wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (EC 7.1.1.2) (A0A1D8PJ73)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75489}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75489}; Matrix side {ECO:0000250|UniProtKB:O75489}.
Interaction partners:
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Nuc2p
- Complex 1 LYR protein domain-containing protein
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase iron-sulfur protein 4
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MISRTLLKRSLPTVQFLRPFTRSSIRRSAHEEDLVNLNELPRQKSLEENYVPLINPTEKYKVQIEELHKFGTYIMACLPKYVQQFSVWKDELTIYVAPSAILPTMLFLKNNTACQFKQVSDVTAADYPSRTNRFDVVYNLLSVRHNSRIRVKTYANETTPVPSITPLFNGANWFERETYDLFGVFFEGHPDLRRILTDYGFEGHPLRKDFPTTGYTEVRYDEEKKRIIYEPLELTQAWRNFTVGSSVWEPVGEGKDFTPESFKLPTPEPEPEKESDEKK
Protein: Immunoglobulin heavy variable 3-48 (Ig heavy chain V-III region WEA) (P01763)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MELGLCWVFLVAILEGVQCEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYEMNWVRQAPGKGLEWVSYISSSGSTIYYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR
Protein: C2H2 and C2HC zinc fingers superfamily protein (Putative zinc finger protein) (Q9LZW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- Nuclear transcription factor Y subunit C-5
- C2H2 type zinc finger transcription factor family
- At1g60280
- At5g41090
- Ethylene-responsive transcription factor ERF112
- Protein RADIALIS-like 6
- Transcription factor MYB64
- Transcription factor bHLH18
- Transcription factor bHLH95
Sequence:
MELNLSTPTSCSSSSISSSSHEAIPRTKGKTKEEVTAEPSKENQQRLEFRFLFNESSTRNEAKARVFACTFCKKEFSTSQALGGHQNAHKQERSLAKRRKEIEINYPELSIYSQYPPSGLSFSSSSSQYDLGVRYNPNIAKTTKPYPFNIFACRFGYRGGLNFPPMSHLSVPKTDDLSINLISNLEGSIHDQAVKKDQPEADPCKDSDIDLSLKL
Protein: Egl-9 family hypoxia inducible factor 2 (M0R110)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVT
Protein: Pre-rRNA-processing protein esf1 (O74828)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2 (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase dbp4
- Pre-rRNA-processing protein esf2
- Uncharacterized protein C3B8.09
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 22
- Probable U3 small nucleolar RNA-associated protein 18
- ATP-dependent rRNA helicase rrp3
- RNA cytidine acetyltransferase
- Ribosome biogenesis protein enp2 homolog
- Probable ATP-dependent RNA helicase prh1
Sequence:
MGKKQTKPINAKSRSESNVVADPRFQSVHSDPRFSRLKRGNFKVKVDERFKSLKEDKDFKTTASVDRYGRPLNQDKATKEIDRLYELENEGSSSSSESSEITDNEEVASASSKSTKSEELTDEESEDEEVYDPARGEGIISTSESSDESDAESETEAQPEISELAGIEPEENIPRGSETNRLAVVNMDWDNLQAVDLFVALSSFCPPGGKLLKVSIYPSEFGKSRMAAEHVQGPPRDIFTPADNQPSSAELHEAQKFGFDNNESDQDEEDALIEEDLGNEFDMVKLRQYQLERLRYYYAVVECDSVRTAKVIYETCDGAEYETSANIYDLRFIPDDVTFDDDESREVCTKAPEKYEPRDFVTDALQHSKVKLSWDAEDPHRKDLIKKAFTSQDIEDLDFSAYIASSESEDEDVDVIRSRYQKLLSGDADDFQANSNPFEDDDKLEGANGEMEVTFTSGFDVDNNANSSEKDETTIEKYKRKAAERKQRRKELRQLKKTKDDEGEGSDVDLGFDDPFFKDKDASRNNKKNKKGKHTQIEDPTAASKEELENLVREDENDSEQLDHFDMKSILKAEKFKKNRKLKKKASNLEGLQEGFEADVSDPRFAALYTNHNFALDPTNPHFKRTKTVEKIMDESRKRRSNQLEQTQDGKPELKIKKRKAEKGDQRQELDRIVKSIKRSGK
Protein: Tumor necrosis factor ligand superfamily member 10 (TNF-related apoptosis-inducing ligand) (Protein TRAIL) (CD antigen CD253) (P50592)
Organism: Mus musculus (Mouse)
Function: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P50591}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P50591}. Secreted {ECO:0000250|UniProtKB:P50591}. Note=Exists both as membrane-bound and soluble form. {ECO:0000250|UniProtKB:P50591}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 10B
- Tumor necrosis factor receptor superfamily member 6
- Tumor necrosis factor ligand superfamily member 6
- FAS-associated death domain protein
- Caspase-8
- Tumor necrosis factor receptor superfamily member 1A
- CASP8 and FADD-like apoptosis regulator
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily, member 25
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MPSSGALKDLSFSQHFRMMVICIVLLQVLLQAVSVAVTYMYFTNEMKQLQDNYSKIGLACFSKTDEDFWDSTDGEILNRPCLQVKRQLYQLIEEVTLRTFQDTISTVPEKQLSTPPLPRGGRPQKVAAHITGITRRSNSALIPISKDGKTLGQKIESWESSRKGHSFLNHVLFRNGELVIEQEGLYYIYSQTYFRFQEAEDASKMVSKDKVRTKQLVQYIYKYTSYPDPIVLMKSARNSCWSRDAEYGLYSIYQGGLFELKKNDRIFVSVTNEHLMDLDQEASFFGAFLIN
Protein: Lipopolysaccharide core heptosyltransferase OpsX (EC 2.-.-.-) (Q57336)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Catalyzes heptose transfer to the lipopolysaccharide core. It transfers the first L-glycero-D-manno-heptose to the phosphorylated 3-deoxy-alpha-D-manno-octulosonic acid (Kdo-P) of the inner core.
Interaction partners:
- 3-deoxy-D-manno-octulosonic acid kinase
- Lipooligosaccharide heptosyltransferase 2
- 3-deoxy-D-manno-octulosonic acid transferase
- Bifunctional protein HldE
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Putative glycosyltransferase HI_0523
- Uncharacterized protein HI_0874
Sequence:
MPLFTEAPKSLCILRLSAVGDVCHALAVVQHIQEYYPQTEMTWIVGKTEMGLLSSIPNITLIPYDKKTGWKGVLSLWKQLKNKQFDALLNMQTAFRASILSLGIKAKFKIGFGEKRSREGQWLFVNRRIRDPFSPHVLDGFMAFAEYIGVPKAEPKWELAISQDDYKFADQFIDFSRKNLLISPCSSKAEKDWLIEGYAEVANIAHQHNINVIFCSSPAKRELEIVEKITALCHFTPTNIAGKTNLKQLTALISKVDLVLSPDSGPAHIATTQGTPVIGLYAYHNPLRTAPYNNLDNVVSVYEENAQKEFGKPSSELPWATKLKGKNLMTEIQVEPVIGQMKKLGLF
Protein: Adenosine transporter 2, putative (Q586N3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAMLGFESTAEFFVYLTFIFFGMSVMNVTNAIYSNYYFFWEYYKFAQGNEHAVSANPSFWKHMFTYYNVVVFTMQVLLEAFMLTPLGRRIPISWRLFFGLSLPMVEIIVILVIPAVGGTSEGGAMATMMIVAFVCGISMTLCDSSNAALAGPFPTKFYGATVWGLAVSGLMTSFLAIVIQASMKDNFESRRTQSQIYFGLVMFLQVVACVLLVLLRKNPYAIKYAAEFRYAARKDGKTDDGEDENDAKGTGPADEDGYPDEKENKNVLNADIDPDKMKDTDQVEGTTNAQQMLDASVMVVVKRIWPMLLSCFFVFFATLLVFPDVFVAVKEGFPTHGGWYFTIVVAMFNLGDFLSRLVLQFKRLHVSPRMVMIGSFARALLIIPLSLCAAGTIPGVWLPYTVSLLWGLTNGYFGGLSMIYGPRTGSLTTAGQRSLAAICINVALLLGLFAGAMFALAVKEGLPE
Protein: Retinaldehyde dehydrogenase 3 (RALDH-3) (RalDH3) (EC 1.2.1.36) (Aldehyde dehydrogenase 6) (Aldehyde dehydrogenase family 1 member A3) (Aldh1a3) (Q8K4D8)
Organism: Rattus norvegicus (Rat)
Function: NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (By similarity). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (By similarity). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9JHW9}.
Interaction partners:
- Retinol dehydrogenase 10
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Cytochrome P450, family 26, subfamily C, polypeptide 1
- Dehydrogenase/reductase SDR family member 9
- Retinol dehydrogenase 5
- NADP-retinol dehydrogenase
- Alcohol dehydrogenase class-3
- All-trans-retinol dehydrogenase [NAD
- Dehydrogenase/reductase
Sequence:
MATANGAVENGQPDGKPPALPRPIRNLEVKFTKIFINNDWHEPKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLIERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVMCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGRNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWVNCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLDEKNP
Protein: TFIIB4 (Q9M2L0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTMKWGHSCRRCKQINVVTDHVTRRTRCFGCGLEFKYRPIGDLSPVAENDTVRLPDPTNTLLSNTDLSIVTTEHKNGSFDDSLSLNLGNSSKPRLDPVSIATAKLMNGSSNDFLSLGTSQNSETITASSDEFLFSDLGHLQKFSFDPLSMASTKPNKALSIVSIEAISNGLKLPATIKGQANEIFKVVESYARGKERNVLFAACIYIACRDNDMTRTMREISRFANKASISDISETVGFIAEKLEINKNWYMSIETANFIKRFCSIFRLDKEAVEAALEAAESYDYMTNGRRAPVSVAAGIVYVIARLSYEKHLLKGLIEATGVAENTIKGTYGDLYPNLPTIVPTWFANANDLKNLGAP
Protein: ADAM 17-like protease (EC 3.4.24.-) (Q9VAC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Angiotensin-converting enzyme
- Neurogenic locus Notch protein
- Tissue inhibitor of metalloproteinase
Sequence:
MFTKCISCCGLAIISVFFACLFVENCAALQKTLRHYEIFHKDDVVHRVVKRGAKHSTNPFNTIKEVEFTTLGKNFRLILHPHRDVLHSKFRAYAVDADGNETVVHMDHDSFYSGRVFGELESSVRAHIEDGTMTMSIHLPEETYHIEPSWRHLPEAKKDTMVAYKASDVKVHKNEAGATPKTCGYIKEGLELEDKEHGDTLDNELHTREKRQSDQYEYTPTKTRCPLLLVADYRFFQEMGGGNTKTTINYLISLIDRVHKIYNDTVWQDRSDQEGFKGMGFVIKKIVVHSEPTRLRGGEAHYNMIREKWDVRNLLEVFSREYSHKDFCLAHLFTDLKFEGGILGLAYVGSPRRNSVGGICTPEYFKNGYTLYLNSGLSSSRNHYGQRVITREADLVTAHEFGHNWGSEHDPDIPECSPSASQGGSFLMYTYSVSGYDVNNKKFSPCSLRSIRKVLQAKSGRCFSEPEESFCGNLRVEGDEQCDAGLLGTEDNDSCCDKNCKLRRNQGAMCSDKNSPCCQNCQFMASGMKCREAQYATCEQEARCTGAHAECPKSPAMADGTTCQERGQCRNGKCVPYCETQGLQSCMCDIIADACKRCCRMSINETCFPVEPPDVLPDGTPCITGFCNKGVCEKTIQDVVERFWDIIEEINVAKTLRFLKDNIVMAVVLVTAVFWIPISCVISYFDRKKLRHEMKLIEWSQKLDLIHPSDERRRVIHIRVPRQKISVARACN
Protein: PAC1 receptor Hop1 isoform (Pituitary adenylate cyclase-activating polypeptide type I receptor isoform 1 precursor) (Q5C8U6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MYRQAARETFLILFLIISLMWPIHSEISNCVIKREEERCLERIALHDPKDDQKFECPWEWDNLTCWQAASVGDVVEVNCPELFEFMSPEEGLGKISRNCTEFGWSEPYPHYVDACMTDENTTKPDMYYASVKALYTVGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIKDGVLYAEEDSDHCFVHTVGCKAVMVFFHYCVMSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTIWAVLRLHFDDSGCWDMNDNTALWWVIKGPVVASIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLSCAQKCFSEPTQAVQHSCRMSELSTITLRLARSTLLLIPLFGIHYTVFAFSPEDFSKRERLVFELGLGSFQGFVVAVLYCFLNGEAQSEIKRKWRSWTVNRYFAVDLKQQRHPSLASSGVNGGTQLSILSKSSSQIRMSSPLAETVNLNLPT
Protein: Exodeoxyribonuclease 1 (EC 3.1.-.-) (Exodeoxyribonuclease I) (EXO I) (Exonuclease I) (Protein DHS1) (P39875)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- ATP-dependent helicase SGS1
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein MSH2
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA mismatch repair protein MLH3
- ATP-dependent DNA helicase II subunit 1
- DNA mismatch repair protein MSH6
- DNA repair protein RAD51
- DNA mismatch repair protein PMS1
- Proliferating cell nuclear antigen
Sequence:
MGIQGLLPQLKPIQNPVSLRRYEGEVLAIDGYAWLHRAACSCAYELAMGKPTDKYLQFFIKRFSLLKTFKVEPYLVFDGDAIPVKKSTESKRRDKRKENKAIAERLWACGEKKNAMDYFQKCVDITPEMAKCIICYCKLNGIRYIVAPFEADSQMVYLEQKNIVQGIISEDSDLLVFGCRRLITKLNDYGECLEICRDNFIKLPKKFPLGSLTNEEIITMVCLSGCDYTNGIPKVGLITAMKLVRRFNTIERIILSIQREGKLMIPDTYINEYEAAVLAFQFQRVFCPIRKKIVSLNEIPLYLKDTESKRKRLYACIGFVIHRETQKKQIVHFDDDIDHHLHLKIAQGDLNPYDFHQPLANREHKLQLASKSNIEFGKTNTTNSEAKVKPIESFFQKMTKLDHNPKVANNIHSLRQAEDKLTMAIKRRKLSNANVVQETLKDTRSKFFNKPSMTVVENFKEKGDSIQDFKEDTNSQSLEEPVSESQLSTQIPSSFITTNLEDDDNLSEEVSEVVSDIEEDRKNSEGKTIGNEIYNTDDDGDGDTSEDYSETAESRVPTSSTTSFPGSSQRSISGCTKVLQKFRYSSSFSGVNANRQPLFPRHVNQKSRGMVYVNQNRDDDCDDNDGKNQITQRPSLRKSLIGARSQRIVIDMKSVDERKSFNSSPILHEESKKRDIETTKSSQARPAVRSISLLSQFVYKGK
Protein: Keratin-associated protein 9-6 (Keratin-associated protein 9-like 2) (A8MVA2)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTHCCSPGCQPTCCRTTCCRTTCWQPTIVTTCSSTPCCQPSCCVSSCCQPYCHPTCCQNTCCRTTCCQPTCVTSCCQPSCCSTPCYQPICCGSSCCGQTSCGSSCGQSSSCAPVYCRRTCYHPTTVCLPGCLNQSCGSSCCQPCYCPACCVSSCCQHSCC
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FRA9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSTFVDLYKRGGNEAVKINPPTGADFHITSRGSDWLWAAFCVFLLLAIVFVLLMFRKPVNNRFVYLTAIAPNVFMAIAYFSIASNLGWIPVRAKYNHVRTSTQQQHPGVRQIFYARYVGWFMALPWPLIQASILGKTPVWHVAFNCTMGCVFSVCFLIAACVHSTYKWGYFTIGCGAGIVSIISLMTTTYTLIKKCGDKEIKRCFLIYVCPIIVLYLVAWPVCFGITDGGNVLQPDSEAIFYGIIDLLLLGIFPALYVPMASHVGYENITYGIFDSAIGGAAPGGMAHSASMDIEKSPMSATSSPTPVSPTPKAGIKKPKLKLKK
Protein: 40S ribosomal protein S24 (Q642J7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNDTVTVRTRKFMTNRLLQRKQMIVDVLHPGKATVPKTEIREKLAKMYKTTPDVVFVFGFKTQFGGGKTTGFGMIYDSLDYAKKNEPKYRLQRHGLYEKKKTSRKQRKERKNRMKKVRGIKKASVGASGKK
Protein: mRNA endoribonuclease toxin LS (EC 3.1.-.-) (RNase LS) (Toxin LS) (P52129)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17895580}. Note=May associate with ribosomes, it sediments in a P100 fraction (pellet of a 100,000 x g centrifugation). {ECO:0000305|PubMed:17895580}.
Interaction partners:
- Antitoxin RnlB
- Endoribonuclease toxin MazF
- mRNA interferase toxin RelE
- Antitoxin MazE
- mRNA interferase toxin MqsR
- Probable mRNA interferase toxin HicA
- mRNA interferase toxin YafQ
- mRNA interferase toxin YafO
- Endoribonuclease toxin ChpB
- Antitoxin RelB
Sequence:
MTIRSYKNLNLVRANIETESRQFIENKNYSIQSIGPMPGSRAGLRVVFTRPGVNLATVDIFYNGDGSTTIQYLTGANRSLGQELADHLFETINPAEFEQVNMVLQGFVETSVLPVLELSADESHIEFREHSRNAHTVVWKIISTSYQDELTVSLHITTGKLQIQGRPLSCYRVFTFNLAALLDLQGLEKVLIRQEDGKANIVQQEVARTYLQTVMADAYPHLHVTAEKLLVSGLCVKLAAPDLPDYCMLLYPELRTIEGVLKSKMSGLGMPVQQPAGFGTYFDKPAAHYILKPQFAATLRPEQINIISTAYTFFNVERHSLFHMETVVDASRMISDMARLMGKATRAWGIIKDLYIV
Protein: Coi1p (Q5A799)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MVSFKSLITLAIAATSVSSFNLLHDDKGFAILPPTNIVLDHLKEVGKKAVTTHYDVLNTIKEDGEIVHVNLHTHETKCTGKYAKDYDNSMYNKLNKKQLFIRTIEDSSLKQCLNKEFEAETSECGFEFIEYNSASGCSSDATKYSCLLDVMKQQDATKKLKDMDDVPAQVRCYHKLEQATKAEVVGGACAK
Protein: FBD, F-box and Leucine Rich Repeat domains containing protein (F4I1V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFLCVIIPCLCSYLCSLFSWLLGQIPSFLFDKINESWLTSTKRNVEIVKNLMDKISQLPDELLVKVLSFLSTKDAVSTSILSMRWKSLWMWLPKLEYNFRHYSVSEGQGLARFITSSLRVHKAPAIESLSLKFRYGAIGSIKPKDIYLWVSLAVHVSNVRELSLKLFNFAELPTKLPKSLCKCKSIVILKLKDEILVDVPRKVCLPSLKTLFLGRVTYSDANSLHRLLSNCPVLEDLVMERDKIDNLGKLSVIVKSLQRLTLKMSRPCHLDGLKMNSPSLKYLKVIDERLESDSDDESDSDSPRYFYDFEDMPKLEEADFVLTFQNIKKFFGSITSVKRLSLCLGVYTEESLYHEGLVFNQLEQLKICSCDSDWSILLARLLKSSPNLRELEAYVIEDHPNGRTDLPNQWDNQLNCVPTCLLSSLETFRWSEMHGLLQNQMDVAKYILKNARCLKSATIFFPTTYAQETRDEMIEELSLSFQGPETCQVFFH
Protein: Chorismate mutase 1, chloroplastic (ZmCM1) (EC 5.4.99.5) (B4FNK8)
Organism: Zea mays (Maize)
Function: May play a role in chloroplast biogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21976020}.
Interaction partners:
- Chorismate synthase
- Arogenate dehydratase
- Arogenate dehydratase
- Arogenate dehydratase
- Arogenate dehydratase
- p-protein
- Chorismate synthase
- anthranilate synthase
- anthranilate synthase
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
Sequence:
MAFKLATKAAAASPAAAHRGGLARGPEGTSRVAFGPAPRNKGLRAANNSATPVAKEERVDRSEILTLDSIRQVLIRLEDSIIFGLLERAQFCYNADTYDSNAFHMDGFGGSLVEYMVRETEKLHAQVGRYKSPDEHPFFPEDLPEPRLPPMQYPRVLHPIADSININKEIWKMYFDELLPRLVKKGSDGNAGSSALCDTTCLQALSKRIHYGKFVAEAKFQESPEAYMPAIIAQDRDQLMHLLTYETVERAIEHRVEAKAKIFGQEVNIGVEDNGSPPVYKIVPSLVAELYSYRIMPLTKEVQIAYLLRRLD
Protein: Spectrin beta, non-erythrocytic 2 (A0A494BBH5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGETLPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEK
Protein: Translationally-controlled tumor protein 1 (TCTP1) (P31265)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General regulator required for the development of the entire plant. Regulates the duration of cell cycle. Probable activator of Rab GTPases and upstream regulator of the cell growth-regulating TOR (target of rapamycin) network. Might also control spatial growth in pollen tubes or root hairs via the TORC2 signaling branch. Involved in the regulation of abscisic acid- and calcium-mediated stomatal closure, but not in light or H(+)-pumping induced stomatal opening. May regulate microtubules depolymerization. Binds calcium and has a cytoprotective function.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24040826}.
Interaction partners:
- Probable elongation factor 1-gamma 2
- Elongation factor 1-delta 2
- Elongation factor 1-delta 1
- Elongation factor 1-beta 2
- Eukaryotic translation initiation factor 5A-3
- Large ribosomal subunit protein uL18y
- Elongation factor 1-beta 1
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL6x
Sequence:
MLVYQDLLTGDELLSDSFPYKEIENGILWEVEGKWVTVGAVDVNIGANPSAEEGGEDEGVDDSTQKVVDIVDTFRLQEQPTYDKKGFIAYIKKYIKLLTPKLSEEDQAVFKKGIEGATKFLLPRLSDFQFFVGEGMHDDSTLVFAYYKEGSTNPTFLYFAHGLKEVKC
Protein: Ubiquitin specific peptidase 33 (E9PQP0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGTCQDCKVQGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKTPLVAVFDDLDIEADEEDELRARGLTGLKNIGNTCYMNAALQA
Protein: Probable lipoprotein aminopeptidase LpqL (EC 3.4.11.1) (Leucine aminopeptidase) (Lipoprotein LpqL) (P96264)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: An aminopeptidase; acts on free N-terminal amino groups with a very strong preference for Leu in the first position.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:24093492}.
Interaction partners:
- Possible lipoprotein peptidase LpqM
- Probable conserved lipoprotein LppZ
- Oligopeptide-binding protein OppA
- Probable conserved transmembrane protein
- Putative diacylated glycolipid transporter LprF
- Lipoprotein LpqN
- Probable conserved lipoprotein LpqU
- Possible para-nitrobenzyl esterase
- Possible para-nitrobenzyl esterase
- Carboxylic ester hydrolase
Sequence:
MVNKSRMMPAVLAVAVVVAFLTTGCIRWSTQSRPVVNGPAAAEFAVALRNRVSTDAMMAHLSKLQDIANANDGTRAVGTPGYQASVDYVVNTLRNSGFDVQTPEFSARVFKAEKGVVTLGGNTVEARALEYSLGTPPDGVTGPLVAAPADDSPGCSPSDYDRLPVSGAVVLVDRGVCPFAQKEDAAAQRGAVALIIADNIDEQAMGGTLGANTDVKIPVVSVTKSVGFQLRGQSGPTTVKLTASTQSFKARNVIAQTKTGSSANVVMAGAHLDSVPEGPGINDNGSGVAAVLETAVQLGNSPHVSNAVRFAFWGAEEFGLIGSRNYVESLDIDALKGIALYLNFDMLASPNPGYFTYDGDQSLPLDARGQPVVPEGSAGIERTFVAYLKMAGKTAQDTSFDGRSDYDGFTLAGIPSGGLFSGAEVKKSAEQAELWGGTADEPFDPNYHQKTDTLDHIDRTALGINGAGVAYAVGLYAQDLGGPNGVPVMADRTRHLIAKP
Protein: Protein inscuteable homolog (Q1MX18)
Organism: Homo sapiens (Human)
Function: May function as an adapter linking the Par3 complex to the GPSM1/GPSM2 complex. Involved in spindle orientation during mitosis. May regulate cell proliferation and differentiation in the developing nervous system. May play a role in the asymmetric division of fibroblasts and participate in the process of stratification of the squamous epithelium (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22074847}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22074847}. Note=Uniformly distributed in the cytoplasm during interphase. During metaphase, detected in the cell cortex, adjacent to the mitotic spindle poles. {ECO:0000269|PubMed:22074847}.
Interaction partners:
- G-protein-signaling modulator 2
- Partitioning defective 3 homolog B
- G-protein-signaling modulator 1
Sequence:
MRRPPGNGEAASEGPGGWGLWGVQESRRLCCAGHDRCKQALLQIGINMMALPGGRHLDSVTLPGQRLHLMQVDSVQRWMEDLKLMTECECMCVLQAKPISLEEDAQGDLILAGGPGPGDPLQLLLKRGWVISTELRRIGQKLAQDRWARVHSMSVRLTCHARSMVSEYSAVSRNSLKEMGEIEKLLMEKCSELSAVTERCLQVENEHVLKSMKACVSETLSMLGQHFGQLLELALTREVQALVRKIDASDNIYTTESTTGNLFSLTQEGAPLCRIIAKEGGVVALFKVCRQDSFRCLYPQALRTLASICCVEEGVHQLEKVDGVLCLADILTDNSHSEATRAEAAAVVAQVTSPHLPVTQHLSSFLESMEEIVTALVKLCQEASSGEVFLLASAALANITFFDTMACEMLLQLNAIRVLLEACSDKQRVDTPYTRDQIVTILANMSVLEQCASDIIQENGVQLIMGMLSEKPRSGTPAEVAACERVQQKAAVTLARLSRDPDVAREAVRLSCMSRLIELCRSPSERNSSDAVLVACLAALRRLAGVCPEGLQDSDFQQLVQPRLVDSFLLCSNMEESFV