wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS11 (40S ribosomal protein S14B) (A0A1D8PDT3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
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 (Probable). RPS14B is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL33
Sequence:
MSTDRSQVFGVARIFASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAAKCKEVGITAVHIKLRATGGTKTKTPGPGGQSALRALARSGLRIGRIEDVTPVPSDSTRRKGGRRGRRL
Protein: PPARG coactivator 1 beta (H0Y713)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XACSNPSQQVRSRPWSRHHSKASWAEFSILRELLAQDVLCDVSKPYRLATPVYASLTPRSRPRPPKDSQASPGRPSSVEEVRIAASPKSTGPRPSLRPLRLEVKREVRRPARLQQQEEEDEEEEEEEEEEEKEEEEEWGRKRPGRGLPWTKLGRKLESSVCPVRRSRRLNPELGPWLTFADEPLVPSEPQGALPSLCLAPKAYDVERELGSPTDEDSGQDQQLLRGPQIPALESPCESGCGDMDEDPSCPQLPPRDSPRCLMLALSQSDPTFGKKSFEQTLTVELCGTAGLTPPTTPPYKPTEEDPFKPDIKHSLGKEIALSLPSPEGLSLKATPGAAHKLPKKHPERSELLSHLRHATAQPASQAGQKRPFSCSFGDHDYCQVLRPEGVLQRKVLRSWEPSGVHLEDWPQQGAPWAEAQAPGREEDRSCDAGAPPKDSTLLRDHEIRASLTKHFGLLETALEEEDLASCKSPEYDTVFEDSSSSSGESSFLPEEEEEEGEEEEEDDEEEDSGVSPTCSDHCPYQSPPSKANRQLCSRSRSSSGSSPCHSWSPATRRNFRCESRGPCSDRTPSIRHARKRREKAIGEGRVVYIQNLSSDMSSRELKRRFEVFGEIEECEVLTRNRRGEKYGFITYRCSEHAALSLTKGAALRKRNEPSFQLSYGGLRHFCWPRYTDYGWQAVPTVQRSSQLPKALGCSHSTVPTHSGRFFNHPVFVSCSLPSPLPCLFTPMPRFQFRRGPSCVREKQV
Protein: Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17) (Q99MC0)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 12A
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Transforming protein RhoA
- Serine/threonine-protein kinase N1
- Myosin regulatory light chain 12B
Sequence:
MAAQRLGKRVLSKLQSPSRARGPGGSPSGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELDSEEERCRKIRGLLEACLNPTEDFVQELLAKLRGLHKQPGFPQPSPSDDPSLSPRQDPAHTAPP
Protein: Splicing factor Cactin C-terminal domain-containing protein (Q383B9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFKRTRGEDEVVEVYATLLRQSGARAIERIRQRRGSGTNSVMPIDALVIRYAMWFLDTSAFPAVSYVTQAQRVVTEAIERVSYPQHFSFIPLSTLVECLVSENTAEVMQQTVVSIEEFIDARDALGRWIDENIGNAGGERYERYNHYSGGEKDEEAEIALERAGILWRSALYWVAVFEYIEALSLSSAKVNVFALRPRYEQELMNLLNSIAAPKDSVYWKRQQGVNAPTDNLSMLPLSASATTRDGGEIADSSTEGEDTERMQADGGDNTSSRATEPTTATKEADPNEVGSDATDGIGKLLVDLIALVNCPSETPGSGTRINPMFYTMVHARLNVIAACERLNRFGSSARVAPPPLTASLQSLQSQREALNAGRHRRDAHLETSGEIGLPLDFVPSEAYLRAALERENITLEEDEELFKDEIVDYYKRQQQHQHAPPRDRSGPKEPTVLMKPHRFCKVKTGYTWTQYNRTHYDVRSNPPPRSVLWYEFTLFYPALASTKRDMSRIYHIEDTSRGSKDDYCVLVFSVGPPYADVAYQIVRKQWDPRPGGVRASFDSSGTYRLFFRFTNSNYRR
Protein: Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) (Q91WK2)
Organism: Mus musculus (Mouse)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MASRKEGTGSTATSSGSAGGAVGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKASITFEHMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKSLQLLMDRVDEMSQDIIKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPHQAPARMDSLLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN
Protein: Serine protease Lpg1137 (EC 3.4.22.-) (Q5ZWE8)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Serine protease effector that inhibits host cell autophagy by targeting SNX17. Localizes to the host endoplasmic reticulum-mitochondria contact site and catalyzes degradation of host SNX17, thereby impairing endoplasmic reticulum-mitochondria communication, leading to inhibit autophagy as well as staurosporine-induced apoptosis.
Subcellular location: Secreted {ECO:0000305|PubMed:28504273}. Host mitochondrion membrane {ECO:0000269|PubMed:28504273}. Note=Localizes to the host mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000269|PubMed:28504273}.
Interaction partners:
Sequence:
MIQRGFTMQERREKQGNNSPYLLTPYEMANLVFKTGAISFTVSAGTQPFQYLLNKLQFSQSGTPSGLSGGLFRGMYRGFLPYAIAGQKRGAVAVTHKQTNKVTEEEEFEAPFRQRWWGTIFFSQADLLVSNGLSGKARLQNVGVINAENFKWSLSNFWKLTSVNWGSRSFAGGVNFALIGFAGDYVSSFYKFDKDLYNKILGGATSGVIATLFTTAPNAYADSKLLQTKVAENNRLITVSPYTMFGQMKSHVKAVGLKEAFMTFFKVSYLQQVAVRAPQAAITFALIFGMDEYMGPQPLKKVWPGRVEELESENPSPSPTKK
Protein: Orf152b protein (Q8HCP4)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MWPSLQAHIWIWSTLFHPILIYFIPAIDSNSLFSNCTLKAKAKKDHINYSPNCRISHRIQMEDRKRRQFKPNGQTLRIQDRKTYSHKRITREQKQLHILLACLSDLLSNCHGSTTEDWLLRPSTRSWAIPDRQADGMDSLYMDGRNASTAEP
Protein: Serine/threonine-protein kinase NLK2 (EC 2.7.11.24) (Nemo-like kinase 2) (Nlk.2) (xNLK) (Q8QGV6)
Organism: Xenopus laevis (African clawed frog)
Function: Negatively regulates Wnt/beta-catenin-signaling during development. Plays a role together with sox11 in neural induction during early embryogenesis. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 to phosphorylate stat3.1. Augments the rnf138/narf-directed ubiquitination and degradation of tcf/lef by enhancing the association of rnf138/narf and tcf/lef. Phosphorylates mef2a to play a role in anterior neural development, including eye formation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}.
Interaction partners:
Sequence:
MAFPGSGRSIPGQLCAGVFSGLIQPPLGQKFYCPNGGGAVPSPLPQALSAPQCNGEGRDPEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPQIDCFEEIYVITELMQTDLHKVIVSPQPLSSDHIKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESQHMTQEVVTQYYRAPEILMGSRHYRSAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPPLTAMRSACEGARAHILRGPHKPPSLSVLYMLSGEATHEAVHLLCRMLLFDPLKRISAKDALAHPYLEEGRLRYHTCMCHCCYSVSSGRVYTADFEPTATNRFDDSYEKSLTSVWQVKELVHRFITDQHQGKRPPLCINPHSAAFKTFIRSTAWHSSKVSKKEER
Protein: Fibronectin type 3 and ankyrin repeat domains 1 protein (Germ cell-specific gene 1 protein) (GSG1) (Q9DAM9)
Organism: Mus musculus (Mouse)
Function: Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17604233}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8TC84}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Cell projection, cilium {ECO:0000269|PubMed:27914912}. Note=Weakly detected in the cytoplasm of elongated spermatids. {ECO:0000269|PubMed:17604233}.
Interaction partners:
Sequence:
MEPHKVVPLSKPHPPVVGKVTHHSIELYWDLEQKEKRQGPQEQWLRFSIEEEDPKMHSYGVIYTGYATRHVVEGLEPRTLYKFRLKVTSPSGEYEYSPVVSVATTREPISSEHFHRAVSVNDEDLLLRILEGGHVMIDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWEARDLGGCTALHWAADGGHCSVIDWMIKDGCEVDVVDTGSGWTPLMRVSAVTGSQKVASLLIEAGADVNIKDKDGKTPLMVAVLNNHEQLVQLLLDKGADATVKNEFGKGVLEMARVFDRQNVLSLLEEKKKKMPRKSSVH
Protein: GATA-type domain-containing protein (GATA-type transcription factor) (G5EF25)
Organism: Caenorhabditis elegans
Interaction partners:
- GATA-type domain-containing protein
- GATA transcription factor END-1
- Transcription factor elt-2
- Transcription factor elt-7
- Probable transcription factor elt-4
- T-box transcription factor tbx-35
- Transcription factor elt-1
- Transcription factor elt-6
- GATA-type domain-containing protein.
Sequence:
MAYPYPVFNAENVFDNTQQQVGFYDYSTPFNGTYSFTTDYSYYNNYYDYVNTYASYYPTAMDSSSLNISPTTGSPNSSHFTTFTHFSTPSTSPSTSTQSSTPPSNSDNKKSFQCSNCSVTETIRWRNIRSKEGIQCNACFIYQRKYNETRPVTAVNKYQKRKLKVQETNGVDSS
Protein: Mitochondrial enolase superfamily member 1 (EC 4.2.1.68) (Antisense RNA to thymidylate synthase) (rTS) (L-fuconate dehydratase) (Q7L5Y1)
Organism: Homo sapiens (Human)
Function: Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16162288}.
Interaction partners:
- Thymidylate synthase
Sequence:
MVRGRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAEDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQYPDGEVWKKLLPAQEN
Protein: Mastermind-like protein 1 (Mam-1) (Q6T264)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15019995}. Note=Nuclear, in a punctate manner.
Interaction partners:
- Recombining binding protein suppressor of hairless
- Neurogenic locus notch homolog protein 1
- Recombining binding protein suppressor of hairless-like protein
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Histone acetyltransferase p300
- Neurogenic locus notch homolog protein 4
- Histone lysine acetyltransferase CREBBP
- SNW domain-containing protein 1
- Mastermind like transcriptional coactivator 2
Sequence:
MVLPTCPMAEFALPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRAGKHRQPPAAATAPVAAPAPASAPAAARLDAADGPEHGRPVAHLHDTVKRSLDSAASPQNGDQPNGYGDLFPGHKKTRREAPLGVSVSANGLPPASPLGQPDKPSGGDTLQTAGKHSLGLDPINKKCLADSGIHLNGGSNSSEPFPLSLSKELKQEPVDDLPCMIAGAGGSVAQSNLMPDLNLNEQEWKELIEELNRSVPDEDMKDLFTEDFEEKKDPEPPGSATQTPLAQDINIKTEFSPAAFEQEQLGSPQVRAGSAGQTFLGASSAPVGTDSPSLGSSQTLFHTTSQPGVDNSSPNLMPASAQAQSAQRALTSVVLPSQGPGGASELSSAHQLQQIAAKQKREQMLQNPQQAAPAPGPGQLATWQQAGPSHSPLDVPYPMEKPASPSGYKQDFTNSKLLMMPGVNKSSPRPGGPYLQPSHSNLLSHQSPSNLNQNPVNNQGSVLDYGNTKPLSHYKADCGQGGPGSGQNKPALMAYLPQQLPHLSNEQNSLFLMKPKSGNMPFRSLVPPGQEQNPSSVPVAAPAASVGTQPTVSVASTHNSSPYLSSQQQAAVMKQHQLLLDQQKQREQQQQQLQQQQFLQRQHLLAEQEKQQFQRHLTRPPPQYQDPTQSTFPQQVGQFTGPSAAVPGMNNLGPSNSSCPRVFPQPGTLMSMGPGHAPVSSLPSSSGQQDRGVAQFTGSQSLPQNSLYGMASGLAQIVAQPPPQATSTHAHIPRQTNVGQNASTSAAYGQNSLGSASLSQQHSKGTLPPGLTKPQVPRVSAAMGSQNASWQHQGMPNLSSQTSGNSSVNPFTAAPSFHIQQAHLKLAGQQFSQAMPSRPMAPLSSAGAAGPMLPPVSAQQRNSAPASAPPQAAPQQGLPGLSPSGPELGAFGQSPTSQMSGRPGLHCAQAYPVRTMGQELPFAYSGQPGSSGLSSVAGHTDLIDSLLKNRTSEEWINELDDLLGSQ
Protein: Histidinol-phosphatase (HolPase) (EC 3.1.3.15) (Histidinol-phosphate phosphatase) (Q9K4B1)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Interaction partners:
- Histidinol dehydrogenase
- Histidinol-phosphate aminotransferase
- Aromatic amino acid aminotransferase
- Aminotransferase
- Phosphatase SCO2771
- ATP phosphoribosyltransferase
- Phosphoribosyl isomerase A
- Imidazole glycerol phosphate synthase subunit HisH
- DNA-directed RNA polymerase subunit omega
- CBS domain-containing protein
Sequence:
MPDYLDDLRLAHVLADAADAATMDRFKALDLKVETKPDMTPVSEADKAAEELIRGHLSRARPRDSVHGEEFGVAGTGPRRWVIDPIDGTKNYVRGVPVWATLIALMEAKEGGYQPVVGLVSAPALGRRWWAVEDHGAFTGRSLTSAHRLHVSQVSTLSDASFAYSSLSGWEEQGRLDGFLDLTREVWRTRAYGDFWPYMMVAEGSVDLCAEPELSLWDMAANAIIVTEAGGTFTGLDGRPGPHSGNAAASNGRLHDELLGYLNQRY
Protein: Gap junction alpha-10 protein (Connexin-62) (Cx62) (Q969M2)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Involved in tracer coupling between horizontal cells of the retina. May play a role in the regulation of horizontal cell patterning (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
Sequence:
MGDWNLLGGILEEVHSHSTIVGKIWLTILFIFRMLVLRVAAEDVWDDEQSAFACNTRQPGCNNICYDDAFPISLIRFWVLQIIFVSSPSLVYMGHALYRLRAFEKDRQRKKSHLRAQMENPDLDLEEQQRIDRELRRLEEQKRIHKVPLKGCLLRTYVLHILTRSVLEVGFMIGQYILYGFQMHPLYKCTQPPCPNAVDCFVSRPTEKTIFMLFMHSIAAISLLLNILEIFHLGIRKIMRTLYKKSSSEGIEDETGPPFHLKKYSVAQQCMICSSLPERISPLQANNQQQVIRVNVPKSKTMWQIPQPRQLEVDPSNGKKDWSEKDQHSGQLHVHSPCPWAGSAGNQHLGQQSDHSSFGLQNTMSQSWLGTTTAPRNCPSFAVGTWEQSQDPEPSGEPLTDLHSHCRDSEGSMRESGVWIDRSRPGSRKASFLSRLLSEKRHLHSDSGSSGSRNSSCLDFPHWENSPSPLPSVTGHRTSMVRQAALPIMELSQELFHSGCFLFPFFLPGVCMYVCVDREADGGGDYLWRDKIIHSIHSVKFNS
Protein: Beta-catenin-like protein 1 homolog (Q9UUK1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable spliceosomal component involved in the activation of pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cwf15
- Pre-mRNA-splicing factor cwf7
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 31
- Pre-mRNA-splicing factor prp5
- Pre-mRNA-splicing factor cwf4
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-processing protein 45
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-processing protein prp40
Sequence:
MDVDSIFKNTEETNKKRNPEEADSLEPASSRRRLAEENSDEENEEFDEEGGRFFGSGLKKSEKTVLDFLDEQEAQEEPASLTPTELKRMVVRLEKTINNNQELRIKYSTSPQRFIESEADLDLEIRSFNVLSEYPILIPIFLKLDCVSTFLELMNHENADITITVLELLIELTDEDVDPDALNSLFTSLIDSGLLPLLSNTIKRFDESNEEDRHGVYCVLSLMENLLSVDNSICSIIVENTTLVEWLLSRSSVDETSISTNLQYAVEILAIILANSKEAKLKVCNLNGIDLLLRRISPYRLRDPTQGSEEEMMENVFDCLCSLVQETKGKSLFLKEEGIELCILNMKHKGKSRYSTIKVLDYLLFGPLSTPYCIRFVEAGGLKYIFAAFMKISAADTLEHILAILASLFRSLPADTVERVRFLRKFIENDFEKMKRLFKIYDRLRIQLKGIDQSRKLDFSPDSEEKSTKWFLQQIDHGLFPFQSTVLILSWLCVENTVTLKKIKMLFSEASIPIDELTDALKNYHENLEEPTVESEEVEANDSYYRIDEKPMVTVLLGSMQASV
Protein: 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10) (Type I DHQase) (Type I dehydroquinase) (DHQ1) (P24670)
Organism: Salmonella typhi
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the active site.
Interaction partners:
- 3-dehydroquinate synthase
- Shikimate dehydrogenase
- Shikimate 5-dehydrogenase
- Chorismate synthase
- Isochorismate synthase EntC
- Shikimate kinase 1
- peptidase Do
- Isochorismate synthase MenF
Sequence:
MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREATFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFTFRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTGDADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVLRLRKMQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPVITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVNDLRSVLMILHNA
Protein: Class E basic helix-loop-helix protein 22 (Class B basic helix-loop-helix protein 5) (F1R9F5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger protein 488
- BarH-class homeodomain transcription factor
- Forkhead box protein N4
- Visual system homeobox 2
- Pancreas transcription factor 1 subunit alpha
- LIM/homeobox protein Lhx1
Sequence:
MDRRINLGGDIFHKTLSAVSSKKMDSFRPTAGIDLSARDSQSPISCFEQNDPDPVQPGGRAGTLGLPTGSLCVKYGESANRTSGAESSGGEQSPDDDSDERCEMMLMTDGRTTVPGAKSEGGKKNKEQKMLRLNINARERRRMHDLNDALDELRAVIPYAHSPSVRKLSKIATLLLAKNYILMQAQALEEMRRLVAYLNQGQAISAASLPATTALTPGLSAYEQPAGYPFPAGVAASSCPDKCALFNNVTSSLCKQCTDKP
Protein: Peroxisomal targeting signal receptor (PTS1 receptor) (PTS1R) (Peroxin-5) (P35056)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15283676, ECO:0000269|PubMed:17452527}. Peroxisome matrix {ECO:0000269|PubMed:15283676, ECO:0000269|PubMed:15632140, ECO:0000269|PubMed:17452527}. Note=Cycles between the cytosol and the peroxisome matrix (PubMed:15283676, PubMed:17452527). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins (PubMed:17452527). Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (PubMed:17452527). Cys-6 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (PubMed:17452527). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (PubMed:21665945). {ECO:0000250|UniProtKB:P50542, ECO:0000269|PubMed:15283676, ECO:0000269|PubMed:17452527, ECO:0000269|PubMed:21665945}.
Interaction partners:
- Peroxisomal membrane protein PEX17
- Peroxisomal targeting signal 2 receptor
- Proteasome subunit beta type-6
- Peroxisomal biogenesis factor 2
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal ATPase PEX6
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein import receptor PEX19
Sequence:
MDVGSCSVGNNPLAQLHKHTQQNKSLQFNQKNNGRLNESPLQGTNKPGISEAFISNVNAISQENMANMQRFINGEPLIDDKRRMEIGPSSGRLPPFSNVHSLQTSANPTQIKGVNDISHWSQEFQGSNSIQNRNADTGNSEKAWQRGSTTASSRFQYPNTMMNNYAYASMNSLSGSRLQSPAFMNQQQSGRSKEGVNEQEQQPWTDQFEKLEKEVSENLDINDEIEKEENVSEVEQNKPETVEKEEGVYGDQYQSDFQEVWDSIHKDAEEVLPSELVNDDLNLGEDYLKYLGGRVNGNIEYAFQSNNEYFNNPNAYKIGCLLMENGAKLSEAALAFEAAVKEKPDHVDAWLRLGLVQTQNEKELNGISALEECLKLDPKNLEAMKTLAISYINEGYDMSAFTMLDKWAETKYPEIWSRIKQQDDKFQKEKGFTHIDMNAHITKQFLQLANNLSTIDPEIQLCLGLLFYTKDDFDKTIDCFESALRVNPNDELMWNRLGASLANSNRSEEAIQAYHRALQLKPSFVRARYNLAVSSMNIGCFKEAAGYLLSVLSMHEVNTNNKKGDVGSLLNTYNDTVIETLKRVFIAMNRDDLLQEVKPGMDLKRFKGEFSF
Protein: HTH-type transcriptional regulator GntR (Gluconate utilization system GNT-I transcriptional repressor) (P0ACP5)
Organism: Escherichia coli (strain K12)
Function: Negative regulator for the gluconate utilization system GNT-I, the gntUKR operon.
Interaction partners:
- Fatty acid metabolism regulator protein
- Thermoresistant gluconokinase
- Deoxyribose operon repressor
- Arabinose operon regulatory protein
- Transcriptional repressor IclR
- Multiple antibiotic resistance protein MarR
- Arsenical resistance operon repressor
- Regulatory protein AsnC
- Low-affinity gluconate transporter
- HTH-type transcriptional regulator EbgR
Sequence:
MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSKSPCLDIAVGFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLDLGFTLSPGGSI
Protein: Small ribosomal subunit protein uS13c (30S ribosomal protein S13, chloroplastic) (CS13) (P42732)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS7cz/uS7cy
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein uL6c
- Small ribosomal subunit protein uS19c
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein eS6y
Sequence:
MAQMVAMPVAHSLSLICNWAKSNPLSRNTLALPASNTPNKQSLSIRCARVGGVEIPANKRIEYSLQYIHGIGRTRARQILVDLQMENKITKDMAEEELIILRDEVSKYMIEGDLRRFNALAIKRLKEIQCYRGVRHIQGLPCRGQRTKNNCRTLKGKKIAIAGKKKVSK