wanglab/gogpt-training-data huggingface dataset:
Protein: Meiosis-specific protein MEI4 (Q8BRM6)
Organism: Mus musculus (Mouse)
Function: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with IHO1 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis.
Subcellular location: Chromosome {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:25795304, ECO:0000269|PubMed:30569039}. Note=Specifically localizes to unsynapsed chromosomal regions during meiosis (PubMed:25795304, PubMed:27723721). Located in discrete foci on the axes of meiotic chromosomes. The number of foci is highest at leptonema, decreases at zygonema and is strongly reduced in pachynema and subsequent stages (PubMed:20551173). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:25795304, ECO:0000269|PubMed:27723721}.
Interaction partners:
- Meiotic recombination protein REC114
Sequence:
MDIQPWYLKTSKLALALAIIHSKPADRSSREYTEYLASLVTQKESTWKSKLEALEAEVLQLRQKLLLSRISSGLFKNGPDVLPTLSDQEPTSSENTLTLMDDSGCVLSNEQRNEPAELSQHFVESTDPPLLPLPLEKRPRTTLENPLSSHMQFFQHLLELKKWTESSSLKVYLTHFEKDSSTVSDSVSQLLDALITFYRNPKLPFSSFWTEAVGTLARLASDFNLSNHIFKRCSKKLEEFEKTLLQAILENNSINRFQVQRYVSQSLVTLGSCSLLRKSIISLLLSEVNSFVDDLGAIDQDQGIYDVTRYENIFSLFWILEQVLQQAPQGDRTAHMDHSIPEMQTFLQKHDEVIFRLSDAFPLFAFYLWRLGVLLNSAEMETVKNESLP
Protein: Protocadherin gamma-A4 (PCDH-gamma-A4) (Q9Y5G9)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin gamma-A2
- Protocadherin gamma-A3
- Protocadherin gamma-B3
- Protocadherin gamma-B1
- Protocadherin gamma-B2
- Protocadherin gamma-A9
- Protocadherin gamma-A8
- Protocadherin gamma-A7
Sequence:
MHFILDPEDPGAPQASTEGKPKHRRLRGGVVMAAPPARPDHTRLLQICLLLGVLVEIRAEQILYSVFEEQEEGSVVGNIAKDLGLAPRELAERGVRIVSRGRTQLFALNPRSGTLVTAGRIDREELCDRSPNCVTNLEILLEDTVKILRVEVEIIDVNDNPPSFGTEQREIKVAENENPGARFPLPEAFDPDVGVNSLQGYQLNSNGYFSLDVQSGADGIKYPELVLERALDREEEAVHHLVLTAFDGGDPVRSGTARILIILVDTNDNAPVFTQPEYHVSVRENVPVGTRLLTVKATDPDEGANGDVTYSFRKVRDKISQLFQLNSLSGDITILGGLDYEDSGFYDIDVEAHDGPGLRARSKVLVTVLDENDNAPEVTVTSLTSSVQESSSPGTVIALFNVHDSDSGGNGLVTCSIPDNLPFTLEKTYGNYYRLLTHRTLDREEVSEYNITVTATDQGTPPLSTETHISLQVMDINDNPPTFPHASYSAYIPENNPRGASILSMTAQDPDSGDNARITYSLAEDTFQGAPLSSYVSINSNTGILYALCSFDYEQFRDLQLLMTASDSGDPPLSSNVSLSLFVLDQNDNVPEILYPTFPTDGSTGVELAPRSADSGYLVTKVVAVDRDSGQNAWLSYSLLKSSEPGLFAVGLHTGEVRTARALLDRDALKQRLVVVVQDHGQPPLSATVTLTVAVADSIPDVLADLGSLKPSADPDDSGLTLYLVVAVAAVSCVFLAFVTVLLALKLRRWHKSRLLHAEGSRLAGVPASHFVGVDGVRAFLQTYSHEVSLTADSRKSHLIFSQPSYADTLISRESCEKSEPLLITQDLLETKGDPNLQQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Pleckstrin homology domain-containing family A member 7 (PH domain-containing family A member 7) (Q6IQ23)
Organism: Homo sapiens (Human)
Function: Required for zonula adherens biogenesis and maintenance. Acts via its interaction with CAMSAP3, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site. Mediates docking of ADAM10 to zonula adherens through a PDZD11-dependent interaction with the ADAM10-binding protein TSPAN33.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}. Cytoplasm {ECO:0000269|PubMed:19041755}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19041755}. Note=Localizes to zonula adherens, recruited via its interaction with CTNND1. {ECO:0000269|PubMed:19041755}.
Interaction partners:
- Calmodulin-regulated spectrin-associated protein 3
- Catenin delta-1
- Kinesin-like protein KIFC3
- PDZ domain-containing protein 11
- Tetraspanin-33
- Afadin
- Cingulin
- Tight junction protein 1
- Cingulin-like protein 1
- Catenin alpha-1
Sequence:
MAAATVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIRSDLPRGWEEGFTEEGASYFIDHNQQTTAFRHPVTGQFSPENSEFILQEEPNPHMSKQDRNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSSLKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRSQRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQNGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSRSLPLDQTLPRQGPGQSLSFPENYQTLPKSTRHPSGGSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPICLGSPEFTDQGRSRSMLEVPRSISVPPSPSDIPPPGPPRVFPPRRPHTPAERVTVKPPDQRRSVDISLGDSPRRARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVTAGLSANKENFRILVESVKNPERKTVPLFPHPPVPSLSTSESKPPPQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVTSPLQSPTKAKPKVEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDRELGQCVNGDSRVELRSYVSEPELATLSGDMAQPSLGLVGPESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAESSKATFPRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLGQGERTGLPSSRYLSRPLPGDLGSVC
Protein: Dual specificity protein phosphatase 7 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST2) (Q16829)
Organism: Homo sapiens (Human)
Function: Dual specificity protein phosphatase. Shows high activity towards MAPK1/ERK2. Also has lower activity towards MAPK14 and MAPK8. In arrested oocytes, plays a role in meiotic resumption (By similarity). Promotes nuclear envelope breakdown and activation of the CDK1/Cyclin-B complex in oocytes, probably by dephosphorylating and inactivating the conventional protein kinase C (cPKC) isozyme PRKCB (By similarity). May also inactivate PRKCA and/or PRKCG (By similarity). Also important in oocytes for normal chromosome alignment on the metaphase plate and progression to anaphase, where it might regulate activity of the spindle-assembly checkpoint (SAC) complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9788880}.
Interaction partners:
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 1
- Dual specificity protein phosphatase 9
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 13
- Speckle-type POZ protein
Sequence:
MKNQLRGPPARAHMSTSGAAAAGGTRAGSEPGAGSGSGAGTGAGAATGAGAMPCKSAEWLQEELEARGGASLLLLDCRPHELFESSHIETAINLAIPGLMLRRLRKGNLPIRSIIPNHADKERFATRCKAATVLLYDEATAEWQPEPGAPASVLGLLLQKLRDDGCQAYYLQGGFNKFQTEYSEHCETNVDSSSSPSSSPPTSVLGLGGLRISSDCSDGESDRELPSSATESDGSPVPSSQPAFPVQILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNAFEHGGEFTYKQIPISDHWSQNLSQFFPEAISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKMNLSLNDAYDFVKRKKSNISPNFNFMGQLLDFERTLGLSSPCDNHASSEQLYFSTPTNHNLFPLNTLEST
Protein: Alpha carbonic anhydrase 4 (AtaCA4) (AtalphaCA4) (EC 4.2.1.1) (Alpha carbonate dehydratase 4) (F4JIK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}. Note=Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system. {ECO:0000250}.
Interaction partners:
- Cyanate hydratase
- Beta carbonic anhydrase 4
- Putative calcium-transporting ATPase 11, plasma membrane-type
- Ribosome production factor 2 homolog
- Calcium-transporting ATPase 3, endoplasmic reticulum-type
- Large ribosomal subunit protein uL18y
Sequence:
MDTNAKTIFFMAMCFIYLSFPNISHAHSEVDDETPFTYEQKTEKGPEGWGKINPHWKVCNTGRYQSPIDLTNERVSLIHDQAWTRQYKPAPAVITNRGHDIMVSWKGDAGKMTIRKTDFNLVQCHWHSPSEHTVNGTRYDLELHMVHTSARGRTAVIGVLYKLGEPNEFLTKLLNGIKAVGNKEINLGMIDPREIRFQTRKFYRYIGSLTVPPCTEGVIWTVVKRVNTISMEQITALRQAVDDGFETNSRPVQDSKGRSVWFYDPNV
Protein: Protein transport protein sec1 (O94590)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the final stage of protein secretion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and barrier septum.
Interaction partners:
- Syntaxin-like protein psy1
- Protein transport protein sec9
- Exocyst complex component sec6
- Synaptobrevin homolog 1
- Exocyst complex component sec15
- Vacuolar protein sorting-associated protein 33
- Integral membrane protein sed5
- Vesicular-fusion protein sec18
- Exocyst complex component exo70
- Syntaxin pep12
Sequence:
MTLLELQKELFLSKINSVECATKWKVLIVDTKTADIINHFITIHSLLEEKIAAVEILENPRTPNSSFEALYILHSEEKLVDCILKDEEYDKRYPGIHIVFLDMVKEPLINKLRTSRIASKIRTVQVAYLDFTSLESRYFQVHDSFSGLRLYHPSNAAIIRQELSKVAHGIFSVCVSLGISPNIRCYYPKNAPHASKTMSFILANQLSEIVEEYCSKHPGYHEAASKSTCLIVDRSLDTAAPFLHEFTYQAMIHDLLPIKNEQYPYEILGPQGTEKRTGKLDDDDLVYTTIRHMHMRDAIEKLMKDFNQFCIDNTLFLDKERATSLNDMRSMLAGLSDFQELRDQYSLHLTMAQECMNIFEKQQLNLIGAIEQDLSTGSNVEGKVPRSVLSELLPLLDEGNAEESTKIRLLLLYIIYRDGIILQDLFRLFRHSNLSTSREQIFQNLEQLGTRVIKNLTDQSSKRKEVANSLPAGEDVYELSRYVPTLKVVLENLIQDKLDPELFPYVRNTTPQTEVSMEQTSLRSSRPSWTRSRSMASKLPREKMLVFVAGGTTFSELRTCYELSDKYNKDIYIGSTVCYSPNEWLDFFSKFQQPREALKFPEDKPRHIPCLEARPSPNRIQEQPNIDVPSTRYENTSSSDAVSIHKDEKKSKGKSHKLGKLMMSSKKDKDKSKEKVPTYGTSDKKKKKRFGVF
Protein: Putative ADP-ribosylation factor-like 2, arl2 (E9AEJ0)
Organism: Leishmania major
Interaction partners:
- Putative tubulin folding cofactor D
- GMP phosphodiesterase delta subunit domain-containing protein
- Tubulin alpha chain
Sequence:
MGLLSIIKKTKRKEREMRILMLGLDNAGKTTCVKKLCGKDTSLISPTLGFQITALTFRGCTLNVWDVGGQQSLRSYWRNYFESTDGLVWVVDSNDVERLLMCKEELHHLLQEERLAGASLLVFLNKIDIPTALSPQEIAGLLDVDTIRQGKRHVHLCACSARTGEGLLDGISWMVDDVSKRMYFSS
Protein: At4g13350 (NSP (Nuclear shuttle protein)-interacting GTPase) (Q8W4K6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NF-X1-type zinc finger protein NFXL2
- B-block binding subunit of TFIIIC
- Protein CDC73 homolog
Sequence:
MAGRVKEDEKNEKIIRSLLKLPENKRCINCNSLGPQYVCTTFWTFVCTNCSGIHREFTHRVKSISMAKFTSQEVTALKEGGNQHAKDIYFKGLDQQRQSVPDGSNVERLRDFIRHVYVNKRYTNEKNDDKSPSETRSSSGSRSPPYEDGYDRRYGDRSSPGGRSPGFETGSRNAVNNRKSPARPEILNDWRREDRFGGRKTSEEGSQSPEQVKDLGSASPPVARPVREILGDSVIPLRVGEPPKPPVSRNTDASAHAKSGTSLSSLMSTNEKPPEVKLETALSLIDFDTDFETPAPSVAIQAPLSTTSQPAPQPTTSSNDNWASFDAAPSAPSLNVSQPPPSGNTLDSLLSQLAVTSSVPGQASTPSNGPVNLGHSTSQIFAPFQNEHSSEQPWNTALASNVQRSMSAPSLQPLQGVPSGGLQSSEVKPSGRSELPADLFAVNYPSYHAPVPGWQAGPPHAMHYGMQQYNNPVPYQNVPQPGKSMNPFDFSPGPPSQTQTENMFPSMAPLQGALPPSGMMPSQGVHNQFNIPSQGSAHPSAMPPRYMPSQIPGSMPPSNVNPIGDINTSYDTQQTYQNFGSSFAAAVPLNPPSFQSGGNPFG
Protein: Guanylate kinase (EC 2.7.4.8) (GMP kinase) (Guanylate kinase 1) (Q64520)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme for recycling GMP and indirectly, cyclic GMP (cGMP). Involved in the cGMP metabolism in photoreceptors (By similarity).
Subcellular location: Photoreceptor inner segment {ECO:0000269|PubMed:29515371}. Cytoplasm, cytosol {ECO:0000269|PubMed:29515371}. Note=Colocalizes with RD3 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer. {ECO:0000269|PubMed:29515371}.
Interaction partners:
- GMP synthase
- Adenine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Adenylate kinase 9
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Nucleoside diphosphate kinase A
- Hypoxanthine-guanine phosphoribosyltransferase
- Cytosolic 5'-nucleotidase 1A
- Nucleoside diphosphate kinase, mitochondrial
- GMP reductase 2
Sequence:
MAGPRPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEPGLFDLVIINDDLDKAYATLKQALSEEIKKAQGTGHA
Protein: Hydroperoxide isomerase ALOXE3 (Epidermis-type lipoxygenase 3) (Epidermal LOX-3) (e-LOX-3) (eLOX-3) (Hydroperoxy dehydratase ALOXE3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Hydroperoxy icosatetraenoate isomerase) (EC 5.4.4.7) (Q9BYJ1)
Organism: Homo sapiens (Human)
Function: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
Interaction partners:
- Magnesium transporter NIPA4
- Protein-glutamine gamma-glutamyltransferase K
- Ultra-long-chain fatty acid omega-hydroxylase
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Protein-lysine 6-oxidase
- Glucosylceramide transporter ABCA12
- Omega-hydroxyceramide transacylase
- Ceramide synthase 3
Sequence:
MAVYRLCVTTGPYLRAGTLDNISVTLVGTCGESPKQRLDRMGRDFAPGSVQKYKVRCTAELGELLLLRVHKERYAFFRKDSWYCSRICVTEPDGSVSHFPCYQWIEGYCTVELRPGTARTICQDSLPLLLDHRTRELRARQECYRWKIYAPGFPCMVDVNSFQEMESDKKFALTKTTTCVDQGDSSGNRYLPGFPMKIDIPSLMYMEPNVRYSATKTISLLFNAIPASLGMKLRGLLDRKGSWKKLDDMQNIFWCHKTFTTKYVTEHWCEDHFFGYQYLNGVNPVMLHCISSLPSKLPVTNDMVAPLLGQDTCLQTELERGNIFLADYWILAEAPTHCLNGRQQYVAAPLCLLWLSPQGALVPLAIQLSQTPGPDSPIFLPTDSEWDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFAMATLRQLPLCHPIYKLLLPHTRYTLQVNTIARATLLNPEGLVDQVTSIGRQGLIYLMSTGLAHFTYTNFCLPDSLRARGVLAIPNYHYRDDGLKIWAAIESFVSEIVGYYYPSDASVQQDSELQAWTGEIFAQAFLGRESSGFPSRLCTPGEMVKFLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGTTTLKTYLDTLPEVNISCNNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRRSIAAFQSRLAQISRDIQERNQGLALPYTYLDPPLIENSVSI
Protein: Trace amine-associated receptor 12h (Q5QNN8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MILNDTDIYSENVLLCYPLLPDSCPRTQRLPALKVAMYAVMVLMILTTVFGNLLVIISISHFKQLQSPTHLIVQSLAACDCLLGSLVMPYSMVRSVEGCWYLGTVVCKVHSSLDMTFSISSILHLSLIAIDRFWAISDPLRYKMRVTNTTVAGFITFTWLFSFVYSFSVVFTGVNNVGLEELILQISCFGGCVLFFNKEWGLICALFVFLIPGTIMSSLYMSIFNVVKRHAKVMSEKVSAAATAGSHFQTSSHRERKAAKTLAIVMGVFYLCWLPFFTATAVDPFLNFSTPGDVFDALVWFGYFNSTCNPLIYGFFYPRFQKAFKILISTYICGSSDSHTLTFE
Protein: Bacteriocin enterocin-M (P85876)
Organism: Enterococcus faecium (Streptococcus faecium)
Function: Bacteriocin that inhibits the growth of closely related Enterococcus species and a wide range of Gram-positive bacterial species. Inhibits the growth of several strains of the Gram-negative bacterium E.coli, but not the growth of Gram-negative Pseudomonas species.
Subcellular location: Secreted {ECO:0000269|PubMed:17551760}.
Interaction partners:
Sequence:
ATRSYGNGVYCNNSKCWNVGEAKENIAGIVISGKASGL
Protein: Transcriptional regulatory protein PhoP (P23836)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). Mediates magnesium influx to the cytosol by activation of MgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein PhoQ
- Phosphate regulon sensor protein PhoR
- Sensor protein BasS
- Sensor histidine kinase EnvZ
- PhoP/PhoQ regulator MgrB
- Signal transduction protein PmrD
- Lipid A palmitoyltransferase PagP
- Phosphoethanolamine transferase EptA
- Sensor histidine kinase CpxA
- Magnesium-transporting ATPase, P-type 1
Sequence:
MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR
Protein: Glutathione S-transferase P 1 (Gst P1) (EC 2.5.1.18) (GST YF-YF) (GST class-pi) (GST-piB) (Preadipocyte growth factor) (P19157)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}.
Interaction partners:
- Peroxiredoxin-6
- Glutathione S-transferase theta-1
- Fanconi anemia group C protein homolog
- Glutathione S-transferase P 2
- Glutathione S-transferase
- Glutathione S-transferase theta-2
- Glutathione S-transferase kappa 1
- Cytochrome P450 2E1
- Glutathione S-transferase omega-1
- Glutathione S-transferase omega-2
Sequence:
MPPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQGLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVKALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVNRPINGNGKQ
Protein: ER lumen protein-retaining receptor (Endoplasmic reticulum retention defective protein 2) (HDEL receptor) (P18414)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor strongly recognizes H-D-E-L and weakly recognizes D-D-E-L and K-D-E-L.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2194670}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein RER1
- Protein ERD1
- Coatomer subunit zeta
- Coatomer subunit beta
- ER-derived vesicles protein ERV29
- Coatomer subunit delta
- Endoplasmic reticulum chaperone BiP
- Coatomer subunit gamma
- Coatomer subunit alpha
- Endoplasmic reticulum vesicle protein 25
Sequence:
MNPFRILGDLSHLTSILILIHNIKTTRYIEGISFKTQTLYALVFITRYLDLLTFHWVSLYNALMKIFFIVSTAYIVVLLQGSKRTNTIAYNEMLMHDTFKIQHLLIGSALMSVFFHHKFTFLELAWSFSVWLESVAILPQLYMLSKGGKTRSLTVHYIFAMGLYRALYIPNWIWRYSTEDKKLDKIAFFAGLLQTLLYSDFFYIYYTKVIRGKGFKLPK
Protein: Polcalcin Cup a 4 (Calcium-binding pollen allergen Cup a 4) (allergen Cup a 4) (A0T2M3)
Organism: Hesperocyparis arizonica (Arizona cypress) (Cupressus arizonica)
Interaction partners:
Sequence:
MDEVPSSDESKSASSGKRVLEQSVHELEEVFKKFDANGDGKISGSELADILRSMGSEVDEAEVKAMMEEADTDGDGYVSLQEFVDLNIKGATVKDLKNAFKVFDRDCNGTISPAELCETLKSVGEPCTIEESKNIIHNVDKNGDGLINVEEFQTMMTSEMTDKSK
Protein: oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) (Q7KML1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMVPAKSLATTCVASKRMMWQIPEKWTMEEASTVPCVYSTVYYALVVRGQMKKGEKILIHAGSGGVGQAAISVALAHGLTVFTTVGSKEKREFLLKRFPKLQERNIGNSRDTSFEQLVLRETKGRGVDLVLNSLSEEKLQASIRCLGLNGRFLEIGKFDLSNNSPLGMSVFLKNTSFHGILLDSVMEGEEEMQNQVVSLVAEGIKTGAVVPLPTSVFNDQQVEQAFRFMASGKHIGKVVIKVRDEEAGKKALQPKPRLINAIPRTYMHPEKSYILVGGLGGFGLELTNWLVTRGARYIVLTSRSGVKTGYQGLMIRRWQERGVKVVIDTSDVTTAAGAKKLLENSNKLALVGGIFNLAAVLRDALIEDQTAKDFKTVADPKVTATKYLDQFSRDICTELDYFICFSSVSCGRGNIGQTNYGLANSAMERICEQRQVSGFPGTAIQWGAIGDTGLVLENLGDNDTVIGGTLPQRMPSCLQTIDLFLQQPHPVVASMVVAEKRKSDQSAGVSLIATIANILGLRDTKNIQDGASLADLGMDSLMSAEIKQTLERNFDIVLSAQEIRQLTFGALKAMDGGADVKPAAAAPAAAAGVPEANITSGGSSRTASPMGDGTQVVFTTSLIPTEAIVQLDTKAPANSKQSPIFFISPIEGFASALEPLAKRLEVPAYGLQYTEAVPSDSLESAAKFFIKQLRTVQPKGPYKLAGYSFGCLLTYVMAGILEETNEVANVIMLDGAPSYVNWYTSSFKQRYTDGTNADNDNQSYGLAYFGIVLANIDYKALVRLLIVIPTWEEKLERFAELMSNEITQPVETIKKSATLFYKKLELADGYQPTLKLKTNVTLVKPTDNSAKLDEDYRLKEVCTKPVEVHTVEGNHRTFLIEDQSLKTIQSILKRLFN
Protein: Transitional endoplasmic reticulum ATPase (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (C9JUP7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG
Protein: Tumor protein p53 binding protein 1 (A0A8I6AB98)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
IPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQALEEDAGSHFSVLSRHLPNLQMHKENPVLDIMSNPEQTVAEQGDSNSSFSEHLKEKKASDPVESSHLGTSGPISQVIERLPQPNRTSSLLFDQLLSTFLFLDSASSQLGFGVLELSQSQDVEEHTVPYDVKQEHLQLVTTNSGSTQLSDVDANTDGKAIKCEEQSTDAISIIEPSKDIPVTVQPSKGSHVVEEQNLPLVRSEDLPSSPQVSVAAVETKEQVPAQELLEGGLQVQVSSEPEVSSTQEDLFDQSSKTASDGCSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQGQRKDEPMDMSVIPEGGEHFQKLQDDEAVDIEKPLLPSQPAVSPQASTPVSRSTPVFTPASLPIPSQPEFSHDIFIPSPSLEEPSNDVEKGGGLHSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSECSQSSKMESLGSPRTEEVGENTQVEDTEPSSPVTKSKLPAESESVLVNPTQDDQVEMSQNVDKAKEDEVEDRGDVDVLAAGCKGREDMVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEEFSGSEVEEVPETPCGSHREESKEEPMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSPQKLPVLDQELEHKDPETWEEATSEDSSVVIVDVKEPSPRVDISCEPVEGVGKCSDSQSLEGAAPEEEPCAENRLNTPEEKRVECDGDSKAETTEKNSVTEDSPQPPLPSVRDEPVRPDQELQQPQVQEKESPVTLDAKVADDKHLGSEGSCQQLEKAPARASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVEINDPLLGNEKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERRNGSTAIAEPVASPQKPMSVFGCIYEAQQEEEAQSGDPPSTPVRTNLLHFPSAQEEDREEPDATPQLRQSEQPVKLIGPVKDAAASEDSASSVSQQRASQGSLSPQEEVMEADLLEGLGANQDRPSKILMERPTQSNIGIQTMDHSLCAPETVSAATQTVKNVCEQGTSTVEQNSGKQDATVQTERGSGEKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHTRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSAIHSSGSSGRGAGPLKGKTSGTEPADFALPSSRGGPGKLSPRKGISQTGAPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGIEDTSPSMSPDDKSFTRIMPRVPDSTKRMDASSGALRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNISSPATPTASSSSSTTPTRKTTESPRASMGVPSGKRKLTTSEEERSPAKRGRKSATVKPGTVGAAELVSPCESGDNTGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLLDGPTGSSEEEEEFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFQQHPKYKHDYVSH