wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha) (eIF2-alpha) (P68101)
Organism: Rattus norvegicus (Rat)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. EIF2S1/eIF-2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming.
Subcellular location: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q6ZWX6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56286}. Mitochondrion {ECO:0000250|UniProtKB:P05198}. Note=Colocalizes with NANOS3 in the stress granules (By similarity). Relocalizes to the surface of mitochondria in response to mitochondrial damage and phosphorylation by EIF2AK1/HRI (By similarity). {ECO:0000250|UniProtKB:P05198, ECO:0000250|UniProtKB:Q6ZWX6}.
Interaction partners:
- Eukaryotic translation initiation factor 2, subunit 2
- Eukaryotic translation initiation factor 2-alpha kinase 3
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Protein phosphatase 1 regulatory subunit 15A
- Interferon-induced, double-stranded RNA-activated protein kinase
- Translation initiation factor eIF2B subunit beta
- eIF-2-alpha kinase GCN2
Sequence:
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTETMPIKINLIAPPRYVMTTTTLERTEGLSVLNQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQLERLERENAEVDGDDDAEEMEAKAED
Protein: Probable glycosyl transferase (Q9HUG1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable carbamoyl transferase
- Uncharacterized protein
- GNAT family N-acetyltransferase
- Spore protein YkvP/CgeB glycosyl transferase-like domain-containing protein
- Lipopolysaccharide kinase
- UDP-glucose:
- Serine/threonine protein kinase
- Heptose kinase
- Lipopolysaccharide core heptose
- Lipopolysaccharide heptosyltransferase 1
Sequence:
MTRSAEPRVLQFCHGYDGPFLDCARQYASLFAGTPYKVTTVFLTGRSDPEVAARCASDEVLFLEYGSRDIRGLKLKAIRDLREIARSRDFRFCIAHRFKPIWIASLATRLPIVGVHHAFGDYQRLSRKVFAGLMSKRLSLLAVSDAVRDDIRRCLPKWPAERIETLYNRIDVAALQAEQVERLSARRQLRLPDEAWVVGNVGRLHPDKDQATLLRGFAAALPRLPQNSLLAILGSGRLEEQLKDLACELGIGERVLFLGQVEEARRYFKAFDAFALSSDHEPFGMVLLEAMVAGVPLIATACGGAREVVEGVGILFPLGDETALAEGLTHLAALDRRQREACARLMLERLETRFSDAAVRREFWRLPTIAGFASESAC
Protein: Kelch-like protein 13 (BTB and kelch domain-containing protein 2) (Q9P2N7)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis.
Interaction partners:
- Cullin-3
- Kelch-like protein 9
- Kelch-like protein 22
- E3 ubiquitin-protein ligase RBX1
- Kelch-like protein 21
- Ectoderm-neural cortex protein 1
- Kelch-like protein 41
- Kelch-like protein 25
- Kelch-like protein 42
- Kelch repeat and BTB domain-containing protein 8
Sequence:
MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYISLVEEEDQHMKLSLGGSEMGLSSHLQSSKAGPTRIFTSNTHSSVVLQGFDQLRLEGLLCDVTLMPGDTDDAFPVHRVMMASASDYFKAMFTGGMKEQDLMCIKLHGVSKVGLRKIIDFIYTAKLSLNMDNLQDTLEAASFLQILPVLDFCKVFLISGVTLDNCVEVGRIANTYNLTEVDKYVNSFVLKNFPALLSTGEFLKLPFERLAFVLSSNSLKHCTELELFKATCRWLRLEEPRMDFAAKLMKNIRFPLMTPQELINYVQTVDFMRTDNTCVNLLLEASNYQMMPYMQPVMQSDRTAIRSDTTHLVTLGGVLRQQLVVSKELRMYDEKAHEWKSLAPMDAPRYQHGIAVIGNFLYVVGGQSNYDTKGKTAVDTVFRFDPRYNKWMQVASLNEKRTFFHLSALKGYLYAVGGRNAAGELPTVECYNPRTNEWTYVAKMSEPHYGHAGTVYGGVMYISGGITHDTFQKELMCFDPDTDKWIQKAPMTTVRGLHCMCTVGERLYVIGGNHFRGTSDYDDVLSCEYYSPILDQWTPIAAMLRGQSDVGVAVFENKIYVVGGYSWNNRCMVEIVQKYDPDKDEWHKVFDLPESLGGIRACTLTVFPPEETTPSPSRESPLSAP
Protein: Guided entry of tail-anchored proteins factor CAMLG (Calcium signal-modulating cyclophilin ligand) (Q6DGG9)
Organism: Rattus norvegicus (Rat)
Function: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1/WRB, acts as a membrane receptor for soluble GET3/TRC40, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. Required for the stability of GET1 (By similarity). Stimulates calcium signaling in T cells through its involvement in elevation of intracellular calcium (By similarity). Essential for the survival of peripheral follicular B cells (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49069}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guided entry of tail-anchored proteins factor 1
- ATPase Get3
- Tumor necrosis factor receptor superfamily member 13B
- Peptidyl-prolyl cis-trans isomerase B
- Guided entry of tail-anchored proteins factor 4
Sequence:
MEPMPSATDGGDRSATPSGLSASQRRAELRRRKLLMNSEQRINRIMGFHRPGSGAEEENQTKSKPLDSDILNPLGVPSVSKRVVLGDSVDGGVTDYQPSGGADIRGAQLGDKLDSFIKAPECSSKDGVELRQRNRGDLTADSAPRGSHHGLEQYLSRFEEAMKLRKQLISEKPSQEDGRTTEEFDSFRIFRLVGCALLALVVRAFVCKYLSIFAPFLTLQLAYMGLYKYFPKGEKKVKTTVLTAALLLSGIPAEVINRSMDTYSKMGEVFTDLCVYFFTFIFCHEVLEYWGPEVP
Protein: 17.6 kDa class I heat shock protein 2 (17.6 kDa heat shock protein 2) (AtHsp17.6B) (Q9ZW31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Chaperone protein ClpB1
- Heat shock 70 kDa protein 4
- Heat shock protein 90-1
- Heat shock 70 kDa protein 8
- HSP20-like chaperones superfamily protein
- Heat shock 70 kDa protein 5
- Heat stress transcription factor A-2
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
Sequence:
MSMIPSFFNNNRRSNIFDPFSLDVWDPFKELTSSSLSRENSAIVNARVDWRETPEAHVFKADLPGLKKEEVKVEIEEDSVLKISGERHVEKEDKNDTWHRVERSSGQFTRRFRLPENVKMDQVKAAMENGVLTVTVPKAETKKADVKSIQISG
Protein: Uncharacterized protein (Q384K8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEPRRWRPRFFNPFTERRRRSSHLPVYRGFFRVMPLHRWSLNNIQAVLGYAAANPSLFGFPEQPTCIVNTAYFLPSHRSRQRGIWVFGTERGCKSIVVPSSCNGGQFDAMDAKLMEPLFRWNPGVEYIYLSQNCQAMASQLVPYLQRCTQLRTLTLEGWNDAVAIHRVVIACKHVDTLDAFSFDDPVRQWKNELSVQALNTLIEMHPKLICVKATRVYLTDWYEATQFSRCKHNIALVPFTCDFVLLHYGFFLLLVSVVAYAVYRETWWLLRDTCSRAYLPFWSALAAVGTFTVIVALDVAGWRSYGRAWVHMHKYVIIARRRWDMIRGRHHKSLMLV
Protein: Substance-P receptor (SPR) (NK-1 receptor) (NK-1R) (Tachykinin receptor 1) (P25103)
Organism: Homo sapiens (Human)
Function: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Protachykinin-1
- Tachykinin-3
- Tachykinin-4
- Beta-arrestin-1
- Beta-arrestin-2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Sodium leak channel NALCN
- Protein unc-80 homolog
- Neurotensin/neuromedin N
Sequence:
MDNVLPVDSDLSPNISTNTSEPNQFVQPAWQIVLWAAAYTVIVVTSVVGNVVVMWIILAHKRMRTVTNYFLVNLAFAEASMAAFNTVVNFTYAVHNEWYYGLFYCKFHNFFPIAAVFASIYSMTAVAFDRYMAIIHPLQPRLSATATKVVICVIWVLALLLAFPQGYYSTTETMPSRVVCMIEWPEHPNKIYEKVYHICVTVLIYFLPLLVIGYAYTVVGITLWASEIPGDSSDRYHEQVSAKRKVVKMMIVVVCTFAICWLPFHIFFLLPYINPDLYLKKFIQQVYLAIMWLAMSSTMYNPIIYCCLNDRFRLGFKHAFRCCPFISAGDYEGLEMKSTRYLQTQGSVYKVSRLETTISTVVGAHEEEPEDGPKATPSSLDLTSNCSSRSDSKTMTESFSFSSNVLS
Protein: 1-Cys peroxiredoxin PER1 (EC 1.11.1.24) (Rehydrin homolog) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin) (O04005)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:14526116}. Cytoplasm {ECO:0000269|PubMed:14526116}.
Interaction partners:
- NADPH-dependent thioredoxin reductase 3
- Sulfiredoxin, chloroplastic/mitochondrial
- Putative inactive glutathione hydrolase 4
- Glutathione hydrolase 2
- Glutathione hydrolase 1
- Glutathione synthetase, chloroplastic
- Glutathione hydrolase 3
- Superoxide dismutase 2, mitochondrial
- 12S seed storage protein CRB
- Peroxiredoxin-2B
Sequence:
MPGITLGDTVPNLEVETTHDKFKLHDYFANSWTVLFSHPGDFTPVCTTELGAMAKYAHEFDKRGVKLLGLSCDDVQSHKDWIKDIEAFNHGSKVNYPIIADPNKEIIPQLNMIDPIENGPSRALHIVGPDSKIKLSFLYPSTTGRNMDEVLRALDSLLMASKHNNKIATPVNWKPDQPVVISPAVSDEEAKKMFPQGFKTADLPSKKGYLRHTEVS
Protein: Cell division cycle protein 48 (P90532)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- UBX domain-containing protein 7 homolog
- NSFL1 cofactor p47 homolog
- Nuclear protein localization protein 4 homolog
- Ubiquitin thioesterase OTU1
- Type-2 histone deacetylase 2
- AAA+ ATPase domain-containing protein
- Ubiquitin fusion degradation protein 1 homolog
- CS domain-containing protein
- Heat shock factor-type DNA-binding domain-containing protein
- OS-9-related protein
Sequence:
MATIEDTSKDNNNPILERKKAPNRLFVEEAINDDNSVVTLNPETMDQLQFFRGDTLLIKGKKRRDTVCIVLSDPTIDPSKIRMNKVVRNNLRVRLGDMISVHQCSDVKYGKRIHVLPIDDTIEGLSGNLFDLYLKPYFLEAYRPVRKGDLFLVRGGMRAVEFKVVETDPGEYCIVAPETFIHCEGEAVKREDEDRLDEVGYDDIGGVRKQLGQIRELVELPLRHPQLFKNIGVKPPKGILLYGPPGCGKTMIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTQGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDITIPDATGRLEIMRIHTKNMKLDETVDLEAVANETHGYVGADLAALCTESALQCIREKMDVIDLEDETISAEILESMSVTQDHFRTALTLSNPSALRETVVEVPTTTWEDIGGLEGVKRELRETVQYPVEHPEKFRKFGMQPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRELFDKARQAAPCVLFFDELDSIARSRGSSQGDAGGAGDRVINQILTEMDGMNAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDLPSRVAILKACLNKSPVAKDVDLEFLGQKTQGFSGADLTEICQRACKLAIRESIEKDIESTKARQESGDTKMEDDSVDPVPEITRDHFQEAMRSARRSVSDNDIRKYESFAQTLVQSRGLGNNFKFPDQESSGQFNQDQSDDLFSN
Protein: Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1) (P22437)
Organism: Mus musculus (Mouse)
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.
Subcellular location: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Interaction partners:
- Prostaglandin E synthase
- Thromboxane-A synthase
- Prostacyclin synthase
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase 3
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Prostaglandin-H2 D-isomerase
- Polyunsaturated fatty acid lipoxygenase ALOX12
Sequence:
MSRRSLSLWFPLLLLLLLPPTPSVLLADPGVPSPVNPCCYYPCQNQGVCVRFGLDNYQCDCTRTGYSGPNCTIPEIWTWLRNSLRPSPSFTHFLLTHGYWLWEFVNATFIREVLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDVQLLAQQLLLRREFIPAPQGTNILFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYHLRLFKDGKLKYQVLDGEVYPPSVEQASVLMRYPPGVPPERQMAVGQEVFGLLPGLMLFSTIWLREHNRVCDLLKEEHPTWDDEQLFQTTRLILIGETIKIVIEEYVQHLSGYFLQLKFDPELLFRAQFQYRNRIAMEFNHLYHWHPLMPNSFQVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQRAGRIGGGRNFDYHVLHVAVDVIKESREMRLQPFNEYRKRFGLKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCQPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKPSTFGGDVGFNLVNTASLKKLVCLNTKTCPYVSFRVPDYPGDDGSVLVRRSTEL
Protein: H/ACA ribonucleoprotein complex subunit 2 (Nucleolar protein family A member 2) (snoRNP protein NHP2) (Q9CRB2)
Organism: Mus musculus (Mouse)
Function: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 3
- Telomerase Cajal body protein 1
- H/ACA ribonucleoprotein complex subunit 1
- H/ACA ribonucleoprotein complex subunit DKC1
- Nucleolar protein 58
- Telomerase reverse transcriptase
- Nucleolar protein 56
- rRNA 2'-O-methyltransferase fibrillarin
- Ubiquitin-like protein FUBI
- RNA cytidine acetyltransferase
Sequence:
MTKVKAAPEESEAQAEGCSEERTYKELLVNLNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMVLAGDTLPIEVYCHLPVLCEDQNLPYVYIPSKTDLGAATGSKRPTCVIMVKPHEEYQETYDKCLEEVQALPTPL
Protein: Unc-45 myosin chaperone A (A0A1W2PNX8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MGIQRRSGPLLTGLSVGLLLLFSWVTLVQPTSLSALVHHPHLCQTTRDVHGRHYPGFFCPRLSDSPEEAYCCHLQAAGGSCCTRAEFEALYQVNLSALPPPPILRGPGPLLVLGLYNLLVVTLMTVDLVHFCCGRGRSLGWSHRRPPSGSSAASSLQASSVEQLRKEGNELFKCGDYGGALAAYTQALGLDATPQDQAVLHRNRAACHLKLEDYDKAETEASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLQRCVSLEPKNKVFQEALRNIGGQIQEKVRYMSSTDAKVEQMFQILLDPEEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDMGETDLMLAALRTLVGICSEHQSRTVATLSILGTRRVVSILGVESQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLDLLTEVGVSGQGRDNALTLLIKAVPRKSLKDPNNSLTLWVIDQGLKKILEVGGSLQDPPGELAVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIKSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKCSEKDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADVKEEFVEDAAALKALFQLSRLEERSVLFAVASALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLLAAGVVSAMVCMVKTESPVLTSSCRELLSRVFLALVEEVEDRGTVVAQGGGRALIPLALEGTDVGQTKAAQALAKLTITSNPEMTFPGERIYEVVRPLVSLLHLNCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMCNLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLQRAAAGGLAMLTSMRPTLCSRIPQVTTHWLEILQALLLSSNQELQHRGAVVVLNMVEASREIASTLMESEMMEILSVLAKGDHSPVTRAAAACLDKAVEYGLIQPNQDGE
Protein: Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P450-P2) (Cytochrome P450-P3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (P00186)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}.
Interaction partners:
- Cytochrome P450 2A12
- Cytochrome P450 2C50
- Cytochrome P450 2C54
- Cytochrome P450 3A11
- Cytochrome P450 2C37
- Cytochrome P450 2C70
- Arylamine N-acetyltransferase 2
- UDP-glucuronosyltransferase
- Cytochrome P450 26A1
- Epoxide hydrolase 1
Sequence:
MAFSQYISLAPELLLATAIFCLVFWMVRASRTQVPKGLKNPPGPWGLPFIGHMLTVGKNPHLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLITNGKSMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSASSCYLEEHVSKEANHLVSKLQKAMAEVGHFEPVSQVVESVANVIGAMCFGKNFPRKSEEMLNIVNNSKDFVENVTSGNAVDFFPVLRYLPNPALKRFKTFNDNFVLFLQKTVQEHYQDFNKNSIQDITSALFKHSENYKDNGGLIPEEKIVNIVNDIFGAGFDTVTTAITWSILLLVTWPNVQRKIHEELDTVVGRDRQPRLSDRPQLPYLEAFILEIYRYTSFVPFTIPHSTTRDTSLNGFHIPKERCIYINQWQVNHDEKQWKDPFVFRPERFLTNNNSAIDKTQSEKVMLFGLGKRRCIGEIPAKWEVFLFLAILLQHLEFSVPPGVKVDLTPNYGLTMKPGTCEHVQAWPRFSK
Protein: PHIKZ131 (Q8SD31)
Organism: Pseudomonas phage phiKZ
Interaction partners:
Sequence:
MAHGETGLYPFDPNGTNPQNFIKGERQTLQVPDGDDYYFIIPFAAPFFVDSLRLFNPLTNQTYVEGVDYLIGHWFIEAMESIGRPIAGSIRIMKRSINAMIGMDYRTIGGQWGFSNQQILAELARKQYNPLIRSWGAIGPLPASFPPLEHNQPIDSLVGSKEILEGIEGIIEAIRAAAAGTTDQHIHDYNNPHRVTKAQVGLSLVPNYAMASDQQHLDANRNDLFTNPRGTLALVNKFAVNPLNAHIAARGNVHGLTAADINLGNVPNYPAATPTTAVDVTNDSVLLTPYTASILYSQIGDASRINELEEKLNQHISNENNPHVVTADQVNAYTKTQVDQLLAGLGGGDASTFGGLTPEQWKDEFPSFGDIERMAAGYNANWDDVQLKIDTLPVIVDDTSEYDRMELIQGVTAGFHAYAGFNSWWDCTIVRDDCVVHPKSPANPYAVIPERLGYAQESWVSHRYGQYWVENGVAKSACIDETKVDEMIPIPVEWTAPIDGNIPSSIWANKTSLYMLTGKFIFSSTGESAIFEHQDLYRCVKGGTSELLVPAANKPWAIFTNTEDTYPGEMTVVVNIGPASSADYVYTAYGIPSFISAFNDFVNNTIKPLNHVIDSMSIGCTHIIMHSIDPLVAPEDYTSESSKVHVMEIIRNGNDTSFMVISPLWFDGRGNDVTANVNSNPIGGVSGLYTHYTVMYGDGQIAFFGNNDNGQCDVDDHAGPYIQLAAGHNFTVTVNTLNQVMFWGDSPDNSLLWNGRGTRVKHIEPTPPTGP
Protein: Major capsid protein (MCP) (P06491)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04016, ECO:0000269|PubMed:8176370}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04016, ECO:0000269|PubMed:8176370}.
Interaction partners:
Sequence:
MAAPNRDPPGYRYAAAMVPTGSLLSTIEVASHRRLFDFFSRVRSDANSLYDVEFDALLGSYCNTLSLVRFLELGLSVACVCTKFPELAYMNEGRVQFEVHQPLIARDGPHPIEQPTHNYMTKIIDRRALNAAFSLATEAIALLTGEALDGTGIGAHRQLRAIQQLARNVQAVLGAFERGTADQMLHVLLEKAPPLALLLPMQRYLDNGRLATRVARATLVAELKRSFCETSFFLGKAGHRREAVEAWLVDLTTATQPSVAVPRLTHADTRGRPVDGVLVTTAPIKQRLLQSFLKVEDTEADVPVTYGEMVLNGANLVTALVMGKAVRSLDDVGRHLLEMQEEQLDLNRQTLDELESAPQTTRVRADLVSIGEKLVFLEALEKRIYAATNVPYPLVGAMDLTFVLPLGLFNPVMERFAAHAGDLVPAPGHPDPRAFPPRQLFFWGKDRQVLRLSLEHAIGTVCHPSLMNVDAAVGGLNRDPVEAANPYGAYVAAPAGPAADMQQLFLNAWGQRLAHGRVRWVAEGQMTPEQFMQPDNANLALELHPAFDFFVGVADVELPGGDVPPAGPGEIQATWRVVNGNLPLALCPAAFRDARGLELGVGRHAMAPATIAAVRGAFDDRNYPAVFYLLQAAIHGSEHVFCALARLVVQCITSYWNNTRCAAFVNDYSLVSYVVTYLGGDLPEECMAVYRDLVAHVEALAQLVDDFTLTGPELGGQAQAELNHLMRDPALLPPLVWDCDALMRRAALDRHRDCRVSAGGHDPVYAAACNVATADFNRNDGQLLHNTQARAADAADDRPHRGADWTVHHKIYYYVMVPAFSRGRCCTAGVRFDRVYATLQNMVVPEIAPGEECPSDPVTDPAHPLHPANLVANTVNAMFHNGRVVVDGPAMLTLQVLAHNMAERTTALLCSAAPDAGANTASTTNMRIFDGALHAGILLMAPQHLDHTIQNGDYFYPLPVHALFAGADHVANAPNFPPALRDLSRQVPLVPPALGANYFSSIRQPVVQHVRESAAGENALTYALMAGYFKISPVALHHQLKTGLHPGFGFTVVRQDRFVTENVLFSERASEAYFLGQLQVARHETGGGVNFTLTQPRANVDLGVGYTAVVATATVRNPVTDMGNLPQNFYLGRGAPPLLDNAAAVYLRNAVVAGNRLGPAQPVPVFGCAQVPRRAGMDHGQDAVCEFIATPVSTDVNYFRRPCNPRGRAAGGVYAGDKEGDVTALMYDHGQSDPSRAFAATANPWASQRFSYGDLLYNGAYHLNGASPVLSPCFKFFTSADIAAKHRCLERLIVETGSAVSTATAASDVQFKRPPGCRELVEDPCGLFQEAYPLTCASDPALLRSARNGEAHARETHFAQYLVYDASPLKGLAL
Protein: Protein transport protein sec16 (E9PK14)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MELWAPQRLPQTRGKATAPSKDPDRGFRRDGHHRPVPHSWHNGERFHQWQDNRGSPQPQQEPRADHQQQPHYASRPGDWHQPVSGVDYYEGGYRNQLYSRPGYENSYQSYQSPTMREEYAYGSYYYHGHPQWLQEERVPRQRSPYIWHEDYREQKYLDEHHYENQHSPFGTNSETHFQSNSRNPCKDSPASNSGQEWPGELFPGSLLAEAQKNKPSLASESNLLQQRESGLSSSSYELSQYIRDAPERDDPPASAAWSPVQAEDVSSAGPKAPMKFYIPHVPVSFGPGGQLVHVGPSSPTDGQAALVELHSMEVILNDSEEQEEMRSFSGPLIREDVHKVDIMTFCQQKAAQSCKSETLGSRDSALLWQLLVLLCRQNGSMVGSDIAELLMQDCKKLEKYKRQPPVANLINLTDEDWPVLSSGTPNLLTGEIPPSVETPAQIVEKFTRLLYYGRKKEALEWAMKNHLWGHALFLSSKMDPQTYSWVMSGFTSTLALNDPLQTLFQLMSGRIPQAATCCGEKQWGDWRPHLAVILSNQAGDPELYQRAIVAIGDTLAGKGLVEAAHFCYLMAHVPFGHYTVKTDHLVLLGSSHRYATWEKGNSKDIFQGTVLALVGFYGSIFHFLM