wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipase A1-IIgamma (EC 3.1.1.-) (DAD1-like seedling establishment-related lipase) (AtDSEL) (Phospholipase DSEL) (O49523)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved in the negative regulation of seedling establishment by inhibiting the breakdown, beta-oxidation and mobilization of seed storage oils.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21477884}.
Interaction partners:
- Lipase class 3 family protein
- Peroxisomal adenine nucleotide carrier 1
- Enoyl-CoA delta isomerase 1, peroxisomal
- Acyl carrier protein 1, mitochondrial
- Triacylglycerol lipase SDP1
Sequence:
MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFPIDTRKSPYMKSPGNLATFHCLEGYLHGVAGTQGTNKADLFRLDVERAIGLVNKSVDGLKDECMVPGKWRVLKNKGMAQQDDGSWELVDHEIDDNEDLDF
Protein: ETS domain-containing transcription factor ERF (P70459)
Organism: Mus musculus (Mouse)
Function: Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation (By similarity). Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment. May be important for regulating trophoblast stem cell differentiation.
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor, arginine/serine-rich 19
Sequence:
MKTPADTGFAFPDWAYKPESSPGSRQIQLWHFILELLRKEEYQGVIAWQGDYGEFVIKDPDEVARLWGVRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVLVNYPFIDMGLAGGAVPQSAPPVPSGGSHFRFPPSTPSEVLSPTEDPRSPPACSSSSSSLFSAVVARRLGRGSVSDCSDGTSELEEPLGEDPRARPPGPPELGAFRGPPLARLPHDPGVFRVYPRPRGGPEPLSPFPVSPLAGPGSLLPPQLSPALPMTPTHLAYTPSPTLSPMYPSGGGGPSGSGGGSHFSFSPEDMKRYLQAHTQSVYNYHLSPRAFLHYPGLVVPQPQRPDKCPLPPMAPETPPVPSSASSSSSSSSSPFKFKLQPPPLGRRQRAAGEKAPGGTDKSSGGSGSGGLAEGAGAVAPPPPPPQIKVEPISEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGVAQCMPLKLRFKRRWSEDCRLEGGGCLSGGPEDEGEDKKVRGDVGPGESGGPLTPRRVSSDLQHATAQLSLEHRDS
Protein: Apoptotic signal-regulating kinase 1, isoform C (EC 2.7.11.25) (Q9VDS9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Thioredoxin-2
- mitogen-activated protein kinase kinase
- LD20987p
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- X-box-binding protein 1
- GH01161p
- Daxx-like protein
- tRNA
- Thioredoxin-1
- Thioredoxin-T
Sequence:
MDVVCVMDTAVGDHLEDRQCALEEIKQAVQSAGANFQRVQFERLDFGETNVLETFYNADVAIIDLSILTQQRPLSYHYGVRESFGMKENILTYNDIDSKQTLSLKLSCANYLFLSYKRNAETNSCHLTSQPNSGNNSKEPNAEGRVPTLQWRLKRKLQDVEIQSKAHMREKFLSDMRTARDTYATNGAKLQSILHEMRKRLDDPHVLSGEVVHSFMCSLRDVQDYDAMVRLVNDLKNIPNTRKYVETGNMSFLYAFALNRRNRKGDREKALESSLKALEKKENHFPDMLCLCGRIYKDIFVESDYTDATSLAHAIKWYRQSFEVQPNEYAGINLATLLVIEGKEFTNTEELQHIGMTLNNLIGKKGSLSSLSEYWDVATFFEISVLANDYAKAIQAAECMFKLKPPNWYLKSTIGNISLIHRFRKKPEERQPPIEEQVFQFWMDFFLEATNTEEVKNSIRFPILILEPQKIYMPSYVTINMDADEKSIQIVNICLAHAKNACKKIHDFLFVASKIKSVSLYKRDDRCAYLYVHHNSDDFQIYFPSTERRQKFYDMILEMTADQVVFVNLSNDDANIEYEYDYDEQNRKMVLGKGTYGTVYAARDKQTQVRIAIKEVPEKNSQDVQPLHEEIKLHSQLRHRNIVRYLGSCSENGFFKIFMEQVPGGSLSDLLETKWGPLKDNESTMAFYSKQILEGLKYLHEQDIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLARINPMTETFTGTLQYMAPEVIDQGVRGYGPAADIWSFGCTNVEMATGKPPFIELGSAHAAMFKVGFYKKHPNIPEELSANAKNFILRCFAISVMDRPSASQLLEDPFLQDKPRKVRPALPINTEFGRSISVPADRFVHKTTPPLSYNTTCNTPTTPELDITHSSSVDIDELPSNQFMLERRNSHGFLLSPEIEPSTPSLRTSISETSETDGFYRLKKDSQRRTTLSKVLALDESKICDIWLKKVDADQNSIAIRKSDLEVLIRGLRDYIMNENEKHLEATINELKQKLNNDAVALDHLHLALYSFQDAVVCVLRYHCIKPHWMFALDNLVKRAVQAAVTIFSPELGANLADKDLSGNDDESLRTSLMQKGSTESQEKQSLEKVLPTSNTREGVGLTPAESGGDALSSSMECARILRDIRDNQQKLQRQLLEQQRQSMRALHNISQELAHIYMGGRKRLRRTINGFNKKCHRMSTSVGGTSGVRPNIAGNPRRQLNKHHFGLHEVDEQLEQWLTQQEIDEFSKTLILNEGFTFDDFIYNMEKLDLMRLGLRVGIEVRLWKLIIQERVCTSSDCVDSPPSTYHKPIGGNSSFALIDNNNTLPSPTTTTPGTPGIKTKIKKSESEYDSCSE
Protein: High mobility group B protein 4 (High mobility group protein G) (AtHMGgamma) (HMG gamma) (Nucleosome/chromatin assembly factor group D 04) (Nucleosome/chromatin assembly factor group D 4) (Q42344)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially double-stranded DNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20123078}. Cytoplasm, cytosol {ECO:0000269|PubMed:20123078}.
Interaction partners:
- Actin-related protein 4
- ARM repeat superfamily protein
- AT-hook motif nuclear-localized protein 13
- Nucleic acid-binding, OB-fold-like protein
- Putative nucleobase-ascorbate transporter 10
- Eukaryotic translation initiation factor 4C
- Single-stranded DNA-binding protein
- At5g12410
- RNA cytidine acetyltransferase 2
- Protein HEAT-INDUCED TAS1 TARGET 3
Sequence:
MKGGESKAEATSTDQRLKTRGRKAGKKTKKDPNQPKRPPSAFFVFLEDFRKEFNLANPNNKSVATVGKAAGARWKAMTDEDKAPYVAKAESRKTEYIKNVQQYNLKLASGTNREEDDSDKSKSEVDEAVSEEEAEDDD
Protein: Basic phospholipase A2 homolog BaTX (svPLA2 homolog) (P86453)
Organism: Bothrops alternatus (Urutu) (Rhinocerophis alternatus)
Function: Snake venom phospholipase A2 homolog that lacks enzymatic activity. Is myotoxic and displays edema-inducing activities. In vitro, produced time-dependent, irreversible neuromuscular blockade in isolated mouse phrenic nerve-diaphragm and chick biventer cervicis preparations. A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:17270350, ECO:0000269|PubMed:19463969}.
Interaction partners:
Sequence:
SLFELGKMILQETGKNPAKSYGAYYCYCGWGGQGQPKDATDRCCYVHKCCYKKLTGCNPKKDRYSYSWKDKTIVCGENNSCLKELCECDKAVAICLRENLNTYNKKYRYYLKPLCKKADAC
Protein: Emb|CAB82975.1 (Q9FGU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g01170)
- AT3g10020/T22K18_16
- At1g73120
- Protein OXIDATIVE STRESS 3
- Nematode resistance protein-like HSPRO2
Sequence:
MEGKGRVGSSSSTSSSFTAELFGSKDPSPPSSSSGIFSTMFPHPSKGSARDGSNSKHGSQAQRRESLNAQEDRVEPCHLSSSLYYGGQDVYARSTTNQTYPPVKNDRRRSGEDDANGQNPQDVSRGNWWQGSLYY
Protein: Phospholipid-transporting ATPase IH (EC 7.6.2.1) (ATPase IS) (ATPase class VI type 11A) (P4-ATPase flippase complex alpha subunit ATP11A) (P98196)
Organism: Homo sapiens (Human)
Function: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane. Does not show flippase activity toward phosphatidylcholine (PC). Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation. May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:34403372, ECO:0000269|PubMed:36300302}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:21914794}. Recycling endosome {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. {ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375}.
Interaction partners:
- Cell cycle control protein 50A
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase VD
- Phospholipid-transporting ATPase IC
- Phospholipid-transporting ATPase VA
- Cell cycle control protein 50B
- Phospholipid-transporting ATPase IF
Sequence:
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
Protein: Shaven, isoform G (Q59DN7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLIMDIQTSTHHIHGLGTHELQHRILHPHILHSTQEETLNTSTGQLEHDSQHLQQHHLTHHQQQDVSPTLHNLQNTRTGDSLSTTINTNQNQHGHQHLSGSNMYTSSQMEDKSKANKYDEYSSRTLSNISDANTTPSANNFITQSQGIEWITAMNDIQNGAEDSHSSQGSISGDGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHNGVRPCDISRQLRVSHGCVSKILSRYYETGSFKAGVIGGSKPKVATPPVVDAIANYKRENPTMFAWEIRDRLLAEAICSQDNVPSVSSINRIVRNKAAEKAKHVHHHQQHHVSQSLGGGHIATESVDSSTGTIGEPQPPTSNSSANSVNTNVSASASVHASIPTSGTDSVQVSVGHINANSNETTHINSTAEQRTTGYSINGILGIQHGHHSHNNNNNSSVNNNNNTESSCKRKRIEAHDENHDTNIHSDNDDGKRQRMSTYSGDQLYTNIWSGKWCIKDDHKLLAELGNLTASTGNCPATYYEASNGFSTTPISGSGATASGNDTSMLYDSITTISQTQSSIYTPAIGPSIGTGSLTPLVPISMHEMKLSANSIQEQTVPPFYTGCSSVVPGSDYAYNPAYTQYGGAYGSYGYGTGSGLISN
Protein: PYK10-binding protein 2 (Jacalin-related lectin 31) (Jasmonate inducible protein isolog) (O04313)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polymerizer-type lectin that may facilitate the correct polymerization of BGLU23/PYK10 upon tissue damage. Activates BGLU21, BGLU22 and BGLU23.
Interaction partners:
- Beta-glucosidase 22
- Beta-glucosidase 21
- Beta-glucosidase 23
- TSA1-like protein
- Transcription factor NAI1
- MD-2-related lipid-recognition protein 3
- Membrane protein of ER body 1
- Membrane protein of ER body 2
- Inactive GDSL esterase/lipase-like protein 23
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MAQKVEAKGGKGGNQWDDGSDHDAVTKIQVAVGGMGIQYIQFDYVKNGQTEQTPLRGIKGSTIPTDPFVINHPEEHLVSIEIWYKPDGLIQGLRFISNKKTSRFIGYDRGTRSFLQVQDKKIIGFHGSAGDNLNSLGAYFAPLTIPLTPAKPLPALGSDDGTAWDDGAYVGVKKVYVGQAQDGISAVKFVYDKSPEEVTGEEHGKSTLLGFEEFVLDYPSEYIIAVEGTYDKIFGSDGSVITMLRFKTNKQTSPPFGLEAGTAFELKEEGHKIVGFHGRADALLHKIGVHVRPVSN
Protein: Chondroitin sulfate synthase 3 (EC 2.4.1.175) (EC 2.4.1.226) (Carbohydrate synthase 2) (Chondroitin glucuronyltransferase 3) (Chondroitin synthase 2) (ChSy-2) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3) (N-acetylgalactosaminyltransferase 3) (Q70JA7)
Organism: Homo sapiens (Human)
Function: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Specific activity is much reduced compared to CHSY1.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:12907687}; Single-pass type II membrane protein {ECO:0000305|PubMed:12907687}.
Interaction partners:
- Chondroitin sulfate synthase 1
- Chondroitin sulfate synthase 2
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Chondroitin sulfate N-acetylgalactosaminyltransferase 1
- Chondroitin sulfate glucuronyltransferase
- Polypeptide N-acetylgalactosaminyltransferase 3
Sequence:
MAVRSRRPWMSVALGLVLGFTAASWLIAPRVAELSERKRRGSSLCSYYGRSAAGPRAGAQQPLPQPQSRPRQEQSPPPARQDLQGPPLPEAAPGITSFRSSPWQQPPPLQQRRRGREPEGATGLPGAPAAEGEPEEEDGGAAGQRRDGRPGSSHNGSGDGGAAAPSARPRDFLYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIALPGVDDSYPPQKKSFMMIKYMHDHYLDKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQTGLGNIEELGKLGLEPGENFCMGGPGMIFSREVLRRMVPHIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHNYMLSRKISELRYRTIQLHRESALMSKLSNTEVSKEDQQLGVIPSFNHFQPRERNEVIEWEFLTGKLLYSAAENQPPRQSLSSILRTALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVNPMHGVEYILDLLLLYKRHKGRKLTVPVRRHAYLQQLFSKPFFRETEELDVNSLVESINSETQSFSFISNSLKILSSFQGAKEMGGHNEKKVHILVPLIGRYDIFLRFMENFENMCLIPKQNVKLVIILFSRDSGQDSSKHIELIKGYQNKYPKAEMTLIPMKGEFSRGLGLEMASAQFDNDTLLLFCDVDLIFREDFLQRCRDNTIQGQQVYYPIIFSQYDPKVTNGGNPPTDDYFIFSKKTGFWRDYGYGITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMQLAELWLEKHLGVRYNRTLS
Protein: Protein inturned (Inturned planar cell polarity effector homolog) (PDZ domain-containing protein 6) (Q9ULD6)
Organism: Homo sapiens (Human)
Function: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26644512}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q059U7}. Note=Enriched at the apical surface in ciliated cells. Localizes at the transition zone, a region between the basal body and the ciliary axoneme. Recruited to the centriole in a TTBK2-dependent manner. {ECO:0000250|UniProtKB:Q059U7, ECO:0000250|UniProtKB:Q2I0E5}.
Interaction partners:
- Protein fuzzy homolog
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Ciliogenesis and planar polarity effector 2
- Mitotic spindle assembly checkpoint protein MAD2A
- Cell division cycle protein 16 homolog
- Cell division cycle protein 27 homolog
- Nephrocystin-4
Sequence:
MASVASCDSRPSSDELPGDPSSQEEDEDYDFEDRVSDSGSYSSASSDYDDLEPEWLDSVQKNGELFYLELSEDEEESLLPETPTVNHVRFSENEIIIEDDYKERKKYEPKLKQFTKILRRKRLLPKRCNKKNSNDNGPVSILKHQSNQKTGVIVQQRYKDVNVYVNPKKLTVIKAKEQLKLLEVLVGIIHQTKWSWRRTGKQGDGERLVVHGLLPGGSAMKSGQVLIGDVLVAVNDVDVTTENIERVLSCIPGPMQVKLTFENAYDVKRETSHPRQKKTQSNTSDLVKLLWGEEVEGIQQSGLNTPHIIMYLTLQLDSETSKEEQEILYHYPMSEASQKLKSVRGIFLTLCDMLENVTGTQVTSSSLLLNGKQIHVAYWKESDKLLLIGLPAEEVPLPRLRNMIENVIQTLKFMYGSLDSAFCQIENVPRLDHFFNLFFQRALQPAKLHSSASPSAQQYDASSAVLLDNLPGVRWLTLPLEIKMELDMALSDLEAADFAELSEDYYDMRRLYTILGSSLFYKGYLICSHLPKDDLIDIAVYCRHYCLLPLAAKQRIGQLIIWREVFPQHHLRPLADSSTEVFPEPEGRYFLLVVGLKHYMLCVLLEAGGCASKAIGSPGPDCVYVDQVKTTLHQLDGVDSRIDERLASSPVPCLSCADWFLTGSREKTDSLTTSPILSRLQGTSKVATSPTCRRTLFGDYSLKTRKPSPSCSSGGSDNGCEGGEDDGFSPHTTPDAVRKQRESQGSDGLEESGTLLKVTKKKSTLPNPFHLGNLKKDLPEKELEIYNTVKLTSGPENTLFHYVALETVQGIFITPTLEEVAQLSGSIHPQLIKNFHQCCLSIRAVFQQTLVEEKKKGLNSGDHSDSAKSVSSLNPVKEHGVLFECSPGNWTDQKKAPPVMAYWVVGRLFLHPKPQELYVCFHDSVTEIAIEIAFKLFFGLTL
Protein: Lysine-specific demethylase 3A (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A) (Testis-specific gene A protein) (Zinc finger protein TSGA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3A) (Q63679)
Organism: Rattus norvegicus (Rat)
Function: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TNP1 which are required for packaging and condensation of sperm chromatin. Directly regulates expression of PPARA and UCP1 and is involved in obesity resistance (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Nuclear in round spermatids. When spermatids start to elongate, localizes to the cytoplasm where it forms distinct foci which disappear in mature spermatozoa (By similarity). {ECO:0000250}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Lysine-specific demethylase
- cAMP-dependent protein kinase catalytic subunit alpha
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- [histone H3]-trimethyl-L-lysine
- Lysine-specific demethylase 4B demethylase 4B)
- Hypoxia-inducible factor 1-alpha
- Histone H3
- Histone H3.1
Sequence:
MYKSLLDKAGLGSITSVRFLGDQQSVFVSKDLLKPIQDVNSLRLSLTDNQTVSKEFQALIVKHLDESHLLQGDKNLVGSEVRIYSLDPSTQWFSATVVHGNPSSKTLQVNCEEIPALKIVDPALIHVEVVHDNFVTCGNSTRIGAVKRKSSENNGSSVSKQAKSCSEVSPSMCPVQSVPTTVCKEILLGCTAATPSSNRQQNTPQAANSPPNIGAKLPQGCHKQSLPEEISSCLNTKSEVLRTKPDVCKAGLLSSKSSQVGAGDLKILSEPKGSCIQPKTNTDQESRLESTPQPVTGLTKECLVTKTSSKAELDNATAPELQKRLEHTASTPDGLSDKPEVEAGVTRLNSCSEKKVGPSDLGSQSQNLKETSVKVDHDSCCTRSSNKTQTPPARKSVLTDPDKLKKLQQSGEAFVQDDSCVNIVAQLPKCRECRLDSLRKDKDQQKDSPVFCRFFHFRRLQFNKHGVLRVEGFLTPNKYDSEAIGLWLPLTKNVVGTDLDTAKYILANIGDHFCQMVISEKEAMSTIEPHRQVAWKRAVKGVREMCDVCDTTIFNLHWVCPRCGFGVCVDCYRLKRKNCQQGAAYKTFSWIRCVKSQIHEPENLMPTQIIPGKALYDVGDIVHSVRAKWGIKANCPCSNRQFKLFSKPALKEDLKQASLSGEKPSLGTMVQQSSPVLEPAAVCGEAPSKPASNVKPICPANTSPLNWLADLTSGNVNKENKEKQLTMPILKNEIKCLPPLPPLNKSSTVLHTFNSTILTPVSNNNSGFLRNLLNSSTGKTENGLKNTPKILDDIFASLVQNKTSSDLSKRPQGLTIKPSILGFDTPHYWLCDNRLLCLQDPNNKSNWNVFRECWKQGQPVMVSGVHHKLNTELWKPESFRKEFGEQEVDLVNCRTNEIITGATVGDFWDGFEDVPNRLKNEKEKEPMVLKLKDWPPGEDFRDMMPSRFDDLMANIPLPEYTRRDGKLNLASRLPNYFVRPDLGPKMYNAYGLITPEDRKYGTTNLHLDVSDAANVMVYVGIPKGQCEQEEEVLRTIQDGDSDELTIKRFIEGKEKPGALWHIYAAKDTEKIREFLKKVSEEQGQENPADHDPIHDQSWYLDRSLRKRLYQEYGVQGWAIVQFLGDVVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFWLTQEFRHLSQTHTNHEDKLQVKNVIYHAVKDAVAMLKAVNPVWANVNSSAHWR
Protein: General alpha-glucoside permease (Maltose permease MAL11) (Maltose transport protein MAL11) (P53048)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity uptake of alpha-glucosides such as maltose, turanose, isomaltose, alpha-methylglucoside, maltotriose, palatinose, trehalose, melezitose and glucose. Acts with the concomitant transport of protons into the cell (symport system).
Subcellular location: Cell membrane {ECO:0000305|PubMed:8594329}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Maltose fermentation regulatory protein MAL13
- Alpha-glucosidase MAL12
- Alpha-glucosidase MAL32
- Oligo-1,6-glucosidase IMA1
- Oligo-1,6-glucosidase IMA2
- Oligo-1,6-glucosidase IMA5
- Putative ATP-dependent RNA helicase ECM32
- Maltose fermentation regulatory protein MAL33
- Oligo-1,6-glucosidase IMA3
- Periplasmic acid trehalase ATH1
Sequence:
MKNIISLVSKKKAASKNEDKNISESSRDIVNQQEVFNTEDFEEGKKDSAFELDHLEFTTNSAQLGDSDEDNENVINEMNATDDANEANSEEKSMTLKQALLKYPKAALWSILVSTTLVMEGYDTALLSALYALPVFQRKFGTLNGEGSYEITSQWQIGLNMCVLCGEMIGLQITTYMVEFMGNRYTMITALGLLTAYIFILYYCKSLAMIAVGQILSAIPWGCFQSLAVTYASEVCPLALRYYMTSYSNICWLFGQIFASGIMKNSQENLGNSDLGYKLPFALQWIWPAPLMIGIFFAPESPWWLVRKDRVAEARKSLSRILSGKGAEKDIQVDLTLKQIELTIEKERLLASKSGSFFNCFKGVNGRRTRLACLTWVAQNSSGAVLLGYSTYFFERAGMATDKAFTFSLIQYCLGLAGTLCSWVISGRVGRWTILTYGLAFQMVCLFIIGGMGFGSGSSASNGAGGLLLALSFFYNAGIGAVVYCIVAEIPSAELRTKTIVLARICYNLMAVINAILTPYMLNVSDWNWGAKTGLYWGGFTAVTLAWVIIDLPETTGRTFSEINELFNQGVPARKFASTVVDPFGKGKTQHDSLADESISQSSSIKQRELNAADKC
Protein: Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha-1] (P01252)
Organism: Bos taurus (Bovine)
Function: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
Subcellular location: Nucleus.
Interaction partners:
- Kelch-like ECH-associated protein 1
- Parathymosin
- Thymosin beta
- Thymosin beta-4
Sequence:
MSDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD
Protein: Pyridoxamine 5'-phosphate oxidase-related, FMN-binding (A0QXP8)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Interaction partners:
- Nitroreductase
- Deazaflavin-dependent nitroreductase family protein
- F420-dependent glucose-6-phosphate dehydrogenase
- Deazaflavin-dependent nitroreductase family protein
- YaeQ protein
- Pyridoxine/pyridoxamine 5'-phosphate oxidase
Sequence:
MVAVPEGYESLLERPLYGHLATVRPDGTPQVNAMWFAWDGEVLRFTHTTKRQKYRNIKANPAVAMSVIDPDNPYRYLEVRGLVEDIVPDPTGAFYLKLNDRYDGPLTEPPADKADRVIIVVRPTAFSKQ
Protein: Uncharacterized protein (Q381U2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDREKLAWAGLSIVSVVFFLYIQNSSPRRSRGLHRPRGTRASPPRPVPNKYRSGSTPGTAACRSEGSRSVVSSRPERTNGLTATSNNTFSSKHEPSAHPQESRTNGENTPARHPHWLTRISGSGLNSAARSRRPSTATAPYMNETPQRRERGTQTTDAAFRVVNENDALVQMVSTDALRCISPIPRQGKETPSPLSQDVDLCLGYSLLGGEKLPSFLLSPALDGGVARELMELIEAVQNPEVDPKEWLELYNFLTELPRSVLCHILKTRKIPELAPPLLTARSPQDKRLTHLSRLQQEVFCLLRGERGRYSKIGRFAMDEREAIIIWCPAEGKATKYENQFHQFTILSSDDDDSEDKDNADDLNGSPQCVRVAEAVEKILLRRRRAKMPSSATQFPESSSVSGGETMWYTNSSFEEAEVATLLKQLMKLRHHEAFSVLQRNGTDYSFILNLLSLSTNAQSMLERSILKKKQRARAKVGAPSSSTSSPSITPSGKSGVKPHEQVGTRSNGMSKHTDVRQYEEPNLNEELSILLDKTPSSSFNDGKEGFMVSKKLFGSERNGERTPRRKGVHEHYARVSTTSTVPSPLDNIVDHKILPYGRMNTHAHVEMNGDNSISSGEGSNFRQKKSVYDRLYTPPKKTVKPAATTSSWAKAPFNVYV