wanglab/gogpt-training-data huggingface dataset:
Protein: Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase) (Lethal protein 721) (Q11190)
Organism: Caenorhabditis elegans
Function: Accepts electrons from ETF and reduces ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Electron transfer flavoprotein subunit beta
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
- STI1 domain-containing protein
- Malate dehydrogenase
- Probable 3-ketoacyl-CoA thiolase
- Probable 2-oxoadipate dehydrogenase complex component E1 homolog
- Carboxylesterase type B domain-containing protein
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MRISGVTLFRVSSQLRNVVNGQWTTTHYTVKDRSTDPRWKDVDLARESDVYDVVIVGGGPSGLSAAIRLRQLAEKAQKELRVCVVEKASVIGGHTLSGAVIETRALDELIPNWKELGAPVYQQVTSESIAILTESGRIPVPVLPGVPLANHGNYIVRLGKVVQWLGEQAEAAGVEVWPEIAASEVLYNEDGSVKGIATSDVGIGKDGAPKDGFARGMEFHAKCTIFAEGCRGHLSKQVLDKFDLRTHAMTYGIGLKELWEIDPAKHRPGYVEHTMGWPLNVDQYGGSFLYHIEDQGQPLVSVGFVVALDYANPNLNPYKEFQKYKTHPSISKQLEGGKRIGYGARALNEGGFQSIPKLHFPGGCLVGCSAGFLNVAKLKGTHNAMKSGMVAAESIFEDIQQKGEDVQTIDPATYDKNIRDTYVVKELKATRNIRPSFNTSLGYIGGLIYSGIFYVFGRGIEPWTLGHGKKDNEKLIPVKDAKEIDYPKPDGKLTFDLLTSVSLTGTNHTEDQPAHLTLKNDQVPLDVNLAVYGGPEARFCPAGVYEFVPSEADESKKRLQINAQNCIHCKTCDIKDPQQNINWVTPEGGGGPKYEGM
Protein: Bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase (Cystathionine beta-lyase (EC 4.4.1.1, EC 4.4.1.8)) (Cystathionine gamma-synthase (EC 2.5.1.48)) (X5E0F1)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
MNKKTKLIHGGHTTDDYTGAVTTPIYQTSTYLQDDIGDLRQGYEYSRTANPTRSSVESVIATLENGKHGFAFSSGVAAISAVVMLLDKGDHIILNSDVYGGTYRALTKVFTRFGIEVDFVDTTHTDSIVQAIRPTTKMLFIETPSNPLLRVTDIKKSAEIAKEHGLISVVDNTFMTPYYQNPLDLGIDIVLHSATKYLGGHSDVVAGLVATSDDKLAERLAFISNSTGGILGPQDSYLLVRGIKTLGLRMEQINRSVIEIIKMLQAHPAVQQVFHPSIESHLNHDVHMAQADGHTGVIAFEVKNTESAKQLIKATSYYTLAESLGAVESLISVPALMTHASIPADIRAKEGITDGLVRISVGIEDTEDLVDDLKQALDTL
Protein: Structural maintenance of chromosomes protein (Q803N2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
Sequence:
MYIKQVIIQGFRSYRDQTVVDPFGSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEDEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSSKRETCGDKSRQLRDAQQDARDKVEETERVVRELKSRISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELQETEPKFNTVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEQNKERNLEQYNKLDQDLNEVKTRVEELDKKYYEVKNRKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVINGYHGIVMNNFECEPAFYTCVEVTAGTRLFYHIVETDEVSTKILMEFNKMNLPGEVTFLPLSKLDVRDTAYPETNDAIPMISKLRYSQNFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDMRKAEEELGELEAKLNENLRRNIETINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGADLLSQLSLEDQRRVDDLNDEIRQLQQDNRQLLNERIKLEGIMTRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELDGINKRIKDTMARSEDLDTLIDKTEVEIKEHQKSMERWKNIEKEQNEAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLTLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQDELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDTEGGQSQDEGEGGDSERASSSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAASDMIMELAGHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVISAEQAKDFVEDDTTHG
Protein: GEO07864p1 (RE54375p) (SoxNeuro Co-Factor) (Q9VU59)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Early boundary activity protein 1
- Halo
- RE73396p
- Uncharacterized protein
- Bard
- RE03769p
- Serendipity locus protein alpha
- RE73577p
- GEO02646p1
- FI01028p
Sequence:
MIDQHKRSHKSEKSSRKSGKKHSDKPHKVKTHDPLKKQKKRALKKLRRKSATVNFPYQLFLYRQELRRASADFSYLRLSKAKIVLTSQLIAKKMGSCNPDCSVDELKELSREVQFQKRLCHQVERLQQFRQLGLTEMILNGKKTTL
Protein: Leucine-rich repeat protein (LRRP), putative (Q57U25)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acyl-CoA thioesterase-like N-terminal HotDog domain-containing protein
Sequence:
MPNAIGLHCMSRMRELHLSGSCVTDRHLCNVGVGKCLVRLSIESCTNLTDVSLLTAVETLEEVRLDGCKNVVKGINEFGRMPYLRVLILKETSVTDRCLRGFASSRSLVKLFIESCSQPTDVSPISAVETLEEVRLDGCKNVVKGINEFGRMPYLRVLILREVGVTDRCLRGLSCCRSLVELALEYCLQLTDVSPISMLETLQKVRFDGCKNVVKGFGELGRVPYLQTLSLNETNVDDRALFTLRATGSLVELSLESCPQLTDVTHLSMIDTLQKIVLEGCANVAKGVGLLGRLPALRELYAGATSIADTSISALSRSGTLTKIDVKFCQGLTDVSPLVDMKLLEEINLEGCKNVEHGLPCLEKLNLLRVLHLTETQMTDDYLRGLCASCSIVVLDVSLCDQLVDMSPLASIETLEVLRANNCKSVVRGVGALGGLRALRELGLKATMIKNKSLCGLGQSRTLVQIDLEACERLTDVTPLSQIRTLEVVNLNGCKNVVSGLKSMAVMPRLRLLHLMDVELGSDVLDELKSMNVWVNK
Protein: Fibroblast growth factor 22 (FGF-22) (Q9ESS2)
Organism: Mus musculus (Mouse)
Function: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Fibroblast growth factor receptor 3
- Pro-epidermal growth factor
- Fibroblast growth factor-binding protein 1
- Vascular endothelial growth factor receptor 2
- Decorin
- Vascular endothelial growth factor receptor 3
Sequence:
MRSRLWLGLAWLLLARAPGAPGGYPHLEGDVRWRRLFSSTHFFLRVDLGGRVQGTRWRHGQDSIVEIRSVRVGTVVIKAVYSGFYVAMNRRGRLYGSRVYSVDCRFRERIEENGYNTYASRRWRHRGRPMFLALDSQGIPRQGRRTRRHQLSTHFLPVLVSS
Protein: Iota-conotoxin LtIIIA (Lt3.1) (Lt3a) (Q2I2Q5)
Organism: Conus litteratus (Lettered cone)
Function: Iota-conotoxins bind to voltage-gated sodium channels and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. This toxin enhances tetrodotoxin-sensitive sodium current in rat dorsal root ganglion neurons.
Subcellular location: Secreted {ECO:0000269|PubMed:19562324}.
Interaction partners:
Sequence:
MLKMGVLLFTFLVLFPLTTLELDTDRPVERHAAIKQDLKPQERRGIRLHAPRDECCEPQWCDGACDCCS
Protein: Mitogen-activated protein kinase kinase kinase dlk-1 (D6VPA3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTSSSRARSPTPYDNDFENAESFVDPESPKNLKNLEKIVNLPESTSYDEALCNSDVTMNPIYTSPITTYSNPCHVELVDEENANDVDLTSSMDSRRSRSDDADVESSEEDEGNGNNILNTSMESEDLRYRIDTSQSTMMSSLERSLEIGATRSDGLSDNEMRVQAVKMSIKTHRRTGSNPQALIHQCIDEYTTSATDDSDDAGAVRI
Protein: T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d) (P04235)
Organism: Mus musculus (Mouse)
Function: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3D plays an essential role in thymocyte differentiation. Indeed, participates in correct intracellular TCR-CD3 complex assembly and surface expression. In absence of a functional TCR-CD3 complex, thymocytes are unable to differentiate properly. Interacts with CD4 and CD8 and thus serves to establish a functional link between the TCR and coreceptors CD4 and CD8, which is needed for activation and positive selection of CD4 or CD8 T-cells.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- T-cell surface glycoprotein CD3 gamma chain
- T-cell surface glycoprotein CD3 epsilon chain
- T-cell surface glycoprotein CD3 zeta chain
- Tyrosine-protein kinase ZAP-70
- T-cell differentiation antigen CD6
- T-cell surface glycoprotein CD8 beta chain
- T-cell surface glycoprotein CD8 alpha chain
- Src kinase-associated phosphoprotein 1
- Tyrosine-protein phosphatase non-receptor type 6
- Proto-oncogene tyrosine-protein kinase LCK
Sequence:
MEHSGILASLILIAVLPQGSPFKIQVTEYEDKVFVTCNTSVMHLDGTVEGWFAKNKTLNLGKGVLDPRGIYLCNGTEQLAKVVSSVQVHYRMCQNCVELDSGTMAGVIFIDLIATLLLALGVYCFAGHETGRPSGAAEVQALLKNEQLYQPLRDREDTQYSRLGGNWPRNKKS
Protein: Gap junction beta-1 protein (Connexin-32) (Cx32) (GAP junction 28 kDa liver protein) (P08034)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction beta-2 protein
- Gap junction alpha-1 protein
- Occludin
- Gap junction alpha-5 protein
- mRNA cap guanine-N
- Peripheral myelin protein 22
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 6
Sequence:
MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC
Protein: WW domain-containing oxidoreductase (EC 1.1.1.-) (Fragile site FRA16D oxidoreductase) (Short chain dehydrogenase/reductase family 41C member 1) (Q9NZC7)
Organism: Homo sapiens (Human)
Function: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14695174, ECO:0000269|PubMed:15070730, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:19366691, ECO:0000269|PubMed:19465938}. Nucleus {ECO:0000269|PubMed:14695174, ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:19366691}. Mitochondrion {ECO:0000269|PubMed:14695174}. Golgi apparatus {ECO:0000269|PubMed:30285739}. Lysosome {ECO:0000269|PubMed:30285739}. Note=Partially localizes to the mitochondria (PubMed:14695174). Translocates to the nucleus upon genotoxic stress or TNF stimulation (By similarity). Translocates to the nucleus in response to TGFB1 (PubMed:19366691). Isoform 5 and isoform 6 may localize in the nucleus. Localized to the lysosome probably upon binding to VOPP1 (PubMed:30285739). {ECO:0000250, ECO:0000269|PubMed:14695174, ECO:0000269|PubMed:19366691, ECO:0000269|PubMed:30285739}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-4
- Transcription factor AP-2 gamma
- Bis
- Cellular tumor antigen p53
- Segment polarity protein dishevelled homolog DVL-2
- Transcription factor Jun
- WW domain-binding protein 2
- Mitogen-activated protein kinase 8
- Activated CDC42 kinase 1
- Serine-protein kinase ATM
Sequence:
MAALRYAGLDDTDSEDELPPGWEERTTKDGWVYYANHTEEKTQWEHPKTGKRKRVAGDLPYGWEQETDENGQVFFVDHINKRTTYLDPRLAFTVDDNPTKPTTRQRYDGSTTAMEILQGRDFTGKVVVVTGANSGIGFETAKSFALHGAHVILACRNMARASEAVSRILEEWHKAKVEAMTLDLALLRSVQHFAEAFKAKNVPLHVLVCNAATFALPWSLTKDGLETTFQVNHLGHFYLVQLLQDVLCRSAPARVIVVSSESHRFTDINDSLGKLDFSRLSPTKNDYWAMLAYNRSKLCNILFSNELHRRLSPRGVTSNAVHPGNMMYSNIHRSWWVYTLLFTLARPFTKSMQQGAATTVYCAAVPELEGLGGMYFNNCCRCMPSPEAQSEETARTLWALSERLIQERLGSQSG
Protein: Phosphatidylglycerophosphatase GEP4, mitochondrial (EC 3.1.3.27) (Genetic interactor of prohibitins 4) (PGP phosphatase GEP4) (P38812)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways. Required for the stability of respiratory chain supercomplexes and for growth at elevated temperature, in presence of ethidium bromide or in absence of prohibitins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:20485265}; Peripheral membrane protein {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:20485265}; Matrix side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:20485265}.
Interaction partners:
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Lysophospholipid acyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- Phosphatidylglycerol phospholipase C
- Cardiolipin-specific deacylase 1, mitochondrial
- Protein UPS1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Mitochondrial distribution and morphology protein 35
- Tafazzin
Sequence:
MNISGTLNTLRLLYNPSLCKPSLVVPTFNDLPIPIHDSIKAVVLDKDNCIAFPHDDKIWPDYLQHWETLRSKYSNKALLIVSNTAGSNSDKDYSQAKLLEDKTGIPVLRHSTKKPGCHNEILDYFYRNKTITNPKEVAVVGDRLFTDILMANLMGSYGVWIRDGVKVSANPLSKFEKKLYNFLGF
Protein: Long-chain specific acyl-CoA dehydrogenase, mitochondrial (LCAD) (EC 1.3.8.8) (P15650)
Organism: Rattus norvegicus (Rat)
Function: Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3813556}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 3
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAARLLLRSLRVLSARSATLPPPSARCSHSGAEARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPYHEEWEKAGEVSRELWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEQFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGKKLHKMGMKAQDTAELFFEDVRLPASALLGEENKGFYYLMQELPQERLLIADLAISACEFMFEETRNYVRQRKAFGKTVAHIQTVQHKLAELKTNICVTRAFVDSCLQLHETKRLDSASASMAKYWASELQNTVAYQCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS
Protein: tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein QRI7) (tRNA threonylcarbamoyladenosine biosynthesis protein QRI7) (P43122)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:23620299}.
Interaction partners:
- EKC/KEOPS complex subunit PCC1
- Threonylcarbamoyl-AMP synthase
- EKC/KEOPS complex subunit BUD32
- EKC/KEOPS complex subunit CGI121
- U3 small nucleolar RNA-associated protein 18
- tRNA N6-adenosine threonylcarbamoyltransferase
- Threonine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase, cytoplasmic
- EKC/KEOPS complex subunit GON7
Sequence:
MISIKGTGRFLLDNYRIWQRRAFNRPIQLRKGYKVLAIETSCDDTCVSVLDRFSKSAAPNVLANLKDTLDSIDEGGIIPTKAHIHHQARIGPLTERALIESNAREGIDLICVTRGPGMPGSLSGGLDFAKGLAVAWNKPLIGVHHMLGHLLIPRMGTNGKVPQFPFVSLLVSGGHTTFVLSRAIDDHEILCDTIDIAVGDSLDKCGRELGFKGTMIAREMEKFINQDINDQDFALKLEMPSPLKNSASKRNMLSFSFSAFITALRTNLTKLGKTEIQELPEREIRSIAYQVQESVFDHIINKLKHVLKSQPEKFKNVREFVCSGGVSSNQRLRTKLETELGTLNSTSFFNFYYPPMDLCSDNSIMIGWAGIEIWESLRLVSDLDICPIRQWPLNDLLSVDGWRTDQL
Protein: Light-harvesting complex stress-related protein 1, chloroplastic (Chlorophyll a-b binding protein LHCSR1) (P93664)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage. Is able to sense luminal acidification of the thylakoid membranes, which occurs along with elevated electron flow caused by excess light, and to induce a large, fast, and reversible pH-dependent quenching in LHCII-containing membranes. Mediates excitation energy transfer from light-harvesting complex II (LHCII) to photosystem I (PSI), rather than photosystem II (PSII), at low pH, which mimics the acidified lumen of the thylakoid membranes in high light-exposed chloroplasts. Activates PSI-dependent fluorescence quenching in addition to dissipating excitation energy in LHCII to avoid photooxidative stress under excess light.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10794530}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem II protein PSBS1
- Photosystem II protein PSBS2
- Photosystem I P700 chlorophyll a apoprotein A1
- Uncharacterized protein
Sequence:
MAMMMRKAAAVPASSRRSVAVNSVSGKRTVSGKAGAPVPEDVLAYAKTLPGVTAPFDNVFDPAGFLATASVKDVRRWRESEITHGRVAMLAALGFIVGEQLQDFPLFFNFDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKTLQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLVLRFEKEVILELEDVERDLGLPLTPLPDNLKAI
Protein: Uncharacterized protein C16C4.20c (Q9P7Z9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- HMG box-containing protein C10F6.08c
- INO80 complex subunit 1
- Probable actin-related protein 8
- INO80 complex subunit 4
- Actin-like protein arp5
- Chromatin-remodeling complex subunit ies6
- INO80 complex subunit 3
- SWI/SNF and RSC complexes subunit arp42
- Chromatin-remodeling ATPase INO80
- INO80 complex subunit 2
Sequence:
MDPQVVNLLQETEEDVYRRKTARIRRKVSEIEKECEMYAVKIYNVERDIQRYRHEAQLLSKVLEKKGLNKEKEAGET
Protein: Probable ATP-dependent helicase (Q9HYU6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- RNA helicase DbpA
- Small ribosomal subunit protein bS1
- Oligoribonuclease
- Ribonuclease D
- Nuclease SbcCD subunit D
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS11
- Nuclease SbcCD subunit C
- RNA 3'-terminal phosphate cyclase
- Ribonuclease 3
Sequence:
MTDQTPSLDQLVRRLDQAQISDRHRLRRQLHELRKQPDDARLAQWVERFQTSCAKVEARRASVPAIRYDDSLPIAAKRDEIKAAIAAHQVVVIAGETGSGKTTQLPKICLELGRGIHGLIGHTQPRRLAARSVATRVAEEIGTPLGALVGYQVRFEDQSDDSTLVKLMTDGILLAETQHDRYLERYDTLIVDEAHERSLNIDFLLGYLKTLLHRRPDLKLIITSATIDLERFSRHFDGAPVIEVSGRTYPVETWYRPLAAETDEEGNRVEDDLSVDQGILAALDEIAAHEREVGKRPGDVLVFLPGEREIRDAAEMLRKANLRHTEVLPLYARLTPAEQQKIFQPRPGRKIVLSTNVAETSLTVPGIRYVIDSGTARISRYSYRAKVQRLPIEAVSQASANQRKGRCGRVEPGICVRLYSEEDFNARPAFTDPEILRTNLAAVILQMLHLRLGDIEAFPFIEPPDGKAIKDGFTLLQELSAVNREGQLTPLGRQLARLPIDPRLGRMLLEAAQQGSLEEVLTVASALSVQDPRERPVERQQAADQAHAQWKDPDSDFAALINLWRGFEEQRQALGSNALRSWCRKNFLNYLRLREWRDAHRQLTLICRELKLPFGRPAKAEARKPEAKKGASADNEREVPGIDYAAVHKAILSGLLSQIGQKAEEGDYLGARQRRFWIHPSSGIARKRPQWIMAAELVETTKLFARMVAKIEPDWLEPLAGHLIKTNHFEPHWEKRRGQVVAFEQVTLYGLIVIGRRPVHYGPIDPPVARELFIREGLVRGEINSRAKCLSANRQLLEKLDELEAKARRRDILADEETLFAYYDARLPADIYQTASFEKWYARERQNQPDLLLMREEDVLAREASEVTAAQYPDRLRLGDLHLSLSYQFEPGTARDGVTVRVPAPLLPQLPAERIDWLVPGLLYDKAVALVRNLPKAIRKSFVPVPDFVRAALERITFGEGSLPQVLGRELQRMTGVRVADEAWAEAATQLDDHLRMNIEVVDAQGKFLGEGRDLAELTARFAEASQAALAIPQADKEQQRPVEAKAFASVAEKAQQKVAGLSMTVYPALVEEQGEVKEGRFPTQAEADYQHRRALQRLLLQQLAEPAKYLRAKLPGQTEMGLLYRELGRVEALVEDILLASLDSCVLQGESLPRDGAALAALAERKRAAWNEHAERLARLVLDILKLWHGLQKRFKGKVELAMTVPLNDVKGQLANLVYPGFVRATPLEWLKEYPRYLKAIEQRLDKVAGQVQRDRVWSGELGELWAQYQARLAKHAQEGKRDAELQVYRWMLEEYRVSLFAQQLGTRLPVSDKRLAKQWSQVEG
Protein: Ethylene-responsive transcription factor ERF012 (Dehydration response element-binding protein 26) (Q9SFE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator involved in the regulation of plant development and tolerance to abiotic stresses. Involved in salt and osmotic stress response pathways. May be regulated by the stress-related genes RD29A, RD22, DREB1A or P5CS during stress response. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:21069430}.
Interaction partners:
- At1g25400
- O-fucosyltransferase 20
- Protein EXORDIUM
- At1g31750
- Probable transcription factor At1g11510
- Heavy metal-associated isoprenylated plant protein 43
- Heavy metal-associated isoprenylated plant protein 33
- F21O3.6 protein)
Sequence:
MVKQERKIQTSSTKKEMPLSSSPSSSSSSSSSSSSSSCKNKNKKSKIKKYKGVRMRSWGSWVSEIRAPNQKTRIWLGSYSTAEAAARAYDVALLCLKGPQANLNFPTSSSSHHLLDNLLDENTLLSPKSIQRVAAQAANSFNHFAPTSSAVSSPSDHDHHHDDGMQSLMGSFVDNHVSLMDSTSSWYDDHNGMFLFDNGAPFNYSPQLNSTTMLDEYFYEDADIPLWSFN
Protein: Ring finger and WD repeat domain 2 (Q5BJY0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGPSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYGTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALSDGESNVLIAANSQGTIKVLELV
Protein: Putative methyltransferase Rv1506c (EC 2.1.1.-) (P71785)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably plays a role in host phagosome maturation arrest, as well as a role in the synthesis of acyltrehalose-containing glycolipids.
Interaction partners:
- Transferase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- Uncharacterized protein Rv1507c
- Probable sugar transferase
- Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
Sequence:
MRIVNAADPFSINDLGCGYGALLDYLDARGFKTDYTGIDVSPEMVRAAALRFEGRANADFICAARIDREADYSVASGIFNVRLKSLDTEWCAHIEATLDMLNAASRRGFSFNCLTSYSDASKMRDDLYYADPCALFDLCKRRYSKSVALLHDYGLYEFTILVRKAS