wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipid hydroperoxide glutathione peroxidase (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4) (EC 1.11.1.9) (P36968)
Organism: Sus scrofa (Pig)
Function: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide. Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (By similarity). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:O70325}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000250|UniProtKB:O70325}.
Interaction partners:
- Glutathione reductase
- Glutathione peroxidase
- glutathione transferase
- Epididymal secretory glutathione peroxidase
- Peroxiredoxin-6
- Glutathione peroxidase
- Glutathione peroxidase 1
- Gamma-glutamylcyclotransferase
- glutathione peroxidase
- Glutathione S-transferase kappa 1
Sequence:
MSFSRLFRLLKPTLLCGTLAVPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGYVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSDAEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
Protein: Tubulin beta chain (A0A384MEE3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
Protein: Uncharacterized RNA-binding protein C3H8.09c (Q10145)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Rpb7-binding protein seb1
- Helicase sen1
- Uncharacterized protein C4G9.04c
- Poly
- Polyadenylate-binding protein 2
- Uncharacterized RNA-binding protein C644.16
- Uncharacterized RNA-binding protein C902.04
- UPF0400 protein C337.03
- Cleavage and termination factor 1
- Nuclear cap-binding protein subunit 2
Sequence:
MSSSSKDSSFQVETPVQNILETSTNSELQDQVSSPYEPDYNSPVKQAAASISALQTQDDTLFNNVDERTLENKDGNKSDDANFDQVSGIPSGSLEIPILNSATSNIRLTPSDTYNNIPVSDTNNEEISKNIYGAPILESTSSDFQSKDSLSTTQPSVSGGNGSTSQSPPSLDVEQNKPFSISNEPVEQETENSSTKDLQVYDFQTASEHLPEQSLQNTTYYDPSKTYSSVNFEEIEYGKSHEKLDLPYRTTDFIPYSKDLSTSPEAHRTSIYSYSANLPNYYNEHNELHEHHNPQTPSSPESAYSPENLQLNHEAQNVEYLGNNAAEKSLQMNLEDEQRFQQFLKDEESIMSNWYPGQFPSASRLFLGHLNTKSLSKRNLWKVFKIYGPLAQIVLKANYGFVQFFTNEDCARALNAEQGNFVRGQKLHLEISKIQKKYQNQIENMKKGSHVTKSNQYSEMIGNLPYPTSSRKRTRSPLMSKGKSYDRKGSISMSKNFSPDCEILVTEDCPKEFVWGVEKVFQERRLNIHTTCLYRDSNLQVIIKSCIINSVKSIILINAGLAHLGKVSVQVFKDGSSDSEVRCDEYAAVDVMVAASIVHHAKTSLMHSAASSTPSYNGERIVPDVPSPCISTNPNLPALVGSLDSVNLHHLLGFIQNTYSTTSYIPTRVSFNPNDTGGSFGTITSQSQFVVNEMPKNYARDNYEALHSQESRQRSSVAGNKQLQKILEQLAELKQPDF
Protein: STAS domain-containing protein (Q57VD7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Endo/exonuclease Mre11
Sequence:
MVSCFVRPVDVFGNPKTALGENLEPQHTWLEWIFMPRHKPLFHNFSSNARAGLTVALVNVPLSIALAIGSGATPEQGIVSCVWAGTVATIVGSSHFNVVGPTGALSGLLASMVAARGPGVLSPLALQAALWIFLFFLLRVNRLLRYVSSGVAHGFGCGVAIVIAVGQIPSALGLKNVTPHESLVEKLKEDYRRIDTISIPDTLLFLSTILPLLILSKRYNKIPWQIVFTMLGIAMARILPSGSLVLLGSKYPNLSLNFFSFQPLHTLIEADYFDFKTVLYGFGIAIVALIETLISSIIANNHVDDKSYLNYSGARDTFGLAMANLMSSLVGGIPSTAALARTALMIHSSAFSRVAGVISCMAVALLCSVLLPLFRDIPMATVAAILMVVAYKLVDLHDLHILHVVDTANLYSTIITCAACVLTDTFVGLVVGVFISVLLNYSDSQEAEVLFEEEDETFASPHRPEPVMFRVLIVRPQESLLFINAEIMKNTIFERSVTFCESTPSGLKRRLVLDMALVNRVDFDGTKALGEIISAHREKNWVVDVINAQHLRNSLALCTPFHDLHKLEYQELY
Protein: Amino-acid permease GAP6 (A0A1D8PNP3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Amino-acid permease with rather broad substrate specificity. Transports many amino acids including proline, methionine, leucine, valine, isoleucine, phenylalanine, tryptophan, threonine and tyrosine, but not basic ones (arginine) and citrulline. Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28028545}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPKEASSPECYTTSTSSNEISEKPGMWRNFKDSFKPPVPIDDIENGSISSTQLKGGQNVPLQQSLKKRQLQMIALGGCVGSGLLVASGAALRNGPASLLIAWFIVSTFLYCTMQCLAELSSTFPVSGSFAVYSIKFIDPSWGTAMGYNYALFWVVVMPLELVASSMTIKFWPSNINTSVWVAVFYVLIIGTNLFGGTRAFGETEFVASVIKLLGIVGFNILAIVLICGGGDQGYIGGKNWHPPFTTGVKGVISVLLTATYSLAGTELVGLTSAEAAGDARKVLPKAIKQVLWRILIFYLLTLTLVGFLVPASDPQLIGGGSGASASPFVIAIREGGIKGLPSVFNVVVLVALLAIANSAVYGFSRTILALAEQGVAPSIFKYVDRQGRPLAGIATSAIVGLLSFVSASKQQEQVFDWLVALSGLSTFFTWGSINAAHIRFRIAMKVQGRSLDELPYKANTGVLGAYYGLIMNVAVLALQFWLAVWPIGGKPDATYFFKQYLAAVLVLAVYVIHKVATRNWKFMVDYKDMDLDSGRSDIDIDILKQELEEEREAYKRQPWYYKFYQFWC
Protein: Flagella basal body P-ring formation protein FlgA (P75933)
Organism: Escherichia coli (strain K12)
Function: Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Basal-body rod modification protein FlgD
- Flagellar basal body rod protein FlgB
- Flagellar basal-body rod protein FlgC
- Flagellar L-ring protein
- Flagellar basal-body rod protein FlgG
- Flagellar protein FliL
- Flagellar motor switch protein FliM
- Flagellar hook protein FlgE
- Negative regulator of flagellin synthesis
- Flagella synthesis protein FlgN
Sequence:
MLIIKRSVAIIAILFSPLSTASNLTSQLHNFFSAQLAGVSDEVRVSIRTAPNLLPPCEQPLLSMSNNSRLWGNVNVLARCGNDKRYLQVNVQATGNYVVAAMPIARGGKLEAGNVKLKRGRLDTLPPRTVLDINQLVDAISLRDLSPDQPIQLTQFRQAWRVKAGQRVNVIASGDGFSANAEGQALNNAAVAQNARVRMVSGQVVSGVVDADGNILINL
Protein: Ankyrin repeat domain-containing protein 6 (Diversin) (Q69ZU8)
Organism: Mus musculus (Mouse)
Function: Recruits CKI-epsilon to the beta-catenin degradation complex that consists of AXN1 or AXN2 and GSK3-beta and allows efficient phosphorylation of beta-catenin, thereby inhibiting beta-catenin/Tcf signals.
Interaction partners:
- Axin-1
- Segment polarity protein dishevelled homolog DVL-1
- Prickle planar cell polarity protein 3
- Predicted gene 21981
- Prickle-like protein 2
- Prickle-like protein 1
- Glycogen synthase kinase-3 beta
- Casein kinase I isoform epsilon
- Vang-like protein 2
Sequence:
MSQQDAVAALSERLLIAAYKGQTENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQILRFSRGRSLRKRRERLKEERRAQSVPRDEVAQSKGSVSAGDTPSSEQAVPQKEEARRDCPPASQEPRKDERRRKSRPEVSALSDPTPAADQQPGHQKNLHSHHHPKKKSRHRCWSPPPPHGFRAYQLYTLYRGEDGKVMQAPIKGCRCEPLINKLENQLEATVEEIRAELGSVQDKVNAKLGQMESKTQHQMCVLDKLMVERLSAERTECMNRLQQHAAAEKQEGEKRQMSLVDELKAWCMLKIQSLELRLSGESRTFRAKSTPPPSDSTPAVDQPVVAAGPGAASDSSSQVVRPKDKALNASAAHSHQQELPPSDCTGSGLRKIKAPGASRCDQQTGSCVNRGTQTKKSGRSGQTKHRGQQPTASSPSGQQPSAASSDVRDASQALELTQYFFEAVSAQMEKWYERKIEEARSQASQKAQQDEATLKEHIRSLEEELARLRTKVQK
Protein: Neuron-specific vesicular protein calcyon (Q9DCA7)
Organism: Mus musculus (Mouse)
Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- D
Sequence:
MVKLGCSFSGKPGKEAGDQDGAAMDSVPLISPLDVSQLQPSFSDQVVINTQTEYQLTSADQPKKFADLEGQRLACSHSEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTEMPAVWGNNYRTAKEEHKGTTPAAMAVSTAAAAAAAEGTEPSGKSLDTREKEDPQKAEGVPSQPPK
Protein: endothelin-converting enzyme 1 (EC 3.4.24.71) (A0A024B5K5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000256|ARBA:ARBA00004250}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004194}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004194}.
Interaction partners:
- Endothelin 1.
- Endothelin-3
- Endothelin-1 receptor
- Endothelin-3a
Sequence:
MSVALQDLRNNMSNYKRATFEEEDGTDVPVDGAISPDSVEVGFRKGGIQLFGPLGRRTQLEVVLAGLLLASLLALFGCAVTLGVRYNRDPARSICLTEACVTVASKIVEALDRSADPCQDFYQYACGGWVRKNPLPDGRSRWSTFNSIWDQNQAVLKHLLENGTFNSSSEAERKTQSYYLSCLNEQRIEELGAQPLMDLITKIGGWNITESWDKENFLDVLKIISGPYRAQPFFTVSVSVDPKNSNSNVIQVDQSGLFLPSRDYYLNKTNEKVLKAYLDYMVELGLLLGGDKNSTRGQMQQILDFETALANITVPQDERRDEEKIYHKITIADLQVLAPAIEWLDYLNSVLSPLELNDTEPVVVYAKEYMQQVSELINKTDHSLLNNYMIWNLVQKGASSLDQRFENAQDKLLESLYGTKKSCTPRWQTCIGNTDDTLGFALGALFVKATFDKQSKEIAEGMINEIRTAFKGALDDLKWMDEQTRQAAKDKADAIYDMIGFPDFILDSKELDDVYDGYEVTEDNFFQNMINFYNFSARVMADQLRKPPNRDQWSMTPPTVNAYYMPTKNGIVFPAGILQAPFYAQDHPKALNFGGIGVVMGHELTHAFDDQGREYDKDGNLRSWWQNSSVEAFKNRTECMVDQYTQYTINGEHINGKQTLGENIADNGGLKAAYHAYRSWVQKNGEEKRLPAVNLTNDQLFFVGFAQVWCSVRTPESAHEGLMTDPHSPPKYRVIGTLSNSPEFAEHFQCPLGSSMNSGHRCEVW
Protein: Elongation factor Tu (EF-Tu) (EC 3.6.5.3) (Q74JU6)
Organism: Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
Interaction partners:
Sequence:
MAEKEHYERTKPHVNIGTIGHVDHGKTTLTAAITTVLAEDGLAQAEDYSQIDAAPEEKERGITINTAHVEYETKNRHYAHMDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVQYIVVFLNKVDLVDDPELIDLVEMEVRDLLSEYDYPGDDVPVIRGSALKALEGDPEQQDVIRKLMETVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEIVGLTDKIEKSTVTGLEMFHKTLDLGEAGDNVGVLLRGIDRDQVERGQVLAAPGSIQTHKNFKGQVYILNKDEGGRHTPFFSDYRPQFYFHTTDVTGKIELPEGTEMVMPGDNVEFTVELIKPVAIEKGTKFTIREGGKTVGAGQVTEILD
Protein: Prolyl endopeptidase (PE) (EC 3.4.21.26) (Post-proline cleaving enzyme) (rPop) (O70196)
Organism: Rattus norvegicus (Rat)
Function: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4-methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23687}.
Interaction partners:
- Thimet oligopeptidase
- Dipeptidyl peptidase 4
- dipeptidyl-peptidase IV
- Lysosomal Pro-X carboxypeptidase
- Pyroglutamyl-peptidase 1
- dipeptidyl-peptidase IV
- Neprilysin
- Acylamino-acid-releasing enzyme
- Membrane metallo-endopeptidase-like 1
- Dipeptidyl peptidase 2
Sequence:
MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLRNVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTREELEPRVFREVTVKGIDASDYQTIQVFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTTSKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDSKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGPGKPTAKVIEEVSDMFAFIARCLNIEWIQ
Protein: Protein CHROMOSOME TRANSMISSION FIDELITY 7 (EC 2.3.1.-) (Cohesion establishment factor CTF7) (Protein ESTABLISHMENT OF COHESION 1) (A7UL74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acetyltransferase required for the establishment of sister chromatid cohesion. Involved in preservation of genome integrity and meiosis. Required for DNA repair and for the regulation of chromosome segregation during mitotic cell division. Knock-down mutants are extremely dwarf. Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of WAPL1 and WAPL2.
Subcellular location: Nucleus {ECO:0000269|PubMed:20671110}. Cytoplasm {ECO:0000269|PubMed:20671110}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 4
- Chromosome transmission fidelity protein 18 homolog
- Structural maintenance of chromosomes protein 5
- Sister chromatid cohesion 1 protein 1
- Wings apart-like protein 1
- Sister chromatid cohesion 1 protein 4
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion protein SCC2
- Structural maintenance of chromosomes protein 6B
Sequence:
MQAKINSFFKPSSSSSIAASVTTDTDDGLAVWENNRNAIVNTYQRRSAITERSEVLKGCIEKTLKKGSSSVPKNHKKKRNYTQFHLELGQSDFLLRHCAECGAKYAPGDELDEKNHQSFHKDYMYGLPFKGWQNEKAFTSPLFIKNRIVMVSENDSPAHRNKVQEVVKMMEVELGEDWILHQHCKVYLFISSQRISGCLVAEPIKEAFKLIASPDDERQLQKESSSSPSTSIQFGNIVLQREVSKRCRTSDDRLDNGVIVCEEEAKPAVCGIRAIWVSPSNRRKGIATWLLDTTRESFCNNGCMLEKSQLAFSQPSSIGRSFGSKYFGTCSFLLYKAQLIDTHFS
Protein: DnaJ homolog dnj-10 (DnaJ domain protein 10) (Q8TA83)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein hsp-6
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum chaperone BiP homolog
- Heat shock protein hsp-1
- Mitochondrial import inner membrane translocase subunit TIM14
- Probable mitochondrial import inner membrane translocase subunit tim-17B.1
- GrpE protein homolog
- Heat shock protein 110
- Mitochondrial-processing peptidase subunit beta
- Heat shock 70 kDa protein C
Sequence:
MFVLNRSSGLIHRSVPLLAQVSTPTTSTTKLAQLHTTHALSKEDYYKTLGVDKKSDAKAIKKAYFQLAKKYHPDVNKTKEAQTKFQEISEAYEVLSDDTKRQEYDAYGSGGGPAGGRGGAGGFHHHGNVDVNEIFRRAFGGGGGMGGFNFDNFAQSAFGHSAAQEMVMDISFEEAVRGATKNVSVNVVEDCLKCHGTQVEPGHKKTSCPYCNGTGAVSQRLQGGFFYQTTCNRCRGSGHYNKNPCQECEGEGQTVQRRQVSFNVPAGTNNGDSLKFQVGKNQLFVRFNVAPSLKFRREKDDIHCDVDISLAQAVLGGTVKVPGINGDTYVHIPAGTGSHTKMRLTGKGVKRLHSYGNGDQYMHIKVTVPKYLTAEQKQIMLAWAATEQLKDGTIKGLEKNQKTEEKETKKNEEKKSEGASESQKRRSEPVAENAETIDENQENEGFFEKIKRKIFG
Protein: Probable cytochrome P450 6g2 (EC 1.14.-.-) (CYPVIG2) (Q9V675)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELVLLILVASLIGIAFLALQQHYSYWRRMGVREIRPKWIVGNLMGLLNMRMSPAEFISQLYNHPDAENEPFVGIHVFHKPALLLRDPEMVRNILVKDFAGFSNRYSSSDPKGDPLGSQNIFFLKNPAWKEVRLKLSPFFTGNRLKQMFPLIEEVGASLDAHLRQQPLHNERMRCFDLEAKELCALYTTDVIATVAYGVSANSFTDPKCEFRRHGRSVFEFNLLRAAEFTLVFFLPHLVPFVRFKVVPAEATRFLRKTINYVMSEREKSGQKRNDLIDILIEFRRSTQLAKASGIKDQFVFEGDILVAQAVLFFTAGFESSSSTMAFAMYELAKDTDVQQRLREEIKDALVESGGQVTLKMIESLEFMQMILLEVLRMYPPLPFLDRECTSGRDYSLAPFHKKFVVPKGMPVYIPCYALHMDPQYFPQPRKFLPERFSPENRKLHTPYTYMPFGLGPHGCIGERFGYLQAKVGLVNLLRNHMITTSERTPHRMQLDPKAIITQAKGGIHLRLVRDALGV
Protein: Dihydrofolate reductase (EC 1.5.1.3) (O85255)
Organism: Streptococcus pneumoniae
Interaction partners:
Sequence:
MTKKIVAIWAQDEEGVIGKDNRLPWYLPAELQHFKETTLNHAILMGRVTFDGIGRRLLPQRETLILTRNSEEKIDGVTTFQDVQSVLDWYQAQEKNLYILGGKQIFQAFEPYLDEVIVTQIHARVEGDTYFPEEFDLSLFETVSSKSYTKDEKNPYDFTIQYRKRKEV
Protein: Dolicholphosphate-mannose synthase (Q38BD1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- ESCRT-II complex subunit VPS22
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 28 homolog
- Uncharacterized protein
- Uncharacterized protein
- SB domain-containing protein
- Class-E vacuolar protein-sorting protein 24
- Vesicular protein trafficking mediator, putative
- Uncharacterized protein
Sequence:
MSKEPGHWDFFKLPPFFTLQPSPSALERQMALWGNLVMDHAAFHAQHRKRDTCPLLRLYSCNSGLFRNETINRRLRPEDVKKVISSLVAQWSEHCVLTSDGDGMGDVSVLVTTSKGGLKELEQSLLAWILERGAGTTVAYLSQKGVVMTFDELVDGQCLLYSRESEQLLPRLTQEAVPIEDVGALSQEQAVRCFLHTLAERPVSHKGLFSVTLFNLDGSDRRPYEGVKFGGAAI
Protein: F12K11.19 (Q9SHJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNLSPLDAGSLPSPLTSRQPVTIPPPPHLSSPWYSPSLFVSRFLICKPRPQGSDGFRIRLSNCSSSLNTVIQRCDNKISFARQASSEQGFFMRPASPDDVLENLGMNLKNTVVRRGDNRLYFARQASSAQGFFMRQASTNERTIPHDAAASTKFSATKTTGFDSSSPAYAAPHFSKPAKEDIFFPSLSPNLQKERPKLDLPKLANLGTVWSPRSNVAESTHSYVVAIELPGASINDIRVEVDNTNLTVTGRRTSICQKVDAGTKASILGYHKQEILQGPFKVSWPLPSNVNKDNVSAEFM
Protein: E3 ubiquitin-protein ligase SlrP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SlrP) (Secreted effector protein SlrP) (Q8ZQQ2)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death.
Subcellular location: Secreted {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS), and delivered into the host cytoplasm. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase SopA
- Secreted effector protein SptP
- Thioredoxin 1
- Secreted effector protein SopD
- Guanine nucleotide exchange factor sopE2
- Inner membrane protein
- Secreted effector protein PipB2
- Secreted effector protein SifA
- Secretion system effector
- Secreted effector protein SifB
Sequence:
MFNITNIQSTARHQSISNEASTEVPLKEEIWNKISAFFSSEHQVEAQNCIAYLCHPPETASPEEIKSKFECLRMLAFPAYADNIQYSRGGADQYCILSENSQEILSIVFNTEGYTVEGGGKSVTYTRVTESEQASSASGSKDAVNYELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLKILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPPELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENLPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNPFSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLHQAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDTQNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISCEDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIFRLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTTMTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALWGPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELEDLRIADDSDAERTTEVQMDAERAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYWR
Protein: Uncharacterized protein Rv2205c (P9WMT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable aldehyde dehydrogenase NAD dependent AldA
- Aldehyde dehydrogenase
- Probable aldehyde dehydrogenase
- aldehyde dehydrogenase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Protein Rv2204c
- Uncharacterized protein Rv2206
- Adenosylcobinamide-GDP ribazoletransferase
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
Sequence:
MKGSQASDDATGSLGPGRLQLPAMRVLVAPDCYGDSLSAVEAAAAIATGWTRSRPGDSFIVAPQSDGGPGFVEVLGSRLGETRRLRVCGPLNTVVNAAWVFDPGSATAYLECAQACGLGLLGGPPTPETALAAHSKGVGQLIAAALRAGAARIVVGLGGSACTDGGKGMIAELGGLDAARRQLADVEVIAASDVEYPLLGPWGTARVFAPQKGADMATVAVLEGRLAAWAIELDAAAGRGVSAEPGAGAAGGIGAGLLAVGGRYQSGAAIIAEHTHFADDLADAELIVTGEGRFDEQSLHGKVVGAIAAAARPLAIPVIVLAGQVSLDKSALRSAGIMAALSIAEYAGSVRLALADAANQLMGLASQVAARLGNSGPSGYR
Protein: Pyridoxine 5'-phosphate synthase (PNP synthase) (EC 2.6.99.2) (P0A794)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Subcellular location: Cytoplasm.
Interaction partners:
- 4-hydroxythreonine-4-phosphate dehydrogenase
- Pyridoxine/pyridoxamine 5'-phosphate oxidase
- Holo-[acyl-carrier-protein] synthase
- DNA repair protein RecO
- Pyridoxine/pyridoxal/pyridoxamine kinase
- Pyridoxal kinase PdxY
- GTPase Era
- Ribonuclease 3
- RNA polymerase sigma factor FliA
- Erythronate-4-phosphate dehydrogenase
Sequence:
MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRILRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDACKRLADAGIQVSLFIDADEEQIKAAAEVGAPFIEIHTGCYADAKTDAEQAQELARIAKAATFAASLGLKVNAGHGLTYHNVKAIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLEARG
Protein: 5,6-dihydroxyindole-2-carboxylic acid oxidase (Tyrosinase-related protein 1) (Q6DGE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Melanosome membrane {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004573}.
Interaction partners:
- Oculocutaneous albinism II.
- Melanocyte-stimulating hormone receptor
- Melanocyte inducing transcription factor a isoform 1
- Melanocyte-inducing transcription factor b
- Premelanosome protein a.
- Dopachrome tautomerase.
- Sodium/potassium/calcium exchanger 5
- Solute carrier family 45 member 2.
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Agouti-signaling protein
Sequence:
MWKSVCLVLMCVVVTRAQFPRQCMTPEGLRSGTCCPSPTGLANDECGSISGRGQCVSITADRRPHGPQYPHDGRDDRERWPLRFFNRTCQCNGNFTGFNCGRCRHGLTGPNCDQRITVVRRNIMQMSADEKRAFVNALDQAKRTVHPDLVICTRRFQEILSPDGASVQVENITIYNYFVWTHYYSVSKTYMGPGQQSFGGVDFSHEGPGFVTWHRYHLLQLERDMQDMLGDPSFALPYWNFAIGGSECDICTDDLIGARSSFDTNGISSNSVFSQWRVICESVEEYETLGTICNNTESSPIRRNPAGNVARPMVQRLPEPQDVIDCLELNTFDTPPYYSTSSQSFRNTIEGYSAPQGNYDPVVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAIFDEWLQRHTAAGTLAYPEENAPIGHNREFNMVPFWPPIRNAEMFVSAPDNLGYTYEVQWPTRAYTISEIITIAIVAVVLVVAVVGGVIGCAVRARSYRSAEGLEPLLGEQFRRYSEDERHASQSVV