wanglab/gogpt-training-data huggingface dataset:
Protein: Mutual gliding-motility protein MglA (Q1DB04)
Organism: Myxococcus xanthus (strain DK1622)
Function: Required for multicellular development and for both mechanisms of gliding: social (S) and adventurous (A) motility. Acts as an intracellular switch to coordinate A and S motilities. Controls the direction of gliding and gliding speed.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1938957}.
Interaction partners:
- Gliding motility protein MglB
- Adventurous-gliding motility protein Z
- GTPase
- Response regulator FrzS
- Response regulator FrzZ
- Signal recognition particle receptor FtsY
- PatA-like N-terminal domain-containing protein
- PatA-like N-terminal domain-containing protein
- Tyrosine-protein kinase MasK
- TPR domain protein
Sequence:
MSFINYSSREINCKIVYYGPGLCGKTTNLQYIYNKTAAETKGKLISLSTETDRTLFFDFLPLSLGEIRGFKTRFHLYTVPGQVFYDASRKLILKGVDGVVFVADSQIERMEANMESLENLRINLAEQGYDLNKIPYVIQYNKRDLPNAVTVEEMRKALNHRNIPEYQAVAPTGVGVFDTLKAVAKLVLTELKKGG
Protein: Large ribosomal subunit protein uL14c (50S ribosomal protein L14, chloroplastic) (P0C440)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds to 23S rRNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein uL16c
- 50S ribosomal protein L16
- 60S ribosomal protein L2
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein uL2cz/uL2cy
- 60S ribosomal protein L29
- Small ribosomal subunit protein uS8c
- Os08g0116500 protein
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein bL36c
Sequence:
MIQPQTLLNVADNSGARKLMCIRVIGAASNQRYARIGDVIVAVIKDAVPQMPLERSEVIRAVIVRTCKEFKCEDGIIIRYDDNAAVIIDQKGNPKGTRVFGAIAEELRELNFTKIVSLAPEVL
Protein: Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (SDH) (EC 1.5.1.7) (Lysine--2-oxoglutarate reductase) (P38998)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysine biosynthesis.
Subcellular location: Peroxisome {ECO:0000269|PubMed:26928762, ECO:0000269|PubMed:28928432}.
Interaction partners:
- Saccharopine dehydrogenase [NADP
- Lysine biosynthesis regulatory protein LYS14
- L-2-aminoadipate reductase
- Homocitrate synthase, cytosolic isozyme
- Homoaconitase, mitochondrial
- Homoisocitrate dehydrogenase, mitochondrial
- Homocitrate synthase, mitochondrial
- Argininosuccinate synthase
- Argininosuccinate lyase
- Protein ARG5,6
Sequence:
MAAVTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYRQAGAIIVPAGSWKTAPRDRIIIGLKEMPETDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDEDLPAVSPYPNEKALVKDVTKDYKEALATGARKPTVLIIGALGRCGSGAIDLLHKVGIPDANILKWDIKETSRGGPFDEIPQADIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPTVLVPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLPQRKTAPVWVRAKKLFDRHCARVKRSSRL
Protein: Protoheme IX farnesyltransferase 2 (EC 2.5.1.141) (Heme B farnesyltransferase 2) (Heme O synthase 2) (Q9I423)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00154}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00154}.
Interaction partners:
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Heme A synthase
- Cytochrome c oxidase assembly protein CtaG
- Ferrochelatase
- Protoheme IX farnesyltransferase 1
- Cytochrome c oxidase subunit 1
- Heme oxygenase PigA
Sequence:
MKLKRYLLVAKPGIIFGNLIAVAGGYFLAARGSVEPMLLLATVIGLSLVVASGCVLNNCIDRDIDRHMERTRGRVTVTGQISLKAALAHGLVLGVAGFGLLWWRTNPLTTALAGFGYFVYVGLYSLWFKRRSQYGTLVGSLSGAMPPVVGYCAVSGQFDAGAASLLAIFCLWQMPHSYAIAIFRLKDYEAAGIPVLPVARGIAVTKIHIVLYILAFMAATLALCLGGYAGYGYLLVAVAVSLWWLAIALTGYWTADDRVWARKLFAFSIVAITALSVMMSIDFQVAPATHLVASLF
Protein: Cell division response regulator DivK (Q45976)
Organism: Caulobacter vibrioides (Caulobacter crescentus)
Interaction partners:
Sequence:
MTKKVLIVEDNELNMKLFHDLLEAQGYETLQTREGLSALSIARENKPDLILMDIQLPEISGLEVTKWLKEDDDLAHIPVVAVTAFAMKGDEERIREGGCEAYISKPISVVHFLETIKRLLERQPA
Protein: Small ribosomal subunit protein bS18m (37S ribosomal protein RSM18, mitochondrial) (P40033)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS42
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS23
Sequence:
MQPIIKGAVSSTFKRALYNFGIKEKKSVNIEMGRTQQTKKIDQSLSKKLPKGTIYDPFDFSMGRIHLDRKYQANKNSNRNDIMKSGANPLEFYARPRILSRYVTSTGRIQHRDITGLSAKNQRRLSKAIRRCQAIGLM
Protein: Transmembrane protein 33 (Protein DB83) (SHINC-3) (P57088)
Organism: Homo sapiens (Human)
Function: Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling. Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis. Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus envelope {ECO:0000269|PubMed:25612671}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Co-localizes with RTN4 at the ER sheets. {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:25612671}.
Interaction partners:
- Reticulon-1
- E3 ubiquitin-protein ligase RNF26
- Endonuclease domain-containing 1 protein
Sequence:
MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLSRAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDARGSNSLPLLRSVLDKLSANQQNILKFIACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRTLFNELRIVVEHIIMKPACPLFVRRLCLQSIAFISRLAPTVP
Protein: FBD-associated F-box protein At3g49020 (Q9SMT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEQKCKIGGEGLRNRGLVNEEDRISELPEALLLLILSSLPTETVIATSVLSKQWKSLWKLVPNLKFDSKYHYHYTFSDNVFRSLISHKAPVLDSLHLKVEDKDDALDVGILIGIAFSRHMRKFVLKITLLEESFVRFPSAWCSCNDTLEILELKYCILLDFPSLVCLKSLRKLYLYHVRFNDEESVCNLLCGCPSLEDLVVHRHSTTDVESYTIAVPSLQRLTIYDDYYGEGVGGYVINAPSLKYLNIDGFNGLEFCLIEKAPELVEAKISAVFEIANENIMDSLTSAKCLSLHLAPFKIKYPTGKIFYQLLSLELRAYSYEWWNLLWFMLDSSPKLQILKLVDPYQFPKEDCSVGWEWSRPKCVPECLLFHLETFVWTRYEWQREDEKAVATYILKNARCLKKATLSTKPIGSEELEKLGKRREMLNELATQASPSNSCNLVFESE
Protein: Son of sevenless homolog (Guanine nucleotide exchange factor for RAS) (Q9N5D3)
Organism: Caenorhabditis elegans
Function: Promotes the exchange of Ras-bound GDP by GTP (By similarity). May regulate signaling pathways downstream of receptor tyrosine kinase, egl-15 and let-23. Required for larval and male spicule development, fluid homeostasis, vulva induction, spermatogenesis, and oogenesis by promoting meiosis prophase exit during oocyte maturation. Required for the delamination of G1 cell by promoting the loss of cell junctions and detachment from the excretory system during larval development. Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine. Regulates synaptic levels of nAchR subunit lev-1 in the nerve cord.
Interaction partners:
- Sex muscle abnormal protein 5
- Ras protein let-60
- Receptor tyrosine-protein kinase let-23
- GTP binding protein
- Tyrosine-protein phosphatase non-receptor type ptp-2
- GTP binding protein
- Inactive tyrosine-protein kinase kin-32
- SHC-transforming protein homolog 1
- Mss4 protein
- Raf homolog serine/threonine-protein kinase
Sequence:
MSIMSISLHSASSDTVSLTSRRTISTSKHWAAIFDERIYQICNIVHPGLPIDNAAVEHIRYFLQSIVFELIEARATSVVEVDKTAKKLFAFGLQTVCKEAWDNMHQQLQKHKYQKALKTVLESQHRLAAVIKETLGPREKEKKDREKKEIERIACYIYYACESVTEDVLRLTGNYVKNIRNSEQKITMANLDVAMNGDKALMELRTKLRNEEEAESPGGFGFLSEFEEFVAEETEEKTLSNSQTYESVAVDFLRDERRFIRELNRINVFRRRIESVAATDVDKQIVCNLFGNLTEIHDLALKIERTLEDAIELSDTQCIGMGIWEHGEAYEFDTYTFYIRRDGGEMNETRHATYVINDNIKALLESERFASLFQSGEHYLGSSLDGQSFRLAVQYVLPQLLHIPIFHIYQYHEYITRLHQLSSSEEDRRDLNDCRSAFERVVGCVSDMSPELKTKITQFLDQQAKSEKIYNVKRLNEIQSSIDGFTGSPIGKTCNELEKDGDLGMIRPSLQFSSEITKNKKWKTERFVYIFDQMIVLCKRHRNTLKFKDRLAVHSIDVFDIPDSEVTNCFKIESHDKSSLPKIYHFVCKNPEEKRQWMAVLVKVTTKSVLDRILDNHEKEEAKRIPLVVPGPDQYRFSEPDTEDNISFEDYTSSSGIPVIKCGTVLKLIERLTYHSYTDSKYILTFLISYRSFCTPNDLFSLLLERFNIPTPKKLQQPKQGGGPLAGRYDTVQSHGLSAISSSSCINPLCEQKFRKEFQQPIQLRVLSVINQWVKLHWYDFQCDPVLLDALELFLNRCCDPREGLSKQHKKFCKTILALIEKRVKNPPGIMQQPNENGDKGAADEGHVNSAFVFGDDQQHPPQHQVYTNESPKETNQVLWHTAQKGDVDHYDLLTLHPIEIGRQLTLLHSDLYRAIQPIELVEAAWTKAEKWRKSPQLLRLTDHSTLLTYWVSRSIVETESLEERMAMFNRVLEVMSVFEELHNFTGLVAFYSALNSSCIFRLKWCWDGLDNEKKKCFDRFNTLCERRWQEMQKRLSSINPPCIPFFGHYLSNIYFLEQGNSTFVNKSPPHGAAGAQKQQKDDLKASDPENSNKQFKQLVSFLKLRKISNVIREIQIFQDQRYSLTLEPTIRQFFESINPKNDFKSNEDLEEYLYNKSLEIQPKGLDTPTAELKPKHNASTLRSPGVKPPKAAGNHYSANHPIGLHLHSQNSHSAPHAMSSQSSTVPNTPLSAHETKRSLSHNQDDAPLQQFVDIRFERKGTHPKIPVLQPPPLLPRSSRANQSNSVSLPPTTQAPMPPAPKSSGMMSTATSPTTLTTTTTPSSAGGPPPKLHPRRMTQQPMSPLAKSPLTPSRDNSSPSAFQFPVVYEASTAPPLPPRPSTSSDVSSSPSTSGSTSSATKENQEQLRVIFDREESHSPTVRLSVPLPPALPPPRGSSVFRAPPPLPPKSNRHNSNSPTLSSEQPFEDPMSPSIFVNTPPPPLPPKTYRSSNK
Protein: Dehydrodolichyl diphosphate synthase 3 (Dedol-PP synthase 3) (EC 2.5.1.-) (Q8RX73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein.
Interaction partners:
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Farnesyl pyrophosphate synthase 1, mitochondrial
- (Z)-gamma-bisabolene synthase 1 (Terpenoid synthase 12) (AtTPS12)
- Alpha-humulene/
- Cysteine/Histidine-rich C1 domain family protein
- Inactive squalene synthase 2
- Phytoene synthase 1, chloroplastic
- Squalene synthase 1
Sequence:
MLSILSSLLSLLFLFIISCFFITSHFWFPLSLPKILGFIKITSSRDDYDNEQRDEGTYVVGVEELQRELMPRHVAVIMDGNRRWAKRAGLLTSQGHEAGAKRLIEFSELCFKLGIHTVSAFAFSTENWGRHKIEVKCLMSLIQHYLKSKIQYFQREETRVSVIGNLTKIPESLLRTVQEIEEATRSYKKKHLILAIDYSGRLDILRACKSIVKKSEKGLIREEDVDEALIERELLTNCTEFPSPDLLIRTSGEQRISNFFLWQLAYTELFFSPVLWPDFDKDKLLEALVSYQRRERRFGCRV
Protein: Systemic RNA interference defective protein 2 (G5EEV9)
Organism: Caenorhabditis elegans
Function: Plays a role in RNA-mediated gene silencing by mediating endocytic uptake of double-stranded RNA (dsRNA) ingested from the environment into intestinal cells from the intestinal lumen. Selective for dsRNAs of at least 50 bp. Required for avoidance behavior induced by small RNAs derived from pathogenic bacteria such as P.aeruginosa.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}; Single-pass type I membrane protein {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}. Cytoplasm {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}. Note=Localizes to the apical membrane of intestinal cells and also to punctate cytoplasmic structures. {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}.
Interaction partners:
- Systemic RNA interference defective protein 1
- Systemic RNA interference defective protein 5
- Tyrosine-protein kinase sid-3
- ENTH domain-containing protein
- DRBM domain-containing protein
- Tudor domain-containing protein
- RSD-2 domain-containing protein
Sequence:
MPRFVYFCFALIALLPISWTMDGILITDVEIHVDVCQISCKASNTASLLINDAPFTPMCNSAGDQIFFTYNGTAAISDLKNVTFILEVTTDTKNCTFTANYTGYFTPDPKSKPFQLGFASATLNRDMGKVTKTIMEDSGEMVEQDFSNSSAVPTPASTTPLPQSTVAHLTIAYVHLQYEETKTVVNKNGGAVAVAVIEGIALIAILAFLGYRTMVNHKLQNSTRTNGLYGYDNNNSSRITVPDAMRMSDIPPPRDPMYASPPTPLSQPTPARNTVMTTQELVVPTANSSAAQPSTTSNGQFNDPFATLESW
Protein: Protein NKG7 (Natural killer cell protein 7) (Q99PA5)
Organism: Mus musculus (Mouse)
Function: Regulates cytotoxic granule exocytosis in effector lymphocytes, thus acting as a critical mediator of inflammation in a broad range of infectious and non-infectious diseases. Essential for cytotoxic degranulation of natural killer (NK) cells and CD8(+) T-cells and for the activation of CD4(+) T-cells following infection. Plays a critical role in CD8(+) T-cell and NK cell-mediated cytolysis of target cells and contributes to the cytolytic activity via the perforin/granzyme pathway by enhancing exocytosis of LAMP1-carrying lytic granules. Contributes to NK cell-mediated control of cancer metastasis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16617}; Multi-pass membrane protein {ECO:0000255}. Cytolytic granule membrane {ECO:0000305|PubMed:32839608}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Granzyme A
- Natural killer cells antigen CD94
- Granzyme K
- Perforin-1
- Cathepsin W
- Granzyme B
- T-cell surface glycoprotein CD3 delta chain
- C-C motif chemokine 5
- Cystatin-F
- T-cell surface glycoprotein CD3 gamma chain
Sequence:
MEPCRSLALFAGSLGLTSSLIALTTDFWIVATGPHFSAHSGLWPTSQETQVAGYIHVTQSFCILAVLWGLVSVSFLILSCIPALSAPGRGPLVSTVMAFSAALSILVAMAVYTSMRWSQTPFSQVQTFFSWSFYLGWVSFILFLFAGCLSLGAHCRTRRAEYETL
Protein: DNA polymerase III subunit theta (EC 2.7.7.7) (P0ABS8)
Organism: Escherichia coli (strain K12)
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Interaction partners:
- DNA polymerase III subunit epsilon
- DNA polymerase III subunit alpha
- Beta sliding clamp
- DNA polymerase III subunit tau
- DNA polymerase III subunit delta'
- DNA polymerase III subunit psi
- DNA polymerase III subunit delta
- DNA polymerase III subunit chi
- Protein UmuD
- Protein UmuC
Sequence:
MLKNLAKLDQTEMDKVNVDLAAAGVAFKERYNMPVIAEAVEREQPEHLRSWFRERLIAHRLASVNLSRLPYEPKLK
Protein: Oxysterol-binding protein 8 (OSBPh) (Q54QP6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Major sperm protein domain-containing protein
Sequence:
MFSGALNYMKGLVGTNENLQVEESGDNKGDIEPEQRKGLLKQLSSYVGKDITSLISLPVWIFEPVSFLQVMSEPLQYNALLSKASKQDSEFLCLAYLAAFNCALYSTAVRTRKPFNPILGETFEIVDKKGEFRFLAEQVSHHPPIGVSETISEDYTLQLETLLKSKFYGNSSEVEIDGTNHFFNKKTNHHYTWNHLVTCCHNIIIGSLWLDHYGDLVIENHTTGSKAVLKFAKSGWLGAGRYGVTGEIVDCEGDVRYRITGKWNESIQLFQVMDNGSSSTTSTCLWEASKEPINNKFLFPRWVEENVIDLNDEYKKILPVTDSRLRADRIALEEGNLDVAAKEKHNLEEKQREDKRQRVAENKEWETAQFKKVDDAKFGYRWNYCGNYWEEREERVKAAASN
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q9W0Q2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Puff-specific protein Bx42
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor Syf2
- Cell division cycle 5, isoform A
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing-splicing factor 8
- RNA helicase
- Pre-mRNA-processing factor 19
- Probable small nuclear ribonucleoprotein G
- peptidylprolyl isomerase
Sequence:
MLSLSDPNNAGGIPDKAWQPHFVTLETSMGEITVELYWKHAPNTCRNFAELSRRGYYNNVVFHRIIRDFMIQGGDPTGTGRGGASIYGSEFADELHGDLRHTGAGILSMANSGPDTNGSQFFITLAPTQWLDGKHTIFGRVYTGMEVVKRIGMVETDKNDRPVDPLRIIKAKVEKL
Protein: DNA dC->dU-editing enzyme APOBEC-3B (A3B) (EC 3.5.4.38) (Phorbolin-1-related protein) (Phorbolin-2/3) (Q9UH17)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.
Subcellular location: Nucleus {ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22915799}.
Interaction partners:
- DNA dC->dU-editing enzyme APOBEC-3A
- Cullin-5
- Cytidine deaminase
- Putative C->U-editing enzyme APOBEC-4
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- DNA dC->dU-editing enzyme APOBEC-3H
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
Sequence:
MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAILQNQGN
Protein: Uncharacterized protein (Q38FG8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- C2H2-type domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Large ribosomal subunit protein uL4m
Sequence:
MRRLGVFCRGQRNSPLLTRGIATGGRVTNEDRRWWLVHLECAPDVTPGTFIAWLDCCGTHTCKKLIERNIWTIEQVAALDSDQVDELKYREGCLKMDVVWEHARTIITPLRQREVTGGVESELQGRIMELRKKRELERRREEILKERANVSEQREETLRKLREAIAAKKAAMLQKKQAASEAYGGSSDGGARKEGAEE
Protein: Outer capsid protein mu-1 (Mu1) [Cleaved into: Outer capsid protein mu-1N; Outer capsid protein mu-1C] (P11077)
Organism: Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Function: Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.
Subcellular location: [Outer capsid protein mu-1]: Virion. Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Host endoplasmic reticulum. Host mitochondrion. Note=Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MGNASSIVQTINVTGDGNVFKPSAETSSTAVPSLSLSPGMLNPGGVPWIAIGDETSVTSPGALRRMTSKDIPETAIINTDNSSGAVPSESALVPYNDEPLVVVTEHAIANFTKAEMALEFNREFLDKLRVLSVSPKYSDLLTYVDCYVGVSARQALNNFQKQVPVITPTRQTMYVDSIQAALKALEKWEIDLRVAQTLLPTNVPIGEVSCPMQSVVKLLDDQLPDDSLIRRYPKEAAVALAKRNGGIQWMDVSEGTVMNEAVNAVAASALAPSASAPPLEEKSKLTEQAMDLVTAAEPEIIASLVPVPAPVFAIPPKPADYNVRTLKIDEATWLRMIPKTMGTPFQIQVTDNTGTNWHLNLRGGTRVVNLDQIAPMRFVLDLGGKSYKETSWDPNGKKVGFIVFQSKIPFELWTAASQIGQATVVNYVQLYAEDSSFTAQSIIATTSLAYNYEPEQLNKTDPEMNYYLLATFIDSAAITPTNMTQPDVWDALLTMSPLSAGEVTVKGAVVSEVVPAELIGSYTPESLNASLPNDAARCMIDRASKIAEAIKIDDDAGPDEYSPNSVPIQGQLAISQLETGYGVRIFNPKGILSKIASRAMQAFIGDPSTIITQAAPVLSDKNNWIALAQGVKTSLRTKSLSAGVKTAVSKLSSSESIQNWTQGFLDKVSTHFPAPKPDCPTNGDGSEPSARRVKRDSYAGVVKRGYTR
Protein: FMN-dependent NADH:quinone oxidoreductase 3 (EC 1.6.5.-) (Azo-dye reductase 3) (FMN-dependent NADH-azo compound oxidoreductase 3) (FMN-dependent NADH-azoreductase 3) (EC 1.7.1.17) (Q9HZ17)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Shows a preference for naphthoquinones such as plumbagin.
Interaction partners:
- GST C-terminal domain-containing protein
- Extradiol ring-cleavage dioxygenase class III enzyme subunit B domain-containing protein
- HTH hxlR-type domain-containing protein
- Nitroreductase domain-containing protein
- NAD
- Cytochrome b561 bacterial/Ni-hydrogenase domain-containing protein
- Probable oxidoreductase
- NADPH:quinone oxidoreductase MdaB
- Probable oxidoreductase
- RidA family protein
Sequence:
MSRVLVIESSARQRGSVSRLLTAEFISHWKIAHPADRFQVRDLAREPLPHLDELLLGAWTTPCDGHSAAERRALERSNRLTEELRMADVLVLAAPMYNFAIPSSLKSWFDHVLRAGLTFRYAEQGPEGLLQGKRAFVLTARGGIYAGGGLDHQEPYLRQVLGFVGIHDVTFIHAEGMNMGPEFREKGLARARERMRQALETDTSLCVPLPTLR
Protein: N-terminal amino-acid N(alpha)-acetyltransferase NatA (EC 2.3.1.255) (Q6P4J0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKRSVKWSPNTMQMGRTPMP