Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P05020 | PYRC_ECOLI | MTAPSQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVEAAVAYRQRILDAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFNRVFLGTDSAPHARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFYGLPVNDTFIELVREEQ... | 3.5.2.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:15826651, ECO:0000269|PubMed:1671037, ECO:0000269|PubMed:6142052}; Note=Binds 2 Zn(2+) ions per subunit (PubMed:11401542, PubMed:15826651, PubMed:6142052... | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; pyrimidine nucleotide biosynthetic process [GO:0006221] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | dihydroorotase activity [GO:0004151]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, DHOase family, Class II DHOase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.0756 mM for dihydroorotate {ECO:0000269|PubMed:6142052}; KM=0.08 mM for dihydroorotate (in the presence of Zn(2+)) {ECO:0000269|PubMed:15610022}; KM=0.7 mM for dihydroorotate (in the presence of Co(2+)) {ECO:0000269|PubMed:15610022}; KM=0.23 mM for dihydroorotate... | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305}. | null | null | FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052}. | Escherichia coli (strain K12) |
P05023 | AT1A1_HUMAN | MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEA... | 7.2.2.13 | null | cardiac muscle cell action potential involved in contraction [GO:0086002]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular response to steroid hormone stimulus [GO:0071383]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; intracellular... | apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; lateral plasma membrane [GO:0016328]; melanosome [GO:0042470]; membrane [GO:0016020]... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; phosphatase activity [GO:0016791]; potassium ion binding [GO:0030955]; protein heterodimerization activity [GO:0046982]; protein-folding chaperone binding [GO:0051087]; sodium ion bindin... | PF13246;PF00689;PF00690;PF00122; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein {ECO:0000255}. Cell proj... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Homo sapiens (Human) |
P05024 | AT1A1_PIG | MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVI... | 7.2.2.13 | null | establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; membrane repolarization [GO:0086009]; potassium ion import across plasma membrane [GO:1990573]; proton transmembrane transport [GO... | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; potassium ion binding [GO:0030955]; sodium ion binding [GO:0031402] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell pr... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; Evidence={ECO:0000269|PubMed:18075585}... | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Sus scrofa (Pig) |
P05026 | AT1B1_HUMAN | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKVGNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS | null | null | ATP metabolic process [GO:0046034]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; innate immune response [GO:0045087]; intrac... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; sarcolemma [G... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; MHC class II protein complex binding [GO:0023026]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:... | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated (By similarity). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34011520}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the int... | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (P... | Homo sapiens (Human) |
P05027 | AT1B1_PIG | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQSQKTEISFRPNDPQSYESYVVSIVRFLEKYKDLAQKDDMIFEDCGNVPSELKERGEYNNERGERKVCRFRLEWLGNCSGLNDETYGYKDGKPCVIIKLNRVLGFKPKPPKNESLETYPVMKYNPYVLPVHCTGKRDEDKEKVGTMEYFGLGGYPGFPLQYYPYYGKLLQPKYLQPLMAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS | null | null | cell adhesion [GO:0007155]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; innate immune response [GO:0045087]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; membrane repolarization [GO:0086009]; positive regulation of P-ty... | apical plasma membrane [GO:0016324]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated (By similarity). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk a... | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. P... | Sus scrofa (Pig) |
P05028 | AT1B1_SHEEP | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEIAFRPNDPKSYMTYVDNIDNFLKKYRDSAQKDDMIFEDCGNVPSELKDRGEFNNEQGERKVCRFKLEWLGNCSGINDETYGYKEGKPCVIIKLNRVLGFKPKPPKNESLETYPVMKYNPYVLPVQCTGKRDEDKEKVGSIEYFGLGGYPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS | null | null | ATP metabolic process [GO:0046034]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; innate immune response [GO:0045087]; intracellular calcium ion homeostasis [GO:0006874]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; membrane repolarizati... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; organelle membrane [GO:0031090]; sodium:potassium-exchanging ATPase complex [GO:0005890]; sperm flagellum [GO:0036126]; T-tubule [GO:0030315] | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated (By similarity). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk a... | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. P... | Ovis aries (Sheep) |
P05030 | PMA1_YEAST | MTDTSSSSSSSSASSVSAHQPTQEKPAKTYDDAASESSDDDDIDALIEELQSNHGVDDEDSDNDGPVAAGEARPVPEEYLQTDPSYGLTSDEVLKRRKKYGLNQMADEKESLVVKFVMFFVGPIQFVMEAAAILAAGLSDWVDFGVICGLLMLNAGVGFVQEFQAGSIVDELKKTLANTAVVIRDGQLVEIPANEVVPGDILQLEDGTVIPTDGRIVTEDCFLQIDQSAITGESLAVDKHYGDQTFSSSTVKRGEGFMVVTATGDNTFVGRAAALVNKAAGGQGHFTEVLNGIGIILLVLVIATLLLVWTACFYRTNGIV... | 7.1.2.1 | null | positive regulation of TORC1 signaling [GO:1904263]; proteasome storage granule assembly [GO:1902906]; proton export across plasma membrane [GO:0120029]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; transmembrane transport [GO:0055085] | cytosol [GO:0005829]; eisosome [GO:0032126]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type proton-exporting transporter activity [GO:0008553] | PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIIA subfamily | PTM: Phosphorylated on multiple Ser and Thr residues. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate; Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1; | null | null | null | null | FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05031 | DDC_DROME | MSHIPISNTIPTKQTDGNGKANISPDKLDPKVSIDMEAPEFKDFAKTMVDFIAEYLENIRERRVLPEVKPGYLKPLIPDAAPEKPEKWQDVMQDIERVIMPGVTHWHSPKFHAYFPTANSYPAIVADMLSGAIACIGFTWIASPACTELEVVMMDWLGKMLELPAEFLACSGGKGGGVIQGTASESTLVALLGAKAKKLKEVKELHPEWDEHTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVQSENHRMRGAALEKAIEQDVAEGLIPFYAVVTLGTTNSCAFDYLDECGPVGNKHNLWIHVDAAYAGSAFICPEYRH... | 4.1.1.28 | COFACTOR: [Isoform Hypoderm]: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20098687, ECO:0000305|PubMed:29037755}; | adult chitin-containing cuticle pigmentation [GO:0048085]; anesthesia-resistant memory [GO:0007615]; catecholamine metabolic process [GO:0006584]; dopamine biosynthetic process from tyrosine [GO:0006585]; long-term memory [GO:0007616]; regulation of adult chitin-containing cuticle pigmentation [GO:0048082]; response to... | cytoplasm [GO:0005737] | 5-hydroxy-L-tryptophan decarboxylase activity [GO:0036467]; aromatic-L-amino-acid decarboxylase activity [GO:0004058]; L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170] | PF00282; | 3.90.1150.10;1.20.1340.10;3.40.640.10; | Group II decarboxylase family | null | null | CATALYTIC ACTIVITY: [Isoform Hypoderm]: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; EC=4.1.1.28; Evidence={ECO:0000269|PubMed:29037755}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12273; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.26 mM for L-dopa {ECO:0000269|PubMed:29037755}; KM=2.2 mM for L-Dopa {ECO:0000269|PubMed:20098687}; KM=0.4 mM for 5-HTP {ECO:0000269|PubMed:20098687}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:20098687}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-60 degrees Celsius. {ECO:0000269|PubMed:20098687}; | FUNCTION: [Isoform Hypoderm]: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) to dopamine and L-5-hydroxytryptophan (5-HTP) to serotonin (PubMed:20098687). Catalyzes the formation of serotonin more efficiently than dopamine (PubMed:20098687). Displays no activity to tyrosine (PubMed:20098687). Va... | Drosophila melanogaster (Fruit fly) |
P05041 | PABB_ECOLI | MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTFGKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFESLPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDRAENLMIVDLMRNDIGRVAVA... | 2.6.1.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2251281}; | folic acid biosynthetic process [GO:0046656]; para-aminobenzoic acid biosynthetic process [GO:0008153]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162] | aminodeoxychorismate synthase complex [GO:0009356]; cytoplasm [GO:0005737] | 4-amino-4-deoxychorismate synthase activity [GO:0046820]; magnesium ion binding [GO:0000287]; protein heterodimerization activity [GO:0046982]; tryptophan binding [GO:0120284] | PF04715;PF00425; | 3.60.120.10; | Anthranilate synthase component I family | null | null | CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85; Evidence={ECO:0000269|PubMed:16605270, ECO:0000269|PubMed:2251281}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.2 uM for chorismate (with PabA and glutamine as the amino donor at pH 7.5) {ECO:0000269|PubMed:14982443, ECO:0000269|PubMed:16605270, ECO:0000269|PubMed:7592344}; KM=18.6 uM for chorismate (with PabA and ammonia as the amino donor at pH 7.5) {ECO:0000269|PubMed:1... | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2. | null | null | FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... | Escherichia coli (strain K12) |
P05042 | FUMC_ECOLI | MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSI... | 4.2.1.2 | null | fumarate metabolic process [GO:0006106]; malate metabolic process [GO:0006108]; response to oxidative stress [GO:0006979]; tricarboxylic acid cycle [GO:0006099] | tricarboxylic acid cycle enzyme complex [GO:0045239] | fumarate hydratase activity [GO:0004333]; identical protein binding [GO:0042802] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Fumarase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for L-malate (at pH 7.3 and 30 degrees Celsius) {ECO:0000269|PubMed:1917897}; KM=207 uM for fumarate (at pH 7.9) {ECO:0000269|PubMed:12021453}; KM=390 uM for fumarate {ECO:0000269|PubMed:3282546}; KM=857 uM for S-malate (at pH 7.9) {ECO:0000269|PubMed:1202145... | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:1917897}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:3282546}; | FUNCTION: Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress (PubMed:7592392). Catalyzes the stereospecific interconversion of fumarate to L-malate (PubMed:1917897, PubMed:3282546). {ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546, ECO:00... | Escherichia coli (strain K12) |
P05043 | SP0E_BACSU | MGGSSEQERLLVSIDEKRKLMIDAARKQGFTGHDTIRHSQELDCLINEYHQLMQENEHSQGIQGLVKKLGLWPRRDVMPAYDANK | 3.1.3.- | null | regulation of sporulation [GO:0043937]; sporulation resulting in formation of a cellular spore [GO:0030435] | null | hydrolase activity [GO:0016787]; protein dimerization activity [GO:0046983] | PF09388; | 4.10.280.10; | Spo0E family | PTM: Probably degraded by FtsH, the last 14 residues seem to form the FtsH recognition site. | null | null | null | null | null | null | FUNCTION: Aspartyl-phosphate phosphatase which specifically dephosphorylates the sporulation transcription factor Spo0A-P and negatively regulates the sporulation initiation pathway in order to control the proper timing of sporulation. {ECO:0000269|PubMed:11112444, ECO:0000269|PubMed:12067336, ECO:0000269|PubMed:150574... | Bacillus subtilis (strain 168) |
P05044 | SORCN_CRIGR | MAYPGHPGAGGGYYPGGYGGAPGGPSFPGQTQDPLYGYFASVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDSDRSGTVDPQELQKALTTMGFRLNPQTVNSIAKRYSTSGKITFDDYIACCVKLRALTDSFRRRDSAQQGMVNFSYDDFIQCVMTV | null | null | null | membrane [GO:0016020]; sarcoplasmic reticulum membrane [GO:0033017] | calcium ion binding [GO:0005509] | PF13405;PF13833; | 6.10.140.900;1.10.238.10; | null | PTM: Phosphorylated; partially. {ECO:0000269|PubMed:15754088}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15754088}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:15754088}; Peripheral membrane protein {ECO:0000269|PubMed:15754088}; Cytoplasmic side {ECO:0000269|PubMed:15754088}. Note=Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium l... | null | null | null | null | null | FUNCTION: Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the sarcoplasmic reticulum in the heart. Modulates the activity of RYR2 calcium channels. {ECO:0000269|PubMed:15754088, ECO:0000269|PubMed:17029407}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P05050 | ALKB_ECOLI | MLDLFADAEPWQEPLAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGGYTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQSFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGDVVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGKKE | 1.14.11.33 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:19706517, ECO:0000269|PubMed:20084272, ECO:0000269|PubMed:21068844}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161, ECO... | DNA dealkylation involved in DNA repair [GO:0006307]; DNA repair [GO:0006281]; oxidative demethylation [GO:0070989]; oxidative RNA demethylation [GO:0035513]; oxidative single-stranded DNA demethylation [GO:0035552]; oxidative single-stranded RNA demethylation [GO:0035553]; response to methyl methanesulfonate [GO:00727... | cytoplasm [GO:0005737] | broad specificity oxidative DNA demethylase activity [GO:0035516]; dioxygenase activity [GO:0051213]; ferrous iron binding [GO:0008198]; oxidative RNA demethylase activity [GO:0035515] | PF13532; | 2.60.120.590; | AlkB family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:3... | null | null | null | null | FUNCTION: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Acc... | Escherichia coli (strain K12) |
P05055 | PNP_ECOLI | MLNPIVRKFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPIRPLFPEGFVNEVQVIATVVSVNPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVAGTEAAVLMVESEAQLLSEDQMLGAVVFGHEQQQVVIQNINELVKEAGKPRWDWQPEPVNEALNARVAALAEARLSDAYRITDKQERYAQVDVIKSETIATLLAEDETLDENELGEILHAIEKNVVRSRVLAGEPRIDGRE... | 2.7.7.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:19327365}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:19327365}; Note=Magnesium. Can also use manganese. {ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubM... | mRNA catabolic process [GO:0006402]; response to heat [GO:0009408]; RNA catabolic process [GO:0006401]; RNA processing [GO:0006396] | bacterial degradosome [GO:1990061]; cytosol [GO:0005829]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; cyclic-di-GMP binding [GO:0035438]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; polyribonucleotide nucleotidyltransferase activity [GO:0004654]; RNA binding [GO:0003723] | PF00013;PF03726;PF01138;PF03725;PF00575; | 3.30.230.70;3.30.1370.10;2.40.50.140; | Polyribonucleotide nucleotidyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:16079137}. Note=Has also been isolated in association with the inner membrane. | CATALYTIC ACTIVITY: Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395; EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:12162954, ECO:0000269|PubMed... | null | null | null | null | FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Also involved, along with RNase II, in tRNA processing. RNases II and R contribute to rRNA degradation during starvation, while RNase R and PNPase are the major contributo... | Escherichia coli (strain K12) |
P05059 | CMGA_BOVIN | MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQ... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation [GO:0086030]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; ... | chromaffin granule [GO:0042583]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; secretory granule [GO:0030141]; transport vesicle [GO:0030133] | calcium ion binding [GO:0005509]; metal ion binding [GO:0046872] | PF01271; | null | Chromogranin/secretogranin protein family | PTM: In secretory granules, is attacked at both N- and C-terminal sides by proteolytic enzymes generating numerous peptides of various activities. Proteolytic processing can give rise to additional longer forms of catestatin peptides which display a less potent catecholamine release-inhibitory activity (PubMed:10781584... | SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000269|PubMed:10781584}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339, ECO:0000269|PubMed:11584008}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secreto... | null | null | null | null | null | FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas. {ECO:0000269|PubMed:2756155}.; FUNCTION: [Chromostatin]: Completely inhibits catecholamine release from chromaffin cells. {ECO:0000269|PubMed:1996343}.; FUNCTION: [Chromacin]: Has antibacterial activity against M.luteus. Not... | Bos taurus (Bovine) |
P05060 | SCG1_HUMAN | MQPTLLLSLLGAVGLAAVNSMPVDNRNHNEGMVTRCIIEVLSNALSKSSAPPITPECRQVLKTSRKDVKDKETTENENTKFEVRLLRDPADASEAHESSSRGEAGAPGEEDIQGPTKADTEKWAEGGGHSRERADEPQWSLYPSDSQVSEEVKTRHSEKSQREDEEEEEGENYQKGERGEDSSEEKHLEEPGETQNAFLNERKQASAIKKEELVARSETHAAGHSQEKTHSREKSSQESGEETGSQENHPQESKGQPRSQEESEEGEEDATSEVDKRRTRPRHHHGRSRPDRSSQGGSLPSEEKGHPQEESEESNVSMAS... | null | null | null | endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | hormone activity [GO:0005179] | PF01271; | null | Chromogranin/secretogranin protein family | PTM: Extensively processed by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues (By similarity). {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}. Note=Neuroendocrine and endocrine secretory granules. | null | null | null | null | null | FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. | Homo sapiens (Human) |
P05062 | ALDOB_HUMAN | MAHRFPALTQEQKKELSEIAQSIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFSVDSSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAAN... | 4.1.2.13 | null | fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate [GO:0061624]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; NADH oxidation [GO:0006116]; negative regulation of pentos... | centriolar satellite [GO:0034451]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815] | ATPase binding [GO:0051117]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-1-phosphate aldolase activity [GO:0061609]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35122041}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:18000879}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:20848650}; Physiol... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:10970798}; KM=0.95 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:20848650}; KM=2.3 mM for fructose 1-phosphate {ECO:0000269|PubMed:10970798}; KM=0.73 mM for fructose 1-phosphate {ECO:0000269|PubMed:208... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12205126, ECO:0000305|PubMed:20848650}.; PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12... | null | null | FUNCTION: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the ph... | Homo sapiens (Human) |
P05063 | ALDOC_MOUSE | MPHSYPALSAEQKKELSDIALRIVTPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDN... | 4.1.2.13 | null | epithelial cell differentiation [GO:0030855]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | axon [GO:0030424]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; postsynaptic cytosol [GO:0099524] | cytoskeletal protein binding [GO:0008092]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | null | Mus musculus (Mouse) |
P05064 | ALDOA_MOUSE | MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKEN... | 4.1.2.13 | null | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096]; glycolytic process through fructose-6-phosphate [GO:0061615]; methylglyoxal biosynthetic process [GO:0019242]; positive regulation of cell migration [GO:0030335]; protein homotetramerization [GO... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; heterochromatin [GO:0000792]; M band [GO:0031430]; membrane [GO:0016020]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sperm fibrous sheath [GO:0035686]; Z disc [GO:0030018] | fructose-bisphosphate aldolase activity [GO:0004332]; protease binding [GO:0002020] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+).... | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000250|UniProtKB:P04075}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Evid... | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04075}. | Mus musculus (Mouse) |
P05065 | ALDOA_RAT | MPHPYPALTPEQKKELADIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSSLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKEN... | 4.1.2.13 | null | ATP biosynthetic process [GO:0006754]; binding of sperm to zona pellucida [GO:0007339]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose metabolic process [GO:0006000]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242]; muscle cell cellular homeostasis [GO:0046716]; prot... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; heterochromatin [GO:0000792]; I band [GO:0031674]; M band [GO:0031430]; sperm head [GO:0061827] | cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+).... | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000250|UniProtKB:P04075}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Evid... | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04075}. | Rattus norvegicus (Rat) |
P05066 | PHR_YEAST | MKRTVISSSNAYASKRSRLDIEHDFEQYHSLNKKYYPRPITRTGANQFNNKSRAKPMEIVEKLQKKQKTSFENVSTVMHWFRNDLRLYDNVGLYKSVALFQQLRQKNAKAKLYAVYVINEDDWRAHMDSGWKLMFIMGALKNLQQSLAELHIPLLLWEFHTPKSTLSNSKEFVEFFKEKCMNVSSGTGTIITANIEYQTDELYRDIRLLENEDHRLQLKYYHDSCIVAPGLITTDRGTNYSVFTPWYKKWVLYVNNYKKSTSEICHLHIIEPLKYNETFELKPFQYSLPDEFLQYIPKSKWCLPDVSEEAALSRLKDFLG... | 4.1.99.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; COFACTOR: Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:15636; Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit.; | circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; photoreactive repair [GO:0000719] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA binding [GO:0003677]; FAD binding [GO:0071949]; mRNA binding [GO:0003729] | PF00875;PF03441; | 1.25.40.80;1.10.579.10;3.40.50.620; | DNA photolyase class-1 family | null | SUBCELLULAR LOCATION: Nucleus. Mitochondrion. | CATALYTIC ACTIVITY: Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.3; | null | null | null | null | FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05067 | A4_HUMAN | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | null | null | adult locomotory behavior [GO:0008344]; amyloid fibril formation [GO:1990000]; astrocyte activation [GO:0048143]; astrocyte activation involved in immune response [GO:0002265]; axo-dendritic transport [GO:0008088]; axon midline choice point recognition [GO:0016199]; axonogenesis [GO:0007409]; cell adhesion [GO:0007155]... | apical part of cell [GO:0045177]; axon [GO:0030424]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; ciliary rootlet [GO:0035253]; clathrin-coated pit [GO:0005905]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic shaft [... | DNA binding [GO:0003677]; enzyme binding [GO:0019899]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein serine/threonine kinase binding [GO:0120283]; PTB domain binding [GO:0051425]; receptor ligand activity [GO:0048018]; RNA polymerase II cis-regulatory region sequence-specific DNA binding... | PF10515;PF12924;PF12925;PF02177;PF03494;PF00014; | 1.20.120.770;4.10.230.10;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30; | APP family | PTM: Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 an... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383380, ECO:0000269|PubMed:20580937, ECO:0000269|PubMed:2649245, ECO:0000305|PubMed:25122912}; Single-pass type I membrane protein {ECO:0000269|PubMed:30630874, ECO:0000305|PubMed:10383380, ECO:0000305|PubMed:25122912}. Membrane {ECO:0000269|PubMed:2900137, ECO:... | null | null | null | null | null | FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regu... | Homo sapiens (Human) |
P05081 | KAD1_CHICK | MSTEKLKHHKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSERGKKLQAIMEKGELVPLDTVLDMLRDAMLAKADTSKGFLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYKGRGIVRQLNAEGTVDEVFQQVCSYLDKL | 2.7.4.10; 2.7.4.3; 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:1958702}; | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; magnesium ion binding [GO:0000287]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2229026}. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:1958702, ECO:0000269|PubMed:2161682, ECO:0000269|PubMed:2229026, ECO:0000269|PubMed:2542324, ECO:0000269|PubMed:84314... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for ATP {ECO:0000269|PubMed:2542324}; KM=0.6 mM for ADP {ECO:0000269|PubMed:2542324}; KM=0.17 mM for AMP {ECO:0000269|PubMed:2542324}; KM=0.094 mM for AMP {ECO:0000269|PubMed:2161682}; KM=2.25 mM for ThDP {ECO:0000269|PubMed:2229026}; KM=2.3 mM for ThDP {EC... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for ThTP synthesis. {ECO:0000269|PubMed:1958702, ECO:0000269|PubMed:8431472}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:1958702, ECO:0000269|PubMed:8431472}; | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (PubMed:1958702, PubMed:2161682, PubMed:2229026, PubMed:2542324). Exhibits nucleoside diphosphate kinase catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrate... | Gallus gallus (Chicken) |
P05084 | HUNB_DROME | MQNWETTATTNYEQHNAWYNSMFAANIKQEPGHHLDGNSVASSPRQSPIPSTNHLEQFLKQQQQQLQQQPMDTLCAMTPSPSQNDQNSLQHYDANLQQQLLQQQQYQQHFQAAQQQHHHHHHLMGGFNPLTPPGLPNPMQHFYGGNLRPSPQPTPTSASTIAPVAVATGSSEKLQALTPPMDVTPPKSPAKSSQSNIEPEKEHDQMSNSSEDMKYMAESEDDDTNIRMPIYNSHGKMKNYKCKTCGVVAITKVDFWAHTRTHMKPDKILQCPKCPFVTEFKHHLEYHIRKHKNQKPFQCDKCSYTCVNKSMLNSHRKSHS... | null | null | anterior/posterior axis specification [GO:0009948]; ganglion mother cell fate determination [GO:0007402]; generation of neurons [GO:0048699]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast fate determination [GO:0007400]; positive regulation of transcription by RNA polymerase II [GO:... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-speci... | PF00096; | 3.30.160.60; | Hunchback C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Gap class segmentation protein that controls development of head structures. | Drosophila melanogaster (Fruit fly) |
P05089 | ARGI1_HUMAN | MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNP... | 3.5.3.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323, ECO:0000269|PubMed:18802628}; Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323, ECO:0000269|PubMe... | adaptive immune response [GO:0002250]; arginine catabolic process [GO:0006527]; arginine catabolic process to ornithine [GO:0019547]; defense response to protozoan [GO:0042832]; innate immune response [GO:0045087]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of T cell prolife... | azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; specific granule lumen [GO:0035580] | arginase activity [GO:0004053]; manganese ion binding [GO:0030145] | PF00491; | 3.40.800.10; | Arginase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16141327}. Cytoplasmic granule {ECO:0000269|PubMed:15546957}. Note=Localized in azurophil granules of neutrophils (PubMed:15546957). {ECO:0000269|PubMed:15546957}. | CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17562323, ECO:0000269|PubMed:21728378}; | null | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000305|PubMed:16141327}. | null | null | FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a l... | Homo sapiens (Human) |
P05090 | APOD_HUMAN | MVMLLLLLSALAGLFGAAEGQAFHLGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFENGRCIQANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQVNCPKLS | null | null | angiogenesis [GO:0001525]; brain development [GO:0007420]; glucose metabolic process [GO:0006006]; lipid metabolic process [GO:0006629]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of lipoprot... | cytoplasm [GO:0005737]; cytosolic ribosome [GO:0022626]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471] | cholesterol binding [GO:0015485]; lipid transporter activity [GO:0005319] | PF08212; | 2.40.128.20; | Calycin superfamily, Lipocalin family | PTM: N-glycosylatd. N-glycan heterogeneity at Asn-65: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor); at Asn-98: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (major), dHex1Hex6HexNAc5 (minor) and dHex1Hex7HexNAc6 (minor). {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:1... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts. | Homo sapiens (Human) |
P05091 | ALDH2_HUMAN | MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCC... | 1.2.1.3 | null | alcohol metabolic process [GO:0006066]; aldehyde catabolic process [GO:0046185]; carbohydrate metabolic process [GO:0005975]; ethanol catabolic process [GO:0006068]; regulation of dopamine biosynthetic process [GO:1903179]; regulation of serotonin biosynthetic process [GO:1905627] | extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; aldehyde dehydrogenase [NAD(P)+] activity [GO:0004030]; carboxylesterase activity [GO:0106435]; electron transfer activity [GO:0009055]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; NAD binding [GO:0051287]; nitroglycer... | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. | null | null | FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage. {ECO:0000269|PubMed:33355142}. | Homo sapiens (Human) |
P05093 | CP17A_HUMAN | MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLH... | 1.14.14.19; 1.14.14.32 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:22266943, ECO:0000269|PubMed:25301938}; | androgen biosynthetic process [GO:0006702]; glucocorticoid biosynthetic process [GO:0006704]; hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; sex differentiation [GO:0007548]; steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202] | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; neuronal cell body [GO:0043025] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxygen binding [GO:0019825]; steroid 17-alpha-monooxygenase activity [GO:0004508] | PF00067; | 1.10.630.10; | Cytochrome P450 family | PTM: Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity. {ECO:0000269|PubMed:10720067}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:2808364}. Microsome membrane {ECO:0000305|PubMed:2808364}. | CATALYTIC ACTIVITY: Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 uM for progesterone (17-alpha hydroxylation) {ECO:0000269|PubMed:25301938}; KM=5.87 uM for progesterone (17-alpha hydroxylation) {ECO:0000269|PubMed:36640554}; KM=0.93 uM for pregnenolone (17-alpha hydroxylation) {ECO:0000269|PubMed:25301938}; KM=1.19 uM for p... | PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:22266943, ECO:0000269|PubMed:25301938, ECO:0000269|PubMed:27339894, ECO:0000269|PubMed:9452426}.; PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000269|PubMed:25301938, ECO:0000269|PubMed:9452426}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426). Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an a... | Homo sapiens (Human) |
P05094 | ACTN1_CHICK | MDHHYDPQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMQAMQQKLEDFRDY... | null | null | actin cytoskeleton organization [GO:0030036]; muscle cell development [GO:0055001]; sarcomere organization [GO:0045214]; skeletal muscle fiber development [GO:0048741] | bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cell leading edge [GO:0031252]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; dense body [GO:0097433]; focal adhesion [GO:0005925]; inner dense plaque of desmosome [GO:0090637]; lamellipodium [GO:0030027]; lateral plasma membr... | actin filament binding [GO:0051015]; alpha-actinin binding [GO:0051393]; calcium ion binding [GO:0005509]; LIM domain binding [GO:0030274]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; vinculin binding [GO:0017166] | PF00307;PF13405;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Z1P2}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P12814}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1P2}. Cell junction {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TPR4}. | null | null | null | null | null | FUNCTION: F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. | Gallus gallus (Chicken) |
P05095 | ACTNA_DICDI | MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKG... | null | null | actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; cell motility [GO:0048870]; cellular response to starvation [GO:0009267]; hyperosmotic response [GO:0006972]; phagocytosis [GO:0006909]; sorocarp development [GO:0030587] | actin filament [GO:0005884]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell leading edge [GO:0031252]; cell projection [GO:0042995]; contractile vacuole [GO:0000331]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; macropinocytic cup [GO:0070685]; phagocyti... | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200] | PF00307;PF13499;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7820857}. Cytoplasm, cell cortex {ECO:0000269|PubMed:7820857}. Contractile vacuole {ECO:0000269|PubMed:7820857}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:7820857}. Note=Expressed diffusely throughout the cytoplasm. Accumulates in the cell cortex, contractile... | null | null | null | null | null | FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin... | Dictyostelium discoideum (Social amoeba) |
P05102 | MTH1_HAEPH | MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGDITQVNEKTIPDHDILCAGFPCQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMENVKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIPQKRERIYMICFRNDLNIQNFQFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGERIYSTRGIAITLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYKQFGNSVVINVLQYIAYNIGS... | 2.1.1.37 | null | DNA restriction-modification system [GO:0009307]; methylation [GO:0032259] | null | DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677] | PF00145; | 3.90.120.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 nM for DNA {ECO:0000269|PubMed:7899082}; KM=15 nM for S-adenosyl-L-methionine (SAM) {ECO:0000269|PubMed:7899082}; Vmax=87 nmol/min/mg enzyme {ECO:0000269|PubMed:7899082}; | null | null | null | FUNCTION: A methylase, recognizes the double-stranded sequence 5'-GCGC-3', methylates C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease. {ECO:0000269|PubMed:3549710, ECO:0000269|PubMed:7899082, ECO:0000303|PubMed:12654995}. | Haemophilus parahaemolyticus |
P05106 | ITB3_HUMAN | MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGL... | null | null | activation of protein kinase activity [GO:0032147]; angiogenesis involved in wound healing [GO:0060055]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; blood coagulation [GO:0007596]; blood coagulation, fibrin clot formation [GO:0072378]; cell adhesion [GO:0007155]; c... | alpha9-beta1 integrin-ADAM8 complex [GO:0071133]; alphav-beta3 integrin-HMGB1 complex [GO:0035868]; alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; alphav-beta3 integrin-PKCalpha complex [GO:0035866]; alphav-beta3 integrin-vitronectin complex [GO:0071062]; apical plasma membrane [GO:0016324]; cell surface [GO:0... | cell adhesion molecule binding [GO:0050839]; coreceptor activity [GO:0015026]; enzyme binding [GO:0019899]; extracellular matrix binding [GO:0050840]; fibrinogen binding [GO:0070051]; fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; metal ion binding [GO:0046872];... | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. A peptide (AA 740-762) is capable of binding GRB2 only when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation of Thr-779 inhibits SHC binding. {ECO:0000269|PubMed:10896934... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-pass type I membrane protein {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:20702409}. C... | null | null | null | null | null | FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, ... | Homo sapiens (Human) |
P05107 | ITB2_HUMAN | MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIF... | null | null | amyloid-beta clearance [GO:0097242]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cell-cell signaling [GO:0007267]; cell-matrix adhesion [GO:0007160]; ... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; ficolin-1-rich granule membrane [GO:0101003]; focal adhesion [GO:0005925]; integrin alphaL-beta2 complex [GO:0034687]; integrin alphaM-beta2 complex [GO:0034688]; integrin al... | amyloid-beta binding [GO:0001540]; cell adhesion molecule binding [GO:0050839]; complement component C3b binding [GO:0001851]; heat shock protein binding [GO:0031072]; ICAM-3 receptor activity [GO:0030369]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901] | PF08725;PF07965;PF00362;PF17205; | 6.20.50.10;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters (PubMed:11700305). Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins (PubMed:11700305, PubMed:16301335). {ECO:0000269|PubMed:11700305, ECO:0000269|PubMed:16301335}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:28807980}; Single-pass type I membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21193407}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055). Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third co... | Homo sapiens (Human) |
P05108 | CP11A_HUMAN | MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANV... | 1.14.15.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:21636783}; | C21-steroid hormone biosynthetic process [GO:0006700]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; glucocorticoid biosynthetic process [GO:0006704]; sterol metabolic process [GO:0016125]; vitamin D metabolic process [GO... | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | cholesterol monooxygenase (side-chain-cleaving) activity [GO:0008386]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone; Xref=Rhea:RHEA:35739, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:16581, ChEBI:CH... | null | PATHWAY: Lipid metabolism; C21-steroid hormone metabolism. {ECO:0000269|PubMed:21636783}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:21636783}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones (PubMed:21636783). Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C... | Homo sapiens (Human) |
P05109 | S10A8_HUMAN | MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; astrocyte development [GO:0014002]; autocrine signaling [GO:0035425]; autophagy [GO:0006914]; chronic inflammatory response [GO:0002544]; defense response to bacterium [GO:0042742]; defense res... | calprotectin complex [GO:1990660]; collagen-containing extracellular matrix [GO:0062023]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intermediate filament cytoskeleton [GO:0045111]; nucleus [GO:0005634]; plasm... | arachidonic acid binding [GO:0050544]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; microtubule binding [GO:0008017]; RAGE receptor binding [GO:0050786]; Toll-like receptor 4 binding [GO:0035662]; zinc ion binding [GO:0008270] | PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endot... | null | null | null | null | null | FUNCTION: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The int... | Homo sapiens (Human) |
P05110 | GLUC_CAVPO | MKSVYFVAGLFIMLAQGSWQRSLQDTEEKPRSVSASQTDMLDDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQQFLKWLLNVKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDRK | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to glucagon stimulus [GO:0071377]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of calcium ion import [GO:009... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]; identical protein binding [GO:0042802] | PF00123; | 6.10.250.590; | Glucagon family | PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-te... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01275}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000250|UniProtKB:P01275}. | null | null | null | null | null | FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maint... | Cavia porcellus (Guinea pig) |
P05111 | INHA_HUMAN | MVLHLLLFLLLTPQGGHSCQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFTHRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPSQHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMSLGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAHTRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPYSL... | null | null | cell differentiation [GO:0030154]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; erythrocyte differentiation [GO:0030218]; hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; negative regulation of B cell differentiation [GO:0045578]; negative reg... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512]; inhibin B complex [GO:0043513]; inhibin-betaglycan-ActRII complex [GO:0034673]; neuronal cell body [GO:0043025]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; inhibin binding [GO:0034711]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF00019; | 2.10.90.10; | TGF-beta family | PTM: Proteolytic processing yields a number of bioactive forms. The 20/23 kDa forms consist solely of the mature alpha chain, the 26/29 kDa forms consist of the most N-terminal propeptide linked through a disulfide bond to the mature alpha chain, the 50/53 kDa forms encompass the entire proprotein. Each type can be fur... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Homo sapiens (Human) |
P05112 | IL4_HUMAN | MGLTSQLLPPLFFLLACAGNFVHGHKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS | null | null | activation of Janus kinase activity [GO:0042976]; B cell costimulation [GO:0031296]; B cell differentiation [GO:0030183]; cholesterol metabolic process [GO:0008203]; dendritic cell differentiation [GO:0097028]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; immune response [GO:0006955]; innate... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-4 receptor binding [GO:0005136] | PF00727; | 1.20.1250.10; | IL-4/IL-13 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:1993171, PubMed:3016727). Induces the expression of class II MHC molecules on resting B-c... | Homo sapiens (Human) |
P05113 | IL5_HUMAN | MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES | null | null | immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-5-mediated signaling pathway [GO:0038043]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of eosinophil differentiation [GO:0045645]; positive reg... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-5 receptor binding [GO:0005137] | PF02025; | 1.20.1250.10; | IL-5 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2653458}. | null | null | null | null | null | FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:2653458, PubMed:9010276). Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation ... | Homo sapiens (Human) |
P05114 | HMGN1_HUMAN | MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD | null | null | chromatin organization [GO:0006325]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; post-embryonic camera-type eye morphogenesis [GO:0048597]; pyrimidine dimer repair by nucleotide-excision repair [GO:0000720]; regulation of development, heterochronic [GO:0040034]; regulation of epithelial... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; female germ cell nucleus [GO:0001674]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492] | PF01101; | null | HMGN family | PTM: Phosphorylation on Ser-21 and Ser-25 weakens binding to nucleosomes and increases the rate of H3 phosphorylation (By similarity). Phosphorylation favors cytoplasmic localization. {ECO:0000250, ECO:0000269|PubMed:10739259}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus. | null | null | null | null | null | FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6K... | Homo sapiens (Human) |
P05117 | PGLR_SOLLC | MVIQRNSILLLIIIFASSISTCRSNVIDDNLFKQVYDNILEQEFAHDFQAYLSYLSKNIESNNNIDKVDKNGIKVINVLSFGAKGDGKTYDNIAFEQAWNEACSSRTPVQFVVPKNKNYLLKQITFSGPCRSSISVKIFGSLEASSKISDYKDRRLWIAFDSVQNLVVGGGGTINGNGQVWWPSSCKINKSLPCRDAPTALTFWNCKNLKVNNLKSKNAQQIHIKFESCTNVVASNLMINASAKSPNTDGVHVSNTQYIQISDTIIGTGDDCISIVSGSQNVQATNITCGPGHGISIGSLGSGNSEAYVSNVTVNEAKII... | 3.2.1.15 | null | anther dehiscence [GO:0009901]; cell wall organization [GO:0071555]; fruit dehiscence [GO:0010047]; fruit ripening [GO:0009835]; pectin catabolic process [GO:0045490] | apoplast [GO:0048046] | polygalacturonase activity [GO:0004650] | PF00295; | 2.160.20.10; | Glycosyl hydrolase 28 family | PTM: N-glycosylated. PG2B isozyme has a greater degree of glycosylation than PG2A. {ECO:0000269|PubMed:16666031, ECO:0000269|PubMed:2152163, ECO:0000269|PubMed:6617647}. | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:2152163}. Secreted, cell wall {ECO:0000269|PubMed:2152163}. Note=Associated to the cell wall. | CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15; Evidence={ECO:0000269|PubMed:9701584}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38 uM for polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; KM=75 uM for polygalacturonic acid (for PG1 at pH 4.6 and 35 degrees Celsiu... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.4-4.8 at 35 degrees Celsius. PG1 is resistant to acidic but not to alkaline conditions, at which PG2 is released from the beta subunit. {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is more thermostable than PG2. {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; | FUNCTION: Catalytic subunit of the polygalacturonase isozyme 1 and 2 (PG1 and PG2). Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation. The depolymerization and solubilization of cell wall polyuronides mediated by PG2 during rip... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
P05120 | PAI2_HUMAN | MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYEL... | null | null | fibrinolysis [GO:0042730]; negative regulation of apoptotic process [GO:0043066] | cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family, Ov-serpin subfamily | PTM: The signal sequence is not cleaved. | SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. | Homo sapiens (Human) |
P05121 | PAI1_HUMAN | MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTD... | null | null | angiogenesis [GO:0001525]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-negative bacterium [GO:0050829]; dentinogenesis [GO:0097187]; fibrinolysis [GO:0042730]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell adhesion mediated by integrin [GO:0033629]... | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; peptidase inhibitor complex [GO:1904090]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; serine protease inhibitor complex [GO:0097180... | protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2430793}. | null | null | null | null | null | FUNCTION: Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots... | Homo sapiens (Human) |
P05122 | KCRB_CHICK | MPFSNSHNLLKMKYSVDDEYPDLSVHNNHMAKVLTLDLYKKLRDRQTSSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPVIEDRHGGYKPTDEHKTDLNADNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLSVEALGSLGGDLKGKYYALRNMTDAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFGEVLKRLRLQKR... | 2.7.3.2 | null | ATP biosynthetic process [GO:0006754]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; extracellular membrane-bounded organelle [GO:0065010]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | PTM: Ba-CK and Bb-CK are phosphorylated. {ECO:0000269|PubMed:2307674}.; PTM: The N-terminus of BA-CK is blocked. {ECO:0000269|PubMed:2365692}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04447}. Mitochondrion {ECO:0000250|UniProtKB:Q04447}. Cell membrane {ECO:0000250|UniProtKB:P12277}. | CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10029, ECO:0000269|PubMed:20026305, ECO:0000269|PubMed:8525081}; Physio... | null | null | null | null | FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:20026305, PubMed:8525081). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spe... | Gallus gallus (Chicken) |
P05125 | ANF_MOUSE | MGSFSITLGFFLVLAFWLPGHIGANPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTEEAGAALSSLPEVPPWTGEVNPPLRDGSALGRSPWDPSDRSALLKSKLRALLAGPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR | null | null | cardiac muscle hypertrophy in response to stress [GO:0014898]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of blood pressure [GO:0045776]; negative regulation of cell growth [GO:0030308]; negative regulation of collecting lymphatic ves... | brush border [GO:0005903]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; glycinergic synapse [GO:0098690]; mast cell granule [GO:0042629]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; neuropeptide hormone activity [GO:0005184]; neuropeptide receptor binding [GO:0071855]; signaling receptor binding [GO:0005102] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-122 to produce atrial natriuretic peptide (PubMed:11884416, PubMed:15637153). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additio... | SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kali... | null | null | null | null | null | FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (PubMed:12890708, PubMed:22437503, PubMed:8760210). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activa... | Mus musculus (Mouse) |
P05126 | KPCB_BOVIN | MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIEREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGPGPKTPEEK... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403}; | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; intracellular signal transduction [GO:0035556]; negative regulation of glucose transmembrane transport [GO:0010829]; negative regulation of insulin receptor signaling pa... | cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein serine ki... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling an... | Bos taurus (Bovine) |
P05128 | KPCG_BOVIN | RPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCNLLQKFEACNYPLELYERVRTGPSSSPIPSPSPSPTDSK... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P05129}; | intracellular signal transduction [GO:0035556]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of proteasomal protein catabolic process [GO:1901799]; negative regulation of protein ubiquitination [GO:0031397]; phosphorylation [GO:0016310]; regulation of circadian rhythm [GO:0042752]; ... | cytosol [GO:0005829]; dendrite [GO:0030425]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylation on Thr-659 appears to regulate motor functions of junctophilins, JPH3 and JPH4. {ECO:0000250|UniProtKB:P63318}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P05129}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63318}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Transl... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to op... | Bos taurus (Bovine) |
P05129 | KPCG_HUMAN | MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|Ref.14}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000269|Ref.14}; | chemical synaptic transmission [GO:0007268]; chemosensory behavior [GO:0007635]; innervation [GO:0060384]; intracellular signal transduction [GO:0035556]; learning or memory [GO:0007611]; long-term synaptic potentiation [GO:0060291]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of p... | calyx of Held [GO:0044305]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; dendrite [GO:0030425]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; presynaptic cytosol [GO:0099523]; synaptic mem... | ATP binding [GO:0005524]; calcium,diacylglycerol-dependent serine/threonine kinase activity [GO:0004698]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; prot... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4. {ECO:0000250|UniProtKB:P63318}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:29053796}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translo... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to op... | Homo sapiens (Human) |
P05130 | KPC1_DROME | MSEGSDNNGDPQQQGAEGEAVGENKMKSRLRKGALKKKNVFNVKDHCFIARFFKQPTFCSHCKDFICGYQSGYAWMGFGKQGFQCQVCSYVVHKRCHEYVTFICPGKDKGIDSDSPKTQHNFEPFTYAGPTFCDHCGSLLYGIYHQGLKCSACDMNVHARCKENVPSLCGCDHTERRGRIYLEINVKENLLTVQIKEGRNLIPMDPNGLSDPYVKVKLIPDDKDQSKKKTRTIKACLNPVWNETLTYDLKPEDKDRRILIEVWDWDRTSRNDFMGALSFGISEIIKNPTNGWFKLLTQDEGEYYNVPCADDEQDLLKLKQ... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041}; | intracellular signal transduction [GO:0035556]; positive regulation of clathrin-dependent endocytosis [GO:2000370]; protein phosphorylation [GO:0006468]; regulation of hemocyte proliferation [GO:0035206] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins (By similarity). PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity). Acts in a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uraci... | Drosophila melanogaster (Fruit fly) |
P05131 | KAPCB_BOVIN | MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFR... | 2.7.11.11 | null | negative regulation of TORC1 signaling [GO:1904262]; protein kinase A signaling [GO:0010737]; protein phosphorylation [GO:0006468] | cAMP-dependent protein kinase complex [GO:0005952]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. D... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684253}. Cell membrane {ECO:0000250|UniProtKB:P22694}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000269|PubMed:10684253}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenz... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassemb... | Bos taurus (Bovine) |
P05132 | KAPCA_MOUSE | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK... | 2.7.11.11 | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to cold [GO:0070417]; cellular response to glucagon stimulus [GO:0071377]; cellular response to glucose stimulus [GO:0071333]; cellular response to heat [GO:0034605]; cellular response to parathyroid hormone stimul... | acrosomal vesicle [GO:0001669]; axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; neuromuscular junction... | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinas... | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Autophosphorylated; phosphorylation is enhanced by vitamin K(2) (By similarity). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (PubMed:8395513, PubMed:9707564). Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increase... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18367160}. Cell membrane {ECO:0000269|PubMed:33886552}. Nucleus {ECO:0000250|UniProtKB:P17612}. Mitochondrion {ECO:0000269|PubMed:18367160}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Note=Translocates into the nucleus (monom... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; Evidence={ECO:0000269|PubMed:10805756, ECO:00002... | null | null | null | null | FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:10805756, PubMed:19223768). Regulates the abundance of compartmentalized pools of its regulatory subunits through phospho... | Mus musculus (Mouse) |
P05133 | NCAP_HANTV | MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQDPTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFKDDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWLIEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCL... | 3.1.-.- | null | symbiont-mediated suppression of host apoptosis [GO:0033668] | helical viral capsid [GO:0019029]; host cell Golgi apparatus [GO:0044177]; host cell perinuclear region of cytoplasm [GO:0044220]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | PF00846; | 1.20.58.90; | Hantavirus nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12573574}. Host Golgi apparatus, host cis-Golgi network {ECO:0000269|PubMed:24070985}. Note=Internal protein of virus particle. {ECO:0000305}. | null | null | null | null | null | FUNCTION: Encapsidates the genome protecting it from nucleases (PubMed:26923588). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (PubMed:30638449). As a trimer, specifically binds and ... | Hantaan virus (strain 76-118) (Korean hemorrhagic fever virus) |
P05141 | ADT2_HUMAN | MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWLYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFRGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT | null | null | adaptive thermogenesis [GO:1990845]; adenine nucleotide transport [GO:0051503]; B cell differentiation [GO:0030183]; cellular response to leukemia inhibitory factor [GO:1990830]; chromosome segregation [GO:0007059]; erythrocyte differentiation [GO:0030218]; mitochondrial ADP transmembrane transport [GO:0140021]; mitoch... | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial permeability transition pore complex [GO:0005757]; mitochondrion [GO:0005739]; MMXD complex [GO:0071817]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | adenine nucleotide transmembrane transporter activity [GO:0000295]; adenine transmembrane transporter activity [GO:0015207]; ATP:ADP antiporter activity [GO:0005471]; oxidative phosphorylation uncoupler activity [GO:0017077]; proton transmembrane transporter activity [GO:0015078]; RNA binding [GO:0003723]; ubiquitin pr... | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: Trimethylated by ANTKMT at Lys-52. {ECO:0000269|PubMed:31213526}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:27641616}; Multi-pass membrane protein {ECO:0000255}. Note=May localize to non-mitochondrial membranes. {ECO:0000269|PubMed:27641616}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P51881}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P51881}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-... | Homo sapiens (Human) |
P05150 | OTC_YEAST | MSTTASTPSSLRHLISIKDLSDEEFRILVQRAQHFKNVFKANKTNDFQSNHLKLLGRTIALIFTKRSTRTRISTEGAATFFGAQPMFLGKEDIQLGVNESFYDTTKVVSSMVSCIFARVNKHEDILAFCKDSSVPIINSLCDKFHPLQAICDLLTIIENFNISLDEVNKGINSKLKMAWIGDANNVINDMCIACLKFGISVSISTPPGIEMDSDIVDEAKKVAERNGATFELTHDSLKASTNANILVTDTFVSMGEEFAKQAKLKQFKGFQINQELVSVADPNYKFMHCLPRHQEEVSDDVFYGEHSIVFEEAENRLYAA... | 2.1.3.3 | null | arginine biosynthetic process [GO:0006526]; arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; ornithine carbamoyltransferase inhibitor complex [GO:1903269] | amino acid binding [GO:0016597]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, OTCase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05153 | PCKGC_CHICK | MAPELKTEVNIISKVIQGDLESLPPQVREFIESNAKLCQPESIHICDGSEEENKKILDIMVEQGMIKKLSKYENCWLALTNPRDVARIESKTVIITQEQRDTIPIPKTGSSQLGRWMSEEDFEKAFNTRFPGCMQGRTMYVIPFSMGPIGSPLAKIGIELTDSPYVVASMRMMTRMGTAALKALGNGEFVKCLHSVGCPLPLKEPLINNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASRIAKEEGWLAEHMLILGITNPEGEKKYFAAAFPSACGKTNLAMMNPSRPGWKIECVGDDIAWMKFDEL... | 2.7.11.-; 4.1.1.32 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P35558}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P35558}; | adult feeding behavior [GO:0008343]; alanine metabolic process [GO:0006522]; aspartate metabolic process [GO:0006531]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to ethanol [GO:0071361]; cellular response to fructose stimulus [GO:0071332]; cellula... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | epinephrine binding [GO:0051379]; GTP binding [GO:0005525]; manganese ion binding [GO:0030145]; nucleoside diphosphate kinase activity [GO:0004550]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; protein serine kinase activity (using GTP as donor) [GO:0106264] | PF00821;PF17297; | 3.90.228.20;3.40.449.10;2.170.8.10; | Phosphoenolpyruvate carboxykinase [GTP] family | PTM: Phosphorylation at Ser-90 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity. {ECO:0000250|UniProtKB:P35558}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35558}. | CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000250|UniProtKB:P35558}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Eviden... | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000250|UniProtKB:P35558}. | null | null | FUNCTION: Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces g... | Gallus gallus (Chicken) |
P05154 | IPSP_HUMAN | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPS... | null | null | fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; lipid transport [GO:0006869]; negative regulation of hydrolase activity [GO:0051346]; spermatogenesis [GO:0007283] | acrosomal membrane [GO:0002080]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; platelet alpha granule [GO:0031091]; platelet dense tubular network [GO:0031094]; protein C inhibitor-coagulatio... | acrosin binding [GO:0032190]; glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; phosphatidylcholine binding [GO:0031210]; protease binding [GO:0002020]; retinoic acid binding [GO:0001972]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: N- and O-glycosylated. N-glycosylation consists of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated with core 1 or possibly core 8 glycans. Further mod... | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}. Note=Localized on the plasma membrane overlying the acrosomal head of spermatozoa of ependymal sp... | null | null | null | null | null | FUNCTION: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a pr... | Homo sapiens (Human) |
P05155 | IC1_HUMAN | MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVI... | null | null | blood circulation [GO:0008015]; blood coagulation [GO:0007596]; complement activation, classical pathway [GO:0006958]; fibrinolysis [GO:0042730]; innate immune response [GO:0045087]; negative regulation of complement activation, lectin pathway [GO:0001869] | blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: Highly glycosylated (49%) with N- and O-glycosylation. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|Pub... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and t... | Homo sapiens (Human) |
P05156 | CFAI_HUMAN | MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKS... | 3.4.21.45 | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF21286;PF21287;PF00057;PF00530;PF00089; | 3.30.60.30;4.10.400.10;3.10.250.10;2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. Secreted {ECO:0000269|PubMed:6327681}. | CATALYTIC ACTIVITY: Reaction=Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.; EC=3.4.21.45; | null | null | null | null | FUNCTION: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins (PubMed:17320177, Pu... | Homo sapiens (Human) |
P05160 | F13B_HUMAN | MRLKNLTFIIILIISGELYAEEKPCGFPHVENGRIAQYYYTFKSFYFPMSIDKKLSFFCLAGYTTESGRQEEQTTCTTEGWSPEPRCFKKCTKPDLSNGYISDVKLLYKIQENMRYGCASGYKTTGGKDEEVVQCLSDGWSSQPTCRKEHETCLAPELYNGNYSTTQKTFKVKDKVQYECATGYYTAGGKKTEEVECLTYGWSLTPKCTKLKCSSLRLIENGYFHPVKQTYEEGDVVQFFCHENYYLSGSDLIQCYNFGWYPESPVCEGRRNRCPPPPLPINSKIQTHSTTYRHGEIVHIECELNFEIHGSAEIRCEDGK... | null | null | blood coagulation [GO:0007596]; blood coagulation, fibrin clot formation [GO:0072378] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; transferase complex [GO:1990234] | null | PF00084; | 2.10.70.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26247044, ECO:0000269|PubMed:4405643}. | null | null | null | null | null | FUNCTION: The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin. {ECO:0000303|PubMed:21742792, ECO:0000303|PubMed:3021194}. | Homo sapiens (Human) |
P05161 | ISG15_HUMAN | MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS | null | null | defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; ISG15-protein conjugation [GO:0032020]; modification-dependent protein catabolic process [GO:0019941]; negative regulation of protein ubiquitination ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654] | integrin binding [GO:0005178]; polyubiquitin modification-dependent protein binding [GO:0031593]; protein tag activity [GO:0031386]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | null | PTM: S-nitrosylation decreases its dimerization, thereby increasing the availability as well as the solubility of monomeric ISG15 for its conjugation to cellular proteins. {ECO:0000269|PubMed:18606809}.; PTM: Induced as an inactive, precursor protein that is cleaved by specific proteases to expose the C-terminal diglyc... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22859821}. Secreted {ECO:0000269|PubMed:22859821}. Note=Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein (PubMed:27564865). ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzyme... | Homo sapiens (Human) |
P05162 | LEG2_HUMAN | MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE | null | null | cell-cell adhesion [GO:0098609]; positive regulation of apoptotic process [GO:0043065]; positive regulation of inflammatory response [GO:0050729]; T cell homeostasis [GO:0043029] | galectin complex [GO:1990724] | carbohydrate binding [GO:0030246]; galactoside binding [GO:0016936] | PF00337; | 2.60.120.200; | null | null | null | null | null | null | null | null | FUNCTION: This protein binds beta-galactoside. Its physiological function is not yet known. | Homo sapiens (Human) |
P05164 | PERM_HUMAN | MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACP... | 1.11.2.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per monomer.; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.; | defense response [GO:0006952]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; hydrogen peroxide catabolic process [GO:0042744]; hypochlorous acid biosynthetic process [GO:0002149]; low-density lipoprotein particle remodeling [GO:0034374]; negative regulation of apoptotic process [G... | azurophil granule [GO:0042582]; azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; phagocytic vesicle ... | chromatin binding [GO:0003682]; heme binding [GO:0020037]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=chloride + H(+) + H2O2 = H2O + hypochlorous acid; Xref=Rhea:RHEA:28218, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17996, ChEBI:CHEBI:24757; EC=1.11.2.2; Evidence={ECO:0000269|PubMed:9922160}; | null | null | null | null | FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that gre... | Homo sapiens (Human) |
P05165 | PCCA_HUMAN | MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQA... | 6.4.1.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:5758... | branched-chain amino acid metabolic process [GO:0009081]; fatty acid metabolic process [GO:0006631]; short-chain fatty acid catabolic process [GO:0019626] | catalytic complex [GO:1902494]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; biotin binding [GO:0009374]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]; propionyl-CoA carboxylase activity [GO:0004658]; urea carboxylase activity [GO:0004847] | PF02785;PF00289;PF00364;PF02786;PF18140; | 2.40.50.100;3.30.700.30;3.40.50.20;3.30.1490.20;3.30.470.20; | null | PTM: Acetylated. {ECO:0000250|UniProtKB:Q91ZA3}.; PTM: The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity (PubMed:10329019). Biotinylation is catalyzed by HLCS (PubMed:20443544, PubMed:7753853). {ECO:0000269|PubMed:10329019, ECO:0000269|PubMed... | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10101253, ECO:0000269|PubMed:16023992}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3; Evidence={ECO:0000269|PubMed:6765... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.08 mM for ATP {ECO:0000269|PubMed:6765947}; KM=3 mM for hydrogencarbonate {ECO:0000269|PubMed:6765947}; | PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000269|PubMed:6765947, ECO:0000269|PubMed:8434582}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-8.8 for the propionyl-CoA carboxylase activity measured for the holoenzyme. {ECO:0000269|PubMed:6765947}; | null | FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:6765947, PubMed:8434582). Propionyl-CoA carb... | Homo sapiens (Human) |
P05166 | PCCB_HUMAN | MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDII... | 6.4.1.3 | null | branched-chain amino acid metabolic process [GO:0009081]; fatty acid metabolic process [GO:0006631]; short-chain fatty acid catabolic process [GO:0019626] | catalytic complex [GO:1902494]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; propionyl-CoA carboxylase activity [GO:0004658] | PF01039; | null | AccD/PCCB family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:16023992}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3; Evidence={ECO:0000269|PubMed:1589... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for propanoyl-CoA {ECO:0000269|PubMed:6765947}; KM=0.41 mM for propanoyl-CoA (at 37 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:15890657}; | PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000269|PubMed:15890657, ECO:0000269|PubMed:6765947}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-8.8 for the propionyl-CoA carboxylase activity as measured for the holoenzyme. {ECO:0000269|PubMed:6765947}; | null | FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:15890657, PubMed:6765947). Propionyl-CoA car... | Homo sapiens (Human) |
P05176 | CP1A1_RABIT | MVSDFGLPTFISATELLLASAVFCLVFWVAGASKPRVPKGLKRLPGPWGWPLLGHVLTLGKNPHVALARLSRRYGDVFQIRLGSTPVVVLSGLDTIKQALVRQGDDFKGRPDLYSFSFVTKGQSMIFGSDSGPVWAARRRLAQNALNSFSVASDPASSSSCYLEEHVSQEAENLISKFQELMAAVGHFDPYRYVVMSVANVICAMCFGRRYDHDDQELLSLVNLNDEFGKVAASGSPADFFLILRYLPNPALDTFKDLNERFYSFTQERVKEHCRSFEKGHIRDITDSLIKHYRVDRLDENANVQVSDEKTVGIVLDLFG... | 1.14.14.1; 4.2.1.152 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | amine metabolic process [GO:0009308]; cellular response to organic cyclic compound [GO:0071407]; estrogen metabolic process [GO:0008210]; heterocycle metabolic process [GO:0046483]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide biosynthetic process [GO:0050665]; lipid hydroxylation [GO:0002933]; long-cha... | endoplasmic reticulum membrane [GO:0005789]; mitochondrial inner membrane [GO:0005743] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 prot... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Microsome membrane {ECO:0000250|UniProtKB:P00185}; Per... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P04798}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:P04798}.; PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P04798}. | null | null | 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 NA... | Oryctolagus cuniculus (Rabbit) |
P05177 | CP1A2_HUMAN | MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFD... | 1.14.14.1; 4.2.1.152 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | aflatoxin metabolic process [GO:0046222]; alkaloid metabolic process [GO:0009820]; cellular respiration [GO:0045333]; cellular response to cadmium ion [GO:0071276]; cholesterol metabolic process [GO:0008203]; dibenzo-p-dioxin metabolic process [GO:0018894]; epoxygenase P450 pathway [GO:0019373]; estrogen metabolic proc... | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; demethylase activity [GO:0032451]; electron transfer activity [GO:0009055]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for 17beta-estradiol (2-hydroxylation) {ECO:0000269|PubMed:11555828}; KM=9 uM for all-trans retinol {ECO:0000269|PubMed:10681376}; KM=4 uM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole {ECO:0000269|PubMed:14725854}; KM=21 uM for 2-amino-3-methylimidazo... | PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:10681376}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:21576599}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:21068195, ECO:0000269|PubMed:9435160}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:19965576, PubMed:9435160). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substr... | Homo sapiens (Human) |
P05178 | CP2C6_RAT | MDLVMLLVLTLTCLILLSIWRQSSGRGKLPPGPIPLPIIGNIFQLNVKNITQSLTSFSKVYGPVFTLYFGTKPTVILHGYEAVKEALIDHGEEFAERGSFPVAEKINKDLGIVFSHGNRWKEIRRFTLTTLRNLGMGKRNIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENMKILSSPWTQFCSFFPVLIDYCPGSHTTLAKNVYHIRNYLLKKIKEHQESLDVTNPRDFIDYYLIKWKQENHNPHSEFTLENLSITVTDLFGAGTETTSTTLRYALLLLLKCPEVT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; epoxygenase P450 pathway [GO:0019373]; heterocycle metabolic process [GO:0046483]; long-chain fatty acid metabolic process [GO:0001676]; monoterpenoid metabolic process [GO:0016098]; response to xenobiotic stimulus [GO:0009410]; steroid metabolic process [GO:0008202]; xe... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid 11,12-epoxygenase activity [GO:0008405]; arachidonic acid 14,15-epoxygenase activity [GO:0008404]; arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-1 hy... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P05179 | CP2C7_RAT | MDLVTFLVLTLSSLILLSLWRQSSRRRKLPPGPTPLPIIGNFLQIDVKNISQSLTKFSKTYGPVFTLYLGSQPTVILHGYEAIKEALIDNGEKFSGRGSYPMNENVTKGFGIVFSNGNRWKEMRRFTIMNFRNLGIGKRNIEDRVQEEAQCLVEELRKTKGSPCDPSLILNCAPCNVICSITFQNHFDYKDKEMLTFMEKVNENLKIMSSPWMQVCNSFPSLIDYFPGTHHKIAKNINYMKSYLLKKIEEHQESLDVTNPRDFVDYYLIKQKQANNIEQSEYSHENLTCSIMDLIGAGTETMSTTLRYALLLLMKYPHVT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; response to ethanol [GO:0045471]; response to lipopolysaccharide [GO:0032496]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to organonitrogen compound [GO:0010243]; response to peptide hormone [GO:0043434]; response to retinoic acid... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P05180 | CP2H1_CHICK | MDFLGLPTILLLVCISCLLIAAWRSTSQRGKEPPGPTPIPIIGNVFQLNPWDLMGSFKELSKKYGPIFTIHLGPKKIVVLYGYDIVKEALIDNGEAFSGRGILPLIEKLFKGTGIVTSNGETWRQLRRFALTTLRDFGMGKKGIEERIQEEAHFLVERIRKTHEEPFNPGKFLIHAVANIICSIVFGDRFDYEDKKFLDLIEMLEENNKYQNRIQTLLYNFFPTILDSLPGPHKTLIKNTETVDDFIKEIVIAHQESFDASCPRDFIDAFINKMEQEKENSYFTVESLTRTTLDLFLAGTGTTSTTLRYGLLILLKHPEI... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; response to xenobiotic stimulus [GO:0009410]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Gallus gallus (Chicken) |
P05181 | CP2E1_HUMAN | MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPE... | 1.14.13.n7; 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | 4-nitrophenol metabolic process [GO:0018960]; benzene metabolic process [GO:0018910]; carbon tetrachloride metabolic process [GO:0018885]; epoxygenase P450 pathway [GO:0019373]; halogenated hydrocarbon metabolic process [GO:0042197]; heterocycle metabolic process [GO:0046483]; lipid hydroxylation [GO:0002933]; long-cha... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743] | 4-nitrophenol 2-monooxygenase activity [GO:0018601]; arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; long-chain fatty acid o... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | 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}; Per... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:10553002, ECO:0000269|PubMed:18577768}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids (PubMed:10553002, PubMed:18577768). 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 (NA... | Homo sapiens (Human) |
P05182 | CP2E1_RAT | MAVLGITIALLVWVATLLVISIWKQIYNSWNLPPGPFPLPILGNIFQLDLKDIPKSFTKLAKRFGPVFTLHLGSRRIVVLHGYKAVKEVLLNHKNEFSGRGDIPVFQEYKNKGIIFNNGPTWKDVRRFSLSILRDWGMGKQGNEARIQREAQFLVEELKKTKGQPFDPTFLIGCAPCNVIADILFNKRFDYNDKKCLRLMSLFNENFYLLSTPWIQLYNNFADYLRYLPGSHRKIMKNVSEIKQYTLEKAKEHLQSLDINCARDVTDCLLIEMEKEKHSQEPMYTMENVSVTLADLFFAGTETTSTTLRYGLLILMKYPE... | 1.14.13.n7; 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | 4-nitrophenol metabolic process [GO:0018960]; epoxygenase P450 pathway [GO:0019373]; heterocycle metabolic process [GO:0046483]; lipid hydroxylation [GO:0002933]; long-chain fatty acid metabolic process [GO:0001676]; monoterpenoid metabolic process [GO:0016098]; response to 3-methylcholanthrene [GO:1904681]; response t... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743] | 4-nitrophenol 2-monooxygenase activity [GO:0018601]; arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; long-chain fatty acid o... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:19401463}; Peripheral membrane protein. Microsome membrane {ECO:0000305|PubMed:19401463}; Peripheral membrane protein. Mitochondrion inner membrane {ECO:0000305|PubMed:19401463}; Peripheral membrane protein {ECO:0000305|PubMed:19401463}. Note=Post... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:P05181}. | null | null | 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). Cataly... | Rattus norvegicus (Rat) |
P05183 | CP3A2_RAT | MDLLSALTLETWVLLAVILVLLYRLGTHRHGIFKKQGIPGPKPLPFLGTVLNYYKGLGRFDMECYKKYGKIWGLFDGQTPVFAIMDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIAFFQKFVHRIKETRLDSKHKHRVDFLQLMLNAHNNSKDEVSHKALSDVEIIAQSVIFIFAGYETTSSTLSFVLY... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | alkaloid catabolic process [GO:0009822]; estrogen metabolic process [GO:0008210]; heterocycle metabolic process [GO:0046483]; lipid hydroxylation [GO:0002933]; monoterpenoid metabolic process [GO:0016098]; oxidative demethylation [GO:0070989]; retinoic acid metabolic process [GO:0042573]; retinol metabolic process [GO:... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789] | 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity [GO:0062181]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [G... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P05185 | CP17A_BOVIN | MWLLLAVFLLTLAYLFWPKTKHSGAKYPRSLPSLPLVGSLPFLPRRGQQHKNFFKLQEKYGPIYSFRLGSKTTVMIGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLALNAFALFKDGNLKLEKIINQEANVLCDFLATQHGEAIDLSEPLSLAVTNIISFICFNFSFKNEDPALKAIQNVNDGILEVLSKEVLLDIFPVLKIFPSKAMEKMKGCVQTRNELLNEILEKCQENFSSDSITNLLHILIQAKVNADNNNAGPDQDSKLLSNRHMLATIGDIFGAGVETTTSVIKWIVAYLLH... | 1.14.14.19; 1.14.14.32 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P05093}; | glucocorticoid biosynthetic process [GO:0006704]; hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; steroid metabolic process [GO:0008202] | endoplasmic reticulum membrane [GO:0005789] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05093}. Microsome membrane {ECO:0000250|UniProtKB:P05093}. | CATALYTIC ACTIVITY: Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, C... | null | PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P05093}.; PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000250|UniProtKB:P05093}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of ... | Bos taurus (Bovine) |
P05186 | PPBT_HUMAN | MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQIL... | 3.1.3.1; 3.9.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05187}; Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:25775211}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:25775211}; COFACTOR: Name=Ca(2+); Xref=ChE... | bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cellular homeostasis [GO:0019725]; cellular response to organic cyclic compound [GO:0071407]; cementum mineralization [GO:0071529]; dephosphorylation [GO:0016311]; developmental process involved in reproduction [GO:0003006]; endochondral ossificati... | extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | ADP phosphatase activity [GO:0043262]; alkaline phosphatase activity [GO:0004035]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; inorganic diphosphate phosphatase activity [GO:0004427]; phosphoamidase activity [GO:0050187]; phosphoethanolamine phosphatase activity [GO:0052732]; pyridoxal phosp... | PF00245; | 3.40.720.10; | Alkaline phosphatase family | PTM: N-glycosylated. {ECO:0000269|PubMed:1458595, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2220817, ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064, ECO:0000269|PubMed:33821301}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064}. Extracellular vesicle membrane {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-a... | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:12162492, ECO:0000269|PubMed:2220817, ECO:0000269|PubMed:230... | null | null | null | null | FUNCTION: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed:12162492, PubMed:23688511, PubMed:25982064). Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrate... | Homo sapiens (Human) |
P05187 | PPB1_HUMAN | MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRL... | 3.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11124260, ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919, ECO:0000269|PubMed:20693656}; Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:11124260, ECO:0000269|PubMed:15946677, ECO:0000269|PubMed:16815919, ECO:0000269|PubMed:20693656}; COF... | dephosphorylation [GO:0016311] | cell surface [GO:0009986]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | alkaline phosphatase activity [GO:0004035]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270] | PF00245; | 3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1730777, ECO:0000269|PubMed:2153284}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:1939159, ECO:0000269|PubMed:25775211}; PhysiologicalDirectio... | null | null | null | null | FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. {ECO:0000269|PubMed:1939159, ECO:0000269|PubMed:25775211}. | Homo sapiens (Human) |
P05189 | IPNA_HAPCH | MGSVPVPVANVPRIDVSPLFGDDKEKKLEVARAIDAASRDTGFFYAVNHGVDLPWLSRETNKFHMSITDEEKWQLAIRAYNKEHESQIRAGYYLPIPGKKAVESFCYLNPSFSPDHPRIKEPTPMHEVNVWPDEAKHPGFRAFAEKYYWDVFGLSSAVLRGYALALGRDEDFFTRHSRRDTTLSSVVLIRYPYLDPYPEPAIKTADDGTKLSFEWHEDVSLITVLYQSDVQNLQVKTPQGWQDIQADDTGFLINCGSYMAHITDDYYPAPIHRVKWVNEERQSLPFFVNLGWEDTIQPWDPATAKDGAKDAAKDKPAISY... | 1.21.3.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:3839755}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | penicillin biosynthetic process [GO:0042318] | cytosol [GO:0005829] | iron ion binding [GO:0005506]; isopenicillin-N synthase activity [GO:0016216] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08703}. | CATALYTIC ACTIVITY: Reaction=N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = 2 H2O + isopenicillin N; Xref=Rhea:RHEA:22428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:58399, ChEBI:CHEBI:58572; EC=1.21.3.1; Evidence={ECO:0000269|PubMed:3839755, ECO:0000269|PubMed:3903520, ECO:0000269|PubMed:807679... | null | PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3. {ECO:0000269|PubMed:3903520}. | null | null | FUNCTION: Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:3903520). IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that... | Hapsidospora chrysogena (Acremonium chrysogenum) |
P05193 | AMPC_CITFR | MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVE... | 3.5.2.6 | null | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | outer membrane-bounded periplasmic space [GO:0030288] | beta-lactamase activity [GO:0008800] | PF00144; | 3.40.710.10; | Class-C beta-lactamase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10102}; | null | null | null | null | FUNCTION: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | Citrobacter freundii |
P05194 | AROD_ECOLI | MKTVTVKDLVIGTGAPKIIVSLMAKDIASVKSEALAYREADFDILEWRVDHYADLSNVESVMAAAKILRETMPEKPLLFTFRSAKEGGEQAISTEAYIALNRAAIDSGLVDMIDLELFTGDDQVKETVAYAHAHDVKVVMSNHDFHKTPEAEEIIARLRKMQSFDADIPKIALMPQSTSDVLTLLAATLEMQEQYADRPIITMSMAKTGVISRLAGEVFGSAATFGAVKKASAPGQISVNDLRTVLTILHQA | 4.2.1.10 | null | 3,4-dihydroxybenzoate biosynthetic process [GO:0046279]; amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | cytosol [GO:0005829] | 3-dehydroquinate dehydratase activity [GO:0003855]; protein homodimerization activity [GO:0042803] | PF01487; | 3.20.20.70; | Type-I 3-dehydroquinase family | null | null | CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:2950851, ECO:0000269|PubMed:7592767}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:7592767}; KM=18 uM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:2950851}; Note=kcat is 142 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7 a... | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}. | null | null | FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine ... | Escherichia coli (strain K12) |
P05197 | EF2_RAT | MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLD... | 3.6.5.- | null | cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; glial cell proliferation [GO:0014009]; hematopoietic progenitor cell differentiation [GO:0002244]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of translation [GO:0045727]; response to endoplasmic reticulum... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]; synapse [GO:0045202] | 5S rRNA binding [GO:0008097]; actin filament binding [GO:0051015]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; p53 binding [GO:0002039]; protein kinase binding [GO:0019901]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF00679;PF14492;PF03764;PF00009;PF03144; | 3.30.230.10;3.30.70.240;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-G/EF-2 subfamily | PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. {ECO:0000269|PubMed:4368673}.; PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000250|UniProtKB:P13639}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P13639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P1363... | null | null | null | null | FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... | Rattus norvegicus (Rat) |
P05198 | IF2A_HUMAN | MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED | null | null | cellular response to amino acid starvation [GO:0034198]; cellular response to heat [GO:0034605]; cellular response to oxidative stress [GO:0034599]; cellular response to UV [GO:0034644]; negative regulation of translational initiation in response to stress [GO:0032057]; PERK-mediated unfolded protein response [GO:00364... | cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 2 complex [GO:0005850]; extracellular exosome [GO:0070062]; glial limiting end-foot [GO:0097451]; membrane [GO:0016020]; nucleus [GO:0005634]; synapse [GO:0045202]; ... | ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF07541;PF00575; | 3.30.70.1130;2.40.50.140; | EIF-2-alpha family | PTM: Phosphorylation at Ser-49 and Ser-52 stabilizes the eIF-2/GDP/eIF2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF2 between successive rounds of initiation and leading to global inhibition of translation, while concomitantly initiating the preferential translation of integrated... | SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q6ZWX6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56286}. Note=Colocalizes with NANOS3 in the stress granules. {ECO:0000250|UniProtKB:Q6ZWX6}. | null | null | null | null | null | FUNCTION: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:16289705). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC) (PubMed:16289705). Junction of th... | Homo sapiens (Human) |
P05200 | NGF_CHICK | MHSVMSMLYYTLIIAFLIGTQAAPKSEDNGPLEYPAEHSLPSTQQSNGQHIAKAAPQTTHGRFAWMPDGTEDLNIAMDQNFFKKKRFRSSRVLFSTQPPPVSRKGQSTGFLSSAVSLNRTARTKRTAHPVLHRGEFSVCDSVSMWVGDKTTATDIKGKEVTVLGEVNINNNVFKQYFFETKCRDPRPVSSGCRGIDAKHWNSYCTTTHTFVKALTMEGKQAAWRFIRIDTACVCVLSRKSGRP | null | null | memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:000742... | axon [GO:0030424]; dendrite [GO:0030425]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021] | growth factor activity [GO:0008083]; nerve growth factor receptor binding [GO:0005163] | PF00243; | 2.10.90.10; | NGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survi... | Gallus gallus (Chicken) |
P05201 | AATC_MOUSE | MAPPSVFAQVPQAPPVLVFKLTADFRDDPDPRKVNLGVGAYRTDESQPWVLPVVRKVEQKIANDNSLNHEYLPILGLAEFRSCASRLVLGDNSLAIRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPIYVSSPTWENHNAVFSAAGFKDIRPYCYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIAAVMQRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKESDSVLRVLSQMEKIVRITWSNPPAQGARIVAATLSDPELFKEW... | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; cellular response to insulin stimulus [GO:0032869]; cellular response to mechanical stimulus [GO:0071260]; dicarboxylic acid metabolic process [... | axon terminus [GO:0043679]; cytosol [GO:0005829] | carboxylic acid binding [GO:0031406]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P13221}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825; Evidence={ECO:0000250... | null | null | null | null | FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic gluc... | Mus musculus (Mouse) |
P05202 | AATM_MOUSE | MALLHSSRILSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPP... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20977429}; | 2-oxoglutarate metabolic process [GO:0006103]; amino acid metabolic process [GO:0006520]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; dicarboxylic acid metabolic process [GO:0043648]; fatty acid transport [GO:0015908]; glutamate catabo... | cell surface [GO:0009986]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; perikaryon [GO:0043204]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; T-tubule [GO:0030315] | amino acid binding [GO:0016597]; carboxylic acid binding [GO:0031406]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [... | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | PTM: Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice. | SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000269|PubMed:7878064}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Mus musculus (Mouse) |
P05204 | HMGN2_HUMAN | MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; chromatin organization [GO:0006325]; killing of cells of another organism [GO:0031640] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723] | PF01101; | null | HMGN family | PTM: Phosphorylation favors cytoplasmic localization. {ECO:0000269|PubMed:10739259}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10739259}. Cytoplasm {ECO:0000269|PubMed:10739259}. Note=Cytoplasmic enrichment upon phosphorylation. | null | null | null | null | null | FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
P05205 | HP1_DROME | MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED | null | null | chromatin organization [GO:0006325]; chromosome organization [GO:0051276]; heterochromatin formation [GO:0031507]; mitotic cell cycle [GO:0000278]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase... | chromocenter [GO:0010369]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; chromosome, telomeric region [GO:0000781]; condensed chromosome [GO:0000793]; condensed chromosome, centromeric region [GO:0000779]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus ... | chromatin binding [GO:0003682]; histone binding [GO:0042393]; Hsp70 protein binding [GO:0030544]; methylated histone binding [GO:0035064]; mRNA binding [GO:0003729]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; rDNA binding [GO:0000182]; RNA binding [GO:0003723];... | PF00385;PF01393; | 2.40.50.40; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:26389589, ECO:0000269|PubMed:9378752}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9378752}. Chromosome {ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:1787... | null | null | null | null | null | FUNCTION: Structural component of heterochromatin, involved in gene repression and the modification of position-effect-variegation. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Stabilizes chromatin-associated RNAs probably by binding to them and thereby preventing their... | Drosophila melanogaster (Fruit fly) |
P05207 | KAP2_PIG | SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY | null | null | negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; positive regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904146]; regulation of meiotic cell cycle process involved in oocyte maturation [GO:1903538] | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; germinal vesicle [GO:0042585]; plasma membrane [GO:0005886] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; protein kinase A catalytic subunit binding [GO:0034236] | null | 2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by the activated catalytic chain. {ECO:0000269|PubMed:225318}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. | Sus scrofa (Pig) |
P05208 | CEL2A_MOUSE | MIRTLLLSALVAGALSCGYPTYEVEDDVSRVVGGQEATPNTWPWQVSLQVLSSGRWRHNCGGSLVANNWVLTAAHCLSNYQTYRVLLGAHSLSNPGAGSAAVQVSKLVVHQRWNSQNVGNGYDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATCSSASWWGSSVKSSMVCAGGDGVTSSCNGDSGGPLNCRASNGQWQVHGIVSFGSSLGCNYPRKPSVFTRVSNYIDWINSVMARN | 3.4.21.71 | null | insulin catabolic process [GO:1901143]; proteolysis [GO:0006508]; regulation of insulin secretion [GO:0050796]; regulation of platelet aggregation [GO:0090330]; response to insulin [GO:0032868] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; keratohyalin granule [GO:0036457] | endopeptidase activity [GO:0004175]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31358993}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.; EC=3.4.21.71; Evidence={ECO:0000305|PubMed:31358993}; | null | null | null | null | FUNCTION: Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity. {ECO:0000269|PubMed:31358993}. | Mus musculus (Mouse) |
P05213 | TBA1B_MOUSE | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | cellular response to interleukin-4 [GO:0071353]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; membrane raft [GO:0045121]; microtubule [GO:0005874]; myelin sheath [GO:0043209] | double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]; ubiquitin protein ligase binding [GO:0031625] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Mus musculus (Mouse) |
P05214 | TBA3_MOUSE | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | male germ-line stem cell population maintenance [GO:0036098]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Mus musculus (Mouse) |
P05219 | TBB_SCHPO | MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYVPRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVVRREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVVEPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSFRFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMMVAADPRHGRYLTVAALFRGK... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | cytoplasmic microtubule organization [GO:0031122]; intracellular distribution of mitochondria [GO:0048312]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic spindle elongation [GO:0000022]; mitotic spindle pole body duplication [GO:1903087]; nuclear migration by microtubule m... | astral microtubule [GO:0000235]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle microtubule [GO:0005876] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P05221 | NUPL_XENLA | MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK | null | null | chromatin remodeling [GO:0006338]; positive regulation of DNA replication [GO:0045740]; sperm DNA decondensation [GO:0035041] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | histone binding [GO:0042393]; histone chaperone activity [GO:0140713]; importin-alpha family protein binding [GO:0061676]; nucleosome binding [GO:0031491]; RNA binding [GO:0003723] | PF03066; | 2.60.120.340; | Nucleoplasmin family | PTM: Activated by phosphorylation of multiple serine/threonine residues, along both core and tail domains. The level of phosphorylation gradually increases during egg maturation, reaching an average of 7-10 phosphates per monomer, so that at the time of fertilization the activity of the protein is maximum. {ECO:0000269... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable.; | FUNCTION: Acts as a chaperone for histones, such as histone H2A-H2B, and thus regulates the assembly of nucleosome cores (PubMed:11684019, PubMed:19055325). Involved in chromatin remodeling, especially during fertilization and early embryonic development (By similarity). May be involved in sperm chromatin decondensatio... | Xenopus laevis (African clawed frog) |
P05230 | FGF1_HUMAN | MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD | null | null | activation of protein kinase B activity [GO:0032148]; anatomical structure morphogenesis [GO:0009653]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; branch elongation involved in ureteric bud branching [GO:0060681]; cell differentiation [GO:0030154]; cellular response to heat [GO:0034605]; epithel... | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; Hsp70 protein binding [GO:0030544]; integrin binding [GO:0005178]; S100 protein binding [GO:0044548] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: In the nucleus, phosphorylated by PKC/PRKCD. {ECO:0000269|PubMed:22321063}. | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1 (By sim... | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequent... | Homo sapiens (Human) |
P05231 | IL6_HUMAN | MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM | null | null | acute-phase response [GO:0006953]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-posi... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; interleukin-6 receptor complex [GO:0005896] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-6 receptor binding [GO:0005138] | PF00489; | 1.20.1250.10; | IL-6 superfamily | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1883960}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11080265}. | null | null | null | null | null | FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulate... | Homo sapiens (Human) |
P05300 | LAMP1_CHICK | MGGAARAVLLGFLQASSSFDVRDSTGKVCIIANLTVAFSVEYKSSGQKQFAHFFLPQNATSQSHSSCGEGNTSHPILALSFGAGHLISLNFSKTLDKYQVEELTFHYNLSDETLFPNATEGKVMVATQKSVIQARIGTEYRCINSKYVRMKHVNITFSNVTLEAYPTNDTFSANKTECREDMVSTTTVAPTTPKHATSQVPTTSPAPTAAPSSPAVGKYNVTGANGTCVLASMGLQLNITYVKKDEKMGLDLLNFIPHNTSASGMCESTSAFLNLAFEKTKITFHFVLNASSEKFFLQGVNVSTTLPSEAKAPTFEASND... | null | null | establishment of protein localization to organelle [GO:0072594]; lysosomal lumen acidification [GO:0007042] | cytolytic granule membrane [GO:0101004]; endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ion channel inhibitor activity [GO:0008200] | PF01299;PF21222; | 2.40.160.110; | LAMP family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtK... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis. {ECO:0000250|UniProtKB:P11279}.; FUNCTION: (Microbial infection) Plays an essential role in efficient replication and spread of Marek's disease virus, by facili... | Gallus gallus (Chicken) |
P05305 | EDN1_HUMAN | MDYLLMIFSLLFVACQGAPETAVLGAELSAVGENGGEKPTPSPPWRLRRSKRCSCSSLMDKECVYFCHLDIIWVNTPEHVVPYGLGSPRSKRALENLLPTKATDRENRCQCASQKDKKCWNFCQAGKELRAEDIMEKDWNNHKKGKDCSKLGKKCIYQQLVRGRKIRRSSEEHLRQTRSETMRNSVKSSFHDPKLKGKPSRERYVTHNRAHW | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; artery smooth muscle contraction [GO:0014824]; axon extension [GO:0048675]; axonogenesis involved in innervation [GO:0060385]; body fluid secretion [GO:0007589]; branching involved in blood vessel morphogenesis [GO:0001569]; calcium... | basal part of cell [GO:0045178]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; rough endoplasmic reticulum lumen [GO:0048237]; transport vesicle [GO:0030133]; Weibel-Palade body [GO:0033093] | cytokine activity [GO:0005125]; endothelin A receptor binding [GO:0031707]; endothelin B receptor binding [GO:0031708]; hormone activity [GO:0005179] | PF00322; | null | Endothelin/sarafotoxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides (By similarity). Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells (PubMed:19086031). Also binds the DEAR/FBXW7-AS1 receptor (PubMed:1... | Homo sapiens (Human) |
P05307 | PDIA1_BOVIN | MLRRALLCLALTALFRAGAGAPDEEDHVLVLHKGNFDEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAASTLSDGAAAEALVESSEVAVIGFFKDMESDSAKQFFLAAEVIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLSNFKKAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLI... | 5.3.4.1 | null | peptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; melanosome [GO:0042470] | procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Phosphorylation of Ser-359 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone. It also promotes interaction with ERN1. {ECO:0000250|UniProtKB:P07237}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000250|UniProtKB:P09103}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to b... | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P07237}; | null | null | null | null | FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to for... | Bos taurus (Bovine) |
P05317 | RLA0_YEAST | MGGIREKKAEYFAKLREYLEEYKSLFVVGVDNVSSQQMHEVRKELRGRAVVLMGKNTMVRRAIRGFLSDLPDFEKLLPFVKGNVGFVFTNEPLTEIKNVIVSNRVAAPARAGAVAPEDIWVRAVNTGMEPGKTSFFQALGVPTKIARGTIEIVSDVKVVDAGNKVGQSEASLLNLLNISPFTFGLTVVQVYDNGQVFPSSILDITDEELVSHFVSAVSTIASISLAIGYPTLPSVGHTLINNYKDLLAVAIAASYHYPEIEDLVDRIENPEKYAAAAPAATSAASGDAAPAEEAAAEEEEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735] | PF00428;PF00466;PF17777; | 3.30.70.1730;3.90.105.20; | Universal ribosomal protein uL10 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05318 | RLA1_YEAST | MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; translational elongation [GO:0006414] | cytosolic large ribosomal subunit [GO:0022625] | protein kinase activator activity [GO:0030295]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of ribosome [GO:0003735] | PF00428; | 1.10.10.1410; | Eukaryotic ribosomal protein P1/P2 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:8476850}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05319 | RLA2_YEAST | MKYLAAYLLLNAAGNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAAEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; cytoplasmic translational elongation [GO:0002182] | cytosolic large ribosomal subunit [GO:0022625] | protein kinase activator activity [GO:0030295]; structural constituent of ribosome [GO:0003735] | PF00428; | 1.10.10.1410; | Eukaryotic ribosomal protein P1/P2 family | PTM: Phosphorylation is not involved in the interaction of the acidic P proteins with the ribosome, however it is suggested to affect the ribosome activity and to participate in a possible ribosome regulatory mechanism.; PTM: The N-terminus is not modified. {ECO:0000269|PubMed:8476850}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05326 | IPNA_EMENI | MGSVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQRLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESFCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLSSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTAADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINCGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPNGKSDREPLSYGDYLQNG... | 1.21.3.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:7791906, ECO:0000269|PubMed:9194566}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:7791906, ECO:00... | penicillin biosynthetic process [GO:0042318] | cytosol [GO:0005829] | iron ion binding [GO:0005506]; isopenicillin-N synthase activity [GO:0016216]; L-ascorbic acid binding [GO:0031418] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08703}. | CATALYTIC ACTIVITY: Reaction=N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = 2 H2O + isopenicillin N; Xref=Rhea:RHEA:22428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:58399, ChEBI:CHEBI:58572; EC=1.21.3.1; Evidence={ECO:0000269|PubMed:11755401, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:3319... | null | PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3. {ECO:0000269|PubMed:3319778}. | null | null | FUNCTION: Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:11755401, PubMed:3319778). IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenici... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
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