wanglab/gogpt-training-data huggingface dataset:
Protein: Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11) (B2RID1)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
Subcellular location: Cell surface {ECO:0000269|PubMed:21896480}. Note=Is exclusively cell-associated. {ECO:0000269|PubMed:21896480}.
Interaction partners:
Sequence:
MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQIKIMYSAKYAASQNAYKRAIGANWAIKTRGLRQNKQAMQDRLIAWGAKQGTPRYEEAVHEIDATVAKRADLRRRYWMIEEGIIRGIEFARSPIPTEDETKALQGNDASARKEAIDKIRTRYSKFANKDYSAEVDKKVAVAMLTEYLKEIPYENLPLHLRLVKDRFAGDVQAYVDDIFARSVFGSEAQFDAFAAVPSVEKLAEDPMVLFASSVFDEYRKLYNELRPYDDPILRAQRTYIAGLLEMDGDQDQFPDANLTLRFTYGQVKGYSPRDNVYYGHQTTLDGVMEKEDPDNWEFVVDPKLKAVYERKDFGRYADRSGRMPVAFCATTHTTGGNSGSPVMNANGELIGLNFDRNWEGVGGDIQYLADYQRSIIVDIRYVLLVIDKVGGCQRLLDEMNIVP
Protein: Acd (Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase (EC 3.2.1.96)) (Q5S4P9)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Interaction partners:
- N-acetylmuramoyl-L-alanine amidase
- Lipoprotein
- Uncharacterized protein
Sequence:
MKKKAALATLAMLPLGVVNAHADGDIGIVTINYLNVRNEPTAESSIAFVAKKDDKVLIKDSSNGWYKIKAESGQEGWASSKYIAKSNSDSLRTSTNKEKQVISNSLNMRNGAGTSYRVITVLKKGQKVEVISESNGWSKIKYDGRLGYVSSSYLGDVSNSTNKSKTKQVNTTSLNVRSGPNTSYGLLGKLPKGSKVEVISESNGWSKIKYNGKDAYVSSMYLSDVSQSNSDNSSQSNDKKNTDKVVNTASLNVRSGPGSTYSKLGKVYKGSKVTVLSESSGWAKINFNNKEAFVVGNYLSTSADTSNNNSNSNYDNSSNSNGNNSSSSGQVNGMSGISGAKIDYKSLSYTLESHISKQVEKAASGGNVIAPSNRKSTPSPEFSTFSAQRTSSFVNASSSDIEYYLNPKNFTNTTKGMMQFLKINSYRDGISESSLNSYLNGLSSSVFKNQGAAFINAAKKYNIDVVYLVSHAMWETAYGKSTLAQGQTLTSYKGQPLSKPVKVYNFFGIGAIDKSANVSGAEAAYSNGWTSVETTIDGSAKWISQNYVNSSKYNQNTIYKMKWNYDYTWHQYATDVNWANGISGIMENLIGLYRGGSSLVFEVPQYK
Protein: Keratin, type I cytoskeletal 18 (Cytokeratin-18) (CK-18) (Keratin-18) (K18) (Q5BJY9)
Organism: Rattus norvegicus (Rat)
Function: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection (By similarity). Involved in the uptake of thrombin-antithrombin complexes by hepatic cells.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:16998620}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:16998620}.
Interaction partners:
- Keratin, type II cytoskeletal 8
- Tumor necrosis factor receptor superfamily member 1B
- Cadherin-1
- Keratin, type I cytoskeletal 19
- Desmoplakin
- Alpha-fetoprotein
- Epithelial cell adhesion molecule
- Albumin
Sequence:
MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGVQTEKETMQDLNDRLASYLDKVKNLETENRRLESKIREYLEKRGPQGVRDWGHYFKTIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEQLAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLLELRRTLQTLEIDLDSMKNQNINLENNLGEVEARYRVQMEQLNGVLLHLESELAQTRAEGQRQTQEYEALLNIKVKLEAEIATYRRLLEDGDDFSLNDALDSSNSMQTVQRTTTRKVVDGKVVSETNDTRVLRH
Protein: Intelectin-1b (Intelectin-2) (Q80ZA0)
Organism: Mus musculus (Mouse)
Function: May play a protective role in the innate immune response to parasite infection.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted {ECO:0000250|UniProtKB:Q8WWA0}.
Interaction partners:
Sequence:
MTQLGFLLFIMIATRVCSAAEENLDTNRWGNSFFSSLPRSCKEIKQEDTKAQDGLYFLRTENGVIYQTFCDMTTAGGGWTLVASVHENNLRGRCTVGDRWSSQQGNRADYPEGDGNWANYNTFGSAEGATSDDYKNPGYFDIQAENLGIWHVPNNSPLHTWRNSSLLRYRTFTGFLQRLGHNLFGLYQKYPVKYGEGKCWTDNGPAFPVVYDFGDAQKTASYYSPSGRNEFTAGYVQFRVFNNERAASALCAGVRVTGCNTEHHCIGGGGFFPEFDPEECGDFAAFDANGYGTHIRYSNSREITEAAVLLFYR
Protein: Probable 9-O-acetyl-N-acetylneuraminic acid deacetylase (Neu5,9Ac2 deacetylase) (EC 3.1.1.-) (Probable 9-O-acetyl-N-acetylneuraminate esterase) (Probable sialyl esterase NanS) (P39370)
Organism: Escherichia coli (strain K12)
Function: Probably catalyzes the hydrolysis of the 9-O-acetyl group of 9-O-acetyl-N-acetylneuraminate (Neu5,9Ac2). Is required for growth of E.coli on Neu5,9Ac2, an alternative sialic acid commonly found in mammalian host mucosal sites, in particular in the human intestine.
Subcellular location: Periplasm {ECO:0000305|PubMed:19749043}.
Interaction partners:
- N-acetylneuraminate epimerase
- N-acetylneuraminic acid outer membrane channel protein NanC
- N-acetylneuraminate lyase
- NADH-quinone oxidoreductase subunit C/D
- Putative N-acetylmannosamine-6-phosphate 2-epimerase
- Sialic acid transporter NanT
Sequence:
MNAIISPDYYYVLTVAGQSNAMAYGEGLPLPDREDAPHPRIKQLARFAHTHPGGPPCHFNDIIPLTHCPHDVQDMQGYHHPLATNHQTQYGTVGQALHIARKLLPFIPDNAGILIVPCCRGGSAFTAGSEGTYSERHGASHDACRWGTDTPLYQDLVSRTRAALAKNPQNKFLGACWMQGEFDLMTSDYASHPQHFNHMVEAFRRDLKQYHSQLNNITDAPWFCGDTTWYWKENFPHSYEAIYGNYQNNVLANIIFVDFQQQGERGLTNAPDEDPDDLSTGYYGSAYRSPENWTTALRSSHFSTAARRGIISDRFVEAILQFWRER
Protein: RILP-like protein homolog (Rab-interacting lysosomal protein-like) (O76878)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a role in lysosome distribution by interacting with Arl8.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:30115618}. Note=Localizes to the perinuclear region when associated with Arl8. {ECO:0000269|PubMed:30115618}.
Interaction partners:
- LP14110p
Sequence:
MPGFHLNEMGEMVLDAIDDIGVVDVYDLASDIGKEYERIMDRFGTDAVSGLMPKIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRYTTRELKELISERDELLTTIDTLNEQLAELKPPSQAKGKRQRHFSSSDDSDEDDDGHVADNDDDDDEEEAAAEANELEPPAAGETPPGHDAPVQGPLPYEPDDAPWKKSSESGIRKFFRKLFSDPSDGSNTFPKRSLATLSKMALSATPGSVSASAAAK
Protein: Tropomyosin-1 (P17536)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Actin
- Fimbrin
- N-terminal acetyltransferase B complex subunit MDM20
- Myosin-2
- Protein BNI1
- Tropomyosin-2
- BNI1-related protein 1
- Profilin
- Cofilin
- Myosin-1
Sequence:
MDKIREKLSNLKLEAESWQEKYEELKEKNKDLEQENVEKENQIKSLTVKNQQLEDEIEKLEAGLSDSKQTEQDNVEKENQIKSLTVKNHQLEEEIEKLEAELAESKQLSEDSHHLQSNNDNFSKKNQQLEEDLEESDTKLKETTEKLRESDLKADQLERRVAALEEQREEWERKNEELTVKYEDAKKELDEIAASLENL
Protein: Heme-based aerotactic transducer HemAT (O07621)
Organism: Bacillus subtilis (strain 168)
Function: Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.
Interaction partners:
- Chemotaxis protein CheV
- Chemotaxis protein CheW
- Chemotaxis protein CheA
- Chemotaxis protein CheY
- Chemotaxis protein methyltransferase
- Methyl-accepting chemotaxis protein McpA
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Putative sensory transducer protein YfmS
- Methyl-accepting chemotaxis protein McpB
- Motility protein A
Sequence:
MLFKKDRKQETAYFSDSNGQQKNRIQLTNKHADVKKQLKMVRLGDAELYVLEQLQPLIQENIVNIVDAFYKNLDHESSLMDIINDHSSVDRLKQTLKRHIQEMFAGVIDDEFIEKRNRIASIHLRIGLLPKWYMGAFQELLLSMIDIYEASITNQQELLKAIKATTKILNLEQQLVLEAFQSEYNQTRDEQEEKKNLLHQKIQETSGSIANLFSETSRSVQELVDKSEGISQASKAGTVTSSTVEEKSIGGKKELEVQQKQMNKIDTSLVQIEKEMVKLDEIAQQIEKIFGIVTGIAEQTNLLSLNASIESARAGEHGKGFAVVANEVRKLSEDTKKTVSTVSELVNNTNTQINIVSKHIKDVNELVSESKEKMTQINRLFDEIVHSMKISKEQSGKIDVDLQAFLGGLQEVSRAVSHVAASVDSLVILTEE
Protein: Peroxisome proliferator activated receptor beta (Q9MZG4)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MEQPPEEAPEVREEEKKKEVAEAEGGPELNGGPEHSLPSSSCTDLSQSCSPRALLDQLQMGCDGASCGGLSMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERICKIQKKNRNKCQYCRFQKCLALGMSYNAIRFGRMPEAEXRKLVAGLTANEGSQHNPQVADLKAFSKHLYSAYLKNFNMTKKKARAILTGKASHTAPFVIHDIETLWAGRKGLVWKQLVNGLPPYKEISVHVFYRCQCTTVETVRELTEFAKSIPSFDHLFLNDQVTLLKYGVHEAIFAMLASIVNKDGLLVANGTGFVTREFLRDLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGDRPGLMNVSQVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRIKKTETETSLHPLLQEIYRDMY
Protein: CAP, isoform R (DCAPL2) (Q966V0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKENLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPREILEEFEFIQITPTLTKIRVSTKELEEEVEPVRKAATPPPAPPPPPPPPPHQSLATSRDHKPVKMFSQLSKNLPSFIPLSKKQQVSQQDDPPPRPPHRKSSCTKSTVRVLSSASKSRHEQCFQPPNGTAPGVSTITLRKVATSSCSRREPICRSKSAGAVSTLLQTLTATKETRLTRRVQQQQQQSRLRSSSPSRRPARLLALRHSSRSPVAFGRSISKERSFAEEKKRLENTLPANRTNFEASTNILRDPSLKSPQEVREAVRSYATSRSKSLPRLRHTTVSTTTRQTMCFPQVRPQTLLDCGTRSLRKSSSKTGKGQEKNGSNDSLPRSNSTFSIDSMVRQEIVPIAPPKTYVGKSRGSLSKALVPLQNSRSEGHVPRKRQSGKSTTKPPPPVTVHSYSESVREKTNFWNEYNAKQAMSLPQEYKFCPEDVCDFESHTIQQPCIEDLVWKYEGKEQRPPKQVTVTDIARPQSPQLSQERRFSPTREVRVPQISREVRSPSRRRIDSLRSKDKEQSLARASSLSSADDRKRATPAPSNGLYQCGELAHSATSLTHLERHSPSCRYRNNCERFTELNRFYSTLERVGQLERATSSSSFHPLRKDAELLDFDEWRRVRLHERAEKELQYLVGKLRDDQKQRDLHFRSKDVDSIKWRQEADQSLIAKKKSVEDLRENFEQLNLLRQQQQLQSEPVHRHWRRNTVADLACSLEHQALAEPEMERHLDNDLVSTLSKDQIKKITQQLNEIYSGNRHAPAVEEQYVVTVEKGSRPNGLKVRCNSTISKDQLLGPVQRKRDEQHSNQTLPRSTRSQSPVVVARETRGAIAAKNAELTLTKPPDVPPRPKPTPSQEIKSKPPPKAEPKVEAREPAEDISQKIQYFEDRQFDEPPKTIYHAREDSSPDEAEVMRLINQNMQERQRARQLHHHQELSNSLTDLSGVFGERPAARVNFHLHSPPDRPPDDTELISFGNGSPDHGDGSLELYSDSYYRSRSLSPQSQVSACSSSYLQRVYTGEVRKMRQHFESIQQSGEQSREPSNERRDFFGLSSLRRARSDPEMSAGSKDAPDTVTEAVSKEDVPRLTHKFELRAATPSPERGRKRLRSAQDRLMPHIDIISKTAALKRELPIPVRSSPTRSVSSNSHCFERLRMRYESPEPQTQSYLSTSHPDMRDVHDISPHLSADWVAHKHPEPTKPKDLPKKPQRVVRASSTSPLRPARSQNHQLSSRLTSCMKDIFANQKFDPNKHRPKARYVPDGAENGNQKSKDNGTLERLKKTAMVTFKESPNHYYATDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Cyclic dipurine nucleotide synthase (EC 2.7.7.-) (Cyclic GMP-AMP synthase) (cGAMP synthase) (c-di-AMP synthase) (EC 2.7.7.85) (c-di-GMP synthase) (EC 2.7.7.65) (cGAS/DncV-like nucleotidyltransferase) (CD-NTase) (Em-CdnE) (P0DSP2)
Organism: Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-A(GA) CBASS system.
Interaction partners:
Sequence:
MNFSEQQLINWSRPVSTTEDLKCQNAITQITAALRAKFGNRVTIFLQGSYRNNTNVRQNSDVDIVMRYDDAFYPDLQRLSESDKAIYNAQRTYSGYNFDELKADTEEALRNVFTTSVERKNKCIQVNGNSNRITADVIPCFVLKRFSTLQSVEAEGIKFYSDDNKEIISFPEQHYSNGTEKTNQTYRLYKRMVRILKVVNYRLIDDGEIADNLVSSFFIECLVYNVPNNQFISGNYTQTLRNVIVKIYEDMKNNADYTEVNRLFWLFSNRSPRTRQDALGFMQKCWNYLGYQ
Protein: DNA-directed RNA polymerase subunit (Q6DGK6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369086}.
Interaction partners:
Sequence:
MFVLVEMRDTVRIPPWSFQRPLNEAVAEELNKKLANKVVYNVGLCICLYDITKLEDSYIFPGDGASHTKVHFRYVVFHPFLDEILLGKIKGCSAEGVHVSLGFFDDILIPPESLQQPAKFDEAEQVWVWEYETDEGTHDLYMDQGEEIRFRVTDEVFVDTSPSGPSADKEAPGTGAAAAPPAGAEDAAQQKESPYTLIGSVSEPGLGLLSWWNN
Protein: Dehydration-responsive element-binding protein 2G (Protein DREB2G) (P61827)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein DOG1-like 4
- RING/FYVE/PHD zinc finger superfamily protein
Sequence:
MEEEQPPAKKRNMGRSRKGCMKGKGGPENATCTFRGVRQRTWGKWVAEIREPNRGTRLWLGTFNTSVEAAMAYDEAAKKLYGHEAKLNLVHPQQQQQVVVNRNLSFSGHGSGSWAYNKKLDMVHGLDLGLGQASCSRGSCSERSSFLQEDDDHSHNRCSSSSGSNLCWLLPKQSDSQDQETVNATTSYGGEGGGGSTLTFSTNLKPKNLMSQNYGLYNGAWSRFLVGQEKKTEHDVSSSCGSSDNKESMLVPSCGGERMHRPELEERTGYLEMDDLLEIDDLGLLIGKNGDFKNWCCEEFQHPWNWF
Protein: Homeotic protein ultrabithorax (P20822)
Organism: Drosophila pseudoobscura pseudoobscura (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls development of the cells in the posterior thoracic and first abdominal segments. It activates the synthesis of the decapentaplegic (DPP) growth factor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein extradenticle
Sequence:
MNSYFEQASGFYGHPHQATGMAMGSGGHHDQTASAAAAAYRGFPLSLGMSPYANHHLQRTTQDSPYDASITAACNKIYGDGASAYKQDCLNIKADAVNGYKDIWNTGGSNGGGTGGGGGGGGAGGNASNGSNAGNAANGQNNAAGGMPVRPSACTPDSRVGGYLDTSGGSPVSHRGGSAGGNVSAGGGGQSGQSGAPGVGVGVGVGVGAGAGTAWNANCTISGAAAAQTAAASSLHQASNHTFYPWMAIAGKIRSDLTQYGGISTDMGKRYSESLAGSLLPDWLGTNGLRRRGRQTYTRYQTLELEKEFHTNHYLTRRRRIEMAHALCLTERQIKIWFQNRRMKLKKEIQAIKELNEQEKQAQAQKAAAAAAAAAAVQGGHLDQN
Protein: Sensor-type histidine kinase PrrB (EC 2.7.13.3) (P9WGK7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system PrrB/PrrA that is involved specifically in early intracellular multiplication of Mycobacterium and is essential for its viability. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of PrrA. In turn, PrrA binds to the upstream promoter regions of target genes including itself to positively regulate their expression.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transcriptional regulatory protein PrrA
- Possible two component system response transcriptional positive regulator PhoP
- DNA-binding response regulator MtrA
- Transcriptional regulatory protein TrcR
- Transcriptional regulatory protein TcrA
- Transcriptional regulatory protein KdpE
- Probable transcriptional regulatory protein TcrX
- Response regulator MprA
- Sensory transduction protein RegX3
- Protein PafB
Sequence:
MNILSRIFARTPSLRTRVVVATAIGAAIPVLIVGTVVWVGITNDRKERLDRRLDEAAGFAIPFVPRGLDEIPRSPNDQDALITVRRGNVIKSNSDITLPKLQDDYADTYVRGVRYRVRTVEIPGPEPTSVAVGATYDATVAETNNLHRRVLLICTFAIGAAAVFAWLLAAFAVRPFKQLAEQTRSIDAGDEAPRVEVHGASEAIEIAEAMRGMLQRIWNEQNRTKEALASARDFAAVSSHELRTPLTAMRTNLEVLSTLDLPDDQRKEVLNDVIRTQSRIEATLSALERLAQGELSTSDDHVPVDITDLLDRAAHDAARIYPDLDVSLVPSPTCIIVGLPAGLRLAVDNAIANAVKHGGATLVQLSAVSSRAGVEIAIDDNGSGVPEGERQVVFERFSRGSTASHSGSGLGLALVAQQAQLHGGTASLENSPLGGARLVLRLPGPS
Protein: Small ribosomal subunit protein uS5 (40S ribosomal protein S2) (P27952)
Organism: Rattus norvegicus (Rat)
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. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P15880}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P15880}. Note=Probably localized to nucleolus and cytoplasm in complex with ZNF277. {ECO:0000250|UniProtKB:P15880}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS12
Sequence:
MADDAGAAGGPGGPGGPGLGGRGGFRGGFGSGLRGRGRGRGRGRGRGRGARGGKAEDKEWIPVTKLGRLVKDMKIKSLEEIYLFSLPIKESEIIDFFLGASLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSIVPVRRGYWGNKIGKPHTVPCKVTGRCGSVLVRLIPAPRGTGIVSAPVPKKLLMMAGIDDCYTSARGCTATLGNFAKATFDAISKTYSYLTPDLWKETVFTKSPYQEFTDHLVKTHTRVSVQRTQAPAVATT
Protein: Nuclear factor of activated T-cells 2 (A0A8I6AV80)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDAPEPQSDPDGGDGPGHEPGGSSQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGESDSIGFQNFLSPAKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGMAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVAPQDDGIPAGYPPTAGSAVLMDALNSLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPAVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTGPAGTCETQPLPISLISADRLSPWLSRLQRNPPARSVFRCSVLLPAPGSSLVLLAL
Protein: Putative transporter AraJ (P23910)
Organism: Escherichia coli (strain K12)
Function: May be involved in either the transport or processing of arabinose polymers.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Arabinose-proton symporter
Sequence:
MKKVILSLALGTFGLGMAEFGIMGVLTELAHNVGISIPAAGHMISYYALGVVVGAPIIALFSSRYSLKHILLFLVALCVIGNAMFTLSSSYLMLAIGRLVSGFPHGAFFGVGAIVLSKIIKPGKVTAAVAGMVSGMTVANLLGIPLGTYLSQEFSWRYTFLLIAVFNIAVMASVYFWVPDIRDEAKGNLREQFHFLRSPAPWLIFAATMFGNAGVFAWFSYVKPYMMFISGFSETAMTFIMMLVGLGMVLGNMLSGRISGRYSPLRIAAVTDFIIVLALLMLFFCGGMKTTSLIFAFICCAGLFALSAPLQILLLQNAKGGELLGAAGGQIAFNLGSAVGAYCGGMMLTLGLAYNYVALPAALLSFAAMSSLLLYGRYKRQQAADTPVLAKPLG
Protein: Aldo-keto reductase family 1 member B1 (EC 1.1.1.21) (EC 1.1.1.300) (EC 1.1.1.372) (EC 1.1.1.54) (Aldehyde reductase) (Aldose reductase) (AR) (P07943)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Subcellular location: Cytoplasm.
Interaction partners:
- Sorbitol dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Sepiapterin reductase
- Carbonyl reductase 1])
- Carbonyl reductase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
- Dihydropteridine reductase
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
Sequence:
MASHLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVCALMSCAKHKDYPFHAEV
Protein: Curli production assembly/transport component CsgG (P0AEA4)
Organism: Escherichia coli O157:H7
Function: May be involved in the biogenesis of curli organelles.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Curli production assembly/transport component CsgF
- Curli production assembly/transport component CsgE
- Curli production assembly/transport component CsgF
- Curli production assembly/transport component CsgE
- Transcriptional regulator
- Transcriptional regulator
- Minor curlin subunit
- Minor curlin subunit
- Major curlin subunit
- Curli assembly protein
Sequence:
MQRLFLLVAVMLLSGCLTAPPKEAARPTLMPRAQSYKDLTHLPAPTGKIFVSVYNIQDETGQFKPYPASNFSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTVAINNRIPLQSLTAANIMVEGSIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVNVSTGEILSSVNTSKTILSYEVQAGVFRFIDYQRLLEGEVGYTSNEPVMLCLMSAIETGVIFLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES
Protein: Leucine-rich repeat LGI family member 2 (LGI1-like protein 2) (Leucine-rich glioma-inactivated protein 2) (Q8N0V4)
Organism: Homo sapiens (Human)
Function: Required for the development of soma-targeting inhibitory GABAergic synapses made by parvalbumin-positive basket cells.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 23
- Disintegrin and metalloproteinase domain-containing protein 22
Sequence:
MALRRGGCGALGLLLLLLGAACLIPRSAQVRRLARCPATCSCTKESIICVGSSWVPRIVPGDISSLSLVNGTFSEIKDRMFSHLPSLQLLLLNSNSFTIIRDDAFAGLFHLEYLFIEGNKIETISRNAFRGLRDLTHLSLANNHIKALPRDVFSDLDSLIELDLRGNKFECDCKAKWLYLWLKMTNSTVSDVLCIGPPEYQEKKLNDVTSFDYECTTTDFVVHQTLPYQSVSVDTFNSKNDVYVAIAQPSMENCMVLEWDHIEMNFRSYDNITGQSIVGCKAILIDDQVFVVVAQLFGGSHIYKYDESWTKFVKFQDIEVSRISKPNDIELFQIDDETFFVIADSSKAGLSTVYKWNSKGFYSYQSLHEWFRDTDAEFVDIDGKSHLILSSRSQVPIILQWNKSSKKFVPHGDIPNMEDVLAVKSFRMQNTLYLSLTRFIGDSRVMRWNSKQFVEIQALPSRGAMTLQPFSFKDNHYLALGSDYTFSQIYQWDKEKQLFKKFKEIYVQAPRSFTAVSTDRRDFFFASSFKGKTKIFEHIIVDLSL
Protein: Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (CML33) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) (Q9Y285)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- Leucine-rich repeat-containing protein 47
- Phenylalanine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Valine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
Sequence:
MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPEGLAQSELMRLPSGKVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKERSELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKNLLRTHTTSASARALYRLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVNLQMVYDSPLCRLDAEPRPPPTQEAA