wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VJ90)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein chiffon
- DNA replication licensing factor Mcm5
- DNA replication licensing factor MCM4
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm2
- DNA replication licensing factor Mcm6
- DNA replication licensing factor Mcm7
- Serine/threonine-protein kinase ATR
- Ovarian-specific serine/threonine-protein kinase Lok
- non-specific serine/threonine protein kinase Cdc7
Sequence:
MDKKEVQHHRSQQAMTKSLYAIGMGLLGKSATNMDCANTNLESAGKSSSTNYNRNRFYNERFVPMASGTMPSVSGTNHHSRHQQLLLQQAPKCTADLNEKLVKINRQNANKELSTIQAKDMQSVDKNEEALKELQESIPEINKIFDVHCRIGSGTFSTVLLGTLQRERGLVETQRRRFAIKHHNPTNHPERILRELECMYRIGGVENVIGINCCIRYNDNVAFIMPYMTHDRFHDIYRSLNFPEIRDYLRNLLIALRHVHKFNVIHRDVKPSNILYNRRTGKFLLCDFGLAQRIADDGSVVQSSDLSSREVFSILRDLENGRSVTLTDGNSAQAEAEDYMARRRMRALGGGGSVERAVTGPPSIQKLREQAGGHLTKKDVANQRADTMRLLNRLRLVSPNADPNNYVVSTNTSKKEMHASRAGTPGYRPPEVLLRYPKQSTAVDVWAAGVIMLSLLSGLHPFFKAPHDCGALAEIINLFGDMPVRKTAFLLDRLILLAQKVNTLDLRRVCMRFRHADFFLAPEIQRKYQRPDGTTEMCRSCEQPTFNCLCSNSGHNLERYDGLDIFPAVAYDLLSRLLEVNPQKRITAEEALKHPFFSDQHRITPGIPLHQQQLIMHQQQHIMQHQQHLQRSRETLPSSAARTLKAFVCYPMEITSTASQAAGNI
Protein: Photoreceptor ankyrin repeat protein (Ankyrin repeat domain-containing protein 33) (Q8BXP5)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional repressor for CRX-activated photoreceptor gene regulation.
Subcellular location: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:20026326}. Nucleus {ECO:0000269|PubMed:20026326}.
Interaction partners:
Sequence:
MSEALPFPSNKTSTPECNLKTLYWACVHNDLAELQARLDAGVSPEEASQVDSNGRTGLMVACYHGFGSIVALLSCCPFLDVNQQDKDGNTALMLAAQAGHMSLVTLLLNYFAGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSVDPVRGKTALEWAVLTDSFDTAQKIRQLLRRPQAEQLSLHYQPEWPALAQLVAQAQAQAQAPAAPSLLERLQATLSLSFAQSPQEGGVLDHLVTVTTSLASPFLSTACHTLCPDHPPKLGTRGKSVPELLGTAPPPPPEPHPPQQVPVPQVFAPNQSPQSMFSQWLQSRDSTRSQVPKILLSKAPSPSARYELTLRPQGQQSLAPPVWRFQERKKKEEETEPRGGGLGQAGGSK
Protein: HMG box protein, putative (AFU_orthologue AFUA_1G10040) (Q5BDW3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPLKLIRRGGSILRNFPGTGSLARPVRVFSPQHRVRCITFVARRSPISVTRGLPCSSSTVTTLARSYATHDGPSEEASSKSTKSTKTTKTKKTKKKAGKKPAVRKTRKVLTEEQKEARAQRRKAEELKETKRKLKAAALQTPKLLPTLPWVNAMKDKLSEVDKSDNPSPKEAFSRATELARRATPEERQRYVDQAAANKAANEAALKAWVDSHTPLQILEANNARRRLAQLQGKRRVSIIHDDRLVKPPTSAWIYFFMEKRDKNALVVSDMAQDVAVQWKNLPASEKAPYLEKANADRARYEREYLEVYGQPVPKLKGNKKSSKDE
Protein: Nuclear body protein SP140 (Lymphoid-restricted homolog of Sp100) (LYSp100) (Nuclear autoantigen Sp-140) (Speckled 140 kDa) (Q13342)
Organism: Homo sapiens (Human)
Function: Component of the nuclear body, also known as nuclear domain 10, PML oncogenic domain, and KR body. May be involved in the pathogenesis of acute promyelocytic leukemia and viral infection. May play a role in chromatin-mediated regulation of gene expression although it does not bind to histone H3 tails.
Subcellular location: Nucleus {ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Nucleus, PML body {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Cytoplasm {ECO:0000269|PubMed:8695863}. Note=Localized to nuclear structures termed LANDS, for LYSp100-associated nuclear domains. LANDS are globular, electron-dense structures most often found in the nucleoplasm, but also found at the nuclear membrane and in the cytoplasm, suggesting that these structures may traffic between the cytoplasm and the nucleus (PubMed:8695863). Also colocalizes with PML in a subset of PML nuclear bodies (PubMed:8910577). {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}.
Interaction partners:
- Nuclear body protein SP140-like protein
- Immunoglobulin kappa variable 1-33
Sequence:
MAQQGQQGQMASGDSNLNFRMVAEIQNVEGQNLQEQVCPEPIFRFFRENKVEIASAITRPFPFLMGLRDRSFISEQMYEHFQEAFRNLVPVTRVMYCVLSELEKTFGWSHLEALFSRINLMAYPDLNEIYRSFQNVCYEHSPLQMNNVNDLEDRPRLLPYGKQENSNACHEMDDIAVPQEALSSSPRCEPGFSSESCEQLALPKAGGGDAEDAPSLLPGGGVSCKLAIQIDEGESEEMPKLLPYDTEVLESNGMIDAARTYSTAPGEKQGEEEGRNSPRKRNQDKEKYQESPEGRDKETFDLKTPQVTNEGEPEKGLCLLPGEGEEGSDDCSEMCDGEEPQEASSSLARCGSVSCLSAETFDLKTPQVTNEGEPEKELSLLPGEGEEGSDDCSEMCDGEERQEASSSLARRGSVSSELENHPMNEEGESEELASSLLYDNVPGAEQSAYENEKCSCVMCFSEEVPGSPEARTESDQACGTMDTVDIANNSTLGKPKRKRRKKRGHGWSRMRMRRQENSQQNDNSKADGQVVSSEKKANVNLKDLSKIRGRKRGKPGTRFTQSDRAAQKRVRSRASRKHKDETVDFKAPLLPVTCGGVKGILHKKKLQQGILVKCIQTEDGKWFTPTEFEIKGGHARSKNWRLSVRCGGWPLRWLMENGFLPDPPRIRYRKKKRILKSQNNSSVDPCMRNLDECEVCRDGGELFCCDTCSRVFHEDCHIPPVEAERTPWNCIFCRMKESPGSQQCCQESEVLERQMCPEEQLKCEFLLLKVYCCSESSFFAKIPYYYYIREACQGLKEPMWLDKIKKRLNEHGYPQVEGFVQDMRLIFQNHRASYKYKDFGQMGFRLEAEFEKNFKEVFAIQETNGNN
Protein: Copper transporter 2 (AtCOPT2) (Q9STG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the transport of copper.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Squamosa promoter-binding-like protein 7
- Ferric reduction oxidase 5
- Ferric reduction oxidase 4
- Zinc transporter 2
- Fe
- Metal-nicotianamine transporter YSL2
- Probable copper-transporting ATPase HMA5
- Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic
- Ferric reduction oxidase 2
- Ferric reduction oxidase 3, mitochondrial
Sequence:
MDHDHMHDMPPPSPSSSSMSNHTTPHMMMMHMTFFWGKNTEVLFSGWPGTSSGMYALCLIVIFLLAVIAEWLAHSPILRVSGSTNRAAGLAQTAVYTLKTGLSYLVMLAVMSFNAGVFIVAIAGYGVGFFLFGSTTFKKPSDDQKTAELLPPSSGCVC
Protein: ADP-ribose glycohydrolase MACROD2 (MACRO domain-containing protein 2) (O-acetyl-ADP-ribose deacetylase MACROD2) (EC 3.5.1.-) ([Protein ADP-ribosylaspartate] hydrolase MACROD2) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD2) (EC 3.2.2.-) (A1Z1Q3)
Organism: Homo sapiens (Human)
Function: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}.
Interaction partners:
- Leucine-rich repeat transmembrane protein FLRT3
- ADP-ribose glycohydrolase OARD1
- ADP-ribosylhydrolase ARH3
- Poly
- Protein mono-ADP-ribosyltransferase PARP10
Sequence:
MYPSNKKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEENTQETSQVKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGCDTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNIRSVAFPCISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMNEFFSVDDNNEEEEDVEMKEDSDENGPEEKQSVEEMEEQSQDADGVNTVTVPGPASEEAVEDCKDEDFAKDENITKGGEVTDHSVRDQDHPDGQENDSTKNEIKIETESQSSYMETEELSSNQEDAVIVEQPEVIPLTEDQEEKEGEKAPGEDTPRMPGKSEGSSDLENTPGPDAGAQDEAKEQRNGTK
Protein: Protein-glucosylgalactosylhydroxylysine glucosidase (EC 3.2.1.107) (Acid trehalase-like protein 1) (Q32M88)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins.
Interaction partners:
- Pseudouridine-5'-phosphatase
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- Galactose mutarotase
- N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1
Sequence:
MEDAGEDPTTFAAHSLPSDPRLLATVTNAYLGTRVFHDTLHVSGVYNGAGGDTHRAMLPSPLNVRLEAPAGMGEQLTETFALDTNTGSFLHTLEGPRFRASQCIYAHRTLPHVLAFRVSIARLAPGSGPITLLLRSAFSPESPDLDLHQGPDFQGARYLYGHTLTPEQPGGPQQEVHMLWTPAPPDLTLGEGEEARTWDFLTAVGGSQAEAQACLTEALQLQARGALYTAHAQAWAQLWVECGLDVVGPLQLRQALRGSLYYLLSALPQPKAPGYICHGLSPGGLSNGSREECYWGHVFWDQDLWMFPSILMFHPEAARAILEYRIRTLDGALENAQNLGYQGAKFAWESADSGLEVCPEDIYGVQEVHVNGAVVLAFELYYHTTQDLQLFREAGGWDVVRAVAEFWCSRVEWSPREEKYHLRGVMSPDEYHSGVNNSVYTNVLVQNSLRFAAALAQDLGLPIPSQWLAVADKIKVPFDVEQNFHPEFDGYEPGEVVKQADVVLLGYPVPFSLSPDVRRKNLEIYEAVTSPQGPAMTWSMFAVGWMELKDAVRARGLLDRSFANMAEPFKVWTENADGSGAVNFLTGMGGFLQAVVFGCTGFRVTRAGVTFDPVCLSGISRVSVSGIFYQGNKLNFSFSEDSVTVEVTARAGPWAPHLEAELWPSQSRLSLLPGHKVSFPRSAGRIQMSPPKLPGSSSSEFPGRTFSDVRDPLQSPLWVTLGSSSPTESLTVDPASE
Protein: Pyridoxal dependent decarboxylase domain containing 1 (H3BNL6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKNLKEAVKMLEDSQRRTEEENGKKLISGDIPGPLQGSGQDMVSILQLVQNLMHGDEDEEPQSPRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSDTTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSRYEDFVVDGFNVLYNKKPVIYLSAAARPGLGQYLCNQDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPGPWLGLPAVP
Protein: Actin-binding LIM protein 1 (A0A8I6GGU3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVKEKVAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEATCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQDRQSLGESPRTLSPTPSAEGFQDGRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPDQGINIYRKPPIYKQHDAAALAAQNKASEDIIKFSKFPAAQAPDPNEIPKIETDHWPGPPSLAAIGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKENRERASLLASRYDSPLHSASHAPSSKTSSLPGYGKSGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF
Protein: Phospholipid phosphatase-related protein type 3 (Inactive phospholipid phosphatase PLPPR3) (Lipid phosphate phosphatase-related protein type 3) (Plasticity-related gene 2 protein) (PRG-2) (Q7TPB0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLAMKEKNKTPKDSMTLLPCFYFVELPIVASSIVSLYFLELTDLFKPAKVGFQCYDRALSMPYVETNEELIPLLMLLSLAFAAPAASIMVGEGMVYCLQSRLWGRGPGGVEGSINAGGCNFNSFLRRTVRFVGVHVFGLCATALVTDVIQLATGYHTPFFLTVCKPNYTLLGTSCESNPYITQDICSGHDTHAILSARKTFPSQHATLSAFAAVYVSMYFNAVISDTTKLLKPILVFAFAIAAGVCGLTQITQYRSHPVDVYAGFLIGAGIAAYLACHAVGNFQAPPAEKVPTPAPAKDALRALTQRGHESMYQQNKSVSTDELGPPGRLEGVPRPVAREKTSLGSLKRASVDVDLLAPRSPMGKEGMVTFSNTLPRVSTPSLDDPARRHMTIHVPLDASRSRQLIGEWKQKSLEGRGLGLPDEASPVHLRAPAEQVAEEEEEEEEEEEEEEEEEEEEGPVPPSLYPTVQARPGLGPRVILPPRPGPQPLVHIPEEGVQAGAGLSPKSSSSSVRAKWLSVAEKGGGPVAVAPSQPRVANPPRLLQVIAMSKAAGGPKAETASSSSASSDSSQYRSPSDRDSASIVTIDAHAPHHPVVHLSAGSTPWEWKAKVVEGEGSYELGDLARGFRSSCKQPGMGPGSPVSDVDQEEPRFGAVATVNLATGEGLPPPGASEGALGAGSRESTLRRQVGGLAEREVEAEAESYYRRMQARRYQD
Protein: Uncharacterized protein (A0A1D8PGJ9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- Zinc finger CHCC-type domain-containing protein
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM17
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 5
Sequence:
MKFTFKFPISTLFKYKPQKFNFGLEQEIRSKLNSLPSVTKIYTNPDGSPRVPTDEEFKTIAELQNLYYKRNYSEWNWILPGIPKDQLQLFKDNSQDLTHFGFVSKDSGKIIDKIPYKDASTGELKWKIIRETSKAEGWEIPYFYIVLPVFAYIFYVKYTQQTKLRELEGPDWAEKELRLRAMEDYFHGDTAKAKEFLSNEGKSKREIQDRDDLVVARILAGDYDKLAELKKKLPKDLIKTEEDPVFKY
Protein: Peroxiredoxin-5, mitochondrial (EC 1.11.1.24) (Antioxidant enzyme B166) (AOEB166) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (Thioredoxin peroxidase PMP20) (Thioredoxin-dependent peroxiredoxin 5) (Q9R063)
Organism: Rattus norvegicus (Rat)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P30044}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix {ECO:0000250|UniProtKB:P30044}.
Interaction partners:
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Thioredoxin
- Thioredoxin, mitochondrial
- Peroxiredoxin-2
- Peroxiredoxin-4
- Peroxiredoxin-1
- Superoxide dismutase, mitochondrial
- Peroxiredoxin-6
- Glutathione reductase
- Thioredoxin domain-containing protein 3
Sequence:
MVQLRFCVLGSIAGSVLRASATWTCVAGRAGRKGAGWECGGARSFSSAAVTMAPIKVGDTIPSVEVFEGEPGKKVNLAELFKDKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDAFVTAEWGRAHQAEGKVQLLADPTGAFGKETDLLLDDSLVSLFGNRRLKRFSMVIDKGVVKALNVEPDGTGLTCSLAPNILSQL
Protein: ATP-sensitive inward rectifier potassium channel 10 (Inward rectifier K(+) channel Kir4.1) (Potassium channel, inwardly rectifying subfamily J member 10) (Q9JM63)
Organism: Mus musculus (Mouse)
Function: May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P78508}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P78508}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78508}. Note=In kidney distal convoluted tubules, located in the basolateral membrane where it colocalizes with KCNJ16 (PubMed:33811157). {ECO:0000250|UniProtKB:P78508, ECO:0000269|PubMed:33811157}.
Interaction partners:
- Inward rectifier potassium channel 16
- Aquaporin-4
- Dystrophin
- Caveolin-1
- Pendrin
- Hepatic and glial cell adhesion molecule
- Excitatory amino acid transporter 2
- Disks large homolog 4
- Gap junction beta-6 protein
- Excitatory amino acid transporter 1
Sequence:
MTSVAKVYYSQTTQTESRPLVAPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELGPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38G45)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MIYIVLLALFALPKAVSPAANQNAAEYRALCDLIALKESISTLTEPTADTAVTDIVNDIEMLNISTATDSFIADRDGELKETESGVKKSEKEAWQEKIKKLDQETGEPKTVKYKRLKDKTTRGPANQNINKLLQRAQQLKIAYEQQISEAKSKKTAITTSIKNAIYGKGQEDFQEKALDTNDAKNNCGKAAGSENVGQSLSNDLVCLCIPDQGANGNDLCEHGLQPTAVAVANRGSQTTPQYTTMVNGCKLQHRKRQLTPYLIIQRLAAFDSLLGRQAQTATTAAATRTLGKPHSDGNCDNSATQGMCVNYKQQIETATTGIPWVAQLTQAAHDLTAMNKATEHAAAIKTQLESIQASAWAVYAAAVNTELNQRHPKQNEQPIQATTVNDNKCKPTNATPAECPSDHCVYDDKATDGNKCKPKPGTETTAAAGTGETPKEGAAATGCVAHKDKTTCENDKTGDKQNCAWRRGKDSEPDREKEMCLDSSSLVNKKLDLMAAAFVSLVKF
Protein: Lactose phosphotransferase system repressor (A0A0H2USI3)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MIKDERVLELIEIIKKKKRIAVKELAEITFSSTSTLRRDLIFLENQGLIKRKHGYVTLSSMNTIELSHQIREGESTRQKRLIASLAKDFIRSGMCIYLDSSTTVYELCPYLSELDNLIIFTNGLHTAQTLSETVKDSSKIFITSGEVKHQSCSVVNYDKENSLLDHFNIDLAFCSARGIDDQYVYEASLSQAISKKNIIDKAHETILLIDSSKFYKTGFFKINPLSKYTTFISDTVPDQKLLDAVELFDGEWVSDIQ
Protein: Proton myo-inositol cotransporter hmit-1.2 (H(+)-myo-inositol cotransporter hmit-1.2) (H(+)-myo-inositol symporter hmit-1.2) (Q9XXQ9)
Organism: Caenorhabditis elegans
Function: H(+)-myo-inositol cotransporter (By similarity). Probably by promoting the transport of myo-inositol regulates intracellular osmosis in response to hyperosmotic stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21679696}; Multi-pass membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:21679696}. Note=Localizes to the lumenal side of intestinal cells (PubMed:21679696). Localizes to the endfoot region of glial cells where the cilia of sensory neurons are embedded (PubMed:21679696). In the excretory canal cell, localizes to the basal membrane of the distal canal and at the lumenal membrane of the proximal canal (PubMed:21679696). {ECO:0000269|PubMed:21679696}.
Interaction partners:
- MAM domain-containing protein
- Col_cuticle_N domain-containing protein
- Col_cuticle_N domain-containing protein
- Minor capsid protein
- ShKT domain-containing protein
Sequence:
MVAVEFKVSESGRPRPEKNPKLGFFVYLLGSAAIIGGFLFGYDTSVVSAAMLYVPEAPGLKPMGTVWKEVIVSITPGMAAVGAWFSGAGSDRYGRKPIIIGSTLIFVCGAVICAVAWTKIVMLIGRIFLGVGIGFASMVVPVYLGEASPTHVRGTLVSAFAMMISFGQVVANIMGGVFSYWEPYTIGWRLMFAFAGIPALIQFVCFIFLPETPRWLYENGHTEQAEQVLEKIYGGNTEWIEYELAEIKTYAEERQKQMEEEKKSGPVIWRILKTPHVLKACFIGSMLQAFQQLAGINTILYYTADIIRSAGIENYHTIIWISVILSICNLIGPFAPMFFIEKLGRRKLFLFSCAGVVVSLVLIGVSFLLVGNDSAPNFDRSAYLLAGNYQSNGEAESCLMLSNCDSCVTSEHCGFCEDSETRTGFCLPVDHNDVTLYSSTGLCTNGLDKSNSSFPNATSYVWQKHHCTTSYTILPIVMMGVYLLTFSCGFTSLPWVLNSEFYPMWARSTCVSISTLSNWVFNLIIALTYLSLTHAITKYGAFWLYAIFTIIAFIFIYFLVPETTGYSIDEVEMLFMNKRQRNIAMQARQAKLDAASDKDKNSSTSLSTETITM
Protein: Homeobox-leucine zipper protein ATHB-9 (HD-ZIP protein ATHB-9) (Homeodomain transcription factor ATHB-9) (Protein PHAVOLUTA) (O04292)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the determination of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf fates. Binds to the DNA sequence 5'-GTAAT[GC]ATTAC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein LITTLE ZIPPER 3
Sequence:
MMAHHSMDDRDSPDKGFDSGKYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECPILCNIEPRQIKVWFQNRRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYENGFMKHRIHTASGTTTDNSCESVVVSGQQRQQQNPTHQHPQRDVNNPANLLSIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCSGIAARACGLVSLEPMKVAEILKDRPSWFRDCRCVETLNVIPTGNGGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLTSATGGPNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQIAQETSGEVQYSGGRQPAVLRTFSQRLCRGFNDAVNGFVDDGWSPMSSDGGEDITIMINSSSAKFAGSQYGSSFLPSFGSGVLCAKASMLLQNVPPLVLIRFLREHRAEWADYGVDAYSAASLRATPYAVPCVRTGGFPSNQVILPLAQTLEHEEFLEVVRLGGHAYSPEDMGLSRDMYLLQLCSGVDENVVGGCAQLVFAPIDESFADDAPLLPSGFRVIPLDQKTNPNDHQSASRTRDLASSLDGSTKTDSETNSRLVLTIAFQFTFDNHSRDNVATMARQYVRNVVGSIQRVALAITPRPGSMQLPTSPEALTLVRWITRSYSIHTGADLFGADSQSCGGDTLLKQLWDHSDAILCCSLKTNASPVFTFANQAGLDMLETTLVALQDIMLDKTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSFV
Protein: P antigen family member 5 (PAGE-5) (Cancer/testis antigen 16.1) (CT16.1) (G antigen family E member 1) (Prostate-associated gene 5 protein) (Q96GU1)
Organism: Homo sapiens (Human)
Interaction partners:
- Probable threonine protease PRSS50
- Sarcoma antigen 1
- Melanoma-associated antigen C2
- Sperm surface protein Sp17
Sequence:
MQAPWAGNRGWAGTREEVRDMSEHVTRSQSSERGNDQESSQPVGPVIVQQPTEEKRQEEEPPTDNQGIAPSGEIKNEGAPAVQGTDVEAFQQELALLKIEDAPGDGPDVREGTLPTFDPTKVLEAGEGQL
Protein: Spermidine/putrescine transport system permease protein PotC (P0AFK6)
Organism: Escherichia coli (strain K12)
Function: Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Spermidine/putrescine-binding periplasmic protein
- Putrescine transport system permease protein PotH
- Spermidine/putrescine transport system permease protein PotB
- Spermidine/putrescine import ATP-binding protein PotA
- Putrescine-binding periplasmic protein PotF
- Putrescine transport ATP-binding protein PotG
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- Maltose/maltodextrin import ATP-binding protein MalK
- Iron
- Uncharacterized ABC transporter ATP-binding protein YdcT
Sequence:
MIGRLLRGGFMTAIYAYLYIPIIILIVNSFNSSRFGINWQGFTTKWYSLLMNNDSLLQAAQHSLTMAVFSATFATLIGSLTAVALYRYRFRGKPFVSGMLFVVMMSPDIVMAISLLVLFMLLGIQLGFWSLLFSHITFCLPFVVVTVYSRLKGFDVRMLEAAKDLGASEFTILRKIILPLAMPAVAAGWVLSFTLSMDDVVVSSFVTGPSYEILPLKIYSMVKVGVSPEVNALATILLVLSLVMVIASQLIARDKTKGNTGDVK
Protein: RING finger protein B (Protein rngB) (Q7M3S9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8647262}.
Interaction partners:
- Cysteine proteinase 4
Sequence:
MKIDCKRVSLIGSPEPRWGHTGTTLPNGSGFIVFGGNSNRAFNDIQYYNIFNNSWSKIEAVGNAPSERYGHSAVLYQSQSRPYSDSYQIIFFGGRATSKPFSDINILYVNSNRSFIWKQVTTKSIEGRAGHTAVVYRQNLVVFGGHNNHKSKYYNSVLLFSLESNEWRQQVCGGVIPSARATHSTFQVNNNKMFIFGGYDGKKYYNDIYYLDLETWIWKKVEAKGTPPKPRSGHSATMIQNNKLMIFGGCGSDSNFLNDIHILHIEGANEYRWEQPSYLGLEIPQARFRHTTNFIGGRVYIYAGTGSGNLMGDLHTLEFLDDNNTPLIPITISIPITNSNSIVGSPNTSISCGVSNSGASSSSGGGISGHPSILSSSSSSSYLSTSPLSTSSLASSYQSSQSLQFNQNQNQNNNNNNNNNNNNNIQTTTTTTTNNNNNNNNNNNNNNNNNNVESNQQQQQIQHQTSPMSVLSRSNSNISLNSLNSSSSSILSTPSTLSTTTTTTTTSHASHTSHTSNRSNGSRGGIPSIPPFNGRSSNHNNNNNSNSNNYNNHQQTKTNSAEELILEELKSLNIYDQAACNKDFQTNLKRVEELFNQKIKHEQKYRQSLEEKLGKANHQVSLLTNQIQSIIQKDELTSLKKEYSELKKKHSLLYSEDIDDLPTETCLKLEEIHVKSLEKLRVKKLPSSNQLSTLQQQIPQQPTTIICNNSQIIQQQPLPPLQQQQQQQQQQQQQQQQQQQPLEIQEQLTMLQLQLSQLSQQQQNQIDKQQKQEKLQQEQQQQQLKNINRLSISSNSSTLSSKDSFYFESKIQELSNQLKEKQQAITDRDNKIKDFENQLNKYKLIGLDSLDHYQLLELESSFHNGLKQIGSIKDQRYLNRLVSLEKEKDQLKDQNSCVICASNPPNIVLLPCRHSSLCSDCCSKLTKCPICRSHIENKISIYQ
Protein: Pectate lyase plyB (EC 4.2.2.2) (Q00645)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pectinesterase A
- Probable endopolygalacturonase D
Sequence:
MRFTPLFLLAAVAIASPAPDLNARHELTRRQASESCPIGYCTQNGGTTGGAAGDTVTVTNLADLTEAAESDGPLTIIVSGSISGSAKIRVASDKTIFGESGSSITGIGFYIRRVSNVIMRNLKISKVDADNGDAIGIDASSNVWVDHCDLSGDLSGGKDDLDGLVDISHGAEWITVSNTYFHDHWKGSLIGHSDNNEDEDLGHLHVTYANNYWYNVYSRTPLIRFATVHIINNYWDSLIDTGVNCRMDAQVLIQSSAFHNCPDRAIFFADSDYTGYAVVDDVDLGGSSNSVPEGTLTPSSLPYAAITALGSGQVASVIPGTAGQKL
Protein: Acetylcholine receptor beta subunit (Q6S3I0)
Organism: Torpedo marmorata (Marbled electric ray)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MEDVRRMALGLVVMMALALSGVGASVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLTLTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVILQHALDAKGEREVKEIMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLSVPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFLDASHNVPPDNPFA