wanglab/gogpt-training-data huggingface dataset:
Protein: TF protein (A0PJA6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKKKKKKKKK
Protein: Carboxypeptidase D (EC 3.4.17.22) (CPD-2) (Metallocarboxypeptidase D) (P83852)
Organism: Lophonetta specularioides (Crested duck) (Anas specularioides)
Interaction partners:
Sequence:
QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGIHEAGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQVTDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSKSPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVHRGIWGFVLDATDGRGILNATISVADINHPVTTYKDGDYWRLLVQGTYKVTASARGYDPVTKTVEVDSKGGVQVNFTLSRT
Protein: Urocortin-2 (Urocortin II) (Ucn II) (Q91WW1)
Organism: Rattus norvegicus (Rat)
Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 2
- Corticotropin-releasing factor receptor 1
- Urocortin
- Urocortin 3.
- Corticoliberin
- Corticotropin-releasing factor-binding protein
Sequence:
MTRWALVVFMVLMLDRVPGTPIPTFQLLPQNYPETTPSSVSSESPSDTTTGPSASWSNSKASPYLDTRVILSLDVPIGLLRILLEQARNKAARNQAATNAQILARVGRR
Protein: Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) (Q62622)
Organism: Rattus norvegicus (Rat)
Function: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60876}. Nucleus {ECO:0000250|UniProtKB:Q60876}. Note=Localization to the nucleus is unaffected by phosphorylation status. {ECO:0000250|UniProtKB:Q60876}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Serine/threonine-protein kinase mTOR
- Regulatory-associated protein of mTOR
- Target of rapamycin complex subunit LST8
- Eukaryotic translation initiation factor 4E type 2
- AKT1 substrate 1
- Mitogen-activated protein kinase 3
- GTP-binding protein Rheb
- Ribosomal protein S6 kinase beta-1
- Mitogen-activated protein kinase 1
Sequence:
MSAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPTIPGVTSPTSDEPPMQASQSHLHSSPEDKRAGGEESQFEMDI
Protein: Elongation factor 1-delta, putative (DUF936) (Q9SKA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable elongation factor 1-gamma 2
- Translationally controlled tumor protein 2
- Translationally-controlled tumor protein 1
- Large ribosomal subunit protein uL18y
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS1y
- Elongation factor 1-alpha 2
- Elongation factor 1-alpha 3
- G-type lectin S-receptor-like serine/threonine-protein kinase At1g61390
- Elongation factor 1-alpha 1
Sequence:
MASLTPGVLSNLLNIAAGNSPSSPPLLSSHRSPLLQVIEIVPCLSDDQWRSEAFFVKVSDSLHAAYVAVSTGDDADLIRSDEIQLGQFIYICGGLHVEKGCPVPVIRGLKPVPKRRMCVGNPSDLYSSDLLLPFTQVSVSPTTTKKKNLVETRRLSLDSARRSCWDQTPPVTRRRDAALLLSSPRLKSKLVLNDKSLLKIESPSKYFNCGTSPALRNKNVVKPGSPISMASSPKDGIKSPISKHLNCETPALRSRYVVKPASPISVTRSPKDGIKSLSKAVTPPVALFKVPSSHMTWSDQRMSWSGLPKTIQLLGKEVSSHRQVAVSAAVSALEEASAMESVLFSLQAFAELCDSTKKLSTGQVVARFLDIYHNTQNTCKAVHRLLTQNRNNGSCRLVVNKNATSWVQAAVVTGFSQFNLFKEPGKKGDAADHHYIVMQNSSEKLNPKETTSSRTPSYKGAKPPATKHCSVSDRSSLEGKSSLKDSTSLADELVQVSSQWFLKYLENSLNKGSFLVKTEETNGKESLLVHLKALNHWLDDLNLNRTETNEKVEDLRKKLQRFLLEHIESVIGDTYNMKRKIINSI
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (G4XH65)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV
Protein: Molybdenum-pterin binding domain protein/site-specific recombinase, phage integrase family (Q72E08)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
Sequence:
MEGSLETLFAGVASRANPAGMLTIPDEVRCLDTNDLEKLESAFRAWVAKGRGAGVTLARRRILALFLLLRHTGARLGEASGLEGRSLVLEKGLVRLGTPPRDVLVAETVLAEIVGLVTTGGGRESPVLPEYPFAVDPGHVRRKFYACAEAAGLGREMGSPSVLRRSRAVELLRGGVPLPAVQRLLGHGNAELTAAYVAVPDDAMRRMVGDALDREQRRSSARNAFFGRVEDVRIGDVQASVRLQTPTGLEVLAIITNDSLEALGLARGAYALAEVKAPWVVLQRGEHPRSSAGNVYPGEVVRVRKGAVSAEVIVRLDAGTEVCAVLAADTLATLELCDGAHVWVVINALSVILNAV
Protein: Uncharacterized protein YheO (P64624)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Sulfurtransferase TusD
- Protein TusC
- Protein TusB
Sequence:
MSRSLLTNETSELDLLDQRPFDQTDFDILKSYEAVVDGLAMLIGSHCEIVLHSLQDLKCSAIRIANGEHTGRKIGSPITDLALRMLHDMTGADSSVSKCYFTRAKSGVLMKSLTIAIRNREQRVIGLLCINMNLDVPFSQIMSTFVPPETPDVGSSVNFASSVEDLVTQTLEFTIEEVNADRNVSNNAKNRQIVLNLYEKGIFDIKDAINQVADRLNISKHTVYLYIRQFKSGDFQGQDK
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (Q76NM6)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. During the trophozoite stage, involved in the acidification of the extracellular space next to the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10915784}; Peripheral membrane protein {ECO:0000269|PubMed:10915784}; Cytoplasmic side {ECO:0000269|PubMed:10915784}. Vacuole {ECO:0000269|PubMed:10915784}. Vesicle {ECO:0000269|PubMed:10915784}.
Interaction partners:
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E, putative
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase 21 kDa proteolipid subunit, putative
- V-type proton ATPase subunit F
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit D, putative
- V-type proton ATPase subunit
- V-type proton ATPase subunit a, putative
- V-type proton ATPase subunit C
Sequence:
MTKVAVEKEEPGVVYKVAGSLVIAENMSGTRMYELAKVGWNKLVGEIIRLEGNYAYIQVYEDTSGLSVGDPVIKTGNALSVELGPGILDNIYDGIQRPLERIANVCGDVYIYKGIDMTSLDHDKQWQFYADKKLKLNDIVTGGDIFGFVDENKLFKEHKIMAPPNAKGRLTYIAPDGSYTLKDKIFELEYQGKKYTYGLSHLWPVRDPRPVLEKVTGDTLLLTGQRVLDSLFPTVQGGTCAIPGAFGCGKTCVSQALSKYSNSEVIIYVGCGERGNEMAEILSDFPELTTKVDNEDVGIMQRTCLVANTSNMPVAAREASIYTGITLCEYFRDMGYNATMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGKVKCIGSPSRIGSITIVGAVSPPGGDFSDPVTTATMSIVQAFWGLDKKLAQRKHFPSVNWSTSFSKYVRQLEQYFDNFDQDFLSLRQKISDILQQESDLNDIVQLVGKDSLSEDQKVVMEVAKIIREDFLQQNAFSDYDYMCPLQKTVGMMRIICHFYAQCLRTLQEYDSRERKIGWGSIYNTLRPTINKITHMKFENPKNSDEYFKKYFKALEEEITVGLRNLMEK
Protein: DNA gyrase inhibitor (P33012)
Organism: Escherichia coli (strain K12)
Function: Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell. Protects cells against the natural plasmid-encoded toxins microcin B17 (MccB17) and CcdB, and synthetic quinolones. Can also protect cells against alkylating agents that act independently of DNA gyrase, suggesting a more general role in protecting cells against DNA damage.
Subcellular location: Cytoplasm.
Interaction partners:
- Inner membrane protein YeeA
- Uncharacterized protein YbfE
- Putative acyl-CoA thioester hydrolase YbhC
Sequence:
MNYEIKQEEKRTVAGFHLVGPWEQTVKKGFEQLMMWVDSKNIVPKEWVAVYYDNPDETPAEKLRCDTVVTVPGYFTLPENSEGVILTEITGGQYAVAVARVVGDDFAKPWYQFFNSLLQDSAYEMLPKPCFEVYLNNGAEDGYWDIEMYVAVQPKHH
Protein: 9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic (LeNCED1) (SlNCED1) (EC 1.13.11.51) (Nine-cis-epoxycarotenoid dioxygenase 1) (O24023)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid (ABA) biosynthesis from carotenoids. Required for ABA accumulation upon drought (Ref.2). Required for ABA-mediated regulation of anther/pollen development, including metabolism, cell wall modification and transcription level. Positive regulator of fruit ripening involved in the biosynthesis of abscisic acid (ABA); initiates ABA biosynthesis at the onset of fruit ripening. Modulates the degree of pigmentation and carotenoid composition as well as pectin catabolism during ripening and may regulate the ethylene production and action in climacteric tomato fruit.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9LRR7}. Note=Partially bound to the thylakoid. {ECO:0000250|UniProtKB:Q9LRR7}.
Interaction partners:
- Neoxanthin synthase, chloroplastic
- Xanthoxin dehydrogenase
- Uncharacterized protein
- Zeaxanthin epoxidase, chloroplastic
- indole-3-acetaldehyde oxidase
- indole-3-acetaldehyde oxidase
- Abscisic acid 8'-hydroxylase CYP707A2
- indole-3-acetaldehyde oxidase
- Lycopene beta cyclase, chloroplastic
- Abscisic acid 8'-hydroxylase CYP707A1
Sequence:
MATTTSHATNTWIKTKLSMPSSKEFGFASNSISLLKNQHNRQSLNINSSLQAPPILHFPKQSSNYQTPKNNTISHPKQENNNSSSSSTSKWNLVQKAAAMALDAVESALTKHELEHPLPKTADPRVQISGNFAPVPENPVCQSLPVTGKIPKCVQGVYVRNGANPLFEPTAGHHFFDGDGMVHAVQFKNGSASYACRFTETERLVQEKALGRPVFPKAIGELHGHSGIARLMLFYARGLFGLVDHSKGTGVANAGLVYFNNRLLAMSEDDLPYHVKVTPTGDLKTEGRFDFDGQLKSTMIAHPKLDPVSGELFALSYDVIQKPYLKYFRFSKNGEKSNDVEIPVEDPTMMHDFAITENFVVIPDQQVVFKMSEMIRGGSPVVYDKNKVSRFGILDKYAKDGSDLKWVEVPDCFCFHLWNAWEEAETDEIVVIGSCMTPPDSIFNECDEGLKSVLSEIRLNLKTGKSTRKSIIENPDEQVNLEAGMVNRNKLGRKTEYAYLAIAEPWPKVSGFAKVNLFTGEVEKFIYGDNKYGGEPLFLPRDPNSKEEDDGYILAFVHDEKEWKSELQIVNAMSLKLEATVKLPSRVPYGFHGTFINANDLANQA
Protein: Pre-mRNA-splicing factor srp2 (P78814)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in pre-mRNA splicing where it is involved in spliceosome assembly.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Protein kinase dsk1
- Pre-mRNA-splicing factor srp1
- Uncharacterized RNA-binding protein C25G10.01
- U1 snRNP-associated protein usp107
- Splicing factor U2AF 59 kDa subunit
- Splicing factor U2AF 23 kDa subunit
- Uncharacterized protein C11G11.07
- Branchpoint-bridging protein
- Splicing factor 3B subunit 6-like protein
Sequence:
MSETRLFVGRIPPQATREDMMDFFKGYGQILDCKLMNGFGFVEVEDARDARDIVNDFQGKEFMGSRIVVEPARGERRRRENFRESAASKYPRPRRTGFRLIVENLSEDVSWQDLKDVMRKAGEPTFTDAHRENPGAGVVEFSTEEDMRNALTSLNGEVIKGQAVTLREDPDAANEPLPEVPSRFRSRSPPARRRYRDDYRRGGDYRRDAYRPGRDDERRYAPRGEYRRNNRDEYRRGGRDEYRRNSRSDYRRPHDDEYRRPRGDEYRPGRDEYRRSRDDGRPSHDDEYRRDAYSRSPSPRRDREENRSPAYEGSKSYSAAPEASMESSAPTESYDKPAASEEQQPLQNHSDVGNGSAEGQVAAEW
Protein: Echinoderm microtubule-associated protein-like elp-1 (O45487)
Organism: Caenorhabditis elegans
Function: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Elongator complex protein 4
- Microtubule-associated protein
- MITD1 C-terminal phospholipase D-like domain-containing protein
- Elongator complex protein 2
- Tubulin alpha-3 chain
- WD Repeat protein
- Serine/threonine-protein kinase zyg-8
- Protein maph-9
- Protein KATNIP homolog
- Elongator complex protein 3
Sequence:
MSISNGWSSSSIISDVLPEEEFEEVEEDELILNENDRLKFRVDELEKIVVAQRNEILLLQSSTVEILRRLQNLEIQDQSRSPTCSGYSSLPRRISGSKSSYTMSPSHAPPRSSHANSKSLYINGMNNNSEEVSPGPPRHRPPTRGSDGMVNVSVGKSARGSPMRKWVSTHDMKDTDRFRRLSTSSEASTSATMNPIVNSVRRLSTTHRQSSPSLLSLCSVISRSPSTSSILRKNNRTCQFSNGSGHLPIFIGGKTVQVPVPTGYENMDPTMDQDPPTMKVTLKHVYSYRGKDVRSNIEMLPTGELVFFSANLVVLMNITGEDRSQRIYHGHTCDVKCITLHPNKILVASGQSSCHSVEKFQKPEHTSPIDSPEDLVRQLEMEHTEAHVRIWDTIKLTTLMVLNGFEKGICHVAFSKTDSGSLLAVVDDSLKHLMSVWNWQKGKREGEVKASNDVVFECKWHPTIRNLIVLYGKGHFSFFNYDPATGVLVKTVATFEGRDKPKTVLSMCFGENDQVVTGDSNGTISIWDPRTCKTTKQAHSVHPGGVYSLTLAKSGKILSGGKDRMVSEWDLQDLVRTRRPIELPDEKGFPRVILQNGSELIIGTSSNTLLFGNIENSTNLTSLIEGDPGNLTFLLTCSSNQLITSSQCGTLRIWNHIDKKVEFSKKFIDSVECVDVDVTNTHIILGFAAGLWIVMNITKQQTIQEKKEGTAPITAVKFAPSGATFAVATKDPHLTIYRIDASKNLLVIARIHHIPAPIVALDFSSDSQYLRGQSIGAHLLFWTKAGEICDGTSVKDVKWGSSRVKIGFETALVAHSSNGQVTAVAQCEDISACGMENGTIRIYKNPVTSVTAGFVELLGHGRIIKSVAFSNKIQLFSCSPTDNSVFEWCLE
Protein: Autophagy and beclin 1 regulator 1 (F1LNQ2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Beclin 1-associated autophagy-related key regulator
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin-1
- Phosphoinositide 3-kinase regulatory subunit 4
- UV radiation resistance associated
- TNF receptor-associated factor 6
- Nuclear receptor-binding factor 2
- non-specific serine/threonine protein kinase
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase
Sequence:
MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTTVECCQHPGILCLCSRCAGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGNIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPNSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLNETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGTASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLLSEPGQLAERGLSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDSSNVGEAAGPSGEPRNR
Protein: Uncharacterized protein YjiX (P0ADC8)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Zinc chaperone YjiA
- Pyruvate/proton symporter BtsT
- Peptide transporter CstA
- Zinc chaperone YeiR
Sequence:
MFGNLGQAKKYLGQAAKMLIGIPDYDNYVEHMKTNHPDKPYMSYEEFFRERQNARYGGDGKGGMRCC
Protein: U3 small nucleolar RNA-associated protein 14 (U3 snoRNA-associated protein 14) (U three protein 14) (Q04500)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 15
- rRNA biogenesis protein RRP5
- Ribosome biogenesis protein BMS1
- Nucleolar protein 56
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 11
- Pre-rRNA-processing protein PNO1
- Nucleolar complex protein 4
- U3 small nucleolar RNA-associated protein 22
- Probable ATP-dependent RNA helicase DHR1
Sequence:
MAKKKSKSRSKSSRRVLDALQLAEREINGEFDNSSDNDKRHDARRNGTVVNLLKRSKGDTNSDEDDIDSESFEDEELNSDEALGSDDDYDILNSKFSQTIRDKKENANYQEEEDEGGYTSIDEEDLMPLSQVWDMDEKTAQSNGNDDEDASPQLKLQDTDISSESSSSEESESESEDDEEEEDPFDEISEDEEDIELNTITSKLIDETKSKAPKRLDTYGSGEANEYVLPSANAASGASGKLSLTDMMNVIDDRQVIENANLLKGKSSTYEVPLPQRIQQRHDRKAAYEISRQEVSKWNDIVQQNRRADHLIFPLNKPTEHNHASAFTRTQDVPQTELQEKVDQVLQESNLANPEKDSKFEELSTAKMTPEEMRKRTTEMRLMRELMFREERKARRLKKIKSKTYRKIKKKELMKNRELAAVSSDEDNEDHDIARAKERMTLKHKTNSKWAKDMIKHGMTNDAETREEMEEMLRQGERLKAKMLDRNSDDEEDGRVQTLSDVENEEKENIDSEALKSKLGKTGVMNMAFMKNGEAREREANKETLRQLRAVENGDDIKLFESDEEETNGENIQINKGRRIYTPGSLESNKDMNELNDHTRKENKVDESRSLENRLRAKNSGQSKNARTNAEGAIIVEEESDGEPLQDGQNNQQDEEAKDVNPWLANESDEEHTVKKQSSKVNVIDKDSSKNVKAMNKMEKAELKQKKKKKGKSNDDEDLLLTADDSTRLKIVDPYGGSDDEQGDNVFMFKQQDVIAEAFAGDDVVAEFQEEKKRVIDDEDDKEVDTTLPGWGEWAGAGSKPKNKKRKFIKKVKGVVNKDKRRDKNLQNVIINEKVNKKNLKYQSSAVPFPFENREQYERSLRMPIGQEWTSRASHQELIKPRIMTKPGQVIDPLKAPFK
Protein: Hemolymph clottable protein (Clotting protein) (CP) (P84913)
Organism: Penaeus paulensis (Pink shrimp) (Farfantepenaeus paulensis)
Function: Forms stable clots in the presence of calcium.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:16153866}.
Interaction partners:
Sequence:
LQPGLEYQYRYSARV
Protein: Glutathione S-transferase gliG (EC 2.5.1.18) (Gliotoxin biosynthesis protein G) (A4GYZ0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Interaction partners:
- O-methyltransferase gliM
- Cytochrome P450 monooxygenase gliC
- Thioredoxin reductase gliT
- Dipeptidase gliJ
- Nonribosomal peptide synthetase gliP
- Cytochrome P450 monooxygenase gliF
- Gamma-glutamyl cyclotransferase gliK
- N-methyltransferase gliN
Sequence:
MSERPSDLVVNRLVLFVVKGTATSTHNTVKPLILLEELGVPHDIYVVEKVSAPWFSEINPHKMVPAILDRSPDGRDTLRAWESTSTLMYIADAYDKDGTLGGRNVQERSEINNWLTLHTAALGPTAKYWLYFYKLHPEKLPKTIEKLRSNITVQYDILERRLNEPGQQYLALKDRPTIADIATLPFAMKSTAELFGLEFEKWPKLQEWSVRMGEREAVKRAWQRVAGFGHGEKEYGMLEA
Protein: Metalloprotease StcE (EC 3.4.24.-) (Mucinase) (Neutral zinc metalloprotease StcE) (Secreted protease of C1 esterase inhibitor from EHEC) (O82882)
Organism: Escherichia coli O157:H7
Function: Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes.
Subcellular location: Secreted {ECO:0000269|PubMed:12123444}. Note=Secreted via the etp type II secretion pathway.
Interaction partners:
Sequence:
MNTKMNERWRTPMKLKYLSCTILAPLAIGVFSATAADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAKDKEAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHEVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK
Protein: Large ribosomal subunit protein uL2cz/uL2cy (50S ribosomal protein L2, chloroplastic) (P0C495)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MAKHLYKTPIPSTRKGTIDRQVKSNPRNNLIHGRHRCGKGRNSRGIITARHRGGGHKRLYRKIDFRRNQKDISGRIVTIEYDPNRNAYICLIHYGDGEKGYILHPRGAIIGDTIVSGTKVPISMGNALPLTDMPLGTAIHNIEITRGRGGQLARAAGAVAKLIAKEGKSATLRLPSGEVRLVSQNCLATVGQVGNVGVNQKSLGRAGSKCWLGKRPVVRGVVMNPVDHPHGGGEGKAPIGRKKPTTPWGYPALGRRTRKRKKYSDSFILRRRK
Protein: Toxin coregulated pilus biosynthesis protein R (TCP pilus biosynthesis protein TcpR) (P0C6D5)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Involved in TCP pilus biogenesis.
Subcellular location: Cell membrane; Single-pass membrane protein.
Interaction partners:
- Toxin coregulated pilus biosynthesis protein T
- Toxin coregulated pilus biosynthesis protein D
- Toxin coregulated pilus biosynthesis protein Q
- Toxin coregulated pilus biosynthesis outer membrane protein C
- Toxin coregulated pilus biosynthesis protein S
- Toxin coregulated pilus biosynthesis protein E
- Toxin coregulated pilus biosynthesis protein B
- Toxin coregulated pilus biosynthesis protein F
Sequence:
MTSIWLHESDFRYVNLDVERYQKKYRLTLTNGNKYVFIKDKEDISDVNPFIPYILMEEGMNNVLVKSDDYKDILIYQGVNIQCLDFLNDNDISVEKLVDFETVELKADELNKIKARRLDAQLIEDEVKNNKVFIIGFIAIVIISIGVFWLM