wanglab/gogpt-training-data huggingface dataset:
Protein: Protein STU1 (Suppressor of tubulin 1) (P38198)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for separation of the spindle poles during mitotic spindle formation. May cross-link overlapping antiparallel microtubules in the spindle midzone.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton. Chromosome, centromere, kinetochore. Note=Localizes to kinetochore microtubules and to the overlapping microtubules of the spindle midzone.
Interaction partners:
- Tubulin beta chain
- Protein STU2
- Kinesin-like protein CIN8
- Protein BIM1
- Outer kinetochore KNL1 complex subunit SPC105
- Anaphase spindle elongation protein
- Kinetochore protein SLK19
- Transcription factor TOG1
- Tubulin alpha-3 chain
- Dynein heavy chain, cytoplasmic
Sequence:
MSSFNNETNNNSNTNTHPDDSFPLYTVFKDESVPIEEKMALLTRFKGHVKKELVNESSIQAYFAALLFISGHYAYRSYPRLIFLSHSSLCYLIKRVAMQSPVQFNDTLVEQLLNHLIFELPNEKKFWLASIKAIEAIYLVNPSKIQAILANFLRRPSENQNGDYLNRIKSTLLTIDELIQINEKNNSNHLQLLRFFMLSFTNLLNNNLNEHANDDNNNVIIELIFDIMYKYLKMDDENSQDLIDGFINDLEVEKFKQKFISLAKSQDQHGSQEDKSTLFDEEYEFQLLLAEAKLPQLSNNLSSKDPAMKKNYESLNQLQQDLENLLAPFQSVKETEQNWKLRQSNIIELDNIISGNIPKDNPEEFVTVIKEVQLIELISRATSSLRTTLSLTALLFLKRLIHILNDQLPLSILDQIFVIFKNLLSSTKKISSQTAFHCLITLIIDINHFHNKLFQLSFLLINEKTVTPRFCSAILLRSFLIKFNDSNLSLNNSNTTSPTSKLENNIIYIEEWLKKGISDSQTTVREAMRLTFWYFYKCYPTNAKRLLSSSFSPQLKKATELAIPAHLNINYQVSRVSSTASASSATSRLYSHSSNNSSRKTSLLEQKRNYPSYAQPTQSSSTSLLNAPAVTAGGSVIASKLSNKLKTNLRSTSEYSSKENEKRARHHDSMNSVSNSNTKDNNNVTKRKVSAPPSSTAATKVSENYTNFDDFPSNQIDLTDELSNSYSNPLIKKYMDKNDVSMSSSPISLKGSNKLGEYETLYKKFNDASFPAQIKDALQYLQKELLLTSQQSSSAPKFEFPMIMKKLRQIMIKSPNDFKPFLSIEKFTNGVPLNYLIELYSINSFDYAEILKNRMNPEKPYELTNLIITIADLFNFLNANNCPNDFKLYYMKYKTTFFNYNFKLLLEIFRNLNIKHDNTLRSGTNDLMPKISMILFQIYGKEFDYTCYFNLIFEIYKFDNNRFNKLLADFDIVSTKMKICHELEKKDANFKVEDIISRESSVSFTPIDNKKSEGDEESDDAVDENDVKKCMEMTMINPFKNLETDKTLELKNNVGKRTSSTDSVVIHDDNDKDKKLSEMTKIVSVYQLDQPNPAKEEDDIDMENSQKSDLNLSEIFQNSGENTERKLKDDNEPTVKFSTDPPKIINEPEKLIGNGNENEKPDLETMSPIKINGDENMGQKQRITVKRERDVALTEQDINSKKMKLVNNKKSEKMHLLIMDNFPRDSLTVYEISHLLMVDSNGNTLMDFDVYFNHMSKAINRIKSGSFTMKHINYLIEPLITCFQNQKMTDWLTNENGFDELLDVAIMLLKSTDDTPSIPSKISSKSIILVHCLLVWKKFLNTLSENADDDGVSVRMCFEEVWEQILLMLNKFSDYGNEIYKLAQEFRDSLMLSHFFKKHSATRILSMLVTEIQPDTAGVKETFLIETLWKMLQSPTICQQFKKSNISEIIQTMSYFIMGTDNTSWNFTSAVVLARCLRVLQTTPDYTEQETERLFDCLPKNVFKMIMFIASNE
Protein: Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 1) (2-phosphoglycerate dehydratase 1) (P00924)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Enolase 2
- Fructose-bisphosphate aldolase
- Enolase-related protein 1
- Pyruvate kinase 1
- Phosphoglycerate mutase 1
- Glucose-6-phosphate isomerase
- Phosphoglycerate kinase
- Pyruvate kinase 2
- Phosphoglycerate mutase 2
- Glyceraldehyde-3-phosphate dehydrogenase 2
Sequence:
MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
Protein: (S)-stylopine synthase 1 (STS) (EC 1.14.19.64) (Cytochrome P450 719A2) (EcCYP719A2) (EcCYPB) (Q50LH3)
Organism: Eschscholzia californica (California poppy)
Function: Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (R,S)-cheilanthifoline to (S)-stylopine with a high substrate specificity. Catalyzes an oxidative reaction that does not incorporate oxygen into the product.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEEMKILMMNNPWILTATATTLLISIFLFFTRKSSKMVWPAGPKTLPIIGNMHLLGGTALQVVLHNLAKVHGSVMTIWIGSWRPVIVVSDIERAWEVLVNKSSDYSARDMPDITKIISADWKTISTSDSGPHWTNLRKGLQNVALSPHNLAAQFQFQEKDMTKMIQTLEEEARNNNGIVKPLDHMKKATLRLISRLVFGQDFNNDKYVDDMHLAIEELIRVSGYARLAEAFYYAKYLPSHKKAVREVEEAQRRVQNLVSPFLSLNPPTNTYLHFLRSQKYDDEVIIFAIFEAYLLGVDSTSLTTAWALAFLIREPNVQEKLYQELESFASKNDRRILKVEDINKLQYLQAVIKETMRMKPIAPLAIPHKACRDTSLMGKKIDKGTRVMVNIFALHHNKNVFNDPFKFMPERFMKVDSQDANGKAMEQSLLPFSAGMRICAGMELGKLQFSFALANLAYAFKWSCVADGVLPDMSDQLGFVLLMKTPLEARINRRN
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (Q6FYA7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32324}.
Interaction partners:
- L2
- Small ribosomal subunit protein uS2
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein uS5
- Candida glabrata strain CBS138 chromosome D complete sequence
- Large ribosomal subunit protein uL3
- 60S ribosomal protein L6
- 60S ribosomal protein L8
- Small ribosomal subunit protein eS6
- 40S ribosomal protein S8
Sequence:
MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGEARFMDTRKDEQERGITIKSTAISLYSDLPEEDVKEIPQKSDGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVCINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYSDEVLGDVQVYPSKGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKQKMMERLWGDSFFNPKTKKWTNKETDTDGKPLERAFNMFVLDPIFRLFAAIMNFKKDEIPTLLEKLEINLKSDEKDLEGKALLKVVMRKFLPAADALLEMIVMHLPSPVTAQNYRAEQLYEGPADDANCIAIKKCDPTADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKIRIQGPNYVPGKKDDLFLKAVQRVVLMMGSRVEPIDDCPAGNIVGLVGIDQFLLKTGTLTTSETAYNMKVMKFSVSPVVQVAVDVKNANDLPKLVEGLKRLSKSDPCVLTQMSESGEHIVAGTGELHLEICLQDLENEHAGIPLKISPPVVAYRETVEAESSQVALSKSPNKHNRIYLKAEPMDEEVSLAIEQGKINPRDDFKARARVMADEYGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVSAFQWATKEGPILGETMRSVRVNILDVTLHADAIHRGAGQIMPTMRRATYAGFLLAEPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWATLNSDPLDPTSKAGEIVTAARKRHGMKEEVPGWQEYYDKL
Protein: p53 apoptosis effector related to PMP-22 (Keratinocyte-associated protein 1) (KCP-1) (P53-induced protein PIGPC1) (Transmembrane protein THW) (Q96FX8)
Organism: Homo sapiens (Human)
Function: Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly.
Subcellular location: Cell junction, desmosome {ECO:0000250|UniProtKB:Q9JK95}. Cell membrane {ECO:0000269|PubMed:25486861, ECO:0000269|PubMed:30321533, ECO:0000269|PubMed:31898316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25486861}. Note=Associated with desmosomes (By similarity). Colocalizes with KRT14 in the cell membrane (PubMed:31898316). Clusters in a punctate pattern throughout the epithelial cytoplasm, in response to S.typhimurium infection (PubMed:25486861). {ECO:0000250|UniProtKB:Q9JK95, ECO:0000269|PubMed:25486861, ECO:0000269|PubMed:31898316}.
Interaction partners:
- Tumor protein 63
- Cellular tumor antigen p53
- Desmoplakin
- Desmocollin-3
- Plakophilin-3
- Plakophilin-1
- Desmoglein-1
- Desmoglein-2
- Desmoglein-3
Sequence:
MIRCGLACERCRWILPLLLLSAIAFDIIALAGRGWLQSSDHGQTSSLWWKCSQEGGGSGSYEEGCQSLMEYAWGRAAAAMLFCGFIILVICFILSFFALCGPQMLVFLRVIGGLLALAAVFQIISLVIYPVKYTQTFTLHANPAVTYIYNWAYGFGWAATIILIGCAFFFCCLPNYEDDLLGNAKPRYFYTSA
Protein: Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit) (Q01196)
Organism: Homo sapiens (Human)
Function: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells. Positively regulates the expression of RORC in T-helper 17 cells (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Protein CBFA2T1
- Protein C-ets-1
- Forkhead box protein P3
- Core-binding factor subunit beta
- Histone deacetylase 1
- T-cell acute lymphocytic leukemia protein 1
- Endothelial transcription factor GATA-2
- CCAAT/enhancer-binding protein alpha
- Transcription factor PU.1
- Histone acetyltransferase p300
Sequence:
MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVWRPY
Protein: GH01354p (SECIS-binding protein 2) (Q9VSH1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation elongation factor, selenocysteine-specific
- tRNA selenocysteine-associated protein 1
- Phosphoseryl tRNA kinase, isoform A
- O-phosphoseryl-tRNA
- Endoplasmic reticulum chaperone BiP
- Selenide, water dikinase 2
- Inactive selenide, water dikinase-like protein
Sequence:
MTEKIRRSRNQDVQDTAIKITPRSSKYKNQHRKREQQTSLLDFVIKPRPKTQRQTKAHKLQKTHLAITRGSYIVYKPKGKTRLDPKKKITRLKKSVRVYRTSKKAEREVAENDLEGVPVVGQDINPNAIPLEQQVQNLSLSKTPAPNNPSQAKTVHAIHSRRFRSYCDNCTRPRLKELSTQLLRDLDRFQKRAFAKNEIKARAHPRLVLGVREALARLRINKVKLLFLATDCEICPGESGLDATIEGLKFQCQQQQVPYCFPLLRRELSYALQKRAQICCVAILDFDGANATYADLLNEIEDARAEYKRRTAS
Protein: Collagen and calcium-binding EGF domain-containing protein 1 (Full of fluid protein homolog) (Q3MI99)
Organism: Mus musculus (Mouse)
Function: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6UXH8}.
Interaction partners:
- ADAM metallopeptidase with thrombospondin type 1 motif 3
- Vascular endothelial growth factor C
Sequence:
MVPPPLPSRGGAAKRQLGKSLGPLLLLLALGHTWTYREEPEDRDREVCSENKITTTKYPCLKSSGELTTCFRKKCCKGYKFVLGQCIPEDYDICAQAPCEQQCTDNFGRVLCTCYPGYRYDRERHQKRERPYCLDIDECATSNTTLCAHICINTMGSYHCECREGYILEDDGRTCTRGDKYPNDTGHEEKSENEVKAGTCCATCKEFSQMKQTVLQLKQKMALLPNNAAELGKYVNGDKVLASNAYLPGPPGLPGGQGPPGSPGPKGSPGFPGMPGPPGQPGPRGSMGPMGPSPDLSHIKQGRRGPVGPPGAPGRHGSKGERGAPGPPGSPGPPGSFDFLLLVLADIRNDIAELQEKVFGHRTHSSAEDFPLPQEFSSYPETLDFGSGDDYSRRTEARDPEAPRNFYP
Protein: 14-3-3 protein sigma (Stratifin) (O70456)
Organism: Mus musculus (Mouse)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16710422}. Nucleus {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250|UniProtKB:P31947}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250|UniProtKB:P31947}.
Interaction partners:
- Cellular tumor antigen p53
- G2/mitotic-specific cyclin-B1
- E3 ubiquitin-protein ligase Mdm2
- M-phase inducer phosphatase 3
- Cyclin-dependent kinase 1
- Keratin, type I cytoskeletal 17
- E3 ubiquitin-protein ligase NEDD4-like
- Protein Mdm4
- G2/mitotic-specific cyclin-B2
- Forkhead box protein O1
Sequence:
MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVKEYREKVETELRGVCDTVLGLLDSHLIKGAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADSAGEEGGEAPEEPQS
Protein: Ste13p (Q59M48)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Kexin
- Pheromone-processing carboxypeptidase KEX1
Sequence:
MFTHKRVPQHEEYELVNQVPPTQSPTDSPTRSESDFRNSTDSQLSDIFEDLENYSGSSGQKIEDFNDSPLFQSVLMRYKNEGISGRTCGIFSLVAIFLWIGSVIIYSRVNHSTIGNDLTWKTNIIQLNGENITLNEYNPNFKNITMNDWRKGKYHTFEKQIRWLTSKQSPKSKHGGGFYVLDEHDKIVVNQIGQVDKSDTFLSNKQFEYGNNFFKIQDFILNPSQSIEDSEVVHIIITDTVHQWRHSSFALYWLFKPLVGTYTPIQPPRNNNKGNGLEVDALDKLHYADFSSDGKYIVFGFEHNLFIQDLATGEIQQITDDGSPNIINGKSDWIYEEEVIASNKMIWWSPSGNHFIFAKINETKVQEVDMDYYTKQNTNIGMQYQQVGESKYEGVNQYPINTQLKYPKPGTSNPILSLYIYDIANKKTEEIIDGDDNLGTEYILYYAKWIDANSFLMKQSDRTSSVLTKKLYDLDKNHVSIVSSSNVTKEYKGWVERMNPITLLDDGKYIDNVVIDNRNTLALFDSPHSVSPSKVLVDNKDWDITGEAIYDAQEKFVYFLSTVRSSMDAHLVGIDLADNYKLYNITDTKKDGIFETKFSENGQYLSLVYQGPNQPWQRLINMANVHDFIKSEEYGKSTIEEAVILNQPIVNSLANLKEINLPTVRYKEVTIGKKEDQVTLNIMEILPPNFKAKNQKYPLFVYTYGGPGSQTVMKKFDIGFLQIVSARLNSIILVIDPRGTGGKGWKFESFAKNNIGYWESRDLKTITSEYIKKNKKLIDKERVALWGWSYGGFVTLKTLEYDKGEVFKYGMAVAPVTNWLFYDSIYTERYMGLPDTDPNYETSARINDFDNFKSVKRFLLVHGTGDDNVHVQNLMWLLDQLNIHNVENYDMHLFPDSDHSISYDNAGVIVYDKLYYWLQNAFRGNFDELN
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Alpha-D-glucosyl-1-phosphate uridylyltransferase) (UDP-glucose pyrophosphorylase) (UDPGP) (Uridine diphosphoglucose pyrophosphorylase) (Q9I291)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: May play a role in stationary phase survival.
Interaction partners:
- UDP-glucose 4-epimerase
- UDP-glucose 6-dehydrogenase
- Phosphomannomutase/phosphoglucomutase
- Probable epimerase
- UDP-glucose 6-dehydrogenase
- Glucose-1-phosphate thymidylyltransferase
- Alpha-1,4 glucan phosphorylase
- 4-alpha-glucanotransferase
- Homogentisate 1,2-dioxygenase
- Phosphoglucosamine mutase
Sequence:
MIKKCLFPAAGYGTRFLPATKAMPKEMLPVVNKPLIQYAVEEALEAGLSEIGIVTGRGKRSLEDHFDISYELEHQIRNTDKEKYLVGIRRLIDECTFAYTRQVEMKGLGHAILTGRPLIGDEPFAVVLADDLCLNLEGDSVLKQMVKLYNQFRCSIVAIQEVPPEETNKYGVIAGEMIRDDIFRVNTMVEKPKPEEAPSNLAIIGRYILTPDIFDLIEQTEPGKGGEIQITDALMKQAQDGCVLAYKFKGKRFDCGSAEGYIEATNFCYENLYKTGKAH
Protein: Transcription factor A, mitochondrial (mtTFA) (Q91ZW1)
Organism: Rattus norvegicus (Rat)
Function: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA (By similarity).
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:Q00059}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q00059}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus.
Interaction partners:
- Dimethyladenosine transferase 2, mitochondrial
- DNA-directed RNA polymerase
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear respiratory factor 1
- Dimethyladenosine transferase 1, mitochondrial
- Cellular tumor antigen p53
- DNA polymerase subunit gamma-1
- Single-stranded DNA-binding protein, mitochondrial
- NAD-dependent protein deacetylase sirtuin-1
- Nuclear factor erythroid 2-related factor 2
Sequence:
MALFRGMWGVLRTLGRTGVEMCAGCGGRIPSPVSLICIPKCFSSLGNYPKKPMSSYLRFSTEQLPKFKAKHPDAKVSELIRKIAAMWRELPEAEKKVYEADFKAEWKVYKEAVSKYKEQLTPSQLMGLEKEARQKRLKKKAQIKRRELILLGKPKRPRSAYNIYVSESFQEAKDESAQGKLKLVNQAWKNLSHDEKQAYIQLAKDDRIRYDNEMKSWEEQMAEVGRSDLIRRSVKRPPGDISEN
Protein: Large ribosomal subunit protein uL3m (50S ribosomal protein L3-2, mitochondrial) (Q9LRN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Subcellular location: Mitochondrion {ECO:0000255, ECO:0000303|PubMed:36423343}.
Interaction partners:
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL4m
- 50S ribosomal protein L20
- Putative ribosomal protein L6
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL22c
- At1g43860
- At1g64880
Sequence:
MAAVPRGLLSRINQFLSIRSITPSSSESLPHCSSFFLIRRFSSDTGLMDGGGSDIIGAQTRIIEAKQGEMSSRSKRTGIIAVKCGMTALWDKWGKRIPISILWVDDNIVSQVKTVEKEGIFALQIGCGQKKPKHLSKAVVGHFRAQGVPLKRKLREFPVTEDALLPVGTSLGVRHFVPGQYVDVTGITRGKGFQGCMKRHGFSGMPASHGASLSHRSGGSTGQRDAPGKVFKGRKMAGRMGADQRTVKNVWVYKIDPARNLMWVRGQVPGAEGNFVFIKDAWCKKPDISKLPFPTYLAPEDEDPSELEPLVADLGEVDPFMLAE
Protein: Tripartite motif-containing protein 6 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM6) (Q8BGE7)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase that plays a crucial role in the activation of the IKBKE-dependent branch of the type I interferon signaling pathway. In concert with the ubiquitin-conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-48'-linked polyubiquitin chains that promote the oligomerization and autophosphorylation of IKBKE leading to stimulation of an antiviral response. Ubiquitinates also MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22328504}.
Interaction partners:
Sequence:
MTSTVLVDIRDEVTCPICLELLTEPLSIDCGHSFCQVCIIGNSNNSVFGQGGRSSCPVCRTSYQPGNLRPNRHLAAIVKRLREVALCPGKQLEVIFCALHGEKLQLFCKEDGKLICWLCERSQEHRGHHTFLMEEVAQEYQDMFQESLKKLRREQQEAEKLKALIQEKRESWKSQVEPEKRRIQTEFKQLRSILDREEQRELKKLEVEERKGLSIIEKAEGDLIHQSQSLKDLISDLEHRCQGSTVELLQDVGDVTKRSEFWTLRKPQALPTKLKSLFRAPDLRKMLKVFRELTDVQSYWVDVTLNPQTANLNLVLSKNRRQVRFVGAQLSEPSSLEEHYDCSVLGSQHFSSGKYYWEVDVSKKTAWILGVCSTPVDPMFSFSQYSSKQGAYSRYQPQCGYWVIGLQCKHEYRAYEDSSPSLLLSMTVPPRRIGIFLDCEAGTVSFYNVTNHGLPIYTFSKYYFPSALCPYFNPCSCIVPMTLRRPTS
Protein: Elongin-A (Protein pof4) (O59671)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit rpb1 to trigger its proteolysis; plays a role in global genomic repair.
Interaction partners:
- Elongin-C
- F-box protein pof14
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL13
- Tetratricopeptide repeat protein 1
- Uncharacterized protein C13E7.08c
- FACT complex subunit pob3
Sequence:
MYSLKDLCIQVAQKHVHDIDDIGDCPFELVKPILEKARPEHLIDLEEKSPHLKVDTQPLWKDHVLRDFGLELQKRTILNNIDDWRGLYGKLKKKRNAHYNVASAKLRSAYTKLEQSKQNKRIVPLEREPRAARPPKRPRPMSNYCPKSSLMARAKSDFLKKASATRHIVSATSSSRSFPQLHPLGRSSSNATNTSTKRPLTSNTYPSIPLPPKSFTSQNFKSFNAVKTQPSSSSSPSISRPTSFPMSFFPNPSRFSSQVPKRI
Protein: L-threonine 3-dehydrogenase, mitochondrial (EC 1.1.1.103) (Q8K3F7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8MIR0}.
Interaction partners:
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- L-threonine aldolase
- Serine dehydratase-like
- L-serine dehydratase/L-threonine deaminase
- Ubiquitin-like protein FUBI
- Glycine C-acetyltransferase
Sequence:
MLFLGMLKQVVNGTAQSKASSCRKLVLPLKFLGTSQHRIPADANFHSTSISEAEPPRVLITGGLGQLGVGLANLLRKRFGKDNVILSDIRKPPAHVFHSGPFVYANILDYKSLREIVVNHRISWLFHYSALLSAVGEANVSLARDVNITGLHNVLDVAAEYNVRLFVPSTIGAFGPTSPRNPAPDLCIQRPRTIYGVSKVHTELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYAVQIFHAAAKNGTFECNLEAGTRLPMMYISDCLRATLEVMEAPAERLSMRTYNISAMSFTPEELAQALRKHAPDFQITYCVDPLRQAIAESWPMILDDSNARKDWGWKHDFDLPELVATMLNFHGVSTRVAQVN
Protein: GM06875p (Q8MSZ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEEDLRICSVRPLNEGDRRFCFEVISPTKSHILQADSADMLSLWISALQHSIGAAIQHDSTHHSRPQSTNAPNNSLPAKRRIHWEEFLKIPGNAYCCDCRSPEPRWASINLGITLCIECSGVHRSLGVHYSKVRSLTLDAWESENVKVMMELGNEVVNRIYEARIGDDCGLKKPTEQCEIGVREAWIKAKYVERRFVCGMPKPQELLASETAEVLSIDSGGVVEDGESGGSGIAK
Protein: Striatin 4 (A0A8I6AK86)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
PTGAAQAQVAFLQGERKGQENLKTDLVRRIKMLEYALKQERAKYHKLKFGTDLNQGEKKADLSEQVSNGPVESVTLDNSPLVWKEGRQLLRQYLEEVGYTDTILDMRSKRVRSLLGRSLELNGAGEPVEGAPRASPGPGGLSGGESLLVKQIEEQIKRNAAGKDGKERLGGSVLEQIPFLQNCEDEDSDEDDELDSVQHKKQRVRLPSKALVPEMEDEDEEDDSEDAINEFDFLGSGEDGEGSPDPRRCASEGNPHELESRRVKLQGILADLRDVDGLPPKVTVPPPGTPQPRPHEDVFIMDTIGGGEVSLGDLADLTVTNDNDLSCDLSDSKDAFKKTWNPKFTLRSHYDGIRSLAFHHSQSALLTASEDGTLKLWNLQKAVTAKKNAALDVEPIHAFRAHRGPVLAVTMGSNSEYCYSGGADARIHSWKIPDLNMDPYDGYDPSVLSCVLEGHGDAVWGLAFSPTSQRLASCSADGTIRIWDPSSSGSSCLCTFPMAGEHGIPTSVAFTSTEPAHVVASFRSGDTVLYDLEAGGALLTLESRGSSGPTQINQVVSHPNQPLTITAHDDRGIRFLDNRTGKSVHSMVAHLDAVTCLAVDPNGVFLMSGSHDCSLRLWSLDNKTCVQEITAHRKKHEEAIHAVACHPSKALIASAGADALAKVFV