wanglab/gogpt-training-data huggingface dataset:
Protein: Spliceosome-associated protein 130 A (AtSAP130a) (SAP 130 A) (Pre-mRNA-splicing factor SF3b 130 kDa subunit A) (SF3b130 A) (P0DKL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (By similarity). Required for pollen and ovule development, especially during the transition from microspore to the bicellular stage in pollen development. Involved in the accumulation of QRT1 and QRT3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15393}.
Interaction partners:
- PHD finger-like domain-containing protein 5A
- Small nuclear ribonucleoprotein E
- Nuclear protein-like
- PHD finger-like domain-containing protein 5B
- Uncharacterized protein At3g23325
- Splicing factor 3B subunit 4
- At4g10100 family protein)
- At2g32600/T26B15.16
- Small nuclear ribonucleoprotein Sm D2
- Uncharacterized protein At4g14342
Sequence:
MYLYSLTLQQATGIVCAINGNFSGGKTQEIAVARGKILDLLRPDENGKIQTIHSVEVFGAIRSLAQFRLTGAQKDYIVVGSDSGRIVILEYNKEKNVFDKVHQETFGKSGCRRIVPGQYVAVDPKGRAVMIGACEKQKLVYVLNRDTTARLTISSPLEAHKSHTICYSLCGVDCGFDNPIFAAIELDYSEADQDPTGQAASEAQKHLTFYELDLGLNHVSRKWSNPVDNGANMLVTVPGGADGPSGVLVCAENFVIYMNQGHPDVRAVIPRRTDLPAERGVLVVSAAVHKQKTMFFFLIQTEYGDVFKVTLDHNGDHVSELKVKYFDTIPVASSICVLKLGFLFSASEFGNHGLYQFQAIGEEPDVESSSSNLMETEEGFQPVFFQPRRLKNLVRIDQVESLMPLMDMKVLNIFEEETPQIFSLCGRGPRSSLRILRPGLAITEMAVSQLPGQPSAVWTVKKNVSDEFDAYIVVSFTNATLVLSIGEQVEEVNDSGFLDTTPSLAVSLIGDDSLMQVHPNGIRHIREDGRINEWRTPGKRSIVKVGYNRLQVVIALSGGELIYFEADMTGQLMEVEKHEMSGDVACLDIAPVPEGRKRSRFLAVGSYDNTVRILSLDPDDCLQILSVQSVSSAPESLLFLEVQASIGGDDGADHPANLFLNSGLQNGVLFRTVVDMVTGQLSDSRSRFLGLKPPKLFSISVRGRSAMLCLSSRPWLGYIHRGHFHLTPLSYETLEFAAPFSSDQCAEGVVSVAGDALRIFMIDRLGETFNETVVPLRYTPRKFVLHPKRKLLVIIESDQGAFTAEEREAARKECFEAGGVGENGNGNADQMENGADDEDKEDPLSDEQYGYPKAESEKWVSCIRVLDPKTATTTCLLELQDNEAAYSVCTVNFHDKEYGTLLAVGTVKGMQFWPKKNLVAGFIHIYRFVEDGKSLELLHKTQVEGVPLALCQFQGRLLAGIGPVLRLYDLGKKRLLRKCENKLFPNTIISIQTYRDRIYVGDIQESFHYCKYRRDENQLYIFADDCVPRWLTASHHVDFDTMAGADKFGNVYFVRLPQDLSEEIEEDPTGGKIKWEQGKLNGAPNKVDEIVQFHVGDVVTCLQKASMIPGGSESIMYGTVMGSIGALHAFTSRDDVDFFSHLEMHMRQEYPPLCGRDHMAYRSAYFPVKDVIDGDLCEQFPTLPMDLQRKIADELDRTPAEILKKLEDARNKII
Protein: Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase) (Q16647)
Organism: Homo sapiens (Human)
Function: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase
- Prostaglandin E synthase 3
- Prostaglandin E synthase 2
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Thromboxane-A synthase
- Prostacyclin receptor
- Lanosterol synthase
Sequence:
MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKLLSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITREVVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSRYGFGLMQPEHDVPVRYRIRP
Protein: Cytosolic endo-beta-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) (Q8BX80)
Organism: Mus musculus (Mouse)
Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Alpha-mannosidase 2C1
- Peptide-N
Sequence:
METSSVLTRGAARQRSPAAPEKQARDQTERRPGRRRQGRRINEDQEEEAVFREVVSFTPDPLPARYYDKDTTRPISFYLSTLEELLAWTPLMEDGFNVALEPLVCRRPPLSSPRPRTLLCHDMMGGYLEDRFIQGSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGRLCEAFLAGDEPSFQAVADRLVQIAQFFRFDGWLINIENSLTPAAVRNTPLFLQYLTAQLHQQVPGGLVLWYDSVVQSGQLKWQDELNDQNRVFFDSCDGFFTNYNWREDHLQRMVAQAGERLADVYVGVDVFARSNVVGGRFDTDKSLELIRKHGFSAALFAPGWVYECLEKSDFFQNQDKFWSLLERFLPTHSICSLPFVTSFCLGLGTRRVCYGKEQAVGPWYHPSAQETQPLFGEHKLAGDSRGWVKTHCCLTDAWHGGSSLLLRGLIPPEVDSVAVRLFSLHIPVPPKVFLSMVYKFEGSTDVQVALELTTGDASSCHVGGMLVLNETGSRHSPRPLRVPPTRLARWASSCGQQLSGGWIQRCYEVNLRGCLLQDLLVSFSRPPGSREEESFICRLGEIQVVDASSLLAPLPRVQNVTISQIRWLPLITGSEGLPTRLLLSCTLHWSYLLLRARCFRIHCWKRTGSSSSVAESPETEKPTFLGLAFANQYRVVDLAVEAAGFGQDGRVEFLVEPVPREGFLVPQAEWGKAVLLFSVPQ
Protein: Bystin, putative (Q585M1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S16, putative
- BING4 C-terminal domain-containing protein
- Uncharacterized protein
- HEAT repeat-containing protein 1
- 40S ribosomal protein S14
- U3 small nucleolar RNA-associated protein 18
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- U3 small nucleolar RNA-associated protein 6 N-terminal domain-containing protein
- Ribosomal RNA-processing protein 12-like conserved domain-containing protein
Sequence:
MPGREKKRRIGTRTNPLGEDLHADRFASAKRGAVESKASGASDDVDVDLEGGIVLPGRVASKILKTARQQIEAIAAEEQEDGGGLHGEESSDGDDCNNDPTIVNLQNEEDGEDAGARFYENEDESEEPIVIEYDEAESVVSEIPSEIDMGVDMYDIDDEEARLLQKFQPQSHVQSRNLADMIMEKIKEREDARKVAASSPSGDGCEGMGETGESRVDPRVARVYTAIGTILKNYTSGKVPKAFKVLPNIKNWEQLLMLTKPHEWSPHATYQATRIFAANLNERMAQRFYAAVLLPVVHEHMSAEKKLHPALYMAIRKALFKPVAFYKGFILPLAADDECTLKEALVVASVLQRMHLPPVPTAVTIVKLAQQPFSGPRSVLLRVLIDKKMAMPYQAIDALVAYFHRFIQSHSKEEKLPVLWHQTLLSFSQRYKGDFTAEQVALLLQVCSKHFHYLITPEVRRELHASPVMAKGGNS
Protein: Clarin-2 (B2RVW2)
Organism: Mus musculus (Mouse)
Function: Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle and for mechano-electrical transduction.
Subcellular location: Cell projection, stereocilium membrane {ECO:0000269|PubMed:31448880}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutaredoxin domain-containing cysteine-rich protein 2
Sequence:
MPGWFKKVWYGLASLLSFSSFLLIIVALSLPHWLSGKILCQTGVDLVNATDPELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVTILLLLFLALALALVSMGFAILNIIQVPYRAVNGPGGICLWNVLAGGVVALAIGSFMAAVKFHDLTERIANFQERLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKMEEATVTPEDILY
Protein: Glutamate synthase 1 [NADH], chloroplastic (EC 1.4.1.14) (NADH-dependent glutamate synthase 1) (NADH-GOGAT 1) (Q0JKD0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in glutamate biosynthesis and plays a major role in the primary ammonium ions assimilation in seedling roots. May be involved in the reutilization of glutamine in developing organs. Plays a role in the development of tillers.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9952435}.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- glutamate dehydrogenase
- Glutamine synthetase cytosolic isozyme 1-2
- Glutamate dehydrogenase 1, mitochondrial
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamate dehydrogenase 3, mitochondrial
- Os01g0358900 protein
- Glutamine synthetase, chloroplastic
- Delta-1-pyrroline-5-carboxylate synthase 1
Sequence:
MSAAQGMAYKLRTDAAPTGAGRRARRSHSSVAAPYRAARLVQGGVSIEGGLVGGCQLTEERVAARPPRAAARDAEPVRPLSTLPESSIGLYDPSRERDSCGVGFVAELSGDYKRATVNDALEMLERMAHRGACGCEKNTGDGAGILVALPHNFFREVTKDAGFELPQPGEYAVGMVFLPIDEKRRERSKAEFQKVAESLGHVILGWRRVPTDNSDLGESALQTEPVIEQVFLTKSSSSEADFEQQLYILRRLSILSIRAALNLRRGGKRDFYMCSLSSRTIVYKGQLKPCQLKGYYYADLGHENFTSYMALVHSRFSTNTFPSWDRAQPMRVLGHNGEINTLKGNKNWMKAREGLLECEKLGLTKDQFSKILPIVDATSSDSGAFDGVLELLIRGGRSLPEAVMMMIPEAWQNDVNMEPEKKALYEFLSALMEPWDGPALISFTDGRYLGATLDRNGLRPGRFYVTHSGRVVMGSEVGVVDVPSKDVLRKGRLNPGMMLLVDFENHTVVDDEALKAQYSKAHPYGEWLKRQKIYLKDIVESVPETERVAPGISGSLTQKNEKKEHAGVNGIVTPLKAFGYTVEALEMLLLPMAKDGVEALGSMGNDTPLAVMSNREKLTFEYFKQMFAQVTNPPIDPIREKIVTSMECMIGPEGDLLETTEKQCNRLALEGPLVSIDEMEAIKKMNYRGWRSKVLDITYPKKSGRKGLEETLDRICTEARGAIKKGYTVLVLSDRGFSSDRVAVSSLLAVGAVHQHLVANLERTRVGLLVESAEPREVHHFCTLVGFGADAVCPYLAIEAIWCLQNDGKIPPNGDGKPYSKEELVKKYFYASNYGMMKVLAKMGISTLASYKGAQIFEALGLSSEVIRKCFDGTPSRIEGATFEMLARDALRLHELAFPSRAPPPGSADAKALPNPGDYHWRKNGEVHLNDPLAMAKLQEAARVNSRAAYKEYSRRIQELNKTCNLRGMLKFKDTADMISVDEVEPASEIVKRFVTGAMSYGSISLEAHTALAMAMNKLGGKSNTGEGGEQPSRMEPLANGSMNPKRSAIKQVASGRFGVSSYYLTNADELQIKMAQGAKPGEGGELPGHKVIGDIAVTRHSTAGVGLISPPPHHDIYSIEDLAQLIHDLKNSNPRARISVKLVSEAGVGVVASGVVKGHADHVLISGHDGGTGASRWTGIKNAGLPWELGLAETHQTLVANGLRGRAILQTDGQLKTGKDVAVACLLGAEEFGFSTAPLITLGCIMMRKCHTNTCPVGIATQDPVLREKFAGEPEHVINFFFMLAEELREIMSQLGFRTITEMVGRSDMLEVDPEVVKSNEKLENIDLSLILKPAAEIRPGAAQYCVEKQDHGLDMALDNKLIALSKAALEKEVRVFIETPIQNTNRAVGTMLSHEVTKRYHMKGLPAGTIHVKLTGSAGQSLGAFLCPGITLELEGDSNDYVGKGLSGGKIVVYPPRDSTFIPEDNIVIGNVALYGATIGEAYFNGMAAERFCVRNSGAQAVVEGIGDHGCEYMTGGTVVILGKTGRNFAAGMSGGIAYVYDIDGKFSVRCNHELVDLYHVEEEEDITTLKMMIEQHRLNTGSVVARDILSNFDTLLPKFVKVFPRDYKRVLDNMKAEKAAAKLAKEPKISNGVSVTTKKVQPEQSTNRPTRVSNAKKYRGFISYERESISYRDPNERVKDWKEVAIESVPGPLLNTQSARCMDCGTPFCHQESSGAGCPLGNKIPEFNELVHQNRWREALDRLLETNNFPEFTGRVCPAPCEGSCVLGIIENPVSIKSIECAIIDKGFEEGWMVPRPPLQRTGKKVAIIGSGPAGLAAADQLNKMGHFVTVFERADRIGGLMMYGVPNMKTDKIEIVQRRVNLMAEEGITFVVNANVGSDPLYSIERLRSENDAVILACGATKPRDLGIPGRELSGVHFAMEFLHANTKSLLDSNLEDGRYISAKGKKVVVIGGGDTGTDCIGTSIRHGCTSIVNLELLTKPPSKRAADNPWPQWPRIFRVDYGHQEASSKFGNDPRTYEVLTKRFIGDENGNVKALEVVRVKWEKVDGRFQFKEIEGSNETIEADLVLLAMGFLGPEATIAEKLGLEKDNRSNFKAQFGNFATSVDGIFAAGDCRRGQSLVVWAITEGRQAAAAVDKYLSRNEQDAAEDITPSGAGFVQPVAA
Protein: Purine permease 2 (AtPUP2) (Q94GB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates adenine transport. May be involved in the uptake of cytokinin analogs.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Equilibrative nucleotide transporter 8
- Equilibrative nucleotide transporter 6
- ABC transporter G family member 14
- Equilibrative nucleotide transporter 3
- Equilibrative nucleotide transporter 1
- Adenine/guanine permease AZG2
- Adenylate isopentenyltransferase 3, chloroplastic
Sequence:
MKMKTVLVIINCIFLAIGNCGGPLMMRLYFQNGGERIWFPSFLQTVGCPLIFFPLLLSFLRRRRCLEEQETTPFFLMKPPLFIAAIVVGLLVGFDNYLYSYGLAYIPVSTASLIISAQLGFTALFAFFMVKQKFTPFTINAIVLLTGGAVVLALNSDSDKLANETHKEYVVGFIMTLGAALLYGFILPLVELSYKKSGQRITYTLALEFQMVLCFAATCVCLVGMLAAGDFKVKHALFIFKNRVIAGEARDFKLGESLYYVVIVFTAIIWQAFFVGAIGLIFCASSLVSGIMVSALLPVTVILAVICFQEKFQAGKGVALALSLWGSVSYFYGQVKSEEKTKAQDTQLSQLPVTDYVA
Protein: Small ribosomal subunit protein bS1c (30S ribosomal protein S1, chloroplastic) (Plastid ribosomal protein S1) (PRPS1) (Q93VC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for optimal plastid performance in terms of photosynthesis and growth. Required for the translation of plastid mRNAs. Involved in cellular heat stress response and required for heat tolerance. Required for transcriptional activation of HSFA2 and its target genes in response to heat stress. Plays a critical role in biosynthesis of thylakoid membrane proteins encoded by chloroplast genes.
Subcellular location: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:22570631}.
Interaction partners:
- Uncharacterized protein At3g06530
- Nucleolar protein
- Nucleolar-like protein
- Small ribosomal subunit protein uS13c
- Large ribosomal subunit protein bL28c
- Small ribosomal subunit protein uS2c
- F18K10.11 protein
- Small ribosomal subunit protein uS7cz/uS7cy
- Small ribosomal subunit protein uS13m
- Small ribosomal subunit protein uS12cz/uS12cy
Sequence:
MASLAQQFSGLRCSPLSSSSRLSRRASKNFPQNKSASVSPTIVAAVAMSSGQTKERLELKKMFEDAYERCRTSPMEGVAFTVDDFAAAIEQYDFNSEIGTRVKGTVFKTDANGALVDISAKSSAYLSVEQACIHRIKHVEEAGIVPGMVEEFVIIGENESDDSLLLSLRNIQYELAWERCRQLQAEDVIVKAKVIGANKGGLVALVEGLRGFVPFSQISSKAAAEELLEKEIPLKFVEVDEEQTKLVLSNRKAVADSQAQLGIGSVVLGVVQSLKPYGAFIDIGGINGLLHVSQISHDRVSDIATVLQPGDTLKVMILSHDRDRGRVSLSTKKLEPTPGDMIRNPKLVFEKAEEMAQTFRQRIAQAEAMARADMLRFQPESGLTLSSDGILGPLGSELPDDGVDLTVDDIPSAVDI
Protein: Gibberellin 2-beta-dioxygenase 5 (EC 1.14.11.13) (Gibberellin 2-beta-hydroxylase 5) (Gibberellin 2-oxidase 5) (GA 2-oxidase 5) (OsGA2ox5) (Q8LGZ9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins (GAs), leading to the homeostatic regulation of their endogenous level. Catabolism of GAs plays a central role in plant development. In vitro, converts GA12 and GA53 to the corresponding 2-beta-hydroxylated products GA110 and GA97, respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24475234}. Nucleus {ECO:0000269|PubMed:24475234}.
Interaction partners:
- Gibberellin 20 oxidase 3
- Gibberellin 20 oxidase 1
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 1
- Os05g0257800 protein
- Os04g0517600 protein
Sequence:
MEEHDYDSNSNPPLMSTYKHLFVEQHRLDMDMGAIDVDECELPVIDLAGLMEAEQVCRADMVRAASEWGFFQVTNHGVPQALLRELHDAQVAVFRRPFQEKVTERLLGFSPESYRWGTPTAKCLEQLSWSEAYHIPMTTPRPSTSIRARAVIEEVSRAMYELAQKLAEILMRGLPGAGEGETMVTTREETCFLRLNRYPPCAMAMGGFGLCPHTDSDLLTIVHQQQDTVGGLQLLKGGRWVAVKPSPSTLIVNVGDLLQAWSNDVYKSVEHRVMANATLERFSMAFFLCPSYHTLIIPSSSHVHDDDAHYRSFTFGEYRKQIMEDVRSTGRKIGLHRFRTR
Protein: Nuclear hormone receptor HR78 (dHR78) (Nuclear receptor XR78E/F) (Nuclear receptor subfamily 2 group D member 1) (Q24142)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to direct repeats of the sequence 5'-AGGTCA-3'. Inhibits the ecdysone response. Plays an essential role in regulating molting of the tracheal cuticle during larval development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:7479823}.
Interaction partners:
- LD46863p
Sequence:
MDGVKVETFIKSEENRAMPLIGGGSASGGTPLPGGGVGMGAGASATLSVELCLVCGDRASGRHYGAISCEGCKGFFKRSIRKQLGYQCRGAMNCEVTKHHRNRCQFCRLQKCLASGMRSDSVQHERKPIVDRKEGIIAAAGSSSTSGGGNGSSTYLSGKSGYQQGRGKGHSVKAESAATPPVHSAPATAFNLNENIFPMGLNFAELTQTLMFATQQQQQQQQQHQQSGSYSPDIPKADPEDDEDDSMDNSSTLCLQLLANSASNNNSQHLNFNAGEVPTALPTTSTMGLIQSSLDMRVIHKGLQILQPIQNQLERNGNLSVKPECDSEAEDSGTEDAVDAELEHMELDFECGGNRSGGSDFAINEAVFEQDLLTDVQCAFHVQPPTLVHSYLNIHYVCETGSRIIFLTIHTLRKVPVFEQLEAHTQVKLLRGVWPALMAIALAQCQGQLSVPTIIGQFIQSTRQLADIDKIEPLKISKMANLTRTLHDFVQELQSLDVTDMEFGLLRLILLFNPTLLQQRKERSLRGYVRRVQLYALSSLRRQGGIGGGEERFNVLVARLLPLSSLDAEAMEELFFANLVGQMQMDALIPFILMTSNTSGL
Protein: Transcription factor Sox-3-A (xSox3) (xSox-B1) (P55863)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor with sequence-specific DNA binding activity. Binds to the consensus sequence 5'-[AT][AT]CAA[AT]G-3', showing a preference for 5'-AACAAT-3' and 5'-AACAAAG-3'. Inhibits beta-catenin-mediated dorsal axis specification by binding to sites within the promoter of the beta-catenin-regulated gene nodal5. Acts maternally as a transcriptional repressor of nodal5 and nodal6 to restrict their expression to the vegetal hemisphere of early embryos and thus establish germ layer formation. Acts at multiple points to inhibit nodal signaling, repressing the expression of the other mesoderm-inducing nodal genes nodal, nodal2 and nodal4, and also acting downstream to induce expression of genes including trim33/ectodermin, ema and coco, whose products repress nodal signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:14522872}. Cytoplasm {ECO:0000269|PubMed:14522872}. Note=Primarily cytoplasmic in early embryos. Nuclear localization becomes more pronounced as development proceeds.
Interaction partners:
Sequence:
MYSMLDTDIKSPVQQSNAPIGGPATPGGKGNASTLDQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGADWKLLSDSDKRPFIDEAKRLRAVHMKDYPDYKYRPRRKTKTLLKKDKYSLPGNLLAPGVSPVASSVGVGQRIDTYAHMNGWTNGAYSLMQDQLGYSQHPAMNSPQMQQIQHRYDMSGLQYNPMMTSAQNAYMNAAASTYSMSPAYNQQSSTVMSLASMGSVVKSEPSSPPPAITSHTQRACLGDLRDMISMYLPPGGDASDPSLQNSRLHSVHQHYQSAAGPGVNGTVPLTHI
Protein: Transaldolase B (EC 2.2.1.2) (P0A870)
Organism: Escherichia coli (strain K12)
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Transketolase 1
- Transketolase 2
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase isozyme 1
- Fructose-bisphosphate aldolase class 2
- Fructose-1,6-bisphosphatase class 1
- Glyceraldehyde-3-phosphate dehydrogenase A
- Enolase
- Fructose-1,6-bisphosphatase 1 class 2
Sequence:
MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL
Protein: Paired mesoderm homeobox protein 1 (Homeobox protein PHOX1) (Paired-related homeobox protein 1) (PRX-1) (P54821)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P63013}.
Interaction partners:
- eEF1A lysine and N-terminal methyltransferase
- Nuclear pore complex protein Nup98-Nup96
- Twist-related protein 1
- Paired box protein Pax-9
Sequence:
MTSSYGHVLERQPALGGRLDSPGNLDTLQAKKNFSVSHLLDLEEAGDMVAAQADENVGEAGRSLLESPGLTSGSDTPQQDNDQLNSEEKKKRKQRRNRTTFNSSQLQALERVFERTHYPDAFVREDLARRVNLTEARVQVWFQNRRAKFRRNERAMLANKNASLLKSYSGDVTAVEQPIVPRPAPRPTDYLSWGTASPYSAMATYSATCANNSPAQGINMANSIANLRLKAKEYSLQRNQVPTVN
Protein: CDP-diacylglycerol--serine O-phosphatidyltransferase (EC 2.7.8.8) (Phosphatidylserine synthase) (P23830)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase
- Serine hydroxymethyltransferase
- Glycerol-3-phosphate acyltransferase
- CDP-diacylglycerol pyrophosphatase
- L-serine dehydratase TdcG
- Phosphoserine phosphatase
- L-serine dehydratase 2
- L-serine dehydratase 1
Sequence:
MLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPADFRETLLEKIASAKQRICIVALYLEQDDGGKGILNALYEAKRQRPELDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGVDVPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYLHQHDKYRYDRYHLIRNRKMSDIMFEWVTQNIMNGRGVNRLDDVNRPKSPEIKNDIRLFRQELRDAAYHFQGDADNDQLSVTPLVGLGKSSLLNKTIFHLMPCAEQKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFYIPEDEPFKIIGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLITGNNLNPRAWRLDLENAILIHDPQLELAPQREKELELIREHTTIVKHYRDLQSIADYPVKVRKLIRRLRRIRIDRLISRIL
Protein: ATP synthase F(1) complex subunit alpha, mitochondrial (ATP synthase F1 subunit alpha) (P25705)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:30146159}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000269|PubMed:10077593}; Peripheral membrane protein {ECO:0000269|PubMed:10077593}; Extracellular side {ECO:0000269|PubMed:10077593}. Note=Colocalizes with HRG on the cell surface of T-cells (PubMed:19285951). {ECO:0000269|PubMed:19285951}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
Sequence:
MLSVRVAAAVVRALPRRAGLVSRNALGSSFIAARNFHASNTHLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA
Protein: Inhibitor of carbonic anhydrase (Q9DBD0)
Organism: Mus musculus (Mouse)
Function: Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron ions.
Subcellular location: Secreted {ECO:0000269|PubMed:17511619}.
Interaction partners:
- Transferrin receptor protein 1
- Serotransferrin
- Signal recognition particle receptor subunit beta
Sequence:
MRLLICALLCLGTLGLCLALPEKTIRWCVVSDHEATKCSSFRDNMKKVLPAGGPAVTCVRKMSHPECIRDISANKVDAVTVDGALVAEADLPHHSLKPIMAEYYGSKDDPKTHYYVVAMAKKGTGFQLNQLRGKKSCHTGLGWSAGWYVPLSTLLPSGSRETAAATFFSSSCVPCADGKMFPSLCQLCAGKGTDKCACSSREPYFGSWGALKCLQDGTADVSFVKHLTVFEAMPTKADRDQYELLCMDNTRRPVEEYEQCYLARVPSHVVVARSVDGKEDSIQELLRVAQEHFGKDKSSPFQLFGSPHGEDLLFTDAAHGLLRVPRKIDISLYLGYEFLSAFRNLKRGLEDSQRVKWCAVGQQERTKCDQWSAVSGGALACATEETPEDCIAATMKGEADAMSLDGGFAYVAGHCGLVPVLAENYLSTHSSGRLGSKCVNAPLEGYYVVAVVKKSDVGITWKSLQGKKSCHTAVGTSEGWNVPMGLIYNQTGSCKFDAFFSRSCAPGSDPDSPLCALCVGGNNPAHMCAANNAEGYHGSSGALRCLVEKGDVAFMKHPTVLQNTDGKNPEPWAKGLKHEDFELLCLDGTRKPVTEAQSCHLARVPNRAVFSRKDKADFVRRILFNQQELFGRNGFEYMMFQMFESSAKDLLFSDDTECLSNLQNKTTYKTYLGPQYLTLMDNFRQCLSSELLDACTFHKY
Protein: Neuronal membrane glycoprotein M6-a (Q6DI17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEENMEEGQTQKGCSECCLKCLSGIPYASLIATILLYAGVALFCGCGHEALSGTVTILQTYFDVVRSPVDALDVFTMIDIFKYVIYGVAAAFFVYGILLMVEGFFTTGAIRDLYGDFKITTCGRCVSAWFIMLTYIFMLAWLGVTAFTSLPVFMYFNIWNTCQNMTLLEGSLSSANSANLCFDLRQYGIVSIGEEKRLCADNENFKKMCESNELDLTFHLFVCALAGAGAAVIAMVHYLMVLSANWAYVKDACRMQKYEDIKSKEEQELHDIHSTRSKERLNAYT