wanglab/gogpt-training-data huggingface dataset:
Protein: Probable rRNA-processing protein EBP2 homolog (Q9LUJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the processing of the 27S pre-rRNA (By similarity). Plays an important role in plant growth and senescence by modulating ribosome biogenesis in nucleolus. Associates with ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:26163696}.
Interaction partners:
- At4g01560
- Ribosome biogenesis protein BOP1 homolog
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein WDR12 homolog
- Ribosome biogenesis protein BRX1 homolog 2
- Ribosome biogenesis protein BRX1 homolog 1
- Pescadillo homolog
- AT5g04600/T32M21_200
- AT5g20600/F7C8_190
- 60S ribosome subunit biogenesis protein NIP7 homolog
Sequence:
MSLEEDIVSDDEMNMIDEDDATDSEAESLSDSDTENEITEKLAEPTKTAIYNRDGLLDKLQDISWPEDVDWTHKLTVEIDQGGAVDVNDDLARETAFYTQALEGTREAFGKLNEMGVNFLRPANYYAEMVKSDVHMEKVKSRLLHEKKQIEESEERRKARDNKRMAKEVQSQKMKERAKEKKDNIESVKKWRKQRQQSGFSDKAGEPELDFESGKSFQRGGGKKRPGVSPGDRSGGKGRPTSRMGNKKREFRDSKFGHGGRKGLSKQNTAETTNDFKGGFRGGKASGNKRQKR
Protein: Endothelin-1 (Q9I8G3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MHLRIIFPVLTMLTSGFFDFGAPASLGPGTAPARHSRNKRCSCASFLDKECVYFCHLDIIWVNTPERTVSYGLGNAPRKKRSVTEPVVLESRCKCADSQDKTCSSFCQADSALQFKAASDRAIRAAQGHDCAGKQCKHKLAETQTKIRRLRTTKQTDVLSGKKKIQLLLEKWRMRRNHRSQAWISENS
Protein: Classical arabinogalactan protein 11 (Q9FVE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Arabinogalactan protein 23
- Arabinogalactan protein 40
- Fasciclin-like arabinogalactan protein 3
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 11
- Transcription initiation factor IIF subunit alpha
- FACT complex subunit SSRP1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH subunit TFB4
Sequence:
MARLFVVVALLALAVGTVFAADAPSAAPTASPTKSPTKAPAAAPKSSAAAPKASSPVAEEPTPEDDYSAASPSDSAEAPTVSSPPAPTPEADGPSSDGPSSDGPAAAESPKSGATTNVKLSIAGTVAAAGFFIFSL
Protein: Schlafen family member 4 (A0A0G2K4S0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGNLPRLVEDVNPQTFTEPSVQLKCPGNIFQGGRHAKPGSWKDSQKGFHLGSRDSNCKMSITVDQDTDYAELVLSIGEITLGEKTRKSMKDSQRRKREAKTFQQAVCTLLNSGGGVAKARIKNQNYDFSRDGVGQDLENFLPHILDFPHEYLDFKQVKDYFLMFVKAWKLKQKGPGITTLKTNLYIRSISSSIELKAVNAVKFLKSRLSSPGTIVCNEVLNECLNLFNRDCFTCKEKFCFTKATHAEVKLTPKENILEILPQTVSSFANADGGYLFIGLDGKTQEIIGFEAEKSDLVHLESEIEKCIRQLPVTHFCEEREKIKYTCKFMEVHKPGAACSFVCALRVERFCCAVFAAEPESWHVEDSCVKRFTAEDWVKRQMDGPALISGKVISSPEALCGKLFSTQEAHEQLLWAQLDSLPKGTLVVTKRWALDLPLQDKHGVILDTLHIPQDSLLTLHGFVLGGEDLEDDSTLLRELGAELKGYYKQTAVTLKQTLANHGSYTEKIGIAIKITYLGHNKAVSLYDSSSKIHYPTKYYLTTETAKNLEKALAEILGS
Protein: CheY2 (Response regulator) (Q52884)
Organism: Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
- Chemotaxis protein CheA
- CheY1
- STAS domain-containing protein
- Chemotaxis protein CheW
- Chemotaxis protein
- Chemotaxis protein methyltransferase
- Chemotaxis protein CheW
- Methyl-accepting-chemotaxis-protein
- Flagellar motor switch protein FliN
- Response regulator
Sequence:
MSLAEKIKVLIVDDQVTSRLLLGDALQQLGFKQITAAGDGEQGMKIMAQNPHHLVISDFNMPKMDGLGLLQAVRANPATKKAAFIILTAQGDRALVQKAAALGANNVLAKPFTIEKMKAAIEAVFGALK
Protein: RNA-binding protein KhpB N-terminal domain-containing protein (O25990)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- KH domain-containing protein
- VirB11 homolog
- Membrane protein insertase YidC
- Ribonuclease P protein component
- Putative membrane protein insertion efficiency factor
- Large ribosomal subunit protein bL34
- tRNA modification GTPase MnmE
- 3',5'-cyclic-nucleotide phosphodiesterase
- Outer membrane protein assembly factor BamD
- Plasminogen-binding protein PgbB
Sequence:
MQNFIEIKAKTLEEALIQASIALNCPIINLQYEVIQTPSKGFLSIGKKEAIILAGVKESVKEIKEESVKETNTKEIHQSAEEKKQKLETETPQEEIITPKPSKKNPKEESHSGDKLHEIKQELKDLFSHLPYKINKVEVSLYEPGVLLIDIDGEDSALLIGEKGYRYKALSYLLFNWIHPTYGYSIRLEISTFLQNQEKVMDTQLQSVIMTVHEVGKGQMKAPDGVLTYIALKKLRKAFPNKYVSIKTNLNDEKYIVINDFNNE
Protein: Guanidino acid hydrolase, mitochondrial (EC 3.5.3.-) (Arginase, mitochondrial) (EC 3.5.3.1) (Guanidinobutyrase, mitochondrial) (EC 3.5.3.7) (Guanidinopropionase, mitochondrial) (EC 3.5.3.17) (Q9BSE5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Antizyme inhibitor 2
- Spermidine synthase
- Ornithine decarboxylase
- Diamine acetyltransferase 1
- Diamine oxidase [copper-containing]
- Ornithine aminotransferase, mitochondrial
- Thialysine N-epsilon-acetyltransferase
- Spermine synthase
- Ornithine transcarbamylase, mitochondrial
- Ketimine reductase mu-crystallin
Sequence:
MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMMRLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLMVADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVGLLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQGFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVMGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV
Protein: Dual specificity protein phosphatase 8 (EC 3.1.3.16) (EC 3.1.3.48) (Neuronal tyrosine threonine phosphatase 1) (O09112)
Organism: Mus musculus (Mouse)
Function: Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation. Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8733137}. Nucleus {ECO:0000269|PubMed:8733137}.
Interaction partners:
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
Sequence:
MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSCHVLSSVNICCSKLVKRRLQQGKVTIAELIQPATRSQVDATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPATLPSMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRIPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQTDGPHLGTPEPLMGPAAGIPLPRLPPSTSESAATGSEAATAAREGSPSAGGDAPIPSTAPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDFPGPPDPGEAPKLCKLDSPSGGTLGLPSPSPDSPDSVPECRPRPRRRRPPASSPARSPAHGLGLNFGDTARQTPRHGLSALSAPGLPGPGQPAGPGGWVPPLDSPGTPSPDGPWCFSPEGAQGPGAVFSAFGRVSAGAPGPGNSSSSGGGGGGGGGGGGGGGGGGSSSSNSSSSSSSSSSSSSSSSSSSDLRRRDVRTGWPEEPAADAQFKRRSCQMEFEEGMVEGRARGEELAALGKQTSFSGSVEVIEVS
Protein: Glycerol-3-phosphate transporter (G-3-P transporter) (G-3-P permease) (P08194)
Organism: Escherichia coli (strain K12)
Function: Responsible for glycerol-3-phosphate uptake.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Glycerophosphodiester phosphodiesterase, periplasmic
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Glycerol uptake facilitator protein
- Glycerol kinase
- Anaerobic glycerol-3-phosphate dehydrogenase subunit C
- Anaerobic glycerol-3-phosphate dehydrogenase subunit B
- Lactose permease
- Aerobic glycerol-3-phosphate dehydrogenase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- L-fucose-proton symporter
Sequence:
MLSIFKPAPHKARLPAAEIDPTYRRLRWQIFLGIFFGYAAYYLVRKNFALAMPYLVEQGFSRGDLGFALSGISIAYGFSKFIMGSVSDRSNPRVFLPAGLILAAAVMLFMGFVPWATSSIAVMFVLLFLCGWFQGMGWPPCGRTMVHWWSQKERGGIVSVWNCAHNVGGGIPPLLFLLGMAWFNDWHAALYMPAFCAILVALFAFAMMRDTPQSCGLPPIEEYKNDYPDDYNEKAEQELTAKQIFMQYVLPNKLLWYIAIANVFVYLLRYGILDWSPTYLKEVKHFALDKSSWAYFLYEYAGIPGTLLCGWMSDKVFRGNRGATGVFFMTLVTIATIVYWMNPAGNPTVDMICMIVIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGSVAASAIVGYTVDFFGWDGGFMVMIGGSILAVILLIVVMIGEKRRHEQLLQERNGG
Protein: Cysteine protease 1 (EC 3.4.22.-) (OsCP1) (Q7XR52)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Cysteine protease that may play a role in pollen development. May be regulated by the transcription factor UDT1 in developing anthers and play a role in tapetum development. Positively regulated by the transcription factor TDR in developing anthers and may play a role in tapetum programmed cell death (PCD).
Interaction partners:
- Os07g0295200 protein
- Os01g0347600 protein
- Oryzain alpha chain
- Os05g0508300 protein
- Oryzain beta chain
- Os03g0292200 protein
- Os07g0627800 protein
- Os04g0686300 protein
- Os08g0466050 protein
- DNA polymerase II subunit 2
Sequence:
MAGGGGKSVAAALAMACFLLILAAFAPPAAAAPPDIMSIIRYNAEHGVRGLERTEAEARAAYDLWLARHRRGGGGGSRNGFIGEHERRFRVFWDNLKFVDAHNARADERGGFRLGMNRFADLTNGEFRATYLGTTPAGRGRRVGEAYRHDGVEALPDSVDWRDKGAVVAPVKNQGQCGSCWAFSAVAAVEGINKIVTGELVSLSEQELVECARNGQNSGCNGGIMDDAFAFIARNGGLDTEEDYPYTAMDGKCNLAKRSRKVVSIDGFEDVPENDELSLQKAVAHQPVSVAIDAGGREFQLYDSGVFTGRCGTNLDHGVVAVGYGTDAATGAAYWTVRNSWGPDWGENGYIRMERNVTARTGKCGIAMMASYPIKKGPNPKPSPPSPAPSPPQQCDRYSKCPAGTTCCCNYGIRNHCIVWGCCPVEGATCCKDHSTCCPKEYPVCNAKARTCSKSKNSPYNIRTPAAMARSVPEQPDSISFVVLNREDLV
Protein: Class II histocompatibility antigen, M alpha chain (P28078)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in catalyzing the release of class II-associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides.
Subcellular location: Late endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Localizes to late endocytic compartment. Associates with lysosome membranes.
Interaction partners:
- H2-M beta 2
- Class II histocompatibility antigen, M beta 1 chain
- H2-O alpha
- H-2 class II histocompatibility antigen gamma chain
- H-2 class II histocompatibility antigen, E-B beta chain
- Histocompatibility 2, O region beta locus
- H-2 class II histocompatibility antigen, A beta chain
- T-cell surface glycoprotein CD4
- H-2 class II histocompatibility antigen, A-B alpha chain
- T-cell surface glycoprotein CD3 zeta chain
Sequence:
MEHEQKSGAVLLRLLRLLWLLPHSWAVLEASTPVLWDDPQNHTFRHTLFCQDGIPNIGLSETYDEDELFSFDFSQNTRVPRLPDFAEWAQGQGDASAIAFGKSFCEMLMREVSPKLEGQIPVSRGLSVAEVFTLKPLEFGKPNTLVCFISNLFPPTLTVNWQLHSAPVEGASPTSISAVDGLTFQAFSYLNFTPEPFDLYSCTVTHEIDRYTAIAYWVPQNALPSDLLENALCGVAFALGVLGTIIGIVFFLCSQRPCSGD
Protein: Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D1) (Ubiquitin carrier protein D1) (Ubiquitin-conjugating enzyme E2(17)KB 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase D1) (D3ZDK2)
Organism: Rattus norvegicus (Rat)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4 (By similarity). Mediates ubiquitination of PEX5.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P51668}.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- STIP1 homology and U-Box containing protein 1, isoform CRA_b.
- E3 ubiquitin-protein ligase Mdm2
- E3 ubiquitin-protein ligase RNF4
- Anaphase-promoting complex subunit 11
- Ubiquitin-conjugating enzyme E2 D2B
- Ubiquitin-conjugating enzyme E2 D3
- Polyubiquitin-C
- Ubiquitin conjugating enzyme E2 V1 like 1
- Anaphase-promoting complex subunit 4
Sequence:
MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM
Protein: histone acetyltransferase (EC 2.3.1.48) (B0R0X6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADHSVEITEGCRLPVLRRNQENEDEWPLAEILSVKDISGRKLYYVHYVDFNKRLDEWVTPDRLDIKKLQFPKKEAKTPMKNGLSGSRPSSPERDVKKSLDLHVQSASAPSRGKTVPTPKRKAESVSLATQVTAATPVPSLPASTEASQAALYTAIRDASFNIKSREEHEPLTSLTTNGTTSIQRHLIPPQPGRKRKNCGGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIGCIELGRHRLKPWYFSPYPQELTSLPIIYLCEFCLKYLKSLKCLQRHLTKCNLRHPPGNEIYRKGTISFFEIDGRKNKAYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDPKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMDLKSENGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVEGHECAMQKRHLRIDPKCLHFTPKDWSKRGKW
Protein: Coiled-coil domain-containing protein 39 (Q9UFE4)
Organism: Homo sapiens (Human)
Function: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (By similarity). Not required for outer dynein arm complexes assembly.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:21131972, ECO:0000269|PubMed:21131974, ECO:0000269|PubMed:27120127}. Note=CCDC40 is required for localization to axonemes. {ECO:0000269|PubMed:21131974}.
Interaction partners:
- Coiled-coil domain-containing protein 40
- Dynein regulatory complex subunit 2
- Radial spoke head protein 4 homolog A
- Dynein regulatory complex protein 1
- Dynein axonemal intermediate chain 2
- Radial spoke head protein 9 homolog
- Dynein axonemal assembly factor 3
- Dynein axonemal heavy chain 5
- Dynein axonemal assembly factor 11
- Outer dynein arm-docking complex subunit 2
Sequence:
MSSEFLAELHWEDGFAIPVANEENKLLEDQLSKLKDERASLQDELREYEERINSMTSHFKNVKQELSITQSLCKARERETESEEHFKAIAQRELGRVKDEIQRLENEMASILEKKSDKENGIFKATQKLDGLKCQMNWDQQALEAWLEESAHKDSDALTLQKYAQQDDNKIRALTLQLERLTLECNQKRKILDNELTETISAQLELDKAAQDFRKIHNERQELIKQWENTIEQMQKRDGDIDNCALELARIKQETREKENLVKEKIKFLESEIGNNTEFEKRISVADRKLLKCRTAYQDHETSRIQLKGELDSLKATVNRTSSDLEALRKNISKIKKDIHEETARLQKTKNHNEIIQTKLKEITEKTMSVEEKATNLEDMLKEEEKDVKEVDVQLNLIKGVLFKKAQELQTETMKEKAVLSEIEGTRSSLKHLNHQLQKLDFETLKQQEIMYSQDFHIQQVERRMSRLKGEINSEEKQALEAKIVELRKSLEEKKSTCGLLETQIKKLHNDLYFIKKAHSKNSDEKQSLMTKINELNLFIDRSEKELDKAKGFKQDLMIEDNLLKLEVKRTREMLHSKAEEVLSLEKRKQQLYTAMEERTEEIKVHKTMLASQIRYVDQERENISTEFRERLSKIEKLKNRYEILTVVMLPPEGEEEKTQAYYVIKAAQEKEELQREGDCLDAKINKAEKEIYALENTLQVLNSCNNNYKQSFKKVTPSSDEYELKIQLEEQKRAVDEKYRYKQRQIRELQEDIQSMENTLDVIEHLANNVKEKLSEKQAYSFQLSKETEEQKPKLERVTKQCAKLTKEIRLLKDTKDETMEEQDIKLREMKQFHKVIDEMLVDIIEENTEIRIILQTYFQQSGLELPTASTKGSRQSSRSPSHTSLSARSSRSTSTSTSQSSIKVLELKFPASSSLVGSPSRPSSASSSSSNVKSKKSSK
Protein: Heavy metal-associated isoprenylated plant protein 27 (AtHIP27) (AtHIPP27) (Q67ZW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein. Binds cadmium. May be involved in cadmium transport and play a role in cadmium detoxification.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9SZN7}.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 39
- Heavy metal-associated isoprenylated plant protein 12
- Ubiquitin carboxyl-terminal hydrolase 16
- Heavy metal-associated isoprenylated plant protein 16
- Heavy metal-associated isoprenylated plant protein 3
- Heavy metal-associated isoprenylated plant protein 6
- Heavy metal-associated isoprenylated plant protein 10
Sequence:
MGFRDICYRKHHKKLKQFQKVEIKVKMDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEGFVQPSKVVHRVMHRTGKKAELWPYVPYEVVPHPYAPGAYDKKAPPGYVRNALADPLVAPLARASSFEVKYTSAFSDDNPNACTIM
Protein: Glycine oxidase (GO) (GOX) (EC 1.4.3.19) (GOXK) (Q5L2C2)
Organism: Geobacillus kaustophilus (strain HTA426)
Function: Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes glycine, sarcosine (N-methylglycine), N-ethylglycine, D-proline, D-alanine, glycine-ethyl ester, and some other D-amino acids. Does not act on L-proline. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (By similarity).
Interaction partners:
- Thiazole synthase
- Aminomethyltransferase
- Hypothetical conserved protein
- Thiamin biosynthesis protein
- Thiamine-phosphate pyrophosphorylase
- Hypothetical conserved protein
- Aminopyrimidine aminohydrolase
- Hypothetical conserved protein
- Hypothetical conserved protein
- Hypothetical conserved protein
Sequence:
MTHRYDVAIVGGGVIGAAIGFELAKRRHRVAIFEKGTMGSGASSAAAGMLGAQSEFSTSSPLVPLALQSRALMPALAEELRERTGIDIGLVEKGLIKLATTEEEADDLYRHYTFWRGIGEPVQWLTKGEALEMEPRLAAEALAGAMYIPGDGQVSAPDLAAALAYAAASAGACLYEYTEVFDIRSDSSGHVLDTTGGTFAAEAVVIASGAWAARLGARVGLSLSVYPVKGECVMVRAPVPLLQTTVFAKNGCYIVPKSGNRLLIGATSTPGTFDRRVSAGGVMNLLHRAAHLVPDIEQAEWVASWSGIRPQTEDGLPYLGEHPERRGLFVAAGHYRNGILLSPLTGLLVADLVERKETAFDLAPFSLTRHIGKVGVE
Protein: Transcription factor MafF (V-maf musculoaponeurotic fibrosarcoma oncogene homolog F) (O54791)
Organism: Mus musculus (Mouse)
Function: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2L1/NRF1, and recruiting them to specific DNA-binding sites. Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Nuclear factor erythroid 2-related factor 2
- Transcription factor NF-E2 45 kDa subunit
- Transcription regulator protein BACH2
- Cyclic AMP-dependent transcription factor ATF-3
- Transcription factor MafG
- Endoplasmic reticulum membrane sensor NFE2L1
- Transcription factor Jun
- Nuclear factor erythroid 2-related factor 3
- Transcription factor MafK
Sequence:
MAVDPLSSKALKVKRELSENTPHLSDEALMGLSVRELNRNLRGLSAEEVTRLKQRRRTLKNRGYAASCRVKRVCQKEELQKQKSELEREVDKLARENAAMRLELDALRGKCEALQGFARSVAAARGPAALVAPASVITIVKSAPGPAPAADPAPCS
Protein: Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8) (B9EJ86)
Organism: Mus musculus (Mouse)
Function: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BZF1}.
Interaction partners:
- Regulator of microtubule dynamics protein 3
- Golgi pH regulator
- Phosphatidylinositol-3-phosphatase SAC1
Sequence:
MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKEDISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQHFKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVSEENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGLKKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFLNRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWDSEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDRKTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSPEPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILLQVIINFIFK
Protein: Myosin VI (A0A0D9SGC1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSEAIKSYQGKSLGTRPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEEDEYLKAGSMKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAQSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLVGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLTIPRKSKLAVHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGYPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNENDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLTCSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSVLKDGKPEMNKQIKNLEISIDTLMAKIKSTMMTQEQIQKEYDALVKSSEELLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEKRRRKEEEERRMKLE
Protein: Protoheme IX farnesyltransferase (EC 2.5.1.141) (Heme B farnesyltransferase) (Heme O synthase) (P0AEA5)
Organism: Escherichia coli (strain K12)
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:8253713}; Multi-pass membrane protein.
Interaction partners:
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Ferrochelatase
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase iron-sulfur subunit
- 2-oxoglutarate dehydrogenase E1 component
Sequence:
MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLGMALRGYKVADDRIWARKLFGFSIIAITALSVMMSVDFMVPDSHTLLAAVW