wanglab/gogpt-training-data huggingface dataset:
Protein: Anthracycline acyl carrier protein DauA (Q53878)
Organism: Streptomyces sp. (strain C5)
Function: Involved in the biosynthesis of aklanonate which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers.
Interaction partners:
Sequence:
MAELSLAELREIMRQSLGEDEVPDLADADTVTFEDLGLDSLAVLETVNHIERTYGVKLPEEELAEIRTPHSMLIFVNERLRAAV
Protein: Dehydrogenase/reductase SDR family member 7C (EC 1.1.1.105) (Sarcoplasmic reticulum protein of 35 kDa) (Protein SRP-35) (Short-chain dehydrogenase/reductase family 32C member 2) (Protein SDR32C2) (Q8CHS7)
Organism: Mus musculus (Mouse)
Function: NADH-dependent oxidoreductase which catalyzes the oxidation of all-trans-retinol to all-trans-retinal. Plays a role in the regulation of cardiac and skeletal muscle metabolic functions (Probable). Maintains Ca(2+) intracellular homeostasis by repressing Ca(2+) release from the sarcoplasmic reticulum (SR) in myotubes, possibly through local alternations in NAD/NADH or retinol/retinal. Also plays a role in Ca(2+) homeostasis by controlling Ca(2+) overload in the cytosol and the SR in myotubes. Involved in glucose uptake into skeletal muscles and muscle performance by activating PI3K and mTORC2-mediated AKT1 phosphorylation signaling pathways, possibly through the action of its downstream catalytic product all-trans-retinoic acid.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:21995425, ECO:0000305|PubMed:22143674, ECO:0000305|PubMed:27806939}. Note=The N-terminus region encompasses a short hydrophobic sequence bound to the sarcoplasmic reticulum membrane, whereas the C-terminus catalytic domain faces the myoplasm. In skeletal muscle, enriched in the longitudinal sarcoplasmic reticulum (PubMed:21995425). {ECO:0000269|PubMed:21995425, ECO:0000305|PubMed:21995425}.
Interaction partners:
- RIKEN cDNA 2310002L09 gene
- SAYSvFN domain-containing protein 1
- Mapk-regulated corepressor-interacting protein 1
Sequence:
MGLMAVLMLPLLLLGISGLLFIYQEASRLWSKSAVQNKVVVITDAISGLGKECARVFHAGGARLVLCGKNWEGLESLYATLTSVADPSKTFTPKLVLLDLSDISCVQDVAKEVLDCYGCVDILINNASVKVKGPAHKISLELDKKIMDANYFGPITLTKVLLPNMISRRTGQIVLVNNIQAKFGIPFRTAYAASKHAVMGFFDCLRAEVEEYDVVVSTVSPTFIRSYRASPEQRNWETSICKFFCRKLAYGVHPVEVAEEVMRTVRRKKQEVFMANPVPKAAVFIRTFFPEFFFAVVACGVKEKLNVPEEG
Protein: DEP domain-containing protein 1B (HBV X-transactivated gene 8 protein) (HBV XAg-transactivated protein 8) (Q8WUY9)
Organism: Homo sapiens (Human)
Interaction partners:
- Disks large-associated protein 5
- G2/mitotic-specific cyclin-B1
- Kinesin-like protein KIF11
- Centrosomal protein of 55 kDa
- Kinesin-like protein KIF14
- Kinesin-like protein KIF15
- Hyaluronan mediated motility receptor
- Kinetochore protein Nuf2
- DEP domain-containing protein 1A
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Sequence:
MEHRIVGPGPYRATRLWNETVELFRAKMPLRKHRCRFKSYEHCFTAAEAVDWLHELLRCSQNFGPEVTRKQTVQLLKKFLKNHVIEDIKGKWGEEDFEDNRHLYRFPPSSPLKPYPKKPPNQKDVIKFPEWNDLPPGTSQENIPVRPVVMNSEMWYKRHSIAIGEVPACRLVHRRQLTEANVEEIWKSMTLSYLQKILGLDSLEEVLDVKLVNSKFIIHNVYSVSKQGVVILDDKSKELPHWVLSAMKCLANWPNCSDLKQPMYLGFEKDVFKTIADYYGHLKEPLLTFHLFDAFVSVLGLLQKEKVAVEAFQICCLLLPPENRRKLQLLMRMMARICLNKEMPPLCDGFGTRTLMVQTFSRCILCSKDEVDLDELLAARLVTFLMDNYQEILKVPLALQTSIEERVAHLRRVQIKYPGADMDITLSAPSFCRQISPEEFEYQRSYGSQEPLAALLEEVITDAKLSNKEKKKKLKQFQKSYPEVYQERFPTPESAALLFPEKPKPKPQLLMWALKKPFQPFQRTRSFRM
Protein: Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) (P0AB89)
Organism: Escherichia coli (strain K12)
Function: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Interaction partners:
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Bifunctional purine biosynthesis protein PurH
- Adenylosuccinate synthetase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Phosphoribosylamine--glycine ligase
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylglycinamide formyltransferase
- N5-carboxyaminoimidazole ribonucleotide mutase
Sequence:
MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQFIDGLALPEEEKARLKAMTPANYIGRAITMVDELK
Protein: Translation initiation factor 2 subunit beta (aIF2-beta) (eIF-2-beta) (Q8U3I5)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Interaction partners:
- Translation initiation factor 1A
- Translation initiation factor 2 subunit gamma
- Translation initiation factor 2 subunit alpha
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS15
Sequence:
MEIDYYDYEKLLEKAYQELPENVKHHKSRFEVPGALVTIEGNKTIIENFKDIADALNRDPQHLLKFLLREIATAGTLEGRRVVLQGRFTPYLIANKLKKYIKEYVICPVCGSPDTKIIKRDRFHFLKCEACGAETPIQHL
Protein: Troponin I, fast skeletal muscle (Troponin I, fast-twitch isoform) (P48788)
Organism: Homo sapiens (Human)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin C, skeletal muscle
- Troponin T, fast skeletal muscle
- Troponin C, slow skeletal and cardiac muscles
- Troponin T, slow skeletal muscle
- Troponin T, cardiac muscle
- Tropomyosin beta chain
- Myosin-3
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 11
- Troponin I, cardiac muscle
Sequence:
MGDEEKRNRAITARRQHLKSVMLQIAATELEKEESRREAEKQNYLAEHCPPLHIPGSMSEVQELCKQLHAKIDAAEEEKYDMEVRVQKTSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSKHKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFESES
Protein: Thiamine-triphosphatase (ThTPase) (EC 3.6.1.28) (Q8JZL3)
Organism: Mus musculus (Mouse)
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Thiamine pyrophosphokinase 1
- Cancer-related nucleoside-triphosphatase homolog
Sequence:
MAQGLIEVERKFAPGPDTEERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQREGSGWELKCPGVTGVSGPHNEYVEVTSEAAIVAQLFELLGSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLALSGAHGQEPQLTIDLDSADFGYAVGEVEAMVHEKAEVPAALEKIITVSSMLGVPAQEEAPAKLMVYLQRFRPLDYQRLLEAASSGEATGDSAS
Protein: D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (2-oxoglutarate reductase) (EC 1.1.1.399) (Q54UH8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Interaction partners:
- Probable phosphoserine aminotransferase
- Probable phosphoglycerate mutase
- Serine--pyruvate aminotransferase
- Pantoate--beta-alanine ligase
- Putative folylpolyglutamate synthase
- Glycine dehydrogenase
- Bifunctional protein argC
- phosphoserine phosphatase
- Serine hydroxymethyltransferase 2
- Aminomethyltransferase, mitochondrial
Sequence:
MDPTTSFPKDKIKILLLENIHIAAIKQFEEQGFQVESISSSLPEDKIIEKIKDVHVLGLRSKTKVTEKILSEAKRLLAIGCFCIGTDQVDLIEAEKRGVPVFNSPFCNSRSVAELIICEIITLSRKLGDRSTEMHNKIWRKESANCHEIRGKTLGIIGYGHIGSQLSVLAEAMGMSVLYYDIARRLPLGNSKMCPDMKTLLENSNFVTLHVPDTKETVGLIGEEEINTMKKGSYLLNASRGKVVQIPHLANALRSGHLAGAAVDVYPEEPSANCKDWECELQKCPNTILTPHIGGSTEEAQEAIGLEVSDLIVQFINSGASAGSVNFPEIALPVSPSTHRILNIHNNKPGVLRDINNILSEFNVSAQVLSTRKQIGYIIADVDSEASKEIKKKISSLPNSIKTRVLY
Protein: Heterogeneous nuclear ribonucleoprotein C-like 1 (hnRNP C-like-1) (hnRNP core protein C-like 1) (O60812)
Organism: Homo sapiens (Human)
Function: May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs.
Subcellular location: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}.
Interaction partners:
- RNA-binding Raly-like protein
- Heterogeneous nuclear ribonucleoproteins C1/C2
Sequence:
MASNVTNKMDPHSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIAGCSVHKGFAFVQYDKEKNARAAVAGEDGRMIASQVVDINLAAEPKVNRGNAGVKRSAAEMYGSSFDLDYGFQRDYYDGMYSFPARVPPPPPIALAVVPSKRQRLSGNTSRRGKSGFNSKSGKRGSSKSGKLKGDDLQAIKQELTQIKQKVDSLLENLEKIEKEQSKQEVEVKNAKSEEEQSSSSMKKDETHVKMESEGGAEDSAEEGDPLDDDVNEDQGDDQLELIKDDEKEAEEGEDDRDSTNGQDDS
Protein: Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (cHS6ST-2) (EC 2.8.2.-) (Q76LW2)
Organism: Gallus gallus (Chicken)
Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate (By similarity). May also play a role in limb development.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MEDRSHKVLLALVMLFLFAVIVLQYVCPGTECQLLRLRALSPAAAADPYRAEDETPARFVPRFNFSAGDLLRRVDFNIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRAGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTNCVPSVVDSKKEVRLRPSRNFYYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRSPTTEELPSCYTGDDWSGCSLQEFMDCPYNLANNRQVRMLSDLSLVGCYNLSVMPEEQRNKVLLDSAKENLKRMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNSTRASSVEIDEQTQQRIEALNFLDMELYDYAKDLFLQRYQYMRQKEHQEARRKRQEQRKILRAKQAHLREQGENSSSTDYLGNVERWR
Protein: Filaggrin (P11088)
Organism: Mus musculus (Mouse)
Function: Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:3680218}. Note=In the stratum granulosum of the epidermis, localized within keratohyalin granules. In granular keratinocytes and in lower corneocytes, colocalizes with calpain-1/CAPN1 (By similarity). {ECO:0000250|UniProtKB:P20930}.
Interaction partners:
Sequence:
PDGSGRSSNRRDRPRQLSPSQSSDSQVHSGVQVEGRRGHSSSANRRAGSSSGSGVQGASAGGLAADASRRSGARQGQASAQGRAGSQGQAQGRVSSSADRQGRRGVSESRASDSEGHSDFSEGQAVGAHRQSGAGQRHEQRSSRGQHGSGYYYEQEHSEEESDSQHQHGHQHEQQRGHQHQHQHQHEHEQPESGHRQQQSSGRGHQGAHQEQGRDSARPRGSNQGHSSSRHQADSPRVSARSGSGGRGQSPDASGRSSNRRDRPRQPSPSQSSDSQVHSGVQVEAQRGQSSSANRRAGSSSGSGVQGAAASGQGGYESIFTAKHLDFNQSHSYYYY
Protein: Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (Activating transcription factor 2) (MXBP protein) (cAMP response element-binding protein CRE-BP1) (P16951)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type (By similarity).
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-34 is required for its nuclear localization and negatively regulates its mitochondrial localization. Colocalizes with the MRN complex in the IR-induced foci (IRIF) (By similarity). {ECO:0000250}.
Interaction partners:
- Transcription factor Jun
- Mitogen-activated protein kinase 14
- Histone lysine acetyltransferase CREBBP
- Cyclic AMP-responsive element-binding protein 1
- Mitogen-activated protein kinase 11
- Interferon regulatory factor 3
- Mitogen-activated protein kinase 12
- Cyclic AMP-responsive element-binding protein 5
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 13
Sequence:
MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPPSQAQPSGS
Protein: Aldehyde dehydrogenase 1A1 (EC 1.2.1.19) (EC 1.2.1.28) (EC 1.2.1.3) (EC 1.2.1.36) (3-deoxyglucosone dehydrogenase) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) (Retinal dehydrogenase 1) (RALDH 1) (RalDH1) (P48644)
Organism: Bos taurus (Bovine)
Function: Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid. Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (Probable). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:7786847}. Cell projection, axon {ECO:0000250|UniProtKB:P24549}.
Interaction partners:
- Retinol dehydrogenase 10
- Cytochrome P450 26A1
- Dehydrogenase/reductase SDR family member 4
- Alcohol dehydrogenase class-3
- Cytochrome P450 family 26 subfamily C member 1
- Cytochrome P450 26B1
- Alcohol dehydrogenase 4
- Retinol dehydrogenase 5
- Aldehyde oxidase 1
- Dehydrogenase/reductase SDR family member 9
Sequence:
MSSSAMPDVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEEKLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLIERDHLLLATMEAMNGGKLFSNAYLMDLGGCIKTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQIIPWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGSLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSALQSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTIKISQKNS
Protein: Protein FEV (PC12 ETS domain-containing transcription factor 1) (PC12 ETS factor 1) (Pet-1) (mPet-1) (Q8QZW2)
Organism: Mus musculus (Mouse)
Function: Functions as a transcriptional regulator. May function as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:11875656}.
Interaction partners:
- Sodium-dependent serotonin transporter
- Tryptophan 5-hydroxylase 2
Sequence:
MRQSGTSQPLLINMYLPDPVGDGLFKEGKSPSWGPLSPAVQKGSGQIQLWQFLLELLADRANAGCIAWEGGHGEFKLTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMSKVHGKRYAYRFDFQGLAQACQPPPAHAHAAAAAAAAAAAAQDGALYKLPAGLAPLPFPGLSKLNLMAASAGVAPAGFSYWPGPNATAAAAATAALYPTPGLQPPPGPFGAVAAASHLGGHYH
Protein: Cell adhesion molecule 2 (Immunoglobulin superfamily member 4D) (IgSF4D) (Nectin-like protein 3) (NECL-3) (Synaptic cell adhesion molecule 2) (SynCAM 2) (Q1WIM2)
Organism: Rattus norvegicus (Rat)
Function: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Synapse {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=Found in the axoplasm of myelinated axons. {ECO:0000250}.
Interaction partners:
Sequence:
MIWKRSAVLRFYSVCGLLLLGSQGQFPLTQNVTVVEGGTAILTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISVSDVSLSDEGQYTCSLFTMPVKTSKAYLTVLGVPEKPQISGFSSPVMEGDLMQLTCKTSGSKPAADIRWFKNDKEIKDVKYLKEEDANRKTFTVSSTLDFRVDRSDDGVAVICRVDHESLNATPQVAMQVLEIHYTPSVKIIPSTPFPQEGQALTLTCESKGKPLPEPVLWTKDGAELPDPDRMVVSGRELNILFLNKTDNGTYRCEATNTIGQSSAEYVLIVHDVPNTLLPTTIIPSLTTAPVTTTVAITTSPSTSASSSSRRDPNSLAGQNGPDHALIGGIVAVVVFVTLCSIFLLGRYLARHKGTYLTNEAKGAEDAPDADTAIINAEGSQVNAEEKKEYFI
Protein: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7) (P08503)
Organism: Rattus norvegicus (Rat)
Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3813556, ECO:0000269|PubMed:3968063}.
Interaction partners:
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
Sequence:
MAAALRRGYKVLRSVSHFECRAQHTKPSLKQEPGLGFSFELTEQQKEFQTIARKFAREEIIPVAPDYDKSGEYPFPLIKRAWELGLINTHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAGIKTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYFASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN
Protein: Calmodulin-1 (CaM-1) (P0DH95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27014878}. Cell membrane {ECO:0000269|PubMed:14593172}. Note=Localizes to the plasma membrane when interacting with ZAR1. {ECO:0000269|PubMed:27014878}.
Interaction partners:
- Mitogen-activated protein kinase 8
- Plasma membrane-associated cation-binding protein 1
- Kinesin-like protein KIN-14E
- Glutamate decarboxylase 1
- Calmodulin-binding transcription activator 3
- Two pore calcium channel protein 1
- Protein IQ-DOMAIN 1
- Cyclic nucleotide-gated ion channel 2
- CDPK-related kinase 1
- ATMYB2
Sequence:
MADQLTDEQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMAKKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVEEMIREADVDGDGQINYEEFVKIMMAK
Protein: Adrenocorticotropic hormone receptor (Melanocortin 2 receptor) (Q7ZTA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNPSAESPSSIHTDCAEVQVPGQVFLVIAVASLSENLLVIVAVIKNKNLHSPMYCFICNLAVFNTISSFSKALENILLLFKDAGRLNLRGPFELKIDDIMDSLLCMCFLSSIFSILAIAVDRYISIFHALRYHMLMTMRRVLIILFTIWVLCGTSGALMVGFFEAATVTIFFIVLFFTALLLILLLYVHMFLLARHHANRIASMPGAQAQHRKSGLRGALTLTIKKGVFVACWAPFSLHLLIMMICPENQYCECYRSLFQLHVVLLVSHAVIDPAINAFRSVELRNTYKKQLLSSASRICKRCA
Protein: Fibrinogen silencer-binding protein (O95073)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that down-regulates the expression of the fibrinogen gamma chain. Represses transcription of GSK3B gene promoter via its interaction with APBA1.
Subcellular location: Nucleus {ECO:0000269|PubMed:20531236}.
Interaction partners:
Sequence:
MVGKARSSNFTLSEKLDLLKLVKPYVKILEEHTNKHSVIVEKNRCWDIIAVNYNAIGVDRPPRTAQGLRTLYKRLKEYAKQELLQQKETQSDFKSNISEPTKKVMEMIPQISSFCLVRDRNHIQSANLDEEAQAGTSSLQVMLDHHPVAITVEVKQEEDIKPPPPLVLNSQQSDTLEQREEHELVHVMERSLSPSLSSVDMRMTSSPSSIPRRDDFFRHESGEHFRSLLGYDPQILQMLKEEHQIILENQKNFGLYVQEKRDGLKRRQQLEEELLRAKIEVEKLKAIRLRHDLPEYNSL
Protein: Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) (Q9IAC6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Receptor for both mineralocorticoids (MC) such as cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Note=Cytoplasmic and nuclear in the absence of ligand, nuclear after ligand-binding. {ECO:0000250}.
Interaction partners:
Sequence:
FKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRVRKCLQAGMNLGARKSKKPGKLKGVNEDSTPTKEGGQTCPGSGGGYLSSGEKELSTSPTNALVPHGPGGGLVTPYLPPSICSVLELIEPEVVFAGYDNTQPDTTDHLLSSLNQLAGKQMIRVVKWAKVLPGFRGLPIEDQITLIQYSWMCLSSFSLSWRSYKHTNGQMLYFAPDLVFNEDRMQQSAMYDLCLGMRQVSQEFVRLQLTYQEFLSMKVLLLLSTVPKEGLKNQAAFEEMRVNYIKELRRSVGKAPTTLDRRGNRSSQLTKLLDAMHDLGGELLDFCFYTFRESQALKVEFPEMLVEIISDQIPKVESGNTHTLYFHKK