wanglab/gogpt-training-data huggingface dataset:
Protein: Exostosin-like 3 (EC 2.4.1.223) (EXT-related protein 1) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Hereditary multiple exostoses gene isolog) (Multiple exostosis-like protein 3) (Putative tumor suppressor protein EXTL3) (O43909)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS). Initiates HS synthesis by transferring the first N-acetyl-alpha-D-glucosamine (alpha-GlcNAc) residue (GlcNAcT-I activity) to the tetrasaccharide linker (GlcA-Gal-Gal-Xyl-)Ser core linker. May also transfer alpha-GlcNAc residues during HS elongation (GlcNAcT-II activity). Lacks glucuronyl transferase II (GlcAT-II) activity. Important for both skeletal development and hematopoiesis, through the formation of HS proteoglycans (HSPGs). Through the synthesis of HS, regulates postnatal pancreatic islet maturation and insulin secretion (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000269|PubMed:10639137}. Golgi apparatus {ECO:0000269|PubMed:28132690}. Cell membrane {ECO:0000269|PubMed:19158046}. Nucleus {ECO:0000269|PubMed:19158046}. Note=Interaction with REG3A induces its translocation to the nucleus. {ECO:0000269|PubMed:19158046}.
Interaction partners:
- Exostosin-like 1
- Exostosin-like 2
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- X-box-binding protein 1
- Xylosyltransferase 2
- Heat shock protein 75 kDa, mitochondrial
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Sequence:
MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEAGKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLHNCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVILVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQSTFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEARSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGEREDRLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNEAALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQIPAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDFYRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPREQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVDSVLFKTRLPHDKTKCFKFI
Protein: Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (Eukaryotic translation initiation factor 4E homologous protein) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) (mRNA cap-binding protein 4EHP) (h4EHP) (mRNA cap-binding protein type 3) (O60573)
Organism: Homo sapiens (Human)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). In P-bodies, component of a complex that promotes miRNA-mediated translational repression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23991149}. Cytoplasm, P-body {ECO:0000269|PubMed:23991149}.
Interaction partners:
- GRB10-interacting GYF protein 2
- GRB10-interacting GYF protein 1
- Eukaryotic translation initiation factor 4E-binding protein 1
- Eukaryotic translation initiation factor 4 gamma 3
- RNA-binding protein 4
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4 gamma 1
- Endothelial PAS domain-containing protein 1
- Eukaryotic translation initiation factor 4 gamma 2
- Nuclear cap-binding protein subunit 2
Sequence:
MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP
Protein: Cytochrome P450 2E1 (EC 1.14.14.1) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-ALC) (Cytochrome P450-J) (Q05421)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Microsome membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Note=Post-translationally targeted to mitochondria. TOMM70 is required for the translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein. {ECO:0000250|UniProtKB:P05182}.
Interaction partners:
- Alcohol dehydrogenase 1
- Cytochrome P450 7A1
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 2A3
- Carboxylesterase 1D
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- Aldehyde dehydrogenase, dimeric NADP-preferring
Sequence:
MAVLGITVALLVWIATLLLVSIWKQIYRSWNLPPGPFPIPFFGNIFQLDLKDIPKSLTKLAKRFGPVFTLHLGQRRIVVLHGYKAVKEVLLNHKNEFSGRGDIPVFQEYKNKGIIFNNGPTWKDVRRFSLSILRDWGMGKQGNEARIQREAHFLVEELKKTKGQPFDPTFLIGCAPCNVIADILFNKRFDYDDKKCLELMSLFNENFYLLSTPWIQAYNYFSDYLQYLPGSHRKVMKNVSEIRQYTLGKAKEHLKSLDINCPRDVTDCLLIEMEKEKHSQEPMYTMENISVTLADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRAPAVRDRMNMPYMDAVVHEIQRFINLVPSNLPHEATRDTVFRGYVIPKGTVVIPTLDSLLFDNYEFPDPETFKPEHFLNENGKFKYSDYFKAFSAGKRVCVGEGLARMELFLLLSAILQHFNLKSLVDPKDIDLSPVTIGFGSIPREFKLCVIPRS
Protein: Pregnane X receptor (A5WYG8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSRLYDMCLLQLRMSKEMEELSPLDDSGHGDGSEEETEEDDEPKICQVCGDKSTGYHFNAMTCEGCKGFFRRAMKRPAQLCCPFQSACVITKSNRRQCQSCRLQKCLSIGMKRELIMSDEAVEKRRLQIRRKRMQEEPVTLTPQQEAVIQELLNAHKKTFDMTCAHFSQFRPLDRGQKSVSESSPVTNGSWIDHRPIAEDPVQWVFNSTSLSSSSSSYQSLDKEKKHFKSGSFTSLPHFTDLTTYMIKNVINFGKTLTMFRALVMEDQISLLKGATFEIILIHFNMFFNEVTGIWECGPLQYCMDDAFRAGFQHHLLDPMMNFHYTLRKLRLHEEEYVLMQALSLFSPDHPGVTDHKVIDRNQETLALTLKTYIEAKRNGPEKHLLFPKIMGCLTEMRSMNEEYTKQVLKIQDMQPEVSPLWLEIISKDT
Protein: KANL3/Tex30 alpha/beta hydrolase-like domain-containing protein (P96267)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
- Uncharacterized protein Rv2923c
- Uncharacterized protein
- Phosphomethylpyrimidine synthase
- Probable carboxylesterase Culp7
- DUF4262 domain-containing protein
- Probable antibiotic-resistance protein
- Possible conserved membrane protein
Sequence:
MNLDQIAGVAHQPAGPPHGVVVLTHGAGGSRESTLLQQVCAEWTRRGWLAVRYNLPYRRRRPTGPPSGSGSGDRAGIVEAIQLCRGLAEGPLIAGGHSYGGRQTSMVVAAGQAPVDVLTLFSYPVHPPGKPERVRTEHLPGIAVPTVFTHGTADPFGTLAQVRSAAAMVSAPTEVVEITGARHDLGSKTLDVARLAVDAALRLSAGQIA
Protein: Sex peptide receptor (Q8SWR3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for two functionally unrelated ligands; SP (A70A) for controlling reproductive behaviors and MIP for controlling sleep behavior. MIP-SPR pathway functions as a sleep homeostat which perceives the need for sleep and stabilizes it by providing a slow-acting inhibitory input to the fly arousal system that involve the pigment dispersing factor (pdf) neurons. SP-SPR is one of the multiple SP pathways that induce female post-mating behavioral responses (PMR) such as the suppression of mating receptivity and initiation of egg laying. The PMR switch is achieved by mediating the synaptic output of neurons such as those expressing fruitless (fru), double sex (dsx) and pickpocket (ppk).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18066048}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Accessory gland-specific peptide 70A
- Proctolin receptor, isoform A
Sequence:
MDNYTDVLYQYRLAPSASPEMEMELADPRQMVRGFHLPTNESQLEIPDYGNESLDYPNYQQMVGGPCRMEDNNISYWNLTCDSPLEYAMPLYGYCMPFLLIITIISNSLIVLVLSKKSMATPTNFVLMGMAICDMLTVIFPAPGLWYMYTFGNHYKPLHPVSMCLAYSIFNEIMPAMCHTISVWLTLALAVQRYIYVCHAPMARTWCTMPRVRRCTAYIALLAFLHQLPRFFDRTYMPLVIEWNGSPTEVCHLETSMWVHDYIGVDLYYTSYYLFRVLFVHLLPCIILVTLNILLFAAMRQAQERRKLLFRENRKKECKKLRETNCTTLMLIVVVSVFLLAEIPIAVVTAMHIVSSLIIEFLDYGLANICIMLTNFFLVFSYPINFGIYCGMSRQFRETFKEIFLGRLMAKKDSSTKYSIVNGARTCTNTNETVL
Protein: Cerebral cavernous malformations protein 2 homolog (Malcavernin) (Osmosensing scaffold for MEKK3) (Q8K2Y9)
Organism: Mus musculus (Mouse)
Function: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions. May also function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14634666}. Note=Treatment with sorbitol caused relocalization to ruffle-like structures.
Interaction partners:
- Krev interaction trapped protein 1
- Programmed cell death protein 10
- Mitogen-activated protein kinase kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 3
- Integrin beta-1-binding protein 1
- RAC-alpha serine/threonine-protein kinase
- Mitogen-activated protein kinase kinase kinase 2
Sequence:
MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLALPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDKAKRSHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVIMATESKVAAEELCSLLSQVFQIVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDMKDSYDADASTFCFPDSGDVGGLPPLPFCMQTSPHSKTVSESELSTSATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCISLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSTSTINGNRTTGSPDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA
Protein: Probable enoyl-CoA hydratase EchA12 (EC 4.2.1.17) (P9WNN7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Could possibly oxidize fatty acids using specific components.
Interaction partners:
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- Probable thioredoxin TrxA
- Thioredoxin
- 3-hydroxybutyryl-CoA dehydrogenase
- Probable acyl-CoA dehydrogenase FadE2
- Probable acyl-CoA dehydrogenase FadE4
- Acyl-CoA dehydrogenase FadE7
- Probable acyl-CoA dehydrogenase FadE1
- Possible acyl-CoA dehydrogenase FadE19
- Probable acyl-CoA dehydrogenase FadE13
Sequence:
MPHRCAAQVVAGYRSTVSLVLVEHPRPEIAQITLNRPERMNSMAFDVMVPLKEALAQVSYDNSVRVVVLTGAGRGFSPGADHKSAGVVPHVENLTRPTYALRSMELLDDVILMLRRLHQPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGLTASELGLSYLLPRAIGSSRAFEIMLTGRDVSAEEAERIGLVSRQVPDEQLLDACYAIAARMAGFSRPGIELTKRTLWSGLDAASLEAHMQAEGLGQLFVRLLTANFEEAVAARAEQRAPVFTDDT
Protein: Xrn1 N-terminal domain-containing protein (Q386Z9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGTKGLRNYVEKHGLVRSSSRGRDGVVKRTNHLLLDMNAIVHYIVPTNVFTTKSVIEGVVEAVQKLISAFPPSETLVILFDGVAPCAKLQTQKTRRASYNKRHSSECTSSLELRYNHDYIGQEISFSREEIIAGSEFLLACEDAVRCAFGIGGEFCVPPGEGRNYTIIMSGCAEGGEGELKVVCVLRTIWLEQRKSQTYTGDDEIIVVGNDSDLVLVGVACTPYTKFTIVDPRDYALTDVGELFKHWGSSSPGNQIRPDLLPSYRIDFVFLMLLSGGDWFEGIGKVALVFWRRYRELRLHCGYFKRSLIRGEGFDVDIEFLRAVMAVKDVSSPAKYMSKIKQMTMKESPLSREAIEEGVELLKGAVWALRSIVAGQCYDYKFRAHTKKPTAGMLKGASHVKGLLGKIRPVSESPLPCFSPLEQCIAVLGLRGRFSSPIHMVIKEESVNQGEKLTNSFSSEFLLDETRRLMSQVKVDELTAAEQDLLQVRHMRFLESEDGKITFMSFHPEKQAVADVRVCDGGVK
Protein: Spindlin-W (chSpin-W) (Q90WG2)
Organism: Gallus gallus (Chicken)
Function: May play a role in mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11419793}.
Interaction partners:
- Histidine triad missing
- Uncharacterized protein.
- Zinc finger CCHC domain-containing protein 9
- ATP synthase subunit alpha
- Adhesion G protein-coupled receptor G7
- Nipped-B protein.
Sequence:
MKTPFGKSPAQRSRADAGHTRVSASMMKKRTSHKKHRNNVGPSKPISQPRRNIVGCRIQHGWKEGSGPITQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELHKDERVSALEVLPDRVASSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPIMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS
Protein: Keratin, type I cytoskeletal 17 (Cytokeratin-17) (Keratin-17) (K7EPJ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GSSGLGGGSSRTSCRLSGGLGAGSCRLGSAGGLGSTLGGSSYSSCYSFGSGGGYGSSFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPARDYSQYYRTIEELQNKILTATVDNANILLQIDNARLAADDFRTKVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILNEMRDQYEKMAEK
Protein: Thiamine diphosphate dependent-3-acetyloctanal synthase PigD (ThDP-dependent enzyme PigD) (EC 2.2.1.12) (Terminal condensing enzyme) (Q5W268)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the decarboxylation of pyruvate, followed by the modification of the resulting two-carbon fragment acetaldehyde at the C3 position of the 2-octenal (1,2-addition of acetaldehyde) giving 3-acetyloctanal.
Interaction partners:
- Aminotransferase PigE
- 3-isopropylmalate dehydratase
- acetolactate synthase
- Acetolactate synthase small subunit
- Pyruvate-flavodoxin oxidoreductase
- Pyruvate-flavodoxin oxidoreductase
- Phosphate acetyltransferase
- NADP-dependent malic enzyme
- L-proline--[L-prolyl-carrier protein] ligase
- Beta-ketoacyl synthase PigJ
Sequence:
MTTMIGQTRQAGSSSYEQAWQAEQAPCPGMEPDTLTVGVVVVTRNPTFFQTGLSVLNDIRDYVFNRVHIQSELPLKLSELASDPLYSEAREKAIHFLKNQSKALNIQVIQCASLAEATGKIIYTHALEQQPEFQMGMLFYDQTSLGNVDDSIEKIDRDLDAFYSAMQRGGIPAFYTTFSTVTFIRDVRSSFRYLPQQYREIVRSEDPAIFQTELLCLWMDFFEMNYTNRRVKPIGALALHNTLAEQLIQFFERTAASRWLVSYYTGSIISNLIGYLDRHAEAHGALVLRGPNEHAIACGAMANWQLYRMPFLGVVTSGMMDEFKGTLINLKETAAQGIIVAAENRNNQWYSFQGTQTPTEDMRDVLAAKRIPYVYIDDVDGIADGLAEVFRLYHQAQGPVVILATQNVLESTLSLEPVPGDLPPVSGLPAYDCPPISDSFEQAMALINEGPEKLVWQLGPVSDDEYALVHEIADAAGLALVDSLAHPGSAPKYYQGKRNPHYLGTLAIYGYSPRVYNFLHTNDKLNPMSDQSVFMIKSRVAQITTPFSDGRLERKVHLVQLTHDERHLSPYADLKLHMDCLTFLRAVKANLHVDAALREKRKALIAAYLDSPSDVVSQLPSLPMSANYFFCQLNRVIENLIKTENFDFTGVYDVGRCGISAVRNVAKTRRGFSGWYGRALMGDALLATSYLAHTSPTHVVAFIGDGAKGIVPDILPAFIDNILTHPQLLNKSITIFYFCNGGLSVINTYQERILFNRTSRQMRLVNVDQPAFEQTVDDFHIQGKTLTHFDEDTIRHALMTPKRLNLFSVVLGHNNEGDGISLATAKGWQRDPSDREALQERKDWAARQPESTSTSFDQGQNKEAIS
Protein: Caspase Dronc (EC 3.4.22.62) (Death regulator NEDD2-like caspase) [Cleaved into: Caspase Nc subunit 1; Caspase Nc subunit 2] (Q9XYF4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. Effector of steroid-mediated apoptosis during insect metamorphosis. Overexpression promotes programmed cell death. Interaction with Diap1 is required to suppress Dronc-mediated cell death; via Diap1-mediated ubiquitination of Dronc. Rate-limiting caspase in rpr and hid death pathway.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Death-associated inhibitor of apoptosis 1
- Apoptosome protein Dark
- Caspase drICE
- Cell death protein rpr
- Cell death protein Grim
- Caspase-1
- AT03047p
- Tumor necrosis factor family member eiger
- Death-associated inhibitor of apoptosis 2
- DREAM
Sequence:
MQPPELEIGMPKRHREHIRKNLNILVEWTNYERLAMECVQQGILTVQMLRNTQDLNGKPFNMDEKDVRVEQHRRLLLKITQRGPTAYNLLINALRNINCLDAAVLLESVDESDSRPPFISLNERRTSRKSADIVDTPSPEASEGPCVSKLRNEPLGALTPYVGVVDGPEVKKSKKIHGGDSAILGTYKMQSRFNRGVLLMVNIMDYPDQNRRRIGAEKDSKSLIHLFQELNFTIFPYGNVNQDQFFKLLTMVTSSSYVQNTECFVMVLMTHGNSVEGKEKVEFCDGSVVDMQKIKDHFQTAKCPYLVNKPKVLMFPFCRGDEYDLGHPKNQGNLMEPVYTAQEEKWPDTQTEGIPSPSTNVPSLADTLVCYANTPGYVTHRDLDTGSWYIQKFCQVMADHAHDTDLEDILKKTSEAVGNKRTKKGSMQTGAYDNLGFNKKLYFNPGFFNE
Protein: Phosphatidylglycerol phospholipase C (EC 3.1.4.-) (Q08959)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatidylglycerol phospholipase required for the removal of excess phosphatidylglycerol (PG) via a phospholipase C-type degradation mechanism.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:18434318}; Single-pass type IV membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:24868093}.
Interaction partners:
- Cardiolipin synthase
- Phosphatidylglycerophosphatase GEP4, mitochondrial
- Lysophospholipid acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Lysophospholipase NTE1
Sequence:
MVEIVGHRAFKARYPENTLLAFEKAYAAGADVIETDLQMTSDGMVVVNHDSDTGRMWDKNLVIGESTWEEVKRLRCKEDGSLAMMTLKEILTWAVCHPGAKLMLDIKFTNEKIIMIKTFVIMLEVKNDLKFWQERITWGLWLLDWYDFGIETGVLKDFKVIVISLSLDIASQFVKRSLTLNDPHYKLFGISVHFVSSWTSQFRLRLLPVLMKNDIKVYLWTVNKPIDFKYLCELPIHGAITDDPIKARKLCDGHTVAKKPTAEKKFVAPSLASVDGLRFHAFIKVYNILCTLLYSKWVHIKLCGWSIAYVIFLFLRTIHFL
Protein: Small ribosomal subunit protein uS9m (28S ribosomal protein S9, mitochondrial) (MRP-S9) (S9mt) (Q9D7N3)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82933}.
Interaction partners:
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL14
Sequence:
MAAPCVSCGRVLSLWFTPAVRASLCQRPGYWTASAVGWQTGTRFQLSKLIHTTVVTTKKNVQASRQESYTEDFIKKQIEEFNIGKRHLANMMGEDPETFAEEDIDRAIAYLFPSGLFEKRARPMMKHPEHIFPKQRATQWGEDGRPFHFLFYTGKQSYYSLMHDVYGKVMQLEKHRGPLSASAESRDLIGSRWLIKEELEEMLVEKLSDEDYAQFIRLLEKLLTLPCGPAEEEFVQRFRRSVTIQSKKQLIEPVQYDEQGMAFSTSEGRRKSATAQAVVYEHGSGKIHVNGVDYLIYFPITQDREQLMFPFHFLDRLERHDVTCTVSGGGRSAQAGAIRLAMARALCSFVTEDEVEWMRQAGLLTPDPRIRERKKPGQEGARRKFTWKKR
Protein: Protein PRRC1 (Proline-rich and coiled-coil-containing protein 1) (Protein misty somites) (Q5XJA3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:20018846}. Cytoplasm {ECO:0000269|PubMed:18342848, ECO:0000269|PubMed:20018846}.
Interaction partners:
Sequence:
MMEESGIESTPPATPPPPSTVVASPPPLTSGATRPQTVPSPSGISAFTPGDFSSPVPSVALTSTLPPMQSSVPPLPLSSISSPLGLSGPYGIPSASFASPAAGPPLSTGPPLGPVLSAPPMGPPTTGFSVSGGYDITRGHAGRTPQTPLMPSFSSASPMPGIVTNPMMQQPVSGGLDVSSPITFPEDVEDPRVTPDSNAPGGLWGFIKGVAGNPMVKTVLDKTKHSVESMITTLDPGMAPYIKSGGDVDIVVTSDKEVKVAAVRDAFQEVFGLAMVTGEAGQSNIAPQPVGYAAGVKGAQERIDSLRRAAVIHEKQPVVSVENFIAELFPDKWFDIGCLILDDPGYGIHIETFTQATPVALEHVQQAQSLTPPDYNLRWSGLLVTVGEVLERNVPNVSRTDWHQAFTGMSRRQMIYSAAKALAGMYKLRLPSRTV
Protein: Nuclear receptor ROR-beta (Nuclear receptor RZR-beta) (Nuclear receptor subfamily 1 group F member 2) (Retinoid-related orphan receptor-beta) (Q8R1B8)
Organism: Mus musculus (Mouse)
Function: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:16574740}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q92753}.
Interaction partners:
- Nuclear receptor coactivator 1
- Nuclear receptor ROR-alpha
- Nuclear receptor ROR-gamma
- Basic helix-loop-helix ARNT-like protein 1
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
- Period circadian protein homolog 3
- Cryptochrome-1
- Circadian locomoter output cycles protein kaput
- Cone-rod homeobox protein
Sequence:
MCENQPKTKADGTAQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQNNASYSCPRQRNCLIDRTNRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLYAEVQKHQQRLQEQRQQQSGEAEALARVYSSSISNGLSNLNTETGGTYANGHVIDLPKSEGYYSIDSGQPSPDQSGLDMTGIKQIKQEPIYDLTSVPNLFTYSSFNNGQLAPGITMSEIDRIAQNIIKSHLETCQYTMEELHQLAWQTHTYEEIKAYQSKSREALWQQCAIQITHAIQYVVEFAKRITGFMELCQNDQILLLKSGCLEVVLVRMCRAFNPLNNTVLFEGKYGGMQMFKALGSDDLVNEAFDFAKNLCSLQLTEEEIALFSSAVLISPDRAWLIEPRKVQKLQEKIYFALQHVIQKNHLDDETLAKLIAKIPTITAVCNLHGEKLQVFKQSHPDIVNTLFPPLYKELFNPDCAAVCK
Protein: Transcription factor 7 like 2 (D4A8X6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Catenin beta-1
- Transcription factor 7 like 2
- Histone deacetylase 1
- Junction plakoglobin
- Transducin-like enhancer protein 4
- Transcription factor 4
- Serine/threonine-protein kinase NLK
- Lymphoid enhancer-binding factor 1
- TLE family member 1, transcriptional corepressor
- Transducin-like enhancer protein 3
Sequence:
MSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (F1QJE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- E3 ubiquitin-protein ligase TRIP12
Sequence:
MGAYLSQPNTEKSTGNGGSKNLNYGFSAMQGWRVSMEDAHNCIPELDDETAMFAVYDGHGGEEVALYCSKYLPGIIKEQKTYKEGKLQKALEDAFLDIDARITTEEVIKELVQIAGRPQEETEKVADEDDVDNEEAALLHEEATMTIEELLTRYGQNQNKNAKKPCPEASKESEDGEKSHAEKGINGETECGPSVVDSIGKKPAGAGNAAEGSKMRACRRAAASGGSASEGSAEKSGDAGPSCSSSAAAPPGSAKSKFFEDSEESGEEEEEEEGSEEEDGSEEDGENSSENEEEDDTEEGEEEDTDEEEEMCLPGMDGKEEPGSDSGTTAVVALIRGKQLIVANAGDSRCVVSEKGKALDMSYDHKPEDELELARIKNAGGKVTMDGRVNGGLNLSRAIGDHFYKRNKALPAEEQMISALPDVKVLTLNDDHEFMVIACDGIWNVMSSQEVIDFVSERMKTESGKNNPLSAIIDELLDHCLAPDTSGDGTGCDNMTCMIVTFSPRSGSNVAEGTKKRKPEETAVEENGNDSKKPKTE
Protein: Protein TAX4 (P47030)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With IRS4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP51
- Increased rDNA silencing protein 4
Sequence:
MHFPKKKHSGNLSVVELPKEALQDSLTAAQITFKRYAHPNGNAGSAERPRHLKVESAPVVKSEPSLPRMRQPEPRSINHQYSRETLPGHSEAFSVPTTPLQTIHYDVRNKASNSPSSIAAAETAAYLAHTNSFSNRSSGVGSRDPVMDTETKPPRAPSALKNELQLNRMRIPPPSYDNNVRSRSISPQVSYSTSLSSSCSISSDGEETSYREKSTDEAFPPEPSMSSYSLASKASAKASLTDPSQRQQESDYTAMNKLNGGNIIYKGTLPDLIPRSQRKTSKPRFKHRLLRSPEQQQENLSRVYSDQTQNGRAIINTQQNVKLKTTMRRGKYAITDNDETFPYDRKSVSSDSDTDEDSNVMEIKDKKKKSRRSKIKKGLKTTAAVVGSSTSVLPFPHHHHHHHQLHNPNSHHLHTHHHTSSHKFNEDKPWKSHRDLGFITEQERKRYESMWVSNRYSYLRLLPWWPSLANEDDESHLQPLNLPQDGLMLNLVVKDIWYRSNLPRDLLVQIYNMVDTRKDGTLDRKSFIVGMWLVDQCLYGRKLTNELDQRVWNSVDGYVLGTINVKPATSDHYHNANNPLDKPSKLSVRQELKNIKRDLRNVRI