- Calpain-10
Sequence:
MAAQCCCRQAPGAEAAPVRPPPEPPPALDVASASSAQLFRLRHLQLGLELRPEARELAGCLVLELCALRPAPRALVLDAHPALRLHSAAFRRAPAAAAETPCAFAFSAPGPGPAPPPPLPAFPEAPGSEPACCPLAFRVDPFTDYGSSLTVTLPPELQAHQPFQVILRYTSTDAPAIWWLDPELTYGCAKPFVFTQGHSVCNRSFFPCFDTPAVKCTYSAVVKAPSGVQVLMSATRSAYMEEEGVFHFHMEHPVPAYLVALVAGDLKPADIGPRSRVWAEPCLLPTATSKLSGAVEQWLSAAERLYGPYMWGRYDIVFLPPSFPIVAMENPCLTFIISSILESDEFLVIDVIHEVAHSWFGNAVTNATWEEMWLSEGLATYAQRRITTETYGAAFTCLETAFRLDALHRQMKLLGEDSPVSKLQVKLEPGVNPSHLMNLFTYEKGYCFVYYLSQLCGDPQRFDDFLRAYVEKYKFTSVVAQDLLDSFLSFFPELKEQSVDCRAGLEFERWLNATGPPLAEPDLSQGSSLTRPVEALFQLWTAEPLDQAAASASAIDISKWRTFQTALFLDRLLDGSPLPQEVVMSLSKCYSSLLDSMNAEIRIRWLQIVVRNDYYPDLHRVRRFLESQMSRMYTIPLYEDLCTGALKSFALEVFYQTQGRLHPNLRRAIQQILSQGLGSSTEPASEPSTELGKAEADTDSDAQALLLGDEAPSSAISLRDVNVSA
Protein: Large ribosomal subunit protein uL18 (60S ribosomal protein L5) (Q9W5R8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P26321}. Nucleus {ECO:0000250|UniProtKB:P26321}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein uS11A
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein P2
- Ribosomal protein
Sequence:
MGFVKVVKNKQYFKRYQVKFRRRREGKTDYYARKRLTFQDKNKYNTPKYRLIVRLSNKDITVQIAYARIEGDRVVCAAYSHELPKYGIQVGLTNYAAAYCTGLLVARRVLNKLGLDSLYAGCTEVTGEEFNVEPVDDGPGAFRCFLDVGLARTTTGARVFGAMKGAVDGGLNIPHSVKRFPGYSAETKSFNADVHRAHIFGQHVADYMRSLEEEDEESFKRQFSRYIKLGIRADDLEDIYKKAHQAIRNDPTHKVTAKKSSAVTKKRWNAKKLTNEQRKTKIAAHKAAYVAKLQSETEA
Protein: Tyrosine-protein kinase Mer (EC 2.7.10.1) (Proto-oncogene c-Mer) (Receptor tyrosine kinase MerTK) (P57097)
Organism: Rattus norvegicus (Rat)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12866}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth arrest-specific protein 6
- Vitamin K-dependent protein S
- Multiple epidermal growth factor-like domains protein 10
- Tubby-like protein
- Galectin-3
- CX3C chemokine receptor 1
- Bestrophin
- Triggering receptor expressed on myeloid cells 2
- P2Y purinoceptor 12
- Retinoid isomerohydrolase
Sequence:
MVLAPLLLGLLLLSALWNGGTAEKEEEIKPDQPFSGPLPGSLPADHRPFFAPHSSGDQLSPSQTGRSHPAHTATPQMTSAASNLLPPVAFKNTIGRIVLSEHKSVKFNCSINIPNVYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSITSVQRSDNGSYICKMKVNDREVVSDPIYVEVQGLPYFTKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNENPERSPSVLTVAGLTETAVFSCEAHNDKGLTVSKGVQINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEADQLSNGSVMVFNTSASPHLYEVQQLQALANYSVTVSCRNEIGWSAVSPWILASTTEGAPAVAPLNITVFLNESSNNLEIRWTKPPIKRQDGELVGYRISHVWESAGTSKELSEEVSQNGSWAQVPVQMHNATCTVRIAVITKGGIGPFSEPVDVAIPEHSRVDYAPSSTPAPGNTESMLIILGCFCGFVLMGLILYLSLAIKRRVQETKFGGAFSEEDSQLVVNYRAKKSFCRRAIELTLQSLGVSEELQNKLEDVVVDRNLLILGKVLGEGEFGSVMEGNLKQEDGTSQKVAVKTMKLDNFSLREIEEFLSEAACMKDFNHPNVIRLLGVCIELSSQGIPKPMVILPFMKYGDLHTFLLYSRIESVPKSIPLQTLLKFMVDIAQGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDDLYEIMYSCWSADPLDRPTFSVLRLQLEKLSESLPDAQDKESIIYINTQLLESCEGLANRSSLAGLDMNIDPDSIIASCTAGAAVSVVMAEVHENNLHEERYILNGGNEEWEDVASTPFATVTAGKDGVLPEDRLTKNGISWSHHSTLPLGSPSPDELLFADDSSGDSEVLM
Protein: Membrane cofactor protein (TLX) (Trophoblast leukocyte common antigen) (CD antigen CD46) (P15529)
Organism: Homo sapiens (Human)
Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}; Single-pass type I membrane protein {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}. Note=Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide.
Interaction partners:
- Complement C3
- Complement C4-B
- Complement C4-A
- Myosin-binding protein H
- Moesin
- Complement factor I
- CD59 glycoprotein
- Signaling lymphocytic activation molecule
- Myomesin-2
- Golgi-associated PDZ and coiled-coil motif-containing protein
Sequence:
MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL
Protein: Testis-expressed protein 35 (Q5T0J7)
Organism: Homo sapiens (Human)
Interaction partners:
- Ras-specific guanine nucleotide-releasing factor RalGPS2
- Regulator of G-protein signaling protein-like
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Glutamate receptor-interacting protein 1
Sequence:
MSAKRAELKKTHLSKNYKAVCLELKPEPTKTFDYKAVKQEGRFTKAGVTQDLKNELREVREELKEKMEEIKQIKDLMDKDFDKLHEFVEIMKEMQKDMDEKMDILINTQKNYKLPLRRAPKEQQELRLMGKTHREPQLRPKKMDGASGVNGAPCALHKKTMAPQKTKQGSLDPLHHCGTCCEKCLLCALKNNYNRGNIPSEASGLYKGGEEPVTTQPSVGHAVPAPKSQTEGR
Protein: Calpain-like cysteine peptidase, putative (Q57UN6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDITYENGSPTYTGNTVLKCFRENGNGLLFRIVNDEEKKWAFYNDTKGYNMVVKVAFGKDSTVQPLGNTKMEKDTATGEFKCELEIAPLATEMFIEGVPNGYKINFEANPIPQS
Protein: Fasciclin-like arabinogalactan protein 7 (Q9SJ81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Fasciclin-like arabinogalactan protein 15
- At5g19870)
- Transmembrane E3 ubiquitin-protein ligase FLY2
- Leucine-rich repeat extensin-like protein 6
- Pentatricopeptide repeat-containing protein At5g15300
- Fasciclin-like arabinogalactan protein 19
- AT5g43460/MWF20_18
- Fasciclin-like arabinogalactan protein 14
- Putative pectinesterase 63
- Fasciclin-like arabinogalactan protein 21
Sequence:
MAKMQLSIFIAVVALIVCSASAKTASPPAPVLPPTPAPAPAPENVNLTELLSVAGPFHTFLDYLLSTGVIETFQNQANNTEEGITIFVPKDDAFKAQKNPPLSNLTKDQLKQLVLFHALPHYYSLSEFKNLSQSGPVSTFAGGQYSLKFTDVSGTVRIDSLWTRTKVSSSVFSTDPVAVYQVNRVLLPEAIFGTDVPPMPAPAPAPIVSAPSDSPSVADSEGASSPKSSHKNSGQKLLLAPISMVISGLVALFL
Protein: Perilipin 3 (K7ERZ3)
Organism: Homo sapiens (Human)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
XKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPEQVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQQARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGPFAPGITEKAPEEKK
Protein: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) (Q3UV70)
Organism: Mus musculus (Mouse)
Function: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P35816}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MPAPTQLFFPLVRNCELSRIYGTACYCHHKHLCCSPPYIPQNRLRYTPHPAYATFCRPRENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESADIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ
Protein: C-C motif chemokine (D4ABS1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU361150}.
Interaction partners:
- C-C motif chemokine 2
- C-C motif chemokine ligand 27
- C-C motif chemokine 6
- C-C motif chemokine 7
- Macrophage inflammatory protein-1 alpha receptor
- C-X-C motif chemokine 10
- C-C chemokine receptor type 5
- CX3C chemokine receptor 1
- Transcription factor Jun
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MKISTLLCLLLIAAAISPQVLAGPDSVFTPVTCCYNVAKQKIHIRRLKSYRKITSSQCPREAVIFRTVLDKELCADPKEKWVKDSMNHLDQKSRTQHP
Protein: FMRFamide-like neuropeptides 1 [Cleaved into: PNFMRY-amide; AGSDPNFLRF-amide; SQPNFLRF-amide; ASGDPNFLRF-amide; SDPNFLRF-amide (PF1); AAADPNFLRF-amide; SADPNFLRF-amide (PF2); PNFLRF-amide] (P41855)
Organism: Caenorhabditis elegans
Function: Together with flp-18, plays a homeostatic role by acting on the GABAergic neural transmission at neuromuscular junctions to prevent overexcitation of the locomotor circuit.
Subcellular location: Secreted.
Interaction partners:
- FMRFamide-like neuropeptides 14
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptides 9
- G-protein coupled receptors family 1 profile domain-containing protein
- FMRFamide-like neuropeptides 16
- FMRFamide-like neuropeptides 7
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 6
- FMRFamide-like neuropeptides 13
Sequence:
MTLLYQVGLLLLVAATYKVSAECCTPGATSDFCTVFSMLSTMEQNEVMNFIGENCDGDAEVALQKMEKRKPNFMRYGRSAAVKSLGKKAGSDPNFLRFGRSQPNFLRFGKASGDPNFLRFGRSDPNFLRFGKAAADPNFLRFGKRSADPNFLRFGRSFDNFDRESRKPNFLRFGK
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q388S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MI domain-containing protein
- Peptidyl-prolyl cis-trans isomerase
- ATP-dependent DEAD/H RNA helicase, putative
- Peptidyl-prolyl cis-trans isomerase
- RNA helicase
- RNA-binding protein, putative
- Pre-mRNA-splicing factor SLU7
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA splicing factor, putative
- Uncharacterized protein
Sequence:
MQAHRSSNENSEDEEEDFLPTIPVLLVNTSEADSAEPTRAGEESVRGKRPRSLGPSDLNDEPIDTSDDVQEGVSKCKKQQSTMDMLSAEGYPCSFLYERSYRHGSPVQDIATLADDNGALIVTVDAVGVVRAWRKLPRGVFFTGEYRKFFPKSVESEEVTNAGLHFVLPDPVNSCILFVCVTPHAADDTGNISVNVEVSRVNGPLMALEGRFSLQFNAARRCHPSATQPWKESFTPRPFLFHHDYQPYIAFFAKRDDDTNGVVFIPCGVEKSSRLCGSDFTKEGQPIPTVALSCANLIVCCQQHLPSGLIVLVDEEGIVDYARIVEHLNDEGRTILSLRVVGGFPSRSAADPLKVRQWITFERRQKTGFFALVREVTCAAKTGKVIIPLSVDFSPTGNYFTVSSASLRRGAVCVLLHLFEFASGVCLCSSETSEVPCPQLGELCTLQEAKSNLRGFVFNAVIKDSFNSSPRGVWIFVPEITVVPEPSRECVGGRRIATFRAAPSAKEAGALKSSFYIEKLPCSIGESEVDVRGDSMPMGIINSFSQMACGEFRCFAAPLKLLRLCVPASQALKNLVAQSPVGCALSKEDIKRLFEAASCATPSAGFTEEHNSYADDPTICTTSLGGNALLLYTKYEISLTDFVMQSAVGIPNTDKNTEDDTGNERQRALLLSTLRAKRDFDCDDLLQLQSSLQVLAPRDEEERTTSEVEHSKASENSCGFDGEVEERRVQSIISAASTRVVSWTDICVGATISVRTFGTITVRLMPQFAPKAVTNFSTLSRRGFYNTLTFHRVVPGFMIQGGCPHGDGTGGLSSFGEPFEDEGVDAMDFFSYPRVQWLCMANRGPNTNESQFFITLGEATPWLNGKHTVFGFVTAGKSVVLSVSQVERNGDDKPVMPVVIDQVAVSEEGLSLE
Protein: Keren (LD34429p) (Q9VVJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Epidermal growth factor receptor
- Protein rhomboid
Sequence:
MRAQDLLLLATALIGAYLPLTAACSSRAIAKPRPTAAPILPPDNVEISTTPRPNVTFPIFACPPTYVAWYCLNDGTCFTVKIHNEILYNCECALGFMGPRCEYKEIDGSYLPTRNRVMLEKASIVSGATLALLFMAMCCVVLYLRHEKLQKQKLHDSTTTTTTDGGCQNEGMDEVDGLRPLRPVRRPFGPCRILSLEEAHLQAKASNRPRHCNELLR
Protein: Trypanosoma Tc-38 (p38) protein domain-containing protein (Q38BH8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYRRKVSSIIQLSTLRQLQLMCNAEAMSLPFQVHNAQALLEQLKVYHPAKYEQFSKNPTTQEFVPSRVISNADGGSVTKGAPIFTLPLPKHFINPTDSAEDIIPRTFYHSSVARVVADPDAECYLPRCGLTGLFFSREEVVDNLQAAAAELHFRSPFWIRTDHPALGDFLTLKDDSEAICISLTAAVISIEDVEPFPVDLLHPKLKQALALGKHAFSEQIPPGMNALSGFVTKNPFVQSLPNGGVWLSHKQVLQQSFQIKKKSSAGESPFVLAEIEQWELHNADQLSVPGRLALNHNANNSKRTSVFT
Protein: PrgJ (TraC-F-type conjugal transfer protein) (Q5G3P5)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Interaction partners:
Sequence:
MHIVEDEFSKCYKLGEVDYEIAVEEDQLNTVMGYAEGLNTLDKNSRYQLLVVNKREEESLMEDVLLAYQGDHLDNYRQEINEIITKQYEQDERNFKIEKYAIFTTKSSSMKQANKELEGIMQNFANRFEANQIKLEVTPMTGLERLSLFSYFLRHGQYFGTSYQDIAVSGLTSKAFIVPSKIKFPNNKAYFRLGENYAAVLTIQQYPKYLEDKLIKELCATGRELAISIHARPYDMMEARKAIQGTKTLNDVAIQKQQKQNFRSGVSEDAISGEAKEIQETTNALMDEIKNNGQKLFNGLFSVFLIAETEKELLEAVESVKNVGATWQVVFDTVDNYKEEALNTILPIGKPYLDVEMSYMRDLTTTNIATQVPFTNVELQSPTGQFYGRNQLTKNMITIDRKKDLITPSGLIFGTSGSGKGMATKWEILSTRLKFPKDRFLIVDPESEYLPIGKELDAEILDISTGTKNHLNILGMVDKQLLDEEDQELDLVKEKSNLLSTMFESLLKSYTDVDAGLVDRVTLLTYERFENKETEPTLVDWFRILKEQTDEGAKELANKVETYCVGSQDIFAHQTNIDLTAPFIVFNTKKLDDRLKKFAMKVILDQLWKQVVSGQGKVTSRLYFDELQVNFTTEEEAEWFLNLWARIRKYGAVTTGITQNPTTLLDSKAGQKMIANSEFLILLRQKPIDSQRLVEILSLTPALKKYINDRAPQGTGLISAGGVVVPFENPIPKETHLFEIMNTDA
Protein: DNA-binding transcriptional dual regulator (Q88QR4)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Interaction partners:
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit omega
- Adenylate cyclase
- DNA-binding transcriptional dual regulator
- 3',5'-cyclic-nucleotide phosphodiesterase
Sequence:
MVASALPAKIKNIDKLLVHCQRRRYTAKSNIICAGDRAETLSFIIKGSVTILIEDDDGHEMIIAYLNHGDFFGELGLFEPVDGEQQRSAWVRAKTECEVAEISYEKFRELARQDPEILYALGSQMAQRLRNTTRKVGDLAFFDVTGRVARCLLELCKQPDAMTHPDGMQIKITRQEIGRIVGCSREMVGRVLKDLEERSLVQVKGKTMVVHGTR
Protein: Glutathione S-transferase DHAR3, chloroplastic (EC 2.5.1.18) (Chloride intracellular channel homolog 3) (CLIC homolog 3) (Glutathione-dependent dehydroascorbate reductase 3) (AtDHAR3) (ChlDHAR) (GSH-dependent dehydroascorbate reductase 3) (EC 1.8.5.1) (Q8LE52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Displays a dual function. As a soluble protein, exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses (By similarity).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:19174456}.
Interaction partners:
- Monodehydroascorbate reductase 3
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione reductase, chloroplastic
- Thylakoid lumenal 29 kDa protein, chloroplastic
- Monodehydroascorbate reductase, chloroplastic/mitochondrial
- Monodehydroascorbate reductase 2
- L-ascorbate peroxidase 3
- Glutathione synthetase, chloroplastic
- Monodehydroascorbate reductase 4, peroxisomal
- Putative inactive glutathione hydrolase 4
Sequence:
MISLRFQPSTTAGVLSASVSRAGFIKRCGSTKPGRVGRFVTMATAASPLEICVKASITTPNKLGDCPFCQKVLLTMEEKNVPYDMKMVDLSNKPEWFLKISPEGKVPVVKFDEKWVPDSDVITQALEEKYPEPPLATPPEKASVGSKIFSTFVGFLKSKDSGDGTEQVLLDELTTFNDYIKDNGPFINGEKISAADLSLAPKLYHMKIALGHYKNWSVPDSLPFVKSYMENVFSRESFTNTRAETEDVIAGWRPKVMG
Protein: Type IV pilus retractation ATPase PilT (P24559)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Acts as a molecular motor to provide the energy that is required for T4P retraction while antagonist PilB ATPase activity is required for T4P extension. Promotes also PilU retractation activity through direct interaction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15659660}. Note=Localizes to cell poles. {ECO:0000269|PubMed:15659660}.
Interaction partners:
- Type IV pilus inner membrane component PilM
- Prepilin leader peptidase/N-methyltransferase
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilO
- Type IV pilus inner membrane component PilN
- Protein PilH
- Type IV pilus non-core minor pilin PilE
- Type IV pilus inner membrane component PilP
- Type IV pilus assembly protein PilF
- Type IV pilus biogenesis factor PilY1
Sequence:
MDITELLAFSAKQGASDLHLSAGLPPMIRVDGDVRRINLPPLEHKQVHALIYDIMNDKQRKDFEEFLETDFSFEVPGVARFRVNAFNQNRGAGAVFRTIPSKVLTMEELGMGEVFKRVSDVPRGLVLVTGPTGSGKSTTLAAMLDYLNNTKYHHILTIEDPIEFVHESKKCLVNQREVHRDTLGFSEALRSALREDPDIILVGEMRDLETIRLALTAAETGHLVFGTLHTTSAAKTIDRVVDVFPAEEKAMVRSMLSESLQSVISQTLIKKIGGGRVAAHEIMIGTPAIRNLIREDKVAQMYSAIQTGGSLGMQTLDMCLKGLVAKGLISRENAREKAKIPENF
Protein: NAD(P)H dehydrogenase [quinone] 1 (EC 1.6.5.2) (Azoreductase) (DT-diaphorase) (DTD) (Menadione reductase) (NAD(P)H:quinone oxidoreductase 1) (Phylloquinone reductase) (Quinone reductase 1) (QR1) (P15559)
Organism: Homo sapiens (Human)
Function: Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion. Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential. Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P05982}.
Interaction partners:
- Nuclear factor erythroid 2-related factor 2
- Kelch-like ECH-associated protein 1
- Ornithine decarboxylase
- Glutamate--cysteine ligase regulatory subunit
- Cellular tumor antigen p53
- Vitamin K epoxide reductase complex subunit 1
- Vitamin K-dependent gamma-carboxylase
- Heme oxygenase 1
- Quinone oxidoreductase
- Vitamin K epoxide reductase complex subunit 1-like protein 1
Sequence:
MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK