wanglab/gogpt-training-data huggingface dataset:
Protein: Cilia- and flagella-associated protein 299 (Q6V702)
Organism: Homo sapiens (Human)
Function: May be involved in spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q810M1}. Nucleus {ECO:0000250|UniProtKB:Q810M1}. Note=Mainly cytoplasmic. {ECO:0000250|UniProtKB:Q810M1}.
Interaction partners:
- Cilia- and flagella-associated protein 90
Sequence:
MDQEEGLKALDNIVTQFNAYEDFLDSQITTVDLYYLEDETLARQLVELGYRGTGERVKREDFEARKAAIEIARLAERAQQKTLTSAGKDLQDNFLTALAMREEDNRSGKLSSVIFIRDRNSHGQEISGYIDYAHRLKTEDFEVYFTGKKRLLPRPTDISFYNWDADIAVSNSSPNYQVIADNPEGLLFRYKRDRKILNVDPKAQPGDNSTRITILTELYVQAVIFDHISRRKT
Protein: Transmembrane protein (Q57X92)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cullin family profile domain-containing protein
Sequence:
MRLSYADQLIELDRQRRNIVYGRETKRFHLKIIAAISGVLYATLYVMAWLYPRGVTHVWIDDVLVEVLEDSMIEQVGGVSGCIFVASLVLLLCMSLLKESSDKDRHGKKHRSPFAGACGPYRKAPGLSVPFSPATVQSTTTAGATEVLTEPIGVKGHHDLEGEYAIRTRAELDKFLSAKELPKRMEGSLPTAHNSVNATGTVSGSMATAPAAATSISAPLAAGGGFGSVSSEGIRVQYGSGGERASAAASADRPAETMWNGLGIVDPERSQVKVRKWLSDLCQTLVEEVDSTNRWFVERQLRHFDCGHSLDETIVVPPPSSAPRVGFGVPAQPVSSPPSVRKMDALMDERNKIATQGQNVQNIDVTMHIDQRLQLEMKLDTTATFTPSSPASVAEQQARRTYVVGRIRTFASQKSLASYHHNCGDISTWRDDFPTDAHLLTHILRTCVPGFTNYVRFPHQPLNAQQHLALVVGDTGEPYFYVRYRTGAVDKTYPTQPGPNSLFEALLLFSAVARTHHGGSYGGIWGVMDLSRSGLLDVL
Protein: Scm-like with four MBT domains protein 1 (hSFMBT) (Renal ubiquitous protein 1) (Q9UHJ3)
Organism: Homo sapiens (Human)
Function: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17599839}.
Interaction partners:
- REST corepressor 1
- Transcriptional repressor protein YY1
- Proteasome subunit beta type-8
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- High mobility group protein 20A
- Proteasome subunit beta type-9
Sequence:
MNGEQQLDADAGSGMEEVELSWEDYLEETGSTAVPYGSFKHVDTRLQNGFAPGMKLEVAVRTDPETYWVATVITTCEQLLLLRYDGYGEDRRADFWCDIRKADLYPIGWCEQNKKTLEAPEGIRDKVSDWDEFLRQTLIGACSPPVPLLEGLRNGRNPLDLIAPGSRLECQAFQDSLSTWIVTVVENIGGRLKLRYEGLESSDNYEHWLYYLDPFLHHVGWAAQQGYELQPPSAIRHLKNEAEWQEILAKVKEEEEEPLPSYLFKDKQVIGIHTFSVNMKLEAVDPWSPFGISPATVVKVFDEKYFLVEMDDLRPENHARRSFVCHADSPGIFPVQWSLKNGLHISPPPGYPSQDFDWADYLKQCGAEAAPQRCFPPLISEHEFKENMKLEAVNPILPEEVCVATITAVRGSYLWLQLEGSKKPIPECIVSVESMDIFPLGWCETNGHPLSTPRRARVYKQRKIAVVQPEKQVPSSRTVHEGLRNQELNSTESVMINGKYCCPKIYFNHRCFSGPYLNKGRIAELPQCVGPGNCVLVLREVLTLLINAAYKPSRVLRELQLDKDSVWHGCGEVLKAKYKGKSYRATVEIVKTADRVTEFCRQTCIKLECCPNLFGPRMVLDKCSENCSVLTKTKYTHYYGKKKNKRIGRPPGGHSNLACALKKASKRRKRRKNVFVHKKKRSSASVDNTPAGSPQGSGGEDEDDPDEGDDDSLSEGSTSEQQDELQEESEMSEKKSCSSSPTQSEISTSLPPDRQRRKRELRTFSFSDDENKPPSPKEIRIEVAERLHLDSNPLKWSVADVVRFIRSTDCAPLARIFLDQEIDGQALLLLTLPTVQECMDLKLGPAIKLCHHIERIKFAFYEQFAN
Protein: GM02257p (Q8MSZ7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTNAAIDLALDRVDWRDLAAQTEEQPRVYTPGEVLMPEAGFMRGHGTFVEDENIKSSVAGVIQKVNKLISVRPLKSRYVGEIGDVVVARVSEVQQKRWRVDTNSRLDSILLLSSVNLPGGELRRRSAEDEQMMRRYLDEGDLISAEVQNIFEEGSLSLYTRSLKYGKLSQGILVKVFPALVKRRKMHFHNLPCGASVILGNNGYIWISPTKGQEEEGGEGGFAQNLNEHVPRADREVIARLRNSILALAKCKLMIYDTSIQYAYEESLRYEAHELLQQNAIYDIGQQTQGRLRDADE
Protein: Single-strand DNA endonuclease 1 (AtSEND1) (EC 3.1.-.-) (Flap endonuclease GEN-like 2) (XPG-like endonuclease 2) (Q9M2Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA with a specific cleavage site in the 5' overhang strand exactly one nucleotide 3' of the branch point. Structure- and sequence-specific nuclease that resolves holliday junctions (HJs) by symmetrically oriented incisions in two opposing strands near the junction point, thus leading to ligatable products; HJs are physical links between homologous DNA molecules that arise as central intermediary structures during homologous recombination and repair in meiotic and somatic cells. Structure-specific nuclease with 5'-flap endonuclease activity, preferentially cleaving static flaps 5' overhang strand exactly one nucleotide in the 3' direction of the branch point and, to lower extent, on the two neighboring positions. Also able to cleave double-stranded flap strand 1 one nucleotide in the 3' direction of the branch point. Together with MUS81, essential for the resolution of toxic replication structures to ensure genome stability, and to maintain telomere integrity and replication.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q17RS7}.
Interaction partners:
- DNA ligase 6
- Proliferating cell nuclear antigen 2
- Proliferating cellular nuclear antigen 1
- Serine/threonine-protein kinase ATG1t
- DNA polymerase delta catalytic subunit
- DNA replication ATP-dependent helicase/nuclease JHS1
- DNA polymerase delta small subunit
- DNA mismatch repair protein MSH1, mitochondrial
- DNA repair protein RAD50
- Chlorophyll a-b binding protein 3, chloroplastic
Sequence:
MGVKYLWDVLEPCKKTFPLDHLQNKRVCVDLSCWMVELHKVNKSYCATKEKVYLRGFFHRLRALIALNCSIILVSDGAIPGIKVPTYKRRLKARFEIADDGVEPSKETSLKRNMGSEFSCIIKEAKVIASTLGILCLDGIEEAEAQCALLNSESLCDACFSFDSDIFLFGAKTVYREICLGEGGYVVCYEMDDIKKKLGLGRNSLIALALLLGSDYSQGVRGLRQEKACELVRSIGDNVILEKVASEGLSFAEKPRKSKKQVRPSVCSKKGTLPLVVINGNNRDPERLEEIKQVIDAFMNPKCHQADSNTVSRALAEFSFQRTKLQEICHQFFEWPPEKTDEYILPKVAERNLRRFANLQSRSTEVEVNLPLHKPQMPEKCPVSEIIKTRKVQGRECFEVSWNDLEGLESSIVPADLVERACPEKIIEFKEKMAAKKKKPKPKQKQKETSSPTKSSSLVELSLELQHLDLNSTSLVSRSTLEEAEQENEQQNSKKHDYLRLIDSPDRENCNNAWSNRDRLGVGMSSFPLYPETEVIDLISPCPEARSRSVSRSYQEQKSHDHQLETVIELSDSETDDEEHCKKARELRIFLQNIRKDIIL
Protein: Outer envelope pore protein 24B, chloroplastic (Chloroplastic outer envelope pore protein of 24 kDa B) (Q8H0Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-conductance voltage-dependent solute channel with a slight selectivity for cations transporting triosephosphates, dicarboxylic acids, ATP, inorganic phosphate (Pi), sugars, and positively or negatively charged amino acids.
Subcellular location: Plastid, etioplast membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Plastid, chloroplast outer membrane; Multi-pass membrane protein. Note=Present in non-green root plastids. {ECO:0000250}.
Interaction partners:
- Putative pumilio homolog 7, chloroplastic
- F21B7.2
- At2g39980/T28M21.14
- Outer envelope pore protein 24A, chloroplastic
Sequence:
MAMKASIKGKYDTDKTSGIGSLAFNAGDIKLRATMTDATLVAGPTLTGLALAVEKPGSFIVEYNVPKKDVRFQFMNTVRIAEKPLNLTYIHSRADNRTIVDGSLVIDSANKLSANHMVGTNNCKIKYTYAHGGLATFEPCYDLAKNTWDFAVSRRFYSGDNVRATYQTSSKLLGMEWSRNNKASGFKVCASVNLADELKTPKLTAETTWNLEM
Protein: Nuclear receptor coactivator 4 (E9PVM8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAQGTVSRMNTSLEQSGCYSNRETLLRCSDARRELELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLNEQVDLIYQLKEETLQQQAQQLYWLMGQFNCLIHQLEYTQNKDLANQVSVCLE
Protein: Type III chaperone ShcS1 (Q87WF2)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- Type III effector HopS1
Sequence:
MNAFATGQLEYSLKKLGYDAAALQALREEGYLLWKGKNDQTSLLVPSADLDALFVINTLSYIDPEHDGRLLALALHLNLSPVHTMSACIALDVEQNTLCLRYTHDLGGSGADTLLLALENAQALAEQVRQVIETFRRDQGRPSGQTSLSRQSSALMR
Protein: Ethylene-responsive transcription factor ABI4 (ERF ABI4) (Protein ABSCISIC ACID INSENSITIVE 4) (Protein GLUCOSE INSENSITIVE 6) (Protein IMPAIRED SUCROSE INDUCTION 3) (Protein SALOBRENO 5) (Protein SUCROSE UNCOUPLED 6) (Protein SUGAR INSENSITIVE 5) (A0MES8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription regulator that probably binds to the GCC-box pathogenesis-related promoter element. Binds also to the S-box (5'-CACTTCCA-3') photosynthesis-associated nuclear genes-related (PhANGs-related) promoter element, and thus acts as a transcription inhibitor. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. May have a function in the deetiolation process. Confers sensitivity to abscisic acid (ABA), and regulates the ABA signaling pathway during seed germination, upon nitrate-mediated lateral root inhibition, in hexokinase-dependent sugar responses (including feed-back regulation of photosynthesis and mobilization of storage lipid during germination), and in response to osmotic stress mediated by NaCl, KCl or mannitol. Plays a role in sucrose sensing or signaling, especially at low fluence far red light. Also involved in plant response to glucose treatment, especially at low concentration and in young seedlings. Required for the trehalose-mediated root inhibition and starch accumulation in cotyledons, probably by inhibiting starch breakdown. However, seems to not be involved in sugar-mediated senescence. Required for the ABA-dependent beta-amino-butyric acid (BABA) signaling pathway. BABA primes ABA synthesis and promotes resistance to drought and salt, and leads to a prime callose accumulation that confers resistance against necrotrophic pathogens such as A.brassicicola and P.cucumerina. Seems to be involved in resistance to S.sclerotiorum probably by regulating the ABA-mediated stomatal closure apparently by antagonistic interaction with oxalate. Negative regulator of low water potential-induced Pro accumulation whose effect is decreased by high levels of sugar.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:24451981}.
Interaction partners:
- Protein ABSCISIC ACID-INSENSITIVE 5
- B3 domain-containing transcription factor ABI3
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- Protein phosphatase 2C 56
- Xanthoxin dehydrogenase
- Protein phosphatase 2C 77
- Histone deacetylase 9
- Abscisic acid 8'-hydroxylase 2
- Molybdenum cofactor sulfurase
- GDP-L-galactose phosphorylase 1
Sequence:
MDPLASQHQHNHLEDNNQTLTHNNPQSDSTTDSSTSSAQRKRKGKGGPDNSKFRYRGVRQRSWGKWVAEIREPRKRTRKWLGTFATAEDAARAYDRAAVYLYGSRAQLNLTPSSPSSVSSSSSSVSAASSPSTSSSSTQTLRPLLPRPAAATVGGGANFGPYGIPFNNNIFLNGGTSMLCPSYGFFPQQQQQQNQMVQMGQFQHQQYQNLHSNTNNNKISDIELTDVPVTNSTSFHHEVALGQEQGGSGCNNNSSMEDLNSLAGSVGSSLSITHPPPLVDPVCSMGLDPGYMVGDGSSTIWPFGGEEEYSHNWGSIWDFIDPILGEFY
Protein: Zn-dependent hydrolases, including glyoxylases (Q8NQQ1)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
Sequence:
MTNELTLHHISVSQMDNNCYLLAANGNGLLIDAADDAAALLKLAEDAGVTITKVLTTHRHADHVRALPEVLQKTGATHYAPFLEVPALPSAVDVELHHGDSIEFEGHVFPISILRGHTPGGAVLTAEIDGKTHLFVGDSLFPGGLGKTSSEGDFVRLFNDVKERIFDTYDDDSIVWPGHGKETTLGAERPQLEIWWERRW
Protein: Apoptosis regulator BAX (Q07813)
Organism: Mus musculus (Mouse)
Function: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. BAX deficiency leads to lymphoid hyperplasia and male sterility, because of the cessation of sperm production.
Subcellular location: [Isoform Alpha]: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}. Nucleus {ECO:0000250|UniProtKB:Q07812}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane (By similarity). {ECO:0000250|UniProtKB:Q07812}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000250}.
Interaction partners:
- Apoptosis regulator Bcl-2
- BH3-interacting domain death agonist
- Bcl-2-like protein 11
- Bcl-2-like protein 1
- Cytochrome c, somatic
- Cytochrome c, testis-specific
- Bcl-2 homologous antagonist/killer
- Cellular tumor antigen p53
- Apoptosis-inducing factor 1, mitochondrial
- Bcl-2-binding component 3
Sequence:
MDGSGEQLGSGGPTSSEQIMKTGAFLLQGFIQDRAGRMAGETPELTLEQPPQDASTKKLSECLRRIGDELDSNMELQRMIADVDTDSPREVFFRVAADMFADGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLVWIQDQGGWEGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG
Protein: Prominin-2 (PROM-2) (Prominin-like protein 2) (mPROML2) (Q3UUY6)
Organism: Mus musculus (Mouse)
Subcellular location: Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium membrane; Multi-pass membrane protein. Note=Colocalizes with PROM1 (By similarity). Associates with membrane in a cholesterol-dependent manner. Localizes to the apical and basolateral membranes of epithelial cells. {ECO:0000250}.
Interaction partners:
Sequence:
MTRSPGLMVPLLGLSLGLALSLPEAVTDDCGSLGRVEHLAFARVPRTRELAPLVRASGPLNSLYGTVRRFLSVVQLNPFPAELIKTLLNDPSSVKTDEVVRYEAGYVVCAVIAGLYLLLVPITGLCFCCCRCRQRCGGRVKTEHKAMACERGTLMIFLLLTTLVLLIGMVCAFATNQHTHSQTGPSVKAVPETLLSLRGLVSDVPEELRAIAEQFSVPQKQVSKELDGVGENLGNVIHNRLKSTVYPVLASVHSLGQALQVSIDHLRALNTTSVELQEAQRHLEPPVQAHRERLLALLQDSWCHEENCKRVLSQAGALQLGADFSQTPPVDDVLHRLKDVPETNFSSMVQEEKATFNNLPLLVQVQAVSVVKDVKKALAEQPEGLRMLAQAFPGSEAASRWSQALEGLEQRSRPYLQEVQQYETYRWILGCVLCSAILLVVICNLLGLSLGIWGLFAREDPSHSETKGEAGARLLMAGVAFSFLFAVPLILLVFVTFLVGGNVQTLVCRSWESGELYEFADTPGNLPPSMNLSYLLGLKKNISIVQAYRQCKAGAVLWKVLQLNDSYDLDKHLDIKQYTHKIQQELQSFQVDLKELDLLSPTARQDLEALQRSGLEKIHYRGFLVQIQKPVVNTDMWQLAQELEGLAQAQNDSLLRQQLREEARELRSLYQEKVVPQESLVTKLNFSVKTLESLAPSLQVNTSDFLDSVTRLKGELPVQINHILRNATECFLTREMGYFSQYVTWVRAEVTQRIATCQPFSTALDNGHVILCDMMADPWNAFWFCLGWCTFFLIPSIIFAVKTSKYFRPIRKRLSSTSSEETQLFHIPRVTSLKL
Protein: Aminopeptidase YpdF (EC 3.4.11.-) (P76524)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.
Interaction partners:
- Aminopeptidase YpdE
- PTS system fructose-like EIIB component 1
- Cytosol aminopeptidase
- Fructose-like permease IIC component 1
- Multiphosphoryl transfer protein 1
Sequence:
MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYVEVEARAQGYQLHLLDATNTLTTIVNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAESHLLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLLTGEA
Protein: Predicted transcriptional regulators (Q8NP59)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Phage shock protein A
- Uncharacterized protein
- RNA polymerase-binding protein RbpA
- DUF4193 domain-containing protein
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
Sequence:
MVTYTTLLDKPISESAPRKAPEPLLREALGAALRSFRADKGVTLRELAEASRVSPGYLSELERGRKEVSSELLASVCHALGASVADVLIEAAGSMALQAAQEDLARV
Protein: Ubiquitin-ribosomal protein eL40A fusion protein [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40A (60S ribosomal protein L40-A) (CEP52)] (P0CH08)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40A]: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Polyubiquitin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL6A
- Large ribosomal subunit protein eL30
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCDKSVCRKCYARLPPRATNCRKRKCGHTNQLRPKKKLK
Protein: Non-structural protein 1 (NS1) (NS1A) (Q99AU3)
Organism: Influenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
Function: Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Note=In uninfected, transfected cells, NS1 is localized in the nucleus. Only in virus infected cells, the nuclear export signal is unveiled, presumably by a viral protein, and a fraction of NS1 is exported in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04066}.
Interaction partners:
Sequence:
MDSNTVSSFQVDCFLWHVRKRFADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILKEESDEALKMTIASVPASRYLTDMTLEEMSRDWFMLMPKQKVAGSLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTDEDVKNAVGVLIGGLEWNDNTVRVSETLQRFAWRSSNENGRPPLPPKQKRKMARTIKSEV
Protein: Olfactory receptor 14A2 (Olfactory receptor 5AX1) (Olfactory receptor OR1-31) (Q96R54)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MANVTLVTGFLLMGFSNIQKLRILYGVLFLLIYLAALMSNLLIITLITLDVKLQTPMYFFLKNLSFLDVFLVSVPIPKFIVNNLTHNNSISILGCAFQLLLMTSFSAGEIFILTAMSYDRYVAICCPLNYEVIMNTGVCVLMASVSWAIGGLFGTAYTAGTFSMPFCGSSVIPQFFCDVPSLLRISCSETLMVIYAGIGVGACLSISCFICIVISYIYIFSTVLKIPTTKGQSKAFSTCFPHLTVFTVFIITAYFVYLKPPSNSPSVIDRLLSVIYTVMPPVFNPVTYSLRNNDMKCALIRLLQKTYGQEAYFI
Protein: C-C chemokine receptor type 7 (C-C CKR-7) (CC-CKR-7) (CCR-7) (Epstein-Barr virus-induced G-protein coupled receptor 1) (EBI1) (EBV-induced G-protein coupled receptor 1) (MIP-3 beta receptor) (CD antigen CD197) (P47774)
Organism: Mus musculus (Mouse)
Function: Receptor for the MIP-3-beta chemokine.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 19
- C-C motif chemokine
- Stromal cell-derived factor 1
- C-C motif chemokine 21a
- C-C motif chemokine 25
- C-X-C motif chemokine 13
- C-C motif chemokine 4
- C-C motif chemokine 20
- C-C motif chemokine 21b
- C-C motif chemokine 5
Sequence:
MDPGKPRKNVLVVALLVIFQVCFCQDEVTDDYIGENTTVDYTLYESVCFKKDVRNFKAWFLPLMYSVICFVGLLGNGLVILTYIYFKRLKTMTDTYLLNLAVADILFLLILPFWAYSEAKSWIFGVYLCKGIFGIYKLSFFSGMLLLLCISIDRYVAIVQAVSAHRHRARVLLISKLSCVGIWMLALFLSIPELLYSGLQKNSGEDTLRCSLVSAQVEALITIQVAQMVFGFLVPMLAMSFCYLIIIRTLLQARNFERNKAIKVIIAVVVVFIVFQLPYNGVVLAQTVANFNITNSSCETSKQLNIAYDVTYSLASVRCCVNPFLYAFIGVKFRSDLFKLFKDLGCLSQERLRHWSSCRHVRNASVSMEAETTTTFSP
Protein: AT4g32480/F8B4_180 (Sugar phosphate exchanger, putative (DUF506)) (Q9SUU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Early nodulin-like protein 4
- ATP-dependent 6-phosphofructokinase 3
Sequence:
MDRQSSDDIMKFLDGMASSDDVLFGFLDEGNHSPEDYNFAAGDESEVDNDTTDCNSEENRKFWQEHEQLLQATLYRTSSIETKIRQATKEALKVVRSKGLVCVCRRPVTDGCRSCLRGEVSSLLREAGYDCVISKSKWRSSHEIPAGEHEYLEVVDKSVSKKGEIRVVIELCFRAEFEMARGSEEYKRLIGMLPEVYVGKTERLKSLIKILCTAAKKCMKDKKMHMGPWRKHKYMQAKWFGTCERKSVSPVSETEENMFPVAKQRVSMLNYGLFGAGIGRPTVVAVV
Protein: Viral late gene transcription factor 3 (VLTF-3) (Trans-activator protein A2) (P68318)
Organism: Vaccinia virus (strain Copenhagen) (VACV)
Function: Acts with RNA polymerase to initiate transcription from late gene promoters.
Interaction partners:
Sequence:
MNLRLCSGCRHNGIVSEQGYEYCIFCESVFQKCTKVQKKSNFHVSNKLIHLRNVLRRLLSHQCSGEIISELLDIMEKNQISTDDVDANFVSSFLKANERINKKDYKLVFEIINQVKDEKLNLSTEKINEVVEIFKHLVFFCQENTPSKTINYSFFLDKIFDITSVTKNLKPQTVKNYTKNNSNQLVWENFLAHMRSKKRVTMVEDYGHEYVFVDERFSTCSLEV
Protein: Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) (Q5T9B7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03171}.
Interaction partners:
Sequence:
MGCCSSSDPRREDDLRAREKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK