wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein eS10B (40S ribosomal protein S10-B) (P46784)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eS10 plays a role as a positive regulator of the GCN2 kinase activity by stimulating GCN1-mediated GCN2 activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS26A
- Serine/threonine-protein kinase RIO2
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS7B
- Small ribosomal subunit protein eS24A
- Small ribosomal subunit protein uS9A
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS15
Sequence:
MLMPKQERNKIHQYLFQEGVVVAKKDFNQAKHEEIDTKNLYVIKALQSLTSKGYVKTQFSWQYYYYTLTEEGVEYLREYLNLPEHIVPGTYIQERNPSQRPQRRY
Protein: Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Q9D0I9)
Organism: Mus musculus (Mouse)
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
Interaction partners:
- Glutamine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Lysine--tRNA ligase
- Nuclear receptor corepressor 2
- Tyrosine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
Sequence:
MDGLVAQCSARLLQQEREIKALTAEIDRLKNCGCLEASPSLEQLREENLKLKYRLNILRRSLQEERRKPTKNMININSRLQEVFGCAIRAAYPDLENPPLIVTPSQQPKFGDYQCNSAMGISQMLKAKEQKVSPREIAENITKHLPNNKYIDKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPVLGDKEKVIVDFSSPNIAKEMHVGHLRSTIIGESMSRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQAFYKESKKRFDADEEFKKRAYQCVVLLQSKNPDIMKAWNLICDVSREEFKKIYDALDITLIERGESFYQDRMKDIVKEFEDKGFVQVDDGRKIVFVPGCSVPLTIVKSDGGYTYDTSDLAAIKQRLFEEKANKIIYVVDNGQAIHFQTIFAAAQMIGWYDPKVTLVTHVGFGVVLGEDKKKFKTRSGETVRLMDLLEEGLKRSMDKLKEKERDKVLTEEELKAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEAMLQRAARETKIILDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATTFTEFYDSCYCVEKDRQTGKVLKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM
Protein: Cystatain (T2BRR7)
Organism: Nicotiana tabacum (Common tobacco)
Interaction partners:
Sequence:
MAFKINSFLLMTLSIVVIASIFCHVSAANDGRKLLDSSDLVSNTPALSQLFGDWQPIKDAKDPKVVKVGEFAVDAYNRISNSFPLTFESVLGGQFQVVNGITYKLVISARQNVTTTNYLAVVNEHSGDNVKTLISFEKFA
Protein: Ghrelin (Preproghrelin) (Q3ZV42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPLRCRASSMFLLLCVSLSLCLESVSGGTSFLSPTQKPQGRRPPRVGRREAADPEIPVIKEDDRFMMSAPFELSMSLSEAEYEKYGPVLQNLLEDLLRDSSFEF
Protein: 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) (Q8UGL3)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
Interaction partners:
- 4-hydroxy-tetrahydrodipicolinate reductase
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Diaminopimelate decarboxylase
- Diaminopimelate decarboxylase
Sequence:
MFKGSIPALITPFTDNGSVDEKAFAAHVEWQIAEGSNGLVPVGTTGESPTLSHDEHKRVVELCIEVAAKRVPVIAGAGSNNTDEAIELALHAQEAGADALLVVTPYYNKPTQKGLFAHFSAVAEAVKLPIVIYNIPPRSVVDMSPETMGALVKAHKNIIGVKDATGKLDRVSEQRISCGKDFVQLSGEDGTALGFNAHGGVGCISVTANVAPRLCSEFQAAMLAGDYAKALEYQDRLMPLHRAIFMEPGVCGTKYALSKTRGGNRRVRSPLMSTLEPATEAAIDAALKHAGLMN
Protein: Basic leucine zipper 25 (AtbZIP25) (bZIP protein 25) (Basic leucine zipper OPAQUE 2 homolog 4) (Basic leucine zipper O2 homolog 4) (Q9M1G6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to the 5'-ACGT-3' box, especially present in G-box-like motif (5'-CCACGTGGCC-3'), ABRE elements, of seed storage protein (SSP) encoding gene promoters (e.g. At2S and CRU3) and promotes their expression in seeds when in complex with ABI3 and BZIP53.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- B3 domain-containing transcription factor ABI3
- bZIP transcription factor 53
- Basic leucine zipper 1
- bZIP transcription factor 28
- Transcription factor HY5
- bZIP transcription factor 17
- Transcription factor HY5-like
- bZIP transcription factor 49
- Basic leucine zipper 8
- F-box protein At3g59000
Sequence:
MHIVFSVDDLTESFWPVPAPAPSPGSSSTPSPTQNVADGMTRSQSEWAFHRLINELSGSDSSPTTNTIERSPPPVQSLSRLEETVDETEDVVEIQKPQNHRRLPVDDQGKNRNRAPSSDPVDSSAPVVVDPNQYHAILKSKLELACAAVARRVGTVKPEDSSASASNQKQAQGSIVAQTSPGASSVRFSPTTSTQKKPDVPARQTSISSRDDSDDDDLDGDADNGDPTDVKRARRMLSNRESARRSRRRKQEQMNEFDTQVGQLRAEHSTLINRLSDMNHKYDAAAVDNRILRADIETLRTKVKMAEETVKRVTGVNPLHWSRPNMGIPFSNTPSASSSIPPNSNHILKPANSSTNTSAGLAQNQRVETANFLPEQVNREGMQNPFAPDSNLYETLPHWNHKH
Protein: DNA utilization protein YhgH (Protein GntX) (P46846)
Organism: Escherichia coli (strain K12)
Function: Required for the use of extracellular DNA as a nutrient. Has been suggested to be involved in gluconate metabolism.
Interaction partners:
- Protein Smf
- Uncharacterized protein YifB
- Uncharacterized protein YcaI
- Fe/S biogenesis protein NfuA
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- UPF0102 protein YraN
- T-protein
Sequence:
MLTVPGLCWLCRMPLALGHWGICSVCSRATRTDKTLCPQCGLPATHSHLPCGRCLQKPPPWQRLVTVADYAPPLSPLIHQLKFSRRSEIASALSRLLLLEVLHARRTTGLQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRATATQHFLSARLRKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL
Protein: Probable cinnamyl alcohol dehydrogenase (CAD) (EC 1.1.1.195) (Brown-midrib 1 protein) (O24562)
Organism: Zea mays (Maize)
Function: Involved in lignin biosynthesis. May catalyze the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol.
Interaction partners:
- Agamous-like MADS-box protein AGL62
- Flavone 3'-O-methyltransferase 1
- Caffeic acid 3-O-methyltransferase
Sequence:
MGSLASERKVVGWAARDATGHLSPYSYTLRNTGPEDVVVKVLYCGICHTDIHQAKNHLGASKYPMVPGHEVVGEVVEVGPEVAKYGVGDVVGVGVIVGCCRECSPCKANVEQYCNKKIWSYNDVYTDGRPTQGGFASTMVVDQKFVVKIPAGLAPEQAAPLLCAGVTVYSPLKHFGLTNPGLRGGILGLGGVGHMGVKVAKAMGHHVTVISSSSKKRAEAMDHLGADAYLVSSDAAAMAAAADSLDYIIDTVPVHHPLEPYLALLKLDGKLVLLGVIGEPLSFVSPMVMLGRKAITGSFIGSIDETAEVLQFCVDKGLTSQIEVVKMGYVNEALERLERNDVRYRFVVDVAGSNVEAEAAAADAASN
Protein: UDP-glucuronate 4-epimerase 5 (EC 5.1.3.6) (UDP-glucuronic acid epimerase 5) (Q9STI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-sugar pyrophosphorylase
- UDP-D-apiose/UDP-D-xylose synthase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Sucrose synthase 3
- Sucrose synthase 1
- Sucrose-phosphate synthase 4
- Sucrose synthase 4
- Sucrose synthase 6
Sequence:
MSHLDDLPSTPGKYKTDKVPPYGILHHHRYLRLSKLTLWASLFLALFLFYLVLSPPPSPSRRNLNDSSSISAAKYGGSHWEKQVRKSARPRSHGGLTVLVTGASGFVGTHVSIALRRRGDGVLGLDNFNRYYDPKLKRARQGLLERSGVFVVEGDINDAVLLRKLFDVVLFTHVMHLAAQAGVRYAMQNPGSYVNSNIAGFVNLLEVSKSANPQPAIVWASSSSVYGLNSKVPFSEKDRTDQPASLYAATKKAGEGIAHTYNHIYGLSLTGLRFFTVYGPWGRPDMAYFFFTKDILKGKTITVFESPDKGSVARDFTYIDDIVKGCLGALDTAEKSTGSGGKKKGPAMFRIYNLGNTSPVPVTKLVTILEKLLKMKAKKKIMPLPRNGDVEFTHANITLAQAELGYKPAVDLETGLKKFVKWYMGFYTGSKKKSSW
Protein: Wilms tumor protein (A0A0A0MT54)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
LDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQGVRDPGGIWAKLGAAEASAERLQGRRSRGASGSEPQQMGSDVRDLNALLPAVPSLGGGGGCALPVSGAAQWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYGPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGSSSSVKWTEGQSNHSTGYESDNHTTPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) (Protein bloated bladder) (Blad) (Q8BNJ3)
Organism: Mus musculus (Mouse)
Function: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor. Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons. Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (By similarity). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23610559}; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasmic vesicle membrane; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZQ4}. Cell projection, axon {ECO:0000269|PubMed:23610559}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000269|PubMed:23610559}.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide phosphoribosyltransferase
- Nicotinamide riboside kinase 1
- NAD kinase
- Glutamine-dependent NAD
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- Nicotinamide riboside kinase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- NAD kinase 2, mitochondrial
Sequence:
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQHENTQPIYQNSNVPTKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
Protein: Thioredoxin domain-containing protein 6 (Thioredoxin-like protein 2) (Txl-2) (Q6IRC5)
Organism: Xenopus laevis (African clawed frog)
Function: May be a regulator of microtubule physiology.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33263282}. Dynein axonemal particle {ECO:0000269|PubMed:33263282}. Note=Associated with microtubules. Detected in cilia of lung epithelium, and associated with the spermatid tail and manchette (By similarity). {ECO:0000250|UniProtKB:A0A1L1SUL6}.
Interaction partners:
Sequence:
MAGKKRESSLQIALSNQEQWEEALSTKGLQVVDVYQAWCGPCKPTVSLFRKIKNELGDDLLHFAVAESDTIDSLVKYRGKCEPTFLFLAGGELVAVVRGANGPLLQKTIIEQLAAEKKVLNQGSERHVIKDEVLLEEEDEIAPVQAQTEDEELVPSGKSYTVAIIKPDAVAHGKTDEIIMKIQESGFEILANEERTMTESEAREFYQHRAGEEKFQELIQFMSSGPCHILIISKSEEDEDVIPAWREFIGPTDVEIAKKEKPESLRAQYGTEVLYNAVHGSNDREQASRELAFFFPNFKISNESLKELTSVKPERTLALIRPEILKERKDEILQSIKDAGFSIAMQKEVMLTEHQVQEFYKEHINEDYYPALLKQMTSGPVLALALVKDNAVGHWRNMLGPASLSQALSEAPDSLRAQFAPSDSETNQLHGSSTTEEAKKEINFFFPVEHTLATIKPDALEEHRDEILEQIQGAGFTISQIKEANLNREMAEEFYKEHKGKPFFEQLVNYMCRGPCLMMILSKENAVHEWRSLMGPTDPAEAQKVLPDSLRGKFAKSILQNAVHGSSNSDHAMEKIKFIFGDIDLDRIVHESFGETPETSASDISRNAAAQGDDPEQDESKEMEE
Protein: Phosphatidylinositol polyphosphate 5-phosphatase type IV (5-phosphatase that induces arborization) (Pharbin) (72 kDa inositol polyphosphate 5-phosphatase) (Inositol polyphosphate-5-phosphatase E) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.86) (Q9WVR1)
Organism: Rattus norvegicus (Rat)
Function: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate PtdIns (4,5)P2 and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Specific for lipid substrates, inactive towards water soluble inositol phosphates (By similarity). Plays an essential role in the primary cilium by controlling ciliary growth and phosphoinositide 3-kinase (PI3K) signaling and stability (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9JII1}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane {ECO:0000269|PubMed:10405344}; Peripheral membrane protein {ECO:0000269|PubMed:10405344}; Cytoplasmic side {ECO:0000269|PubMed:10405344}. Cell projection, ruffle {ECO:0000269|PubMed:10405344}. Cytoplasm {ECO:0000269|PubMed:10405344}. Nucleus {ECO:0000250|UniProtKB:Q9JII1}. Note=Peripheral membrane protein associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- ADP-ribosylation factor like GTPase 13B
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 beta
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MPSKSACLRHTEAPGQLEGRMLQGQLSNPEKKLIPTSASLPAADSQSSQTNSMPPLSMPAKPSNQNLQAKANLITPQPPIRPKLERTLSLDDKGWRRRRFRGSQEDLTVQNGASPCRGSLQDSVAQSPAYSRPLPCLSTSLQEIPKPRRATGSEGGSPSLWSDCLSGMISTSLDLLHREAASGGPHSRLASLRATHTPPAMDLNIASSSLRTANKVDPEHTDYKLRMQNRLVRAHSNLGPSRPRSPLAGDDHSIHSARSSFSLLAPIRTKDIRSRSYLEGSLLASGALLGADELARYFPDRNMALFVATWNMQGQKELPASLDEFLLPTEADYTQDLYVIGVQEGCSDRREWETRLQETLGPQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYNRTIQALALPRNVPDTNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQDPEVDVLALLQHDQLTREMKKGSIFKGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLIGIKRRISKEIQRQEALKSQSSSAVCTVS
Protein: DNA utilization protein HofP (P45750)
Organism: Escherichia coli (strain K12)
Function: Required for the use of extracellular DNA as a nutrient.
Interaction partners:
- DNA utilization protein HofO
- DNA utilization protein HofQ
- DNA utilization protein HofN
- DNA utilization protein HofM
- Uncharacterized fimbrial-like protein YraK
- ABC transporter periplasmic-binding protein YphF
Sequence:
MRVKRWLLAGIALCLLTGMRDPFKPPEDLCRISELSQWRYQGMVGRGERIIGVIKDGQKKWRRVQQNDVLENGWTILQLTPDVLTLGTGTNCEPPQWLWQRQGDTNEAMDSRTTVDADTRRTGGKAAKSDADGG
Protein: Nucleotidylyl transferase superfamily protein (Q8L845)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase MGP4
Sequence:
MGDAAIRTVVEAIHSSPTQAVVYLCGGASLALGWLMSVPGASNTLLESVVPYSRVSMVQLLGRVPSQHCSQALAKEMALLAYNRALKLSKPGYPVLGVGFTGSLVTSRPKRGDHRFFLSMRASDRILESSVTLTKNLRSREEEDKVSSCALIQAMAKACQVSGTLDSGLTESEVPYESETHFTEEQELEQLINGHLCCKIYPFSGEAHGSDEDRKIILPGSFNPLHEGHLKLLEVAMSVCGGGYPCFEISAINADKPPLTIAQIKDRVKQFEVVGKTIIVSNQPYFYKKAELFPGSSFVIGADTAARLVNPKYYEGSIKRMLEILGDCKRTGCTFLVGGRNVDGVFKVLEDVDIPEEIIDMFISIPADIFRMDISSTEIRKKQGGGTN
Protein: Protein bicaudal C (Q24009)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA-binding protein that is involved in oogenesis. Required for correct targeting of the migrating anterior follicle cells and the establishment of anterior-posterior polarity in the oocyte. May act as translational repressor of oskar during oogenesis. Function seems to be sensitive to small changes in expression.
Interaction partners:
- Maternal effect protein oskar
- ATP-dependent RNA helicase me31b
- CG3509 protein
- Bruno 1, isoform B
- CG5272 protein
- Vitellogenin receptor Yl
- Protein matrimony
- Maternal protein pumilio
- Trailer hitch, isoform H
- Maternal protein exuperantia
Sequence:
MLSCASFNKLMYPSAADVAKPPMVGLEVEAGSIGSLSSLHALPSTTSVGSGAPSETQSEISSVDSDWSDIRAIAMKLGVQNPDDLHTERFKVDRQKLEQLIKAESSIEGMNGAEYFFHDIMNTTDTYVSWPCRLKIGAKSKKDPHVRIVGKVDQVQRAKERILSSLDSRGTRVIMKMDVSYTDHSYIIGRGGNNIKRIMDDTHTHIHFPDSNRSNPTEKSNQVSLCGSLEGVERARALVRLSTPLLISFEMPVMGPNKPQPDHETPYIKMIETKFNVQVIFSTRPKLHTSLVLVKGSEKESAQVRDATQLLINFACESIASQILVNVQMEISPQHHEIVKGKNNVNLLSIMERTQTKIIFPDLSDMNVKPLKKSQVTISGRIDDVYLARQQLLGNLPVALIFDFPDNHNDASEIMSLNTKYGVYITLRQKQRQSTLAIVVKGVEKFIDKIYEARQEILRLATPFVKPEIPDYYFMPKDKDLNLAYRTQLTALLAGYVDSPKTPSLLPPSLAGQLTPYANNNHLLLNANGLATPTGVCAPTQKYMQLHNSFQQAQNRSMVAGGQSNNGNYLQVPGAVAPPLKPPTVSPRNSCSQNTSGYQSFSSSTTSLEQSYPPYAQLPGTVSSTSSSTAGSQNRAHYSPDSTYGSEGGGVGGGGGGGARLGRRLSDGVLLGLSNSNGGGGNSGGAHLLPGSAESYRSLHYDLGGNKHSGHRAFDFDMKRALGYKAMERTPVAGELRTPTTAWMGMGLSSTSPAPAPLENGENGAAGGGASSGWRLPPGLGSPYGLSATTGLLDATPVNRRMQLAKHKDIQTLLTSLGLEHYIKIFVLNEIDLEVFTTLTEENLMELGIAAFGARKKLLTAIHTLLANEAACSTMPSSSSSQNSSSPRFSGSAAPGAERRPSNQW
Protein: Protein phosphatase Mn(2+)-dependent 1K (EC 3.1.3.16) (Branched-chain alpha-ketoacid dehydrogenase phosphatase) (BCKDH) (BDP) (EC 3.1.3.52) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C family member) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) ([3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase, mitochondrial) (Q8N3J5)
Organism: Homo sapiens (Human)
Function: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715, ECO:0000269|PubMed:23086801}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:A6K136}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Branched-chain alpha-ketoacid dehydrogenase kinase
- Serotonin N-acetyltransferase
Sequence:
MSTAALITLVRSGGNQVRRRVLLSSRLLQDDRRVTPTCHSSTSEPRCSRFDPDGSGSPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASQIGKRKENEDRFDFAQLTDEVLYFAVYDGHGGPAAADFCHTHMEKCIMDLLPKEKNLETLLTLAFLEIDKAFSSHARLSADATLLTSGTTATVALLRDGIELVVASVGDSRAILCRKGKPMKLTIDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKTSGVIAEPETKRIKLHHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPNEAAHAVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEINFSFSRSFASSGRWA
Protein: Receptor-binding protein pb5 (RBP-pb5) (Tail protein pb5) (P23207)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Structural component of the distal part of the tail. Mediates T5 binding to its host receptor, the E.coli outer membrane ferrichrome transporter fhuA protein. Upon binding to host FhuA, pb5 undergoes conformational changes that are probably the key to the transmission of the signal through the tail to the capsid, triggering DNA release.
Subcellular location: Virion {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36779755}. Note=Localizes at the tip of the central tail fiber. {ECO:0000269|PubMed:36779755}.
Interaction partners:
Sequence:
MSFFAGKLNNKSILSLRRGSGGDTNQHINPDSQTIFHSDMSHVIITETHSTGLRLDQGAGDYYWSEMPSRVTQLHNNDPNRVVLTEIEFSDGSRHMLSGMSMGVGAKAYGIINPQIMSQGGLKTQITASADLSLDVGYFNTGTSGTIPQKLRDGTGCQHMFGAFSGRRGFASSAMYLGGAALYKSAWSGSGYVVADAGTLTIPSDYVRHPGARNFGFNAIYVRGRSCNRVLYGMEGPNYTTGGAVQGASSSGALNFTYNPSNPESPKYSVGFARADPTNYAYWESMGDPNDSANGPIGIYSEHLGIYPSKITWYVTNLVYNGSGYNIDGGLFNGNDIKLSPREFIIKGVNVNNTSWKFINFIEKNFNVGNRADFRDVGCNLSKDSPSTGISGIATFGLPTTESNNAPSIKGGNVGGLHANVVSIYNFLPSASWYVSSNPPKIGNNYGDVWSENLLPLRLLGGSGSTILSGNIVFQGNGSVHVGTVGLDLNSSRNGAIVCTMEFIDDTWLSAGGIGCFNPTEMLSQGAEYGDSRFRIGGNTINKKLHQILSLPAGEYVPFFTIKGTVVNACKLQAAAYNPTPYWVSGLPGSVGQTGYYTLTYYMRNDGNNNISIWLDSSMSNIIGMKACLPNIKLIIQRLT