wanglab/gogpt-training-data huggingface dataset:
Protein: ER-bound oxygenase mpaB' (EC 1.-.-.-) (Mycophenolic acid biosynthesis cluster protein B') (A0A0B5LB52)
Organism: Penicillium brevicompactum
Function: ER-bound oxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaB' catalyzes the oxidative cleavage the C19-C20 double bond in farnesyl-DHMP (FDHMP) to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31209052}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSLSLPPALSELARALPYSRTQWLPILVGFLIGYPLLIKALRYKRLGEMKKKFYFPTRESMAEMTDEEAFLIQKEMAQLEFPFMFLTSGQFALFRTYGIPTISHLLTKTGQFSKPETSFKRYTDTAALIGEMVENSPTSQRAFISVARTRFLHSGYQASGKILDADLLYTLALFAVQPVRFIENFEWRTLSDLELCAIGTFWKSLGDALGISSEILPSGKTGFKDGIQWLEEVDVWSQDYEAKYMVPDPKNRESADQATAVLLYNLPKILHPIGLQFTSYMMDDRLRKAMLYEAPSPGWSAVFSSLLATRKFVLRYLSPPRPAALAVSNIAQKPDKDDRYHRMSWDALPFYIRPTFWNRWGPMAWISWLMAHPVPGDHGQKYYPQGYHIQDIGPKYFEGKGHKEIQEMMKELKISRTGKCPFH
Protein: Eukaryotic translation elongation factor 1 epsilon-1 (Elongation factor p18) (Multisynthase complex auxiliary component p18) (Q9D1M4)
Organism: Mus musculus (Mouse)
Function: Positive modulator of ATM response to DNA damage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15680327}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes at S phase and following DNA damage.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Aspartate--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Arginine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
Sequence:
MAAAAELRLLEKSLGLKPGNKYSAQGERQIPVLQTNNGPSLMGLSTIATHLVKQASKEHLLGSTAEEKAMVQQWLEFRVTRVDGHSSKEDTQTLLKDLNSYLEDKVYLAGHNITLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPDIRQHLSSIVFIKNRLYANSH
Protein: Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (Q9UU89)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Guanylate kinase
- Nucleoside diphosphate kinase
- Adenine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Adenylosuccinate synthetase
- GMP synthase
- Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
- Bifunctional purine biosynthesis protein ade10
- GTP cyclohydrolase 1
- AMP deaminase
Sequence:
MTILQSILFVTGNKHKLADVKNILGDRFEIKNHDYDLPEIQGSVKEVVLEKCKAAAEIVKGPVLVEDTWLGYKAMNGLPGPYVKWFLNSVGPDGLYRMVSAFDTKEAQAGCTFGYTKGPGKPIHLFEGILDGQVVPPRGSNGFGWNSIFQPNGHKHTYAEMTDEERNSCSHRYLAAMKLRDFLESEKN
Protein: Large ribosomal subunit protein bL35 (50S ribosomal protein L35) (Ribosomal protein A) (P0A7Q1)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein uL13
- Elongation factor Tu 1
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL15
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL11
- Translation initiation factor IF-3
Sequence:
MPKIKTVRGAAKRFKKTGKGGFKHKHANLRHILTKKATKRKRHLRPKAMVSKGDLGLVIACLPYA
Protein: Dehydrogenase/reductase SDR family member 6 (EC 1.1.1.-) ((R)-beta-hydroxybutyrate dehydrogenase) (3-hydroxybutyrate dehydrogenase type 2) (EC 1.1.1.30) (4-oxo-L-proline reductase) (EC 1.1.1.104) (Oxidoreductase UCPA) (Short chain dehydrogenase/reductase family 15C member 1) (Q561X9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (By similarity). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BUT1}.
Interaction partners:
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- 3-hydroxy-3-methylglutaryl-CoA lyase.
- Acetoacetyl-CoA synthetase
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- 3-hydroxybutyrate dehydrogenase, type 1
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MGRLDGKVIVLSAAAQGIGKASAIAFAKEGAQVTATDINGEKLKELDGIPGIKTKVVDVTKKDQVDALAKDFDHVDVLFNIAGFVHHGSILDCEESDWDFTMNVNVRSMYLMIKAFLPKMLARKSGNIINMASVASSIKGVVNRCVYSTSKAAVIGLTKSVAADFLEQGIRCNCICPGTVDTPSLRERIQARPDPEQAFKDFMARQRTGRLCTAEEVAHLCVYLASDESTFVTGTEVIIDGGWRL
Protein: histone acetyltransferase (EC 2.3.1.48) (A0A0G2QC09)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Cellular tumor antigen p53
- p300/CBP-associated factor
- Interferon regulatory factor 3
- Hypoxia-inducible factor 1-alpha
- Catenin beta-1
- Histone acetyltransferase
- Histone lysine acetyltransferase CREBBP
- Endothelial PAS domain-containing protein 1
- Cyclic AMP-dependent transcription factor ATF-4
Sequence:
SSSPSHGGLQPSVMRPKALFWYFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGPTQSTAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQSHKMGMMSNPTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMANSLPPSVQQPAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHYDTLSVRQILSR
Protein: Plasmepsin II (PLM II) (EC 3.4.23.39) (Aspartic hemoglobinase II) (PfAPD) (PfPM1) (Plasmepsin 2) (P46925)
Organism: Plasmodium falciparum (isolate HB3)
Function: During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation. May cleave preferentially denatured hemoglobin that has been cleaved by PMI. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).
Subcellular location: Membrane {ECO:0000269|PubMed:9169469}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P39898}. Vacuole lumen {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:9169469}. Vacuole membrane {ECO:0000269|PubMed:9169469}. Note=At the beginning of the asexual blood stage, the transmembrane zymogen is transported to the cytostome, an endocytic structure spanning the parasite cell membrane and the parasitophorous vacuole membrane where host proteins such as hemoglobin are endocytosed (PubMed:9169469). Following endocytosis, localizes to the cytostome vacuole membrane to be then delivered to the digestive (or food) vacuole where it is cleaved into the soluble and active enzyme (PubMed:9169469). In trophozoites, localizes to the digestive vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:11782538, PubMed:9169469). {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:9169469}.
Interaction partners:
Sequence:
MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL
Protein: Far1 (FusB) (Fusidic acid resistance) (Q8GNY5)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
MKTMIYPHQYNYIRSVILRLKNVYKTVNDKETVKVIQSETYNDINEIFGHIDDDIEESLKVLMNIRLSNKEIEAILNKFLEYVVPFELPSPQKLQKVFKKVKKIKIPQFEEYDLKVSSFVGWNELASNRKYIIYYDEKKQLKGLYGEISNQVVKGFCTICNKESNVSLFMKKSKTNSDGQYVKKGDYICRDSIHCNKQLTDINQFYNFIDKLD
Protein: AT4g37300/C7A10_60 (Maternal effect embryo arrest 59) (O23157)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ternary complex factor MIP1 leucine-zipper protein
- Putative RRM-containing protein family protein)
- Protein OXIDATIVE STRESS 3 LIKE 3
- Protein OXIDATIVE STRESS 3 LIKE 4
- UDP-glycosyltransferase 76E4
- Protein RALF-like 31
- AAA-ATPase At5g17760
- CASP-like protein 5A2
- ADP-ribosylation factor-like protein 8c
- LIMR family protein At5g01460
Sequence:
MSTMKPSRSDEISDPEQQIKNANQIRADFDSLAPKRPTKPTRSEPGFPGSFSASDKITDHPEADKFQSLQSQTHGKVLGEGDSSAVQDEFLETEYYSNLTAIDKQHHTTGSGFINVVKEDNGEESEAVTAAAIGDGGEKAVYRSNPATNEWIPATEEDFDSESSSKPNRSESS
Protein: Expansion, isoform A (A1Z8R1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSRRKILSRSRDDLNLDQTFTQQEEEEDIWFQKDKLYKEHIQEVLDKWTQIDDEIWAKVIVFERNRRVAKAYARAPVLTINGSDDGFDGMRIGLCGFDNPMRDQKTDEMKRVIGQGVKIKMDDAGNILIRRYAKSNVYVKSTASSPNEETSIGAEILKLPNQALESEKIVKLFDMKKFQSNVNRELRRAYPDRRRLETQCLSAVAFVKSENDILECPIWVLIVNVVAMDMLKSKLPPVQRPIVDIKNRPRIPIPDEDPYSVAGNGSGGSSGSSGFGSGHQAQLHPQQQLGKHLNGNGGGHVAATREQLLLQTQQLAHKRSEKPPKLPPRDNIYSHDLIPKPDYDDIDLETRIKLSRGKSDKGKDNKKYDDPYYCGLRARVPNFVKSGKPIPAQVAKDQRDGNGNNIGNGGISTLSQKKTSMIHNHLGGMHPHHIQQQQLMAAAAAAHAAQHHHAGHQREQQQHHQIWQTRSYESGIGIYKQGGPNAAHQSHKSHALQMQMHQQLQMQMQHQQQQQPQSLPTDLTATTATATTKTQSTANQARSHQPHPHLHPHSNPHAHPHHRLHRHVHVRCERHAHLQQQHSAPLQSVQHQPQQQQQPYYDNLEDSVARRVTRRHSTRRSAPEESSACNCVSCYALAPLCGAVPPPRPQRSLSQQQLRRHQRLSGSLVEQEVRPAVVKWCSESDVSVLELEPTEPTNERYDDCYDYDDFDMAFDLDDDLGLTENIPRRKGTETVDMYMDRSHLRQLQAPAVLRTKSQSTESFFEQPNEEGSLYMYGGRKRIAVKAPSATNIYDRVRGTIDYSDRRRSAAVAKGGQCHKKPQLPVPSWRGGKRQEQAQNADKRQRYDNATNGNSHGNGNNSSNNQHKRQLTNAKQDNEDMLKSKNYFNSKNKSIAAAAANAAAAAAASAATTAAAKATAASASIATTSGSGGAEPGAGAGATGVAGGKARGGGGPTMAPPLATTPAANNATAVSKAPSAPPPTASRTGRSTSRLDISDMESIYGYLKPRKPRSLSLKKIQILDY
Protein: Nitroreductase, putative (EC 1.6.99.3) (Q57XU3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit beta
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase I subunit RPA1
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerases II subunit, putative
- DNA-directed RNA polymerase II, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit
Sequence:
MNVSRCRWQGVIKSLRSYWKWNAGAALSATNSQNSTSPYETWGSGISRFFTFLRSSIAATAQEVPREPDRIPPTYYSKASRKSLDAFIRVVERRHSSKRFDSSRPVDHTLIARLLEATTRAPTAFNLQPWVAIVVHETSQRGALSHAALDQPQPREAPVTVVFAGDMEPEWRAPAALELGLNSGYYHPLYGAAYLRLVYYHLHGGPFGSMAKAKSCISSWYSNATGTPLLSVPTTMQGYAWKQAMIPATTFIYAATAAGLDTAILEGFDEAKVREVVGLPERYTVPVIISVGYKKADEQGKPPVRSPRFSTGSLVRWNRF
Protein: Zinc finger protein 296 (Hepatocellular carcinoma-associated antigen MHCA108) (E9Q6W4)
Organism: Mus musculus (Mouse)
Function: May be a transcriptional corepressor with KLF4.
Subcellular location: Nucleus {ECO:0000269|PubMed:24161396}.
Interaction partners:
- Growth/differentiation factor 3
Sequence:
MSRRKAGRVPRRVDPDTDTDIEMPDLVMDVKPDLDLRSLAQGPWIARDMPISDVKRQLQTASRPLGAPSTCAPRMPLSSKSSDRQPWTDKHPDLLTCGRCGKIFPLGAIIAFMDHKKQGCQLLQVSDPISESKELKALSCLQCGRQYTSPWKLLCHAQWDHGLCIYQTQHLDTPEAPLLGLAEVAAAMSAVAVVAPVESKPPPVSSAARRSPTCDVCKKTLSSFSNLKVHMRSHTGERPYSCDQCSYACAQSSKLNRHKKTHRQLAPGSPSTSASSRGVSPAAPPEPAAYAAAPASTLPSQTVEKAGAAATAGVQEPGAPGSGAQGGPGFVGWGAPAKVERTDPVKIEKTAPRKSHGPGGKCEFCGKSFTNSSNLTVHRRSHTGERPYTCDQCPYACAQSSKLNRHRRTHGLGTGKTVKCPHCLVPFGLQATLDKHLRQKHPEMA
Protein: Protein penguin (O61345)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein BRX1 homolog
- LD27920p
- Nucleolar GTP-binding protein 1
- Probable rRNA-processing protein EBP2 homolog
- Ribosomal L1 domain-containing protein CG13096
- Probable ATP-dependent RNA helicase pitchoune
- RRM domain-containing protein
- H/ACA ribonucleoprotein complex subunit 4
- Nucleolar protein 58
Sequence:
MVSSEPKGPANVANTASPLKAHESSGKRANGQKFKPGGAGGARKFDKFGGGAGKSFVKPGAGGAKKFDKSGPGGFKKFDKSGATGDKRLGGNKFRGKPQTQPQAPAEGEKQDWNKFKKEKKDLKLKRKSAKDTYEISKEANQIHEKLRCRRTENKDKLVEQIYKVLNVGDTISKVVKAHDTARVIQSMLKYASPALRAEISEKLLPFTVEMCQSKYAQFCVQRMLKYGAPATKAKLVDSLYGHIVRLAGHSIGSGLLDSMYQSATPNQRIYMRQEFYGDLYRKAKDSNVKTLSDTYKEATNMKASILGSVKANLDHVANKQLVDSALVHAVMLEYLRACDEDEEKLEETVTAFAALVPHMLSTKEGSEAAVICFYKSTPKNRRAIIKNIKEHLLKIANHEHGHVFLISLLNALDDTKATKKAIYDHLHGDLKALMSSPYGRRVIQWLVAPGDTTCFHPEFIRTVEEGLAFGKKEKELRRKEILEQIEAPIAQSIAEDAAFWLSNSHIGLVTGDILNHIQGESYEKAASALAQVVVQPEWRISADAAGPQPQDKKKPHNDVEAIIAQATKQRRKLLYVESSSDDEDEDEDEDEESDDEGDEKEQKEAAADDAEPKVKKAKKEPKKPKAKEEEPAAPLVSGIEEAGMHIVLKKILKNDGKREGTPFSQQLLQNLSSDVLKAWLGVNRACFVLLKLVEECPALLDDCKKAIAAERSLSQILADRKTPGAKLLAAKLDIGK
Protein: LD44438p (Q95RC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCHRPSRRPLNQSIVYKIDILEQNGRRIIQEYEIGMALIHCSITEFCNPTHKFISDSLPTTESVTSSMAFNSSIIVPNTERHSAQSNATPISELVVPESIECEMEQDASKPHSEDQASLRKRSHASTVDSSDEEKKSTLSKRAKSDIATKLTMKSKNAILLDSSLEEDVTPAPAPAPVQRVTRQSKAIAEEKSVHPPVPAASKHITRKTKQVFCVDSSDEENENARKPKETPAPTIPSMAKKKTEAPVATRISPRLNGKSLATNITNQPADKHAVPAKRPVLSVASSDEEDEGDLFQFRKSPQKPAETVVQPRIAGKGNAPARISVVDFLEKSQAQEPAPVPPQLESQSQTQPRKRLRLELLNESDSDDCDNLFNFADSKKKRKTQEAQRNDDSTDGLFNFNSERPSDHDDEDSRLTEPFVPETESKKQSKYIVAPRRDRPKKVDISGWLSCSRLNDNIKSEIDADSVKMETSIKADPDEEQWLAAMKDSIEVRMCNLNIVIRSQEEVDASLEDSVNKHGGRKNFKKFVKTKNPHPQKRIVALKSLRLADGMVTCV
Protein: Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5) (Q80Y14)
Organism: Mus musculus (Mouse)
Function: Monothiol glutaredoxin involved in mitochondrial iron-sulfur (Fe/S) cluster transfer. Receives 2Fe/2S clusters from scaffold protein ISCU and mediates their transfer to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export from mitochondrion (By similarity). Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q86SX6}.
Interaction partners:
- BolA-like protein 1
- Cysteine desulfurase
- Iron-sulfur cluster assembly enzyme ISCU
- BolA-like protein 2
- BolA-like protein 3
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- LYR motif-containing protein 4
- Iron-sulfur clusters transporter ABCB7, mitochondrial
Sequence:
MSASLSRAAAALLRWGRSAGGGGLPGAGVRAASSGGQAEQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELKKLGIRSALVDEKDQDSK
Protein: Protein LBH (Q7SXH0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR008130}. Cytoplasm {ECO:0000256|PIRNR:PIRNR008130}.
Interaction partners:
Sequence:
MTDVMISAAPMDDMRLSPSKERLTFQIFPDPSDFERCCKLKERLPSIVVEATEGEVESGELRWPPEDFLITEEKEEEEEEEEEDEDRQNTHNTKH
Protein: Actin, cytoplasmic 1 (Beta-actin) (EC 3.6.4.-) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed] (P29751)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}.
Interaction partners:
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEERPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Dynamin-related protein dnm1 (EC 3.6.5.5) (Q09748)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Microtubule-associated force-producing protein that mediates mitochondrial fission during interphasic growth and at cell division. Fission of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. With vps1, acts redundantly in peroxisome biogenesis, which is under cell cycle control.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19373772}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes at sites of mitochondrial constriction.
Interaction partners:
- Mitochondrial fission 1 protein
- Transmembrane GTPase fzo1
- Mitochondrial distribution and morphology protein 34
- Mitochondrial distribution and morphology protein 12
- Mitochondrial division protein 1
- Mitochondrial distribution and morphology protein 10
- Taz1-interacting factor 1
- Maintenance of mitochondrial morphology protein 1
- Mitochondrial fusion and transport protein ugo1
- Meiotic coiled-coil protein 5
Sequence:
MEQLIPLVNQLQDLVYNTIGSDFLDLPSIVVVGSQSCGKSSVLENIVGKDFLPRGTGIVTRRPLILQLINLKRKTKNNHDEESTSDNNSEETSAAGETGSLEGIEEDSDEIEDYAEFLHIPDTKFTDMNKVRAEIENETLRVAGANKGINKLPINLKIYSTRVLNLTLIDLPGLTKIPVGDQPTDIEAQTRSLIMEYISRPNSIILAVSPANFDIVNSEGLKLARSVDPKGKRTIGVLTKLDLMDQGTNAMDILSGRVYPLKLGFVATVNRSQSDIVSHKSMRDALQSERSFFEHHPAYRTIKDRCGTPYLAKTLSNLLVSHIRERLPDIKARLSTLISQTQQQLNNYGDFKLSDQSQRGIILLQAMNRFANTFIASIDGNSSNIPTKELSGGARLYSIFNNVFTTALNSIDPLQNLSTVDIRTAILNSTGSRATLFLSEMAFDILVKPQLNLLAAPCHQCVELVYEELMKICHYSGDSDISHFPKLQTALVETVSDLLRENLTPTYSFVESLIAIQSAYINTNHPDFLGVQGAMAVVLSRKEQNRLMLSQENDEPISSALDTVKPDGIELYSSDPDTSVKSITNKATNEITTLKSDDSAKMQPLDVLASKRYNNAFSTETAERKTFLSYVFGANNATRKAMSIDKSSSYPLNDSLSGGDTNHKNNHPLKMTDLSNEVETMALEDMSEREEVEVDLIKELITSYFNLTRKIIIDQVPKVIMHLLVNASKDAIQNRLVSKLYREDFFDTLLIEDENVKSEREKCERLLSVYNQANKIISTVF
Protein: Delta-aminolevulinic acid dehydratase (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (P10518)
Organism: Mus musculus (Mouse)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:4981581}.
Interaction partners:
- Porphobilinogen deaminase
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Uroporphyrinogen-III synthase
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Uroporphyrinogen decarboxylase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Protoporphyrinogen oxidase
- Ferrochelatase, mitochondrial
Sequence:
MHHQSVLHSGYFHPLLRSWQTAASTVSASNLIYPIFVTDVPDDVQPIASLPGVARYGVNQLEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPSLLVACDVCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKAALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVARDIQEGADMLMVKPGLPYLDMVREVKDKHPELPLAVYQVSGEFAMLWHGAQAGAFDLRTAVLETMTAFRRAGADIIITYFAPQLLKWLKEE
Protein: tRNA pseudouridine synthase (EC 5.4.99.12) (F4JZU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 2'-phosphotransferase
- 2'-phosphotransferase
- SH2 domain-containing protein A
- Vacuolar-sorting receptor 1
Sequence:
MASRVYVHYHHADACSKARWNARETFRFMYDRPWQHVLDFYSNAVEGNLSVLSLFQPKKSLVHDDGITEEMLLESEPETSTRKDGRSGRWERVNFKIVLSYNGASFDGWQKQPDLHTVQGVVEKSLGGFVDERKAQLLKKKCKPLEGRVLVAGRTDKGVSALNQVCSFYTWRKDIEPIAIEDAINKDASGKLRVVSISKVSRSFHPNFSAKWRRYLYIFPLDDAEPLRKSGENHENFIFDENKKKQRNGLLSEEIAEEVIMSEDDELEIEETSNALEVVEKPSDFSVSKVDQLLQHLQGKVLSYKMFARDTKAARNEGPPTECFMYHARAAEIRLSSSVVHFVAWVFGGSIVLVILATEGSTLDLTDTKLYIASWFLIKRSCEFLFIASDCVEGRRVMCVELVANRFLRKMVRVLVATSIREAAAGAEDDALLKLLEASCRRATAPPAPSEGLCLFDVGYTDFDPQTSLIS
Protein: Adenylosuccinate synthetase isozyme 1 (AMPSase 1) (AdSS 1) (EC 6.3.4.4) (Adenylosuccinate synthetase, basic isozyme) (Adenylosuccinate synthetase, muscle isozyme) (M-type adenylosuccinate synthetase) (Adenylosuccinate synthetase-like 1) (AdSSL1) (IMP--aspartate ligase 1) (Q8N142)
Organism: Homo sapiens (Human)
Function: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:15786719}.
Interaction partners:
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 1
- Inosine-5'-monophosphate dehydrogenase 2
- Trifunctional purine biosynthetic protein adenosine-3
- AMP deaminase 1
- GMP reductase 1
- Hypoxanthine-guanine phosphoribosyltransferase
- AMP deaminase 3
- Inosine triphosphate pyrophosphatase
Sequence:
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIISRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF