wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 41 homolog (E7F590)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Late endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Early endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Lysosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P49754}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P49754}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49754}.
Interaction partners:
Sequence:
MAEVEEQGRKLSEESTDESEEEDTEEEPKLKYERLTNGVTEILQKDAASCMTVHDKFLALGTHFGKVFLLDIQGNVTQKFEISSVKINQISLDESGDHVGICSEDGKVQVFGLYTREGFHENFDCPIKVVALHPQFSKSNNKQFVTGGNKLLLYERNWLNRWKTSVLHEGEGNITSVKWRGNLIAWANNVGVKIYDIGSKQRITNVLRDNTSLRPDMYPCSLCWKDNTTLIIGWGCSVKICAVKERDPTEMRDLPSRYVEIVSAFETEFFISGLAPLADQLVTLYYVKENSDHMEEEFRTRPRLDIIQPLPEGCEEISSDALTVRNFQENQCRDYRLEHSEGESLFYIISPKDIVVAKERDQDDHIDWLLEKKKYEEALMAAEISFKNIKRHDVQKIGMAYINHLVEKGDYDTAARKCQKVLGKNMDLWENEVYRFKTIGQLKAISQYLPRGDLRLRPAIYEMILHDFLKTDYEGFATLIREWPGELYNNMAIVQAVNEHLKKDPTNSILLTTLAELYTYDQRYDRALEIYLRLRHKDVYQLIHKHNLFSSIKDKIVLLMDFDKEKAVDMLLDNEDKISMDKVVEELKDRPELLHVYLHKLFKRDHHKGQKYHERQISLYAEFDRPNLLPFLRESMHCPLEKALEICQQRHFVEETVFLLSRMGNCRRALQMIMEELANVDKAIEFAKEQDDRELWEDLISYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILHDYNLQILLREGCKKILVADSLSLLQRMHRTQKKGVRVDEENICESCHTPILPSDTAQAFGVVVFHCRHMFHKECLPSPGSIPGIQYCNICSAKRRGPGSGILEMKK
Protein: Prefoldin subunit 4 (Protein C-1) (Q9NQP4)
Organism: Homo sapiens (Human)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:17936702}. Cytoplasm {ECO:0000269|PubMed:17936702}. Mitochondrion {ECO:0000269|PubMed:17936702}.
Interaction partners:
- Prefoldin subunit 6
- Prefoldin subunit 2
- Prefoldin subunit 1
- Prefoldin subunit 3
- Prefoldin subunit 5
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
Sequence:
MAATMKKAAAEDVNVTFEDQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDCLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQRVLADLKVQLYAKFGSNINLEADES
Protein: Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) [Cleaved into: T1-TrpRS; T2-TrpRS] (P32921)
Organism: Mus musculus (Mouse)
Function: T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23381}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Methionine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Serine--tRNA ligase, mitochondrial
Sequence:
MADMPSGESCTSPLELFNSIATQGELVRSLKAGNAPKDEIDSAVKMLLSLKMSYKAAMGEEYKAGCPPGNPTAGRNCDSDATKASEDFVDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQDVFNVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDINKTFIFSDLEYMGQSPGFYRNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDRLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEFMTPRQLSFHFQCFCFDT
Protein: Beta-defensin 1 (BD-1) (hBD-1) (Defensin, beta 1) (P60022)
Organism: Homo sapiens (Human)
Function: Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility.
Subcellular location: Secreted {ECO:0000269|PubMed:7628632}. Membrane {ECO:0000269|PubMed:23938203}. Note=Associates with tumor cell membrane-derived microvesicles (PubMed:23938203). {ECO:0000269|PubMed:23938203}.
Interaction partners:
- Defensin beta 4A
- Beta-defensin 103
- C-C chemokine receptor type 6
- C-C chemokine receptor-like 2
- Bromodomain-containing protein 4
- Beta-defensin 104
- Neutrophil defensin 1
- Bromodomain testis-specific protein
- Defensin alpha 5
- Neutrophil defensin 3
Sequence:
MRTSYLLLFTLCLLLSEMASGGNFLTGLGHRSDHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK
Protein: Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) (EC 2.4.1.-) (Q91X88)
Organism: Mus musculus (Mouse)
Function: Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins. Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties. Is specific for alpha linked terminal mannose.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WZA1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8WZA1}.
Interaction partners:
- Protein O-mannosyl-transferase 2
- Protein O-mannosyl-transferase 1
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Dystroglycan 1
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
- Beta-1,4-galactosyltransferase 1
- Ribitol-5-phosphate transferase FKTN
- Ribitol 5-phosphate transferase FKRP
- Beta-1,4-galactosyltransferase 3
- Beta-1,4-galactosyltransferase 2
Sequence:
MDDWKPSPLIKPFGARKKRSWYLTWKYKLTNQRALRRFCQTGAVLFLLVTVIVNIKLILDTRRAISEANEDPEPEQDYDEALGRLESPRRRGSSPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVLGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRKSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRMETDDDFATWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLVVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAAEQT
Protein: Lys-gingipain W83 (EC 3.4.22.47) (Lysine specific cysteine protease) (Lysine-specific cysteine proteinase) (Porphypain) (PrtK48) [Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin (PrtK39); 15 kDa adhesin (PrtK15); 44 kDa adhesin (PrtK44)] (Q51817)
Organism: Porphyromonas gingivalis (Bacteroides gingivalis)
Function: Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity). Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain.
Subcellular location: [Lys-gingipain catalytic subunit]: Secreted {ECO:0000269|PubMed:9245829}.; SUBCELLULAR LOCATION: [39 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.; SUBCELLULAR LOCATION: [15 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.; SUBCELLULAR LOCATION: [44 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.
Interaction partners:
Sequence:
MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKVLLIAGADYSWNSQVGQPTIKYGMQYYYNQEHGYTDVYNYLKAPYTGCYSHLNTGVSFANYTAHGSETAWADPLLTTSQLKALTNKDKYFLAIGNCCITAQFDYVQPCFGEVITRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVSMTKQITENGNYDVVITRSNYLPVIKQIQVGEPSPYQPVSNLTATTQGQKVTLKWEAPSAKKAEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLVPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSSVGQKVTLKWDAPNGTPNPNPNPNPNPGTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPKAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLDWLTAHGGSNVVSSFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKKCVDVTVNSTQFNPVQNLTAEQAPNSMDAILKWNAPASKRAEVLNEDFENGIPASWKTIDADGDGNNWTTTPPPGGSSFAGHNSAICVSSASHINFEGPQNPDNYLVTPELSLPGGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRAQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVVITSGNAPSYTYTIYRNNTQIASGVTETTYRDPDLATGFYTYGVKVVYPNGESAIETATLNITSLADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGHYAVMVVVDGKSYVEKLAVK
Protein: Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (EC 1.13.11.58) (Manganese 9S/11S-lipoxygenase) (9S/11S-MnLOX) (G4NAP4)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S-HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end product.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8X151}.
Interaction partners:
- Bifunctional dioxygenase
- Lysophospholipase
- Patatin-like phospholipase domain-containing protein
Sequence:
MRVLVWIAGLAPLAVAVPSSSYRVAVAARADNTSASVAPSQNVSGAAPPELVVYTLPCEDGNSTARTAEIRLKQATLLYGPSLLGNASYFPGGPLGDAISLRDQTVWEGAAVVQSLRAFTDAAKVAANIKQNGGLNSLDDFKVLYQDGWKGSVPQGIARGQSENYTSDLLFSMERLSVNPYILKRLHPTEDALPFQVDRATVKQLTKTSLKALHAAGRLFVADHSYQRNYTRLANRYSAACTALFYLDPRSNQFLPLAIKTNVGADLTYTPLDTDNNNWLLAKIMFNNNDLFHGQIFHVAYPHAIAEIVHLAALRTMSARHPVLALMERLMYQAYAVRPLGERVLFNKGGLFEQNFAYPQDMVYKFVGDSYPTTGRWRAGYLDTDVRARGLVDADYGPELPHFPFYEDGSRLVEVIRRFVRSFVDATYHESDEMVAKDAELQAWVAEANGPAGVEDFEPGPLDTRERLVEVLTHMAWLTGCAHHVLNQGEPVTASGVLPMHPTALYAPVPTSKANTTADLLGYLPSAQKSVDQVTLLARFNRPDVVPTNQTLRYMFAAPQLLLGNGEAYRRANQRFVRAMGRISDEVKARRFDDRGLSQGMPFIWQALDPGNIPFYLSV
Protein: La-related protein 4 (La ribonucleoprotein domain family member 4) (Q71RC2)
Organism: Homo sapiens (Human)
Function: RNA binding protein that binds to the poly-A tract of mRNA molecules. Associates with the 40S ribosomal subunit and with polysomes. Plays a role in the regulation of mRNA translation. Plays a role in the regulation of cell morphology and cytoskeletal organization.
Subcellular location: Cytoplasm, Stress granule {ECO:0000269|PubMed:21098120}. Cytoplasm, cytosol {ECO:0000269|PubMed:21098120, ECO:0000269|PubMed:27615744}. Note=Localized throughout the cytosol. Partially localized in stress granules in response to arsenite treatment. {ECO:0000269|PubMed:21098120}.
Interaction partners:
- Polyadenylate-binding protein 1
- Small ribosomal subunit protein RACK1
- La-related protein 6
Sequence:
MLLFVEQVASKGTGLNPNAKVWQEIAPGNTDATPVTHGTESSWHEIAATSGAHPEGNAELSEDICKEYEVMYSSSCETTRNTTGIEESTDGMILGPEDLSYQIYDVSGESNSAVSTEDLKECLKKQLEFCFSRENLSKDLYLISQMDSDQFIPIWTVANMEEIKKLTTDPDLILEVLRSSPMVQVDEKGEKVRPSHKRCIVILREIPETTPIEEVKGLFKSENCPKVISCEFAHNSNWYITFQSDTDAQQAFKYLREEVKTFQGKPIMARIKAINTFFAKNGYRLMDSSIYSHPIQTQAQYASPVFMQPVYNPHQQYSVYSIVPQSWSPNPTPYFETPLAPFPNGSFVNGFNSPGSYKTNAAAMNMGRPFQKNRVKPQFRSSGGSEHSTEGSVSLGDGQLNRYSSRNFPAERHNPTVTGHQEQTYLQKETSTLQVEQNGDYGRGRRTLFRGRRRREDDRISRPHPSTAESKAPTPKFDLLASNFPPLPGSSSRMPGELVLENRMSDVVKGVYKEKDNEELTISCPVPADEQTECTSAQQLNMSTSSPCAAELTALSTTQQEKDLIEDSSVQKDGLNQTTIPVSPPSTTKPSRASTASPCNNNINAATAVALQEPRKLSYAEVCQKPPKEPSSVLVQPLRELRSNVVSPTKNEDNGAPENSVEKPHEKPEARASKDYSGFRGNIIPRGAAGKIREQRRQFSHRAIPQGVTRRNGKEQYVPPRSPK
Protein: Protein NRT1/ PTR FAMILY 7.2 (AtNPF7.2) (Nitrate transporter 1.8) (Q8GXN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity nitrate transporter. Involved in nitrate removal from xylem sap. Not involved in oligopeptides transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20501909}; Multi-pass membrane protein {ECO:0000269|PubMed:20501909}.
Interaction partners:
- High-affinity nitrate transporter 2.1
- Chloride channel protein CLC-a
- High affinity nitrate transporter 2.7
- High affinity nitrate transporter 2.4
- Nitrate regulatory gene2 protein
- High-affinity nitrate transporter 2.2
- High affinity nitrate transporter 2.6
- High affinity nitrate transporter 2.5
- Nitrate reductase 1
- F16L1.2 protein
Sequence:
MDQKVRQFEVCTQDGSVDRHGNPAIRANTGKWLTAILILVNQGLATLAFFGVGVNLVLFLTRVMGQDNAEAANNVSKWTGTVYIFSLLGAFLSDSYWGRYKTCAIFQASFVAGLMMLSLSTGALLLEPSGCGVEDSPCKPHSTFKTVLFYLSVYLIALGYGGYQPNIATFGADQFDAEDSVEGHSKIAFFSYFYLALNLGSLFSNTVLGYFEDQGEWPLGFWASAGSAFAGLVLFLIGTPKYRHFTPRESPWSRFCQVLVAATRKAKIDVHHEELNLYDSETQYTGDKKILHTKGFRFLDRAAIVTPDDEAEKVESGSKYDPWRLCSVTQVEEVKCVLRLLPIWLCTILYSVVFTQMASLFVVQGAAMKTNIKNFRIPASSMSSFDILSVAFFIFAYRRFLDPLFARLNKTERNKGLTELQRMGIGLVIAIMAMISAGIVEIHRLKNKEPESATSISSSSTLSIFWQVPQYMLIGASEVFMYVGQLEFFNSQAPTGLKSFASALCMASISLGNYVSSLLVSIVMKISTTDDVHGWIPENLNKGHLERFYFLLAGLTAADFVVYLICAKWYKYIKSEASFSESVTEEEEV
Protein: Acetate kinase (EC 2.7.2.1) (Acetokinase) (P0A6A3)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. The main pathway for acetate production during exponential phase.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphate acetyltransferase EutD
- Phosphate acetyltransferase
- Acetyl-coenzyme A synthetase
- Pyruvate dehydrogenase
- Aldehyde dehydrogenase B
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Formate acetyltransferase 1
- Propionate--CoA ligase
- Isocitrate lyase
- Acylphosphatase
Sequence:
MSSKLVLVLNCGSSSLKFAIIDAVNGEEYLSGLAECFHLPEARIKWKMDGNKQEAALGAGAAHSEALNFIVNTILAQKPELSAQLTAIGHRIVHGGEKYTSSVVIDESVIQGIKDAASFAPLHNPAHLIGIEEALKSFPQLKDKNVAVFDTAFHQTMPEESYLYALPYNLYKEHGIRRYGAHGTSHFYVTQEAAKMLNKPVEELNIITCHLGNGGSVSAIRNGKCVDTSMGLTPLEGLVMGTRSGDIDPAIIFHLHDTLGMSVDAINKLLTKESGLLGLTEVTSDCRYVEDNYATKEDAKRAMDVYCHRLAKYIGAYTALMDGRLDAVVFTGGIGENAAMVRELSLGKLGVLGFEVDHERNLAARFGKSGFINKEGTRPAVVIPTNEELVIAQDASRLTA
Protein: Capsid protein F (F protein) (GPF) (P03641)
Organism: Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174)
Function: Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F. Upon virus binding to host cell, one of the spikes dissociates from the capsid and the virus interacts with LPS through the exposed EF loops on the F proteins. After the genome had been ejected, the channel formed by the F proteins at the unique fivefold axis remains open.
Subcellular location: Virion {ECO:0000269|PubMed:10329166, ECO:0000269|PubMed:1370343, ECO:0000269|PubMed:29229840, ECO:0000269|PubMed:8158636, ECO:0000269|PubMed:9305849}.
Interaction partners:
Sequence:
MSNIQTGAERMPHDLSHLGFLAGQIGRLITISTTPVIAGDSFEMDAVGALRLSPLRRGLAIDSTVDIFTFYVPHRHVYGEQWIKFMKDGVNATPLPTVNTTGYIDHAAFLGTINPDTNKIPKHLFQGYLNIYNNYFKAPWMPDRTEANPNELNQDDARYGFRCCHLKNIWTAPLPPETELSRQMTTSTTSIDIMGLQAAYANLHTDQERDYFMQRYHDVISSFGGKTSYDADNRPLLVMRSNLWASGYDVDGTDQTSLGQFSGRVQQTYKHSVPRFFVPEHGTMFTLALVRFPPTATKEIQYLNAKGALTYTDIAGDPVLYGNLPPREISMKDVFRSGDSSKKFKIAEGQWYRYAPSYVSPAYHLLEGFPFIQEPPSGDLQERVLIRHHDYDQCFQSVQLLQWNSQVKFNVTVYRNLPTTRDSIMTS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q387H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine-protein kinase, putative
Sequence:
MPLNSSHRERVSVGGLTPCIKKATVTAPETAFTSHGGGHRVLDVAASGSEGLHPDSGEGQRLHPMSDFESLYKVRRQLGSGGYSVVFEVVDCITHERKAAKFVVGKVERRAARARLTGPVELRLHGDGRNGDRRKVSSIGGLEKARSANSRPTVSDSLVKEVAMGLMAQHANLVHTSDVFVHDTEDLRRRLREYAPQLSLETVRRSEGAGPYDVARGAACGESPSKSWQPHRLRQRSGGSGSDTTASVRGGDAPILHECNTSSADQITQGVETAKRYLQESRVQCILVMELLTGNDLFTLVSRGPLNERMAASYMFDLFLALRYLHNRNIVHRDVKVENMALDSENRVRLIDYGFCEVLRRSGDANPNGVEGKNPEGLLTQFCGSHHYVAPEVITSAWLTRHGSKNSETTTHSGVSLPPIAQLSATGAPPPKESVEGCVVGRQNVGSAGALRTHLTRRGVGYGLSADIWSAGIVMFVLLHSAFPYHDERRSRLLKMIVSNKRSLGSASRLSSDARDLLRKLLTHDASRRPPVNEVLEHCWFRKQLGEKVGGKLSLVA
Protein: Tripartite motif-containing protein 66 (Transcriptional intermediary factor 1 delta) (Q924W6)
Organism: Mus musculus (Mouse)
Function: May function as transcription repressor; The repressive effects are mediated, at least in part, by recruitment of deacetylase activity. May play a role as negative regulator of postmeiotic genes acting through CBX3 complex formation and centromere association.
Subcellular location: Nucleus {ECO:0000269|PubMed:15322135}. Note=Forms discrete foci within the centromeric chromocenter and surrounding nucleoplasm.
Interaction partners:
- Histone H3.2
- Histone H3.3
- Histone H3.1
- E3 ubiquitin-protein ligase TRIM8
Sequence:
MSPGLPVSIPSQPHCSTDERVEALAPTCSMCGRDLQAEGSRLLPCQHLLCKDCYQGFMQELGHATRAYPGKLISCPGCQRVYLTRDVTEHIFLQCFSPVKPTMARNCSECKEKRAAHILCTYCNRWLCSSCTEEHRHVPAPGGPLFARAQKGSSGVNGGSGDFALYCPLHTQEVLKLFCETCDVLTCHSCLMVEHKEHRCRHVEEVLQNQRMLLESVTSQVAHKKSSLQTSAKQIEDRIFEVKHQHRKVENQIKMAKMVLMNELNKQANGLIEELEGITNERKRKLEQQLQSIMVLNRQFEHVQNFINWAVCSKSSVPFLFSKELIVFQMQRLLETRCNTDPGSPWSIRFTWEPNFWTKQLASLGCITTEGGQLTRADAAAASYGSLQGQPSFYQSHQAPMAQQEALSHPSHKFQSPALCSSSVCCSHCSPVSPSLKGQVPPPSIHPAHSFRQPSEMVPHQLGSLQCSTLLPREKELACSPHPPKLMQPWLEPQPPAEQESTSQRPGPQLVSQPVCIVPPQDVQPGAHAQPTIQTPSIQVQLGHHQKLKLSHFQQQPQQQPPPPPPPPPPPQHAPPPLPPSQHLASSQHESPPGPACSQNVDIMHHKFELEEMQKDLELLLQAQQPSLQLSQTKSPQHLQQTIVGQINYIVRQPAPVQSQSQEETLQVTEEPPAPEGPKPALPVDKNTAAPLPQTSGEETPHSVPPVDGTSQHSSPNVVRKHATSVSIMGFSNTVEMELSSTRLARTIEPQIHRVSSLTAAPTHTIPSLLSGPPQTVSSLMSVSNHAMPSLTASHLQPVPNLVRGTFQSTSNLRGDSSQAITGLASNHSQAGPSLMSGHTQAAPSLATCPLQGMPPVSDVHVEPRSVSSPGSGPAAESLGTRDGAESSLGNALCKMESEDCTRFSDSVGQGPTASSLDGPKDLAIPSELEEPINLSVKKPFLAPVINTSTALQQYRNPKEYENFEQGALELDTKENSDIRAISSEPKIPYVRLERLKICAASSGEMPVFKLKPQKNSQDGNFLLVIECGTESSSMSIKVSQNSLPDASQGPGLGGRKVTVTSLTGQQPQEVESTSEEHRLIPRAPGAKKNTPAPIENEDFCAVCINGGELLCCDRCPKVYHLSCHVPALLSFPGGEWVCTLCRSLTQPEMEYDCENARYGHPGVRVLPGLSMYDQKKCEKLVLSLCCNSLSLPFHEPVSPLARHYYQIIKRPMDLSIIRRKLQKKDPAHYTTPEEVVSDVRLMFWNCAKFNYPDSEVAEAGRCLEVFFEGWLKEIYPDKCFAQPQQEDSDSEDVSGESGCSTPQGFPWPPYMQEGIQPKRRRRHMENEKTKRVSFRLANSISQV
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (38 kDa BFA-dependent ADP-ribosylation substrate) (BARS-38) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) (P04797)
Organism: Rattus norvegicus (Rat)
Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15312048}. Nucleus {ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794, ECO:0000269|PubMed:20972425}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (PubMed:15951807). Colocalizes with CHP1 to small punctate structures along the microtubules tracks (PubMed:15312048). {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807}.
Interaction partners:
- Phosphoglycerate kinase 1
- Triosephosphate isomerase
- Triosephosphate isomerase.
- Large ribosomal subunit protein uL13
- Phosphoglycerate kinase
- Triosephosphate isomerase
- E3 ubiquitin-protein ligase SIAH1
- Fructose-bisphosphate aldolase A
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
Sequence:
MVKVGVNGFGRIGRLVTRAAFSCDKVDIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQAAEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE
Protein: Protein BTG4 (BTG family member 4) (Protein PC3b) (Q9NY30)
Organism: Homo sapiens (Human)
Function: Adapter protein that bridges CNOT7, a catalytic subunit of the CCR4-NOT complex, to EIF4E (By similarity). Facilitates maternal mRNAs decay during the maturation of oocytes and in the fertilized egg, and is required for the maternal-zygotic transition (MZT), zygotic cleavage and initiation of embryonic development.
Interaction partners:
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 8
Sequence:
MRDEIATTVFFVTRLVKKHDKLSKQQIEDFAEKLMTILFETYRSHWHSDCPSKGQAFRCIRINNNQNKDPILERACVESNVDFSHLGLPKEMTIWVDPFEVCCRYGEKNHPFTVASFKGRWEEWELYQQISYAVSRASSDVSSGTSCDEESCSKEPRVIPKVSNPKSIYQVENLKQPFQSWLQIPRKKNVVDGRVGLLGNTYHGSQKHPKCYRPAMHRLDRIL
Protein: 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Allergen Der f 34) (Enamine/imine deaminase) (allergen Der f 34.0101) (A0A1J1DL12)
Organism: Dermatophagoides farinae (American house dust mite)
Function: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase (By similarity). Preferentially digests Leu and Met in cooperation with L-amino acid oxidase, but digests Phe poorly.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52758}.
Interaction partners:
Sequence:
MSPKRIISTPLAPQPIGPYSQAVQVGNTVYLSGQIGMNVRTNEMVTGPIRDEAQQAFTNMKAVVEASGAKMSDVVKVNIFIRNFNDFPAINDVMKEFFQSPFPARSTVGVAELPKNARVEIESIVVIE