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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P08906 | AATC_HORSE | MTSPSIFVEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCQPWVLPVVRKVEQKIANNSSLNHEYLPILGLAEFRSCASRLALGDDSPALQEKRVGGVQSLGGTGALRIGAEFLSRWYNGTNNKNTPVYVSSPTWENHNGVFSGAGFKDIRSYHYWDATKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIASVMKRRFLFPFFDSAYQGFASGNLDRDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVAKEPDSILRVLSQMQKIVRITWSNPPAQGARIVAFTLSDPGLFKEW... | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | aspartate biosynthetic process [GO:0006532]; glycerol biosynthetic process [GO:0006114] | cytosol [GO:0005829] | L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; 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... | Equus caballus (Horse) |
P08907 | AATM_HORSE | SSWWAHVEMGPPDPILGVTEAYKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEALKSGRYVTVQSISGTGALRIGANFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGLQLHAYRYYDPKTCGFDVTGALEDISKIPQQSIILLHACAHNPTGVDPRPEQWKEIATLVKKNNLFAFFDMAYQGFASGDGNKDAWAVRYFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPLYSNPPLNGARIASTILTSPDLRKQWLQEVKGMAD... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lipid transport [GO:0006869] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | 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 [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000250}. | 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... | Equus caballus (Horse) |
P08908 | 5HT1A_HUMAN | MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCAVLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAALISLTWLIGFLISIPPMLGWRTPEDRSDPDACTISKDHGYTIYSTFGAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPKKSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNSKEHLPLPSEAGPTPCAPAS... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting serotonin receptor signaling pathway [GO:0007198]; behavioral fear response [GO:0001662]; chemical synaptic transmission [GO:0007268]; exploration behavior [GO:0035640]; G protein-coupled receptor signaling pat... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; synapse [GO:0045202] | dopamine neurotransmitter receptor activity, coupled via Gs [GO:0001588]; G protein-coupled serotonin receptor activity [GO:0004993]; neurotransmitter receptor activity [GO:0030594]; receptor-receptor interaction [GO:0090722]; serotonin binding [GO:0051378] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, 5-hydroxytryptamine receptor subfamily, HTR1A sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:26365466, ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}; Multi-pass membrane protein {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041... | null | null | null | null | null | FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effecto... | Homo sapiens (Human) |
P08909 | 5HT2C_RAT | MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFF... | null | null | animal organ regeneration [GO:0031100]; behavioral fear response [GO:0001662]; behavioral response to nicotine [GO:0035095]; cGMP-mediated signaling [GO:0019934]; chemical synaptic transmission [GO:0007268]; feeding behavior [GO:0007631]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second... | cell surface [GO:0009986]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; G protein-coupled serotonin receptor complex [GO:0098666]; plasma membrane [GO:0005886]; synapse [GO:0045202] | 1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding [GO:0071886]; G protein-coupled serotonin receptor activity [GO:0004993]; Gq/11-coupled serotonin receptor activity [GO:0001587]; identical protein binding [GO:0042802]; neurotransmitter receptor activity [GO:0030594]; serotonin binding [GO:0051378] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3399891}; Multi-pass membrane protein {ECO:0000269|PubMed:3399891}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change... | Rattus norvegicus (Rat) |
P08910 | ABHD2_HUMAN | MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKKTYPLTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEY... | 3.1.1.23; 3.1.1.6; 3.1.1.79 | null | acrosome reaction [GO:0007340]; acylglycerol catabolic process [GO:0046464]; medium-chain fatty acid biosynthetic process [GO:0051792]; medium-chain fatty acid catabolic process [GO:0051793]; negative regulation of smooth muscle cell migration [GO:0014912]; response to progesterone [GO:0032570]; response to wounding [G... | acrosomal vesicle [GO:0001669]; sperm flagellum [GO:0036126]; sperm plasma membrane [GO:0097524] | acetylesterase activity [GO:0008126]; acylglycerol lipase activity [GO:0047372]; hormone binding [GO:0042562]; hormone-sensitive lipase activity [GO:0033878]; nuclear steroid receptor activity [GO:0003707]; triglyceride lipase activity [GO:0004806] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, AB hydrolase 4 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000305|PubMed:26989199}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:27247428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.4 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:27247428}; KM=11.76 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:27247428}; KM=17.66 mM for p-nitrophenyl palmitate {ECO:0000269|PubMed:27247428}; Vmax=2.69 umol/sec/mg enzyme toward p-nitrophenyl acetate {... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for p-nitrophenyl palmitate and 7.5 for p-nitrophenyl acetate and p-nitrophenyl butyrate. {ECO:0000269|PubMed:27247428}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with p-nitrophenyl palmitate and 30 degrees Celsius with p-nitrophenyl acetate and p-nitrophenyl butyrate. {ECO:0000269|PubMed:27247428}; | FUNCTION: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane (PubMed:26989199). Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-... | Homo sapiens (Human) |
P08911 | ACM5_RAT | MEGESYNESTVNGTPVNHQALERHGLWEVITIAVVTAVVSLMTIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTTYILMGRWVLGSLACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLVSFILWAPAILCWQYLVGKRTVPPDECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYRETEKRTKDLADLQGSDSVAEAKKREPAQRTLLRSFFSCPRPSLAQRERNQASWSSSRRSTSTTGKTTQATDLSADWEKAEQVTTCSSYPSSEDEAKPTTDPVF... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; dopamine transport [GO:0015872]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; gastric acid secretion [GO:0001696... | dendrite [GO:0030425]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM5 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Rattus norvegicus (Rat) |
P08912 | ACM5_HUMAN | MEGDSYHNATTVNGTPVNHQPLERHRLWEVITIAAVTAVVSLITIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTTYILMGRWALGSLACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLISFILWAPAILCWQYLVGKRTVPLDECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYRETEKRTKDLADLQGSDSVTKAEKRKPAHRALFRSCLRCPRPTLAQRERNQASWSSSRRSTSTTGKPSQATGPSANWAKAEQLTTCSSYPSSEDEDKPATDPV... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; dopamine transport [GO:0015872]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nuc... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993]; phosphatidylinositol phospholipase C activity [GO:0004435] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM5 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Homo sapiens (Human) |
P08913 | ADA2A_HUMAN | MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERP... | null | null | actin cytoskeleton organization [GO:0030036]; activation of protein kinase activity [GO:0032147]; activation of protein kinase B activity [GO:0032148]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189];... | axon terminus [GO:0043679]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; dopaminergic synapse [GO:0098691]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic act... | alpha-1B adrenergic receptor binding [GO:0031692]; alpha-2C adrenergic receptor binding [GO:0031696]; alpha2-adrenergic receptor activity [GO:0004938]; epinephrine binding [GO:0051379]; heterotrimeric G-protein binding [GO:0032795]; norepinephrine binding [GO:0051380]; protein heterodimerization activity [GO:0046982]; ... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA2A sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105096}; Multi-pass membrane protein {ECO:0000269|PubMed:23105096}. | null | null | null | null | null | FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotoni... | Homo sapiens (Human) |
P08920 | CD2_MOUSE | MKCKFLGSFFLLFSLSGKGADCRDNETIWGVLGHGITLNIPNFQMTDDIDEVRWVRRGTLVAEFKRKKPPFLISETYEVLANGSLKIKKPMMRNDSGTYNVMVYGTNGMTRLEKDLDVRILERVSKPMIHWECPNTTLTCAVLQGTDFELKLYQGETLLNSLPQKNMSYQWTNLNAPFKCEAINPVSKESKMEVVNCPEKGLSFYVTVGVGAGGLLLVLLVALFIFCICKRRKRNRRRKDEELEIKASRTSTVERGPKPHSTPAAAAQNSVALQAPPPPGHHLQTPGHRPLPPGHRTREHQQKKRPPPSGTQIHQQKGPP... | null | null | cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of tumor necrosis factor production [GO:0032760]; positive ... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102] | PF05790;PF07686; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:2440689}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2440689}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. | Mus musculus (Mouse) |
P08921 | CD2_RAT | MRCKFLGSFFLLFSLSSKGADCRDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILANGDLKIKNLTRDDSGTYNVTVYSTNGTRILNKALDLRILEMVSKPMIYWECSNATLTCEVLEGTDVELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAVNRVSQESEMEVVNCPEKGLPLYLIVGVSAGGLLLVFFGALFIFCICKRKKRNRRRKGEELEIKASRMSTVERGPKPHSTQASAPASQNPVASQAPPPPGHHLQTPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGP... | null | null | cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of tumor necrosis factor production [GO:0032760]; positive ... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102] | PF05790;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3102667}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. {ECO:0000269|PubMed:2901293}. | Rattus norvegicus (Rat) |
P08922 | ROS1_HUMAN | MKNIYCLIPKLVNFATLGCLWISVVQCTVLNSCLKSCVTNLGQQLDLGTPHNLSEPCIQGCHFWNSVDQKNCALKCRESCEVGCSSAEGAYEEEVLENADLPTAPFASSIGSHNMTLRWKSANFSGVKYIIQWKYAQLLGSWTYTKTVSRPSYVVKPLHPFTEYIFRVVWIFTAQLQLYSPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQEEQWLFLSRKTSLRKRSLKHLVDEAHCLRLDA... | 2.7.10.1 | null | cell differentiation [GO:0030154]; columnar/cuboidal epithelial cell development [GO:0002066]; protein phosphorylation [GO:0006468]; regulation of cell growth [GO:0001558]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of TOR signaling [GO:0032006]; spermatogenesis [GO:0007283]; transmembrane receptor pr... | membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00041;PF07714; | 2.60.40.10;2.120.10.30;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Phosphorylated. Probably autophosphorylates. Phosphorylation at Tyr-2274 is required for the interaction with PTPN6 that mediates ROS1 dephosphorylation. Phosphorylation at Tyr-2274 stimulates the kinase activity and the activation of the ERK1 signaling cascade (By similarity). Phosphorylation at Tyr-2274 and/or T... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000269|PubMed:11094073, ECO:0... | null | null | null | null | FUNCTION: Receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. NELL2 is an endogenous ligand for ROS1. Upon endogenous stimulation by NELL2, ROS1 activates the intracellular signaling pathway and triggers epididymal epithelial dif... | Homo sapiens (Human) |
P08923 | LTK_MOUSE | MGCSHRLLLWLGAAGTILCSNSEFQTPFLTPSLLPVLVLNSQEQKVTPTPSKLEPASLPNPLGTRGPWVFNTCGASGRSGPTQTQCDGAYTGSSVMVTVGAAGPLKGVQLWRVPDTGQYLISAYGAAGGKGAQNHLSRAHGIFLSAVFFLRRGEPVYILVGQQGQDACPGGSPESQLVCLGESGEHATTYGTERIPGWRRWAGGGGGGGGATSIFRLRAGEPEPLLVAAGGGGRSYRRRPDRGRTQAVPERLETRAAAPGSGGRGGAAGGGSGWTSRAHSPQAGRSPREGAEGGEGCAEAWAALRWAAAGGFGGGGGACA... | 2.7.10.1 | null | cell population proliferation [GO:0008283]; cellular response to retinoic acid [GO:0071300]; negative regulation of apoptotic process [GO:0043066]; peptidyl-tyrosine autophosphorylation [GO:0038083]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of neuron projection deve... | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; receptor signaling protein tyrosine kinase activator activity [GO:0030298]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF12810;PF07714; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. {ECO:0000250|UniProtKB:P29376}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2836739, ECO:0000269|PubMed:8995435}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform A]: Endoplasmic reticulum {ECO:0000305|PubMed:8380920}. Note=Retained in the endoplasmic reticulum. {ECO:0000305|PubMed:8380920}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000250|UniProtKB:P29376, ECO:... | null | null | null | null | FUNCTION: Receptor with a tyrosine-protein kinase activity. Following activation by ALKAL1 or ALKAL2 ligands at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activat... | Mus musculus (Mouse) |
P08928 | LAM0_DROME | MSSKSRRAGTATPQPGNTSTPRPPSAGPQPPPPSTHSQTASSPLSPTRHSRVAEKVELQNLNDRLATYIDRVRNLETENSRLTIEVQTTRDTVTRETTNIKNIFEAELLETRRLLDDTARDRARAEIDIKRLWEENEELKNKLDKKTKECTTAEGNVRMYESRANELNNKYNQANADRKKLNEDLNEALKELERLRKQFEETRKNLEQETLSRVDLENTIQSLREELSFKDQIHSQEINESRRIKQTEYSEIDGRLSSEYDAKLKQSLQELRAQYEEQMQINRDEIQSLYEDKIQRLQEAAARTSNSTHKSIEELRSTRV... | null | null | central nervous system development [GO:0007417]; chitin-based cuticle development [GO:0040003]; compound eye morphogenesis [GO:0001745]; digestive tract morphogenesis [GO:0048546]; gonad morphogenesis [GO:0035262]; heterochromatin formation [GO:0031507]; heterochromatin organization [GO:0070828]; male meiosis cytokines... | cytoplasm [GO:0005737]; lamin filament [GO:0005638]; nuclear envelope [GO:0005635]; nuclear envelope lumen [GO:0005641]; nuclear inner membrane [GO:0005637]; nuclear lamina [GO:0005652]; nucleus [GO:0005634]; spindle pole [GO:0000922] | chromatin binding [GO:0003682]; signaling receptor binding [GO:0005102]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Three forms of lamin have been identified in D.melanogaster, lamin Dm0 is rapidly processed to lamin Dm1 in the cytoplasm, Dm1 is then assembled in the nuclear envelope and is then phosphorylated, forming lamin Dm2. {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:3126192}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}. Nucleus inner membrane {ECO:0000269|PubMed:16439308}. Nucleus envelope {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}. Nucleus lamina {E... | null | null | null | null | null | FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (PubMed:15035436, PubMed:3126192). May have a role in the localization of the LEM domain p... | Drosophila melanogaster (Fruit fly) |
P08934 | KNG1_RAT | MKLITILLLCSRLLPSLAQEEDAQEMDCNDESLFQAVDTALKKYNAGLKSGNQFVLYQVTEGTKKDGSKTFYSFKYQIKEGNCSVQSGFAWQDCDFKDAEEAATGECTATLEKRRNNKFSIATQICNITPGKGPIVTNEYHCLGCMHPISVDSPELGPVLKHAVEHFNNNTKHTHLFALGEVKSADRQVVAGMNYQIIYSIVQTNCSKEDFPSLHEDCVPLPSGDDGECKGNAFVDIHKTIAGFSDSCEFYPGDDLFELLPEDCPGCPRNIPVDSPELKEALGHSIAQLNAENNHTFYFKIDTVKKATSQVVAGTKYVIE... | null | null | blood coagulation [GO:0007596]; Factor XII activation [GO:0002542]; negative regulation of blood coagulation [GO:0030195]; negative regulation of lymphocyte proliferation [GO:0050672]; negative regulation of proteolysis [GO:0045861]; negative regulation of T cell proliferation [GO:0042130]; positive regulation of cytos... | blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; protease binding [GO:0002020] | PF00031; | 3.10.450.10; | null | PTM: Bradykinin is released from kininogen by plasma kallikrein.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01042}.; PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus. {ECO:0000250|UniProtKB:P01042}. | SUBCELLULAR LOCATION: Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation... | Rattus norvegicus (Rat) |
P08941 | ROS1_CHICK | MRNACLLLNRLGAFYFIWISAAYCSFSKNCQDLCTSNLEGELGIANLCNVSDINVACTQGCQFWNATEQVNCPLKCNKTYTRECETVSCKFGCSRAEDAYGVEAQNCLNKPGAPFASSIGSHNITLGWKPANISEVKYIIQWKFHQLPGDWRYTEVVSETSYTVKDLQAFTEYEFRVVWIITSQLQLHSPPSPSYRTHASGVPTTAPIIKDIQSSSPNTVEVSWFPPLFPNGLIVGYNLVLTSENHELLRASRGHSFQFYSTFPNSTYRFSIVAVNEAGAGPPAEANITTPESKVKEKAKWLFLSRNQSLRKRYMEHFLE... | 2.7.10.1 | null | cell differentiation [GO:0030154]; columnar/cuboidal epithelial cell development [GO:0002066]; protein phosphorylation [GO:0006468]; regulation of cell growth [GO:0001558]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of TOR signaling [GO:0032006]; transmembrane receptor protein tyrosine kinase signalin... | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00041;PF07714; | 2.60.40.10;2.120.10.30;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8657124}; Single-pass type I membrane protein {ECO:0000305|PubMed:8657124}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Orphan receptor tyrosine kinase (RTK) that may activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and ac... | Gallus gallus (Chicken) |
P08949 | NMB_HUMAN | MARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK | null | null | antiviral innate immune response [GO:0140374]; arachidonic acid secretion [GO:0050482]; cell-cell signaling [GO:0007267]; Leydig cell proliferation [GO:0160024]; negative regulation of hormone secretion [GO:0046888]; negative regulation of interleukin-6 production [GO:0032715]; neuropeptide signaling pathway [GO:000721... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuron projection [GO:0043005] | hormone activity [GO:0005179]; neuromedin B receptor binding [GO:0031710]; neuropeptide hormone activity [GO:0005184] | PF02044; | null | Bombesin/neuromedin-B/ranatensin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9CR53}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9CR53}. Note=In neurons of the retrotrapezoid nucleus//parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q9CR53}. | null | null | null | null | null | FUNCTION: Stimulates smooth muscle contraction (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following ... | Homo sapiens (Human) |
P08953 | TOLL_DROME | MSRLKAASELALLVIILQLLQWPGSEASFGRDACSEMSIDGLCQCAPIMSEYEIICPANAENPTFRLTIQPKDYVQIMCNLTDTTDYQQLPKKLRIGEVDRVQMRRCMLPGHTPIASILDYLGIVSPTTLIFESDNLGMNITRQHLDRLHGLKRFRFTTRRLTHIPANLLTDMRNLSHLELRANIEEMPSHLFDDLENLESIEFGSNKLRQMPRGIFGKMPKLKQLNLWSNQLHNLTKHDFEGATSVLGIDIHDNGIEQLPHDVFAHLTNVTDINLSANLFRSLPQGLFDHNKHLNEVRLMNNRVPLATLPSRLFANQPE... | null | null | antifungal innate immune response [GO:0061760]; cell adhesion [GO:0007155]; cell competition in a multicellular organism [GO:0035212]; defense response to Gram-positive bacterium [GO:0050830]; defense response to oomycetes [GO:0002229]; detection of virus [GO:0009597]; dorsal/ventral axis specification [GO:0009950]; he... | cell surface [GO:0009986]; cleavage furrow [GO:0032154]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; identical protein binding [GO:0042802]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling receptor activity [GO:0038023]; TIR domain binding [GO:0070976]; transmembrane signaling receptor activity [GO:0004888]; virion binding ... | PF00560;PF13306;PF13855;PF01463;PF01462;PF13676; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15373972, ECO:0000269|PubMed:1879347}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15373972}. Note=In the fat body, detected in puntate structures along the cell periphery. Becomes evenly distributed in the cytoplasm 1 hour aft... | null | null | null | null | null | FUNCTION: Receptor for the cleaved activated form of spz, spaetzle C-106 (PubMed:12872120). Binding to spaetzle C-106 activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin (PubMed:10973475, PubMed:12872120, PubMed:8808632). Component of the extracellular signaling pathway that... | Drosophila melanogaster (Fruit fly) |
P08955 | PYR1_MESAU | MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSENHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQSGTEPSTLPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWNHELDSQKYDGLFLSNGPGDPASYPGVVATLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWTPLFTNANDCSN... | 2.1.3.2; 3.5.1.2; 3.5.2.3; 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P27708}; Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity). {ECO:0000250|UniProtKB:P27708}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035;... | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; peptidyl-threonine phosphorylation [GO:0018107]; protein autophosphorylation [GO:0046777]; UTP biosynthetic process ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleus [GO:0005634] | aspartate binding [GO:0070335]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:0004359... | PF01979;PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729; | 3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380; | CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oli... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydrooro... | null | null | FUNCTION: Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-d... | Mesocricetus auratus (Golden hamster) |
P08956 | T1RK_ECOLI | MMNKSNFEFLKGVNDFTYAIACAAENNYPDDPNTTLIKMRMFGEATAKHLGLLLNIPPCENQHDLLRELGKIAFVDDNILSVFHKLRRIGNQAVHEYHNDLNDAQMCLRLGFRLAVWYYRLVTKDYDFPVPVFVLPERGENLYHQEVLTLKQQLEQQVREKAQTQAEVEAQQQKLVALNGYIAILEGKQQETEAQTQARLAALEAQLAEKNAELAKQTEQERKAYHKEITDQAIKRTLNLSEEESRFLIDAQLRKAGWQADSKTLRFSKGARPEPGVNKAIAEWPTGKDETGNQGFADYVLFVGLKPIAVVEAKRNNIDV... | 3.1.21.3 | null | DNA restriction-modification system [GO:0009307] | cytosol [GO:0005829]; type I site-specific deoxyribonuclease complex [GO:0019812] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; type I site-specific deoxyribonuclease activity [GO:0009035] | PF08463;PF00271;PF04313;PF04851; | 3.90.1570.30;3.40.50.300; | HsdR family | PTM: Upon purification after overexpression about one-third has the initiating methionine removed. {ECO:0000269|PubMed:9033396}. | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000269|PubMed:4868368}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0 for DNA restriction. {ECO:0000269|PubMed:4868368}; | null | FUNCTION: The subtype A restriction (R) subunit of a type I restriction enzyme that recognizes 5'-AACN(6)GTGC-3' and cleaves a random distance away. The R subunit is required for both endonuclease and ATPase activities but not for modification (PubMed:12654995, PubMed:4868368, PubMed:6255295, PubMed:9033396). Has endon... | Escherichia coli (strain K12) |
P08958 | GVPA1_HALSA | MAQPDSSGLAEVLDRVLDKGVVVDVWARVSLVGIEILTVEARVVAASVDTFLHYAEEIAKIEQAELTAGAEAAPEA | null | null | null | gas vesicle shell [GO:0033172]; vesicle membrane [GO:0012506] | structural molecule activity [GO:0005198] | PF00741; | null | Gas vesicle GvpA family | null | SUBCELLULAR LOCATION: Gas vesicle shell {ECO:0000255|HAMAP-Rule:MF_00576, ECO:0000269|PubMed:14695294, ECO:0000269|PubMed:21158390, ECO:0000269|PubMed:21542854, ECO:0000269|PubMed:8423144, ECO:0000269|Ref.10}. Note=Both the N- and C-termini of the protein (but not interior sequences between Ser-5 and Gl-55) are accessi... | null | null | null | null | null | FUNCTION: Gas vesicles are hollow, gas filled proteinaceous nanostructures found in several microbial planktonic microorganisms. They allow positioning of halobacteria at the optimal depth for growth in the poorly aerated shallow brine pools of their habitat. GvpA forms the protein shell (PubMed:1956294, PubMed:2586485... | Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) |
P08962 | CD63_HUMAN | MAVEGGMKCVKFLLYVLLLAFCACAVGLIAVGVGAQLVLSQTIIQGATPGSLLPVVIIAVGVFLFLVAFVGCCGACKENYCLMITFAIFLSLIMLVEVAAAIAGYVFRDKVMSEFNNNFRQQMENYPKNNHTASILDRMQADFKCCGAANYTDWEKIPSMSKNRVPDSCCINVTVGCGINFNEKAIHKEGCVEKIGGWLRKNVLVVAAAALGIAFVEVLGIVFACCLVKSIRSGYEVM | null | null | cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; endosome to melanosome transport [GO:0035646]; pigment granule maturation [GO:0048757]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of receptor internalization [GO:0002092]; protein transport [GO:0015031]; r... | azurophil granule membrane [GO:0035577]; cell surface [GO:0009986]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:000576... | null | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | PTM: Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). {ECO:0000269|PubMed:19640571}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15351990, ECO:0000269|PubMed:19640571, ECO:0000269|PubMed:23632027}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:19640571, ECO:0000269|PubMed:1993697, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Functions as a cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell a... | Homo sapiens (Human) |
P08964 | MYO1_YEAST | MTGGQSCSSNMIVWIPDEKEVFVKGELMSTDINKNKFTGQEEQIGIVHPLDSTEVSNLVQVRISDVFPVNPSTFDKVENMSELTHLNEPSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRLSKSRLDENSHEKLPPHIFAIAEEAYENLLSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYKILSN... | null | null | actin filament organization [GO:0007015]; mitotic actomyosin contractile ring assembly [GO:1903475]; mitotic actomyosin contractile ring contraction [GO:1902404]; primary cell septum biogenesis [GO:0031671]; protein localization to mitotic actomyosin contractile ring [GO:1904498]; septum digestion after cytokinesis [GO... | cellular bud neck [GO:0005935]; cellular bud neck contractile ring [GO:0000142]; cytoplasm [GO:0005737]; incipient cellular bud site [GO:0000131]; mitotic actomyosin contractile ring [GO:0110085]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]; myosin II light chain binding [GO:0032033]; myosin light chain binding [GO:0032027] | PF00063; | 1.10.10.820;1.20.5.340;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | null | null | null | null | null | null | FUNCTION: Required for cell division. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08965 | MEI2_SCHPO | MIMETESPLSITSPSPSDSTFQVDMEKTMHALPSSLLDSPLLSTNEHYPPKSTLLLSGPSPIRNIQLSATKSSESNSIDYLTDTQNIFPNFVNNENNYQFSTAPLNPIDACRVGERKVFTTGNVLLSADRQPLSTWQQNISVLSESPPQNGIQSYISSSEQAAQALTRKPSVTGFRSSSLNSNSDDIDIFSHASRYLFVTNLPRIVPYATLLELFSKLGDVKGIDTSSLSTDGICIVAFFDIRQAIQAAKSLRSQRFFNDRLLYFQFCQRSSIQKMINQGATIQFLDDNEGQLLLNMQGGSVLSILQLQSILQTFGPLLI... | null | null | meiotic cell cycle [GO:0051321]; negative regulation of conjugation with zygote [GO:0140538]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of meiotic nuclear division [GO:0045836]; positive regulation of metaphase/anaphase transition of meiosis II [GO:1905191]; regulation of DNA-templated... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Mei2 nuclear dot complex [GO:0033620]; Nrd1 complex [GO:0035649]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; Tor2-Mei2-Ste11 complex [GO:0034064] | lncRNA binding [GO:0106222]; poly(U) RNA binding [GO:0008266]; protein sequestering activity [GO:0140311]; RNA binding [GO:0003723] | PF00076;PF04059; | 3.30.70.330; | null | PTM: Inactivated by phosphorylation by ran1/pat1. | null | null | null | null | null | null | FUNCTION: Crucial for commitment to meiosis but it is not sufficient itself for the commitment. May be a splicing regulator. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P08970 | SUHW_DROME | MSASKEGKEKKGKLLGVENISPPKDKRPATRMKLLNDVGAGEDSEASTTTTTSRTPSNKQEKRGSVAGSRIKILNEEILGTPKTEKRGATKSTAPAASTVKILNEKKTPSATVTAVETTKIKTSPSKRKKMEHYVLQAVKSENTKADTTVTVVTEEDDTIDFILADDEEVVPGRIENNNGQEIVVTEDDEDLGEDGDEDGEDSSGKGNSSQTKIKEIVEHVCGKCYKTFRRVQSLKKHLEFCRYDSGYHLRKADMLKNLEKIEKDAVVMEKKDICFCCSESYDTFHLGHINCPDCPKSFKTQTSYERHIFITHSEFSDFP... | null | null | heterochromatin boundary formation [GO:0033696]; negative regulation of DNA-templated transcription [GO:0045892]; protein localization to euchromatin [GO:1905632]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ecdysone [GO:0035075] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; chromatin insulator sequence binding [GO:0043035]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; euchromatin binding [GO:1990188]; metal ion binding [GO:0046872]; RNA p... | PF00096;PF13912; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with other elements of the gypsy chromatin insulator complex at multiple sites on polytene chromosomes and at nuclear insulator bodies. | null | null | null | null | null | FUNCTION: Component of the gypsy chromatin insulator complex which is required for the function of the gypsy chromatin insulator and other endogenous chromatin insulators. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators h... | Drosophila melanogaster (Fruit fly) |
P08980 | UCRIA_SPIOL | MASFTLSSATPSQLCSSKNGMFAPSLALAKAGRVNVLISKERIRGMKLTCQATSIPADNVPDMQKRETLNLLLLGALSLPTGYMLLPYASFFVPPGGGAGTGGTIAKDALGNDVIAAEWLKTHAPGDRTLTQGLKGDPTYLVVESDKTLATFGINAVCTHLGCVVPFNAAENKFICPCHGSQYNNQGRVVRGPAPLSLALAHCDVDDGKVVFVPWTETDFRTGEAPWWSA | 7.1.1.6 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:9438861}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:9438861}; | null | chloroplast thylakoid membrane [GO:0009535]; plasma membrane [GO:0005886] | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity [GO:0045158]; metal ion binding [GO:0046872]; plastoquinol--plastocyanin reductase activity [GO:0009496] | PF00355; | 2.102.10.10;1.20.5.700; | Rieske iron-sulfur protein family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:9438861}; Single-pass membrane protein {ECO:0000305|PubMed:9438861}. Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]; Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEB... | null | null | null | null | FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. {ECO:0000250}. | Spinacia oleracea (Spinach) |
P08985 | H2AV_DROME | MAGGKAGKDSGKAKAKAVSRSARAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKEETVQDPQRKGNVILSQAY | null | null | DNA repair [GO:0006281]; heterochromatin organization [GO:0070828]; male germ-line stem cell population maintenance [GO:0036098]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; protein localization to chromatin [GO:0071168]; somatic stem cell population maintenance [GO:0035019] | chromosome [GO:0005694]; euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634]; polytene chromosome [GO:0005700]; polytene chromosome chromocenter [GO:0005701]; site of double-strand break [GO:0035861] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated. Phosphorylation of Ser-138 occurs in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents. Phosphorylation is dependent on the DNA damage checkpoint kinases ATR and ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitme... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10801889}. Chromosome {ECO:0000269|PubMed:10801889}. Note=Widely distributed in the genome, irrespective of the transcriptional status or coding capacity of the sequence. | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... | Drosophila melanogaster (Fruit fly) |
P08987 | GTFB_STRMU | MDKKVRYKLRKVKKRWVTVSVASAVMTLTTLSGGLVKADSNESKSQISNDSNTSVVTANEESNVTTEVTSKQEAASSQTNHTVTTISSSTSVVNPKEVVSNPYTVGETASNGEKLQNQTTTVDKTSEAAANNISKQTTEADTDVIDDSNAANLQILEKLPNVKEIDGKYYYYDNNGKVRTNFTLIADGKILHFDETGAYTDTSIDTVNKDIVTTRSNLYKKYNQVYDRSAQSFEHVDHYLTAESWYRPKYILKDGKTWTQSTEKDFRPLLMTWWPSQETQRQYVNYMNAQLGINKTYDDTSNQLQLNIAAATIQAKIEAK... | 2.4.1.5 | null | glucan biosynthetic process [GO:0009250] | extracellular region [GO:0005576] | dextransucrase activity [GO:0047849]; glucosyltransferase activity [GO:0046527] | PF01473;PF19127;PF02324;PF19258; | 2.30.30.20;2.10.270.10;3.20.20.470;2.30.30.420; | Glycosyl hydrolase 70 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:18825, Rhea:RHEA-COMP:11144, Rhea:RHEA-COMP:11145, ChEBI:CHEBI:17992, ChEBI:CHEBI:18269, ChEBI:CHEBI:37721; EC=2.4.1.5; | null | null | null | null | FUNCTION: Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris. | Streptococcus mutans serotype c (strain ATCC 700610 / UA159) |
P08989 | GRP_CANLF | MRGRELPLVLLALVLCQAPRGPAAPVPGGQGTVLDKMYPRGNHWAVGHLMGKKSTRESPYVYEEGSLKQQLQGYIRWEEAARNLLSLMEAKGTRSHQTPQREPLGIRQSAWDYQDDSNFKVIGPTREVGGLSASGSQPEGRNPPRN | null | null | mast cell degranulation [GO:0043303]; negative regulation of voltage-gated potassium channel activity [GO:1903817]; negative regulation of voltage-gated sodium channel activity [GO:1905151]; neuropeptide signaling pathway [GO:0007218]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of... | extracellular space [GO:0005615]; neuron projection [GO:0043005]; secretory granule lumen [GO:0034774] | neuropeptide hormone activity [GO:0005184] | PF02044; | null | Bombesin/neuromedin-B/ranatensin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07492}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q863C3}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which... | null | null | null | null | null | FUNCTION: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By sim... | Canis lupus familiaris (Dog) (Canis familiaris) |
P08992 | H2AV_TETTS | MAGGKGGKGGKGGKGGKVGGAKNKKTPQSRSYKAGLQFPVGRIHRFLKGRVSAKNRVGATAAVYAAAILEYLTAEVLELAGNASKDFKVRRITPRHLLLAIRGDEELDILIKATIAGGGVIPHIHKALLGKHSTKNRSSAKTAEPR | null | null | null | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated on the C-terminal half. {ECO:0000269|PubMed:3944120}.; PTM: Acetylation occurs almost exclusively in the MAC. {ECO:0000269|PubMed:11430834, ECO:0000269|PubMed:3944120, ECO:0000269|PubMed:7061439}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8276246}. Chromosome {ECO:0000269|PubMed:8276246}. Note=Localizes to the large, transcriptionally active, somatic macronucleus (MAC) at all stages of the cell cycle. Usually absent from the small, transcriptionally inert, germ line micronucleus (MIC), it is shortly foun... | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes, preferentially in transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in... | Tetrahymena thermophila (strain SB210) |
P08998 | SOMA_CHICK | MAPGSWFSPLLIAVVTLGLPQEAAATFPAMPLSNLFANAVLRAQHLHLLAAETYKEFERTYIPEDQRYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMELLRFSLVLIQSWLTPVQYLSKVFTNNLVFGTSDRVFEKLKDLEEGIQALMRELEDRSPRGPQLLRPTYDKFDIHLRNEDALLKNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI | null | null | animal organ development [GO:0048513]; cellular response to insulin stimulus [GO:0032869]; growth hormone receptor signaling pathway [GO:0060396]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; oviduct epithelium development [GO:0035846]; positive regulation ... | extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; trans-Golgi network [GO:0005802] | cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth hormone plays an important role in growth control. | Gallus gallus (Chicken) |
P08F94 | PKHD1_HUMAN | MTAWLISLMSIEVLLLAVRHLSLHIEPEEGSLAGGTWITVIFDGLELGVLYPNNGSQLEIHLVNVNMVVPALRSVPCDVFPVFLDLPVVTCRTRSVLSEAHEGLYFLEAYFGGQLVSSPNPGPRDSCTFKFSKAQTPIVHQVYPPSGVPGKLIHVYGWIITGRLETFDFDAEYIDSPVILEAQGDKWVTPCSLINRQMGSCYPIQEDHGLGTLQCHVEGDYIGSQNVSFSVFNKGKSMVHKKAWLISAKQDLFLYQTHSEILSVFPETGSLGGRTNITITGDFFDNSAQVTIAGIPCDIRHVSPRKIECTTRAPGKDVRL... | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; cilium assembly [GO:0060271]; epithelial cell morphogenesis [GO:0003382]; establishment of centrosome localization [GO:0051660]; establishment of mitotic spindle orientation [GO:000... | 9+0 non-motile cilium [GO:0097731]; apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular ex... | signaling receptor activity [GO:0038023] | PF13229;PF10162;PF01833; | 2.60.40.10;2.160.20.10; | null | PTM: Several proteolytic cleavages occur within the extracellular domain, whereas at least one cleavage occurs within the cytoplasmic domain (PubMed:16956880). Cleaved by a probable proprotein convertase which produces an extracellular domain (polyductin extracellular domain, (PECD)) and a C-terminal fragment (polyduct... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15458427}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15458427}. Cell projection, cilium {ECO:0000269|PubMed:14978161, ECO:0000269|PubMed:15458427, ECO:0000269|PubMed:17470460}. Cytoplasm, cytoskeleton, cilium basal body {ECO:... | null | null | null | null | null | FUNCTION: Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity). Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome ... | Homo sapiens (Human) |
P09006 | SPA3N_RAT | MTRLVTLELLMAGIGSALLCFPDCILGEDTLFHEDQDKGTQLDSLTLASINTDFAFSLYKKLALRNPDKNVVFSPLSISAALAVVSLGAKGNSMEEILEGLKFNLTETPETEIHRGFGHLLQRLSQPRDEIQISTGNALFIEKRLQVLAEFQEKAKALYQAEAFTADFQQSREAKKLINDYVSKQTQGKIQGLITNLAKKTSMVLVNYIYFKGKWKVPFDPRDTFQSEFYSGKRRPVKVPMMKLEDLTTPYVRDEELNCTVVELKYTGNASALFILPDQGKMQQVEASLQPETLRRWKDSLRPSMIDELYLPKFSISADY... | null | null | cellular response to cAMP [GO:0071320]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; cellular response to type II interferon [GO:0071346]; response to bacterium [GO:0009617]; response to cytokine [GO:0034097]... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: N-glycosylated. {ECO:0000269|PubMed:1694763}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | null | Rattus norvegicus (Rat) |
P09010 | LMNB1_XENLA | MATATPSGPRSSGRRSSMSTPLSPTRITRLQEKVDLQELNDRLALYIDTVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLDDTAREKARLQLELSKVSVEHQDLQASFSKRESELESTQARFRETEALLNSKNAALATAQSENKSLQGEVEDLKAEIGQLGSALALAKKQLEEEILMKVDLENRCQSLIEELNFRKNIYEEEIKETSRRHETRLVEVDSGRQVDYEYKLSQALSEMREQQESQIGLYKEELEQTYQSKLENARLASEMNSSAVNSTREELMESRIRIDSLTSQLSELQKESRAWHDR... | null | null | heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] | structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration. Phosphorylation by CDK1 at Ser-23 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown. {ECO:0000250|UniProtKB:P14732}. | SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:3762708}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P02545}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. | null | null | null | null | null | FUNCTION: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:3762708). Lamins provide a framework for the nuclear envelope, bridging the nucl... | Xenopus laevis (African clawed frog) |
P09011 | MIP_RAT | ELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL | null | null | canalicular bile acid transport [GO:0015722]; gap junction-mediated intercellular transport [GO:1990349]; lens development in camera-type eye [GO:0002088]; positive regulation of cell adhesion [GO:0045785]; protein homotetramerization [GO:0051289]; visual perception [GO:0007601]; water transport [GO:0006833] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; gap junction [GO:0005921]; intracellular canaliculus [GO:0046691]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; structural constituent of eye lens [GO:0005212]; water channel activity [GO:0015250] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity). {ECO:0000250}.; PTM: Fatty acylated at Lys-236. The acyl modifications, in decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl (C16:0) >... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction, gap junction {ECO:0000250|UniProtKB:P30301}. | null | null | null | null | null | FUNCTION: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhe... | Rattus norvegicus (Rat) |
P09012 | SNRPA_HUMAN | MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK | null | null | mRNA splicing, via spliceosome [GO:0000398] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U4/U6 x U5 tri-snRNP complex [GO:0046540] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; U1 snRNA binding [GO:0030619]; U1 snRNP binding [GO:1990446] | PF00076; | 3.30.70.330; | RRM U1 A/B'' family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA... | Homo sapiens (Human) |
P09015 | HME2A_DANRE | MDENEQSARDVEQRGASDESNSAIRPLLQAPGNLQLPHRITNFFIDNILRPDFGRKKEANITRYEDNHGARENHNPTGPSTGQVGSTVPAEEASTTHTSSGGKEAEIESEEPLKPRGENVDQCLGSESDSSQSNSNGQTGQGMLWPAWVYCTRYSDRPSSGPRSRKPKKKAASKEDKRPRTAFTAEQLQRLKAEFQTNRYLTEQRRQSLAQELGLNESQIKIWFQNKRAKIKKASGVKNGLAIHLMAQGLYNHSTTSKEDKSDSD | null | null | anterior/posterior pattern specification [GO:0009952]; apoptotic process involved in morphogenesis [GO:0060561]; axonogenesis involved in innervation [GO:0060385]; cell fate specification [GO:0001708]; midbrain development [GO:0030901]; midbrain-hindbrain boundary development [GO:0030917]; midbrain-hindbrain boundary m... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF10525;PF00046; | 1.10.10.60; | Engrailed homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | null | Danio rerio (Zebrafish) (Brachydanio rerio) |
P09016 | HXD4_HUMAN | MVMSSYMVNSKYVDPKFPPCEEYLQGGYLGEQGADYYGGGAQGADFQPPGLYPRPDFGEQPFGGSGPGPGSALPARGHGQEPGGPGGHYAAPGEPCPAPPAPPPAPLPGARAYSQSDPKQPPSGTALKQPAVVYPWMKKVHVNSVNPNYTGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQIKIWFQNRRMKWKKDHKLPNTKGRSSSSSSSSSCSSSVAPSQHLQPMAKDHHTDLTTL | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic organ development [GO:0048568]; embryonic skeletal system morphogenesis [GO:0048704]; positive regulation of transcription by RNA polymerase II [GO:0045944]; stem cell differentiation [GO:0048863] | cell junction [GO:0030054]; chromatin [GO:0000785]; nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specif... | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P09017 | HXC4_HUMAN | MIMSSYLMDSNYIDPKFPPCEEYSQNSYIPEHSPEYYGRTRESGFQHHHQELYPPPPPRPSYPERQYSCTSLQGPGNSRGHGPAQAGHHHPEKSQSLCEPAPLSGASASPSPAPPACSQPAPDHPSSAASKQPIVYPWMKKIHVSTVNPNYNGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRIEIAHSLCLSERQIKIWFQNRRMKWKKDHRLPNTKVRSAPPAGAAPSTLSAATPGTSEDHSQSATPPEQQRAEDITRL | null | null | anterior/posterior pattern specification [GO:0009952]; cartilage development [GO:0051216]; embryonic skeletal system morphogenesis [GO:0048704]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromatin [GO:0000785]; nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; HMG box domain binding [GO:0071837]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-str... | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P09021 | HXA5_MOUSE | MSSYFVNSFCGRYPNGPDYQLHNYGDHSSVSEQFRDSASMHSGRYGYGYNGMDLSVGRSGSGHFGSGERARSYAAGASAAPAEPRYSQPATSTHSPPPDPLPCSAVAPSPGSDSHHGGKNSLGNSSGASANAGSTHISSREGVGTASAAEEDAPASSEQAGAQSEPSPAPPAQPQIYPWMRKLHISHDNIGGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSMAAAGGAFRP | null | null | anterior/posterior pattern specification [GO:0009952]; bronchiole development [GO:0060435]; cartilage morphogenesis [GO:0060536]; cell migration [GO:0016477]; cell-cell signaling involved in mammary gland development [GO:0060764]; embryonic skeletal system development [GO:0048706]; embryonic skeletal system morphogenes... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'. | Mus musculus (Mouse) |
P09022 | HXA1_MOUSE | MNSFLEYPILGSGDSGTCSARAYPSDHGITTFQSCAVSANSCGGDDRFLVGRGVQISSPHHHHHHHHHHHPQTATYQTSGNLGISYSHSSCGPSYGAQNFSAPYGPYGLNQEADVSGGYPPCAPAVYSGNLSTPMVQHHHHHQGYAGGTVGSPQYIHHSYGQEQQTLALATYNNSLSPLHASHQEACRSPASETSSPAQTFDWMKVKRNPPKTGKVGEYGYVGQPNAVRTNFTTKQLTELEKEFHFNKYLTRARRVEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPISPATPPGSDEKTEESSEKSSPSPSAPSPA... | null | null | anatomical structure formation involved in morphogenesis [GO:0048646]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; cellular response to ethanol [GO:0071361]; cellular response to retinoic acid [GO:0071300]; central nervous system neuron differentiation [GO:002... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, Labial subfamily | PTM: Glycosylated by OGT. {ECO:0000269|PubMed:29465778}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29465778}. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor (PubMed:29465778). Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior (By similarity). Also part of a developmental regulatory system that ... | Mus musculus (Mouse) |
P09024 | HXB7_MOUSE | MSSLYYANALFSKYPAASSVFAPGAFPEQTSCAFASNPQRPGYGAGPGAPFSASVQGLYSGGGAMAGQSAAGVYAAGYGLEPSSFNMHCAPFEQNLSGVCPGDPAKAAGAKEQRDSDLAAESNFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHTLCLTERQIKIWFQNRRMKWKKENKTSGPGTTGQDKAEAEEEEEE | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; myeloid cell differentiation [GO:0030099]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09025 | HXC8_MOUSE | MSSYFVNPLFSKYKGGESLEPAYYDCRFPQSVGRSHALVYGPGGSAPGFQHASHHVQDFFHHGTSGISNSGYQQNPCSLSCHGDASKFYGYEALPRQSLYGAQQEASVVQYPDCKSSANTNSSEGQGHLNQNSSPSLMFPWMRPHAPGRRSGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKLPGARDEEKVEEEGNEEEEKEEEEKEENKD | null | null | anterior/posterior pattern specification [GO:0009952]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system morphogenesis [GO:0048705] | microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09026 | HXB3_MOUSE | MQKATYYDNTAAALFGGYSSYPGSNGFGYDGPPQPPFQAATHLEGDYQRSACSLQSLGNAAPHAKSKELNGSCMRPGLAPEPLPAPPGSPPPSAAPTSTTSNSNNGGGPSKSGPPKCGAGSNSTLTKQIFPWMKESRQTSKLKNSSPGTAEGCGGGGGGGGGGGGGGGGSSGGGGGGGGGGDKSPPGSAASKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLSERQIKIWFQNRRMKYKKDQKAKGLASSSGGPSPAGSPPQPMQSTAGFMNALHSMTPSYDSPSPPAFGKGHQNAYALPSNYQPPLKGCGA... | null | null | angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; cartilage development [GO:0051216]; definitive hemopoiesis [GO:0060216]; embryonic skeletal system morphogenesis [GO:0048704]; face development [GO:0060324]; glossopharyngeal nerve morphogenesis [GO:0021615]; hematopoietic progenitor cell... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF13293;PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09027 | HXD3_MOUSE | MLFEQGQLTLELPECTMQKAAYYENPGLFGGYGYSKATDTYGYSTPHQPYPPPAAANSLDSDYPSSACSIQSSAPLRAPAHKGAELNGSCMRPGTGNSQGGGGGNQPPGLNSEQQPPQPPPPPPPTLPPSSPTNPGSGVPAKKTKGGLSASSSSSTISKQIFPWMKESRQNSKQKNSCATSGENCEDKSPPGPASKRVRTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKAKGILHSPAGQSPERSPPLGGAAGHVAYSGQLPPVPGLAYDAPSPPAFAKSQPNMYGLAAYTAPL... | null | null | anterior/posterior pattern specification [GO:0009952]; cartilage development [GO:0051216]; cell-matrix adhesion [GO:0007160]; DNA-templated transcription [GO:0006351]; embryonic skeletal system morphogenesis [GO:0048704]; glossopharyngeal nerve morphogenesis [GO:0021615]; Notch signaling pathway [GO:0007219]; positive ... | aggresome [GO:0016235]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF13293;PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09029 | PURK_ECOLI | MKQVCVLGNGQLGRMLRQAGEPLGIAVWPVGLDAEPAAVPFQQSVITAEIERWPETALTRELARHPAFVNRDVFPIIADRLTQKQLFDKLHLPTAPWQLLAERSEWPAVFDRLGELAIVKRRTGGYDGRGQWRLRANETEQLPAECYGECIVEQGINFSGEVSLVGARGFDGSTVFYPLTHNLHQDGILRTSVAFPQANAQQQAQAEEMLSAIMQELGYVGVMAMECFVTPQGLLINELAPRVHNSGHWTQNGASISQFELHLRAITDLPLPQPVVNNPSVMINLIGSDVNYDWLKLPLVHLHWYDKEVRPGRKVGHLNL... | 6.3.4.18 | null | 'de novo' IMP biosynthetic process [GO:0006189] | cytosol [GO:0005829] | 5-(carboxyamino)imidazole ribonucleotide synthase activity [GO:0034028]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylaminoimidazole carboxylase activity [GO:0004638] | PF02222;PF17769; | 3.40.50.20;3.30.1490.20;3.30.470.20; | PurK/PurT family | null | null | CATALYTIC ACTIVITY: Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEB... | null | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:8117684}. | null | null | FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:8117684}. | Escherichia coli (strain K12) |
P09030 | EX3_ECOLI | MKFVSFNINGLRARPHQLEAIVEKHQPDVIGLQETKVHDDMFPLEEVAKLGYNVFYHGQKGHYGVALLTKETPIAVRRGFPGDDEEAQRRIIMAEIPSLLGNVTVINGYFPQGESRDHPIKFPAKAQFYQNLQNYLETELKRDNPVLIMGDMNISPTDLDIGIGEENRKRWLRTGKCSFLPEEREWMDRLMSWGLVDTFRHANPQTADRFSWFDYRSKGFDDNRGLRIDLLLASQPLAECCVETGIDYEIRSMEKPSDHAPVWATFRR | 3.1.11.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250}; | DNA damage response [GO:0006974]; DNA repair [GO:0006281] | cytosol [GO:0005829] | DNA binding [GO:0003677]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; | null | null | null | null | FUNCTION: Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities. | Escherichia coli (strain K12) |
P09032 | EI2BG_YEAST | MSIQAFVFCGKGSNLAPFTQPDFPFQTQNKDSTAATSGDKLNELVNSALDSTVINEFMQHSTRLPKALLPIGNRPMIEYVLDWCDQADFKEISVVAPVDEIELIESGLTSFLSLRKQQFELIYKALSNSNHSHHLQDPKKINFIPSKANSTGESLQKELLPRINGDFVILPCDFVTDIPPQVLVDQFRNRDDNNLAMTIYYKNSLDSSIDKKQQQKQKQQQFFTVYSENEDSERQPILLDVYSQRDVTKTKYLQIRSHLLWNYPNLTVSTKLLNSFIYFCSFELCQLLKLGPQSMSRQASFKDPFTGNQQQQNPPTTDDD... | null | null | cytoplasmic translational initiation [GO:0002183]; negative regulation of cellular response to amino acid starvation [GO:1903574]; regulation of translational initiation [GO:0006446] | cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]; guanyl-nucleotide exchange factor complex [GO:0032045] | guanyl-nucleotide exchange factor activity [GO:0005085]; translation initiation factor activity [GO:0003743] | null | 2.160.10.10; | EIF-2B gamma/epsilon subunits family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56288}. | null | null | null | null | null | FUNCTION: Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subun... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09034 | ASSY_RAT | MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDVLEIEFKKGVPVKVTNVKDGTTHSTSLDLFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAEL... | 6.3.4.5 | null | acute-phase response [GO:0006953]; arginine biosynthetic process [GO:0006526]; argininosuccinate metabolic process [GO:0000053]; aspartate metabolic process [GO:0006531]; cellular response to amine stimulus [GO:0071418]; cellular response to amino acid stimulus [GO:0071230]; cellular response to ammonium ion [GO:007124... | cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204] | amino acid binding [GO:0016597]; argininosuccinate synthase activity [GO:0004055]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; toxic substance binding [GO:0015643] | PF20979;PF00764; | 3.90.1260.10;3.40.50.620;1.20.5.470; | Argininosuccinate synthase family, Type 1 subfamily | PTM: Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases. {ECO:0000250|UniProtKB:P00966}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:19491403}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000269|PubMe... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. {ECO:0000305|PubMed:19491403}.; PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. {ECO:0000305|PubMed:19491403}. | null | null | FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals (Probable). Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for t... | Rattus norvegicus (Rat) |
P09036 | ISK1_MOUSE | MKVAVIFLLSALALLSLAGNTFSAKVTGKEASCHDAVAGCPRIYDPVCGTDGITYANECVLCFENRKRIEPVLIRKGGPC | null | null | negative regulation of calcium ion import [GO:0090281]; negative regulation of nitric oxide mediated signal transduction [GO:0010751]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; nitric oxide mediated signal transduction [GO:0007263]; regulation of acrosome reaction [GO:0060046]; regulation o... | extracellular space [GO:0005615] | peptidase inhibitor activity [GO:0030414]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00050; | 3.30.60.30; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1929395}. | null | null | null | null | null | FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:14645103, PubMed:22228629, PubMed:3428272). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (PubMed:16083722). {ECO:0000269|PubMed:14645103, ECO:0000269|PubMed:16083722, ECO:0000269|PubMed:22228629, ECO... | Mus musculus (Mouse) |
P09038 | FGF2_HUMAN | MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS | null | null | angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cell migration involved in sprouting angiogenesis [GO:0002042]; ... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chemoattractant activity [GO:0042056]; chemokine binding [GO:0019956]; cytokine activity [GO:0005125]; fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; nuclear receptor coacti... | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: Phosphorylation at Tyr-215 regulates FGF2 unconventional secretion. {ECO:0000269|PubMed:20230531}.; PTM: Several N-termini starting at positions 94, 125, 126, 132, 143 and 162 have been identified by direct sequencing. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20230531}. Nucleus {ECO:0000269|PubMed:22321063}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (PubMed:20230531). Binding of exogenous F... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Retains almost half of its activity after treatment at pH 2.0 for 3 hours at 20 degrees Celsius. {ECO:0000269|PubMed:1721615}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Inactivated after 3 minutes at 60 degrees Celsius or 1 minute at 80 degrees Celsius. {ECO:0000269|PubMed:1721615}; | FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:8663044). Also acts as an integrin ligand which is required for FGF2 signaling (PubMed:28302677). Binds to integrin ITGAV:ITGB3 (PubMed:28302677). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell... | Homo sapiens (Human) |
P09040 | DSK_DROME | MGPRSCTHFATLFMPLWALAFCFLVVLPIPAQTTSLQNAKDDRRLQELESKIGGEIDQPIANLVGPSFSLFGDRRNQKTMSFGRRVPLISRPIIPIELDLLMDNDDERTKAKRFDDYGHMRFGKRGGDDQFDDYGHMRFGR | null | null | adult feeding behavior [GO:0008343]; adult locomotory behavior [GO:0008344]; inter-male aggressive behavior [GO:0002121]; larval locomotory behavior [GO:0008345]; multicellular organismal response to stress [GO:0033555]; neuromuscular junction development [GO:0007528]; neuropeptide signaling pathway [GO:0007218]; posit... | extracellular space [GO:0005615] | neuropeptide hormone activity [GO:0005184]; neuropeptide receptor binding [GO:0071855] | PF08257; | null | Gastrin/cholecystokinin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Involved in diverse biological roles including regulating aspects of gut function, satiety and food ingestion, hyperactivity, and aggression (PubMed:17632121, PubMed:24142897, PubMed:25187989). Regulates gut muscle contraction in adults but not in larvae (PubMed:17632121). Functions downstream of TfAP-2 and t... | Drosophila melanogaster (Fruit fly) |
P09041 | PGK2_MOUSE | MALSAKLTLDKVDLKGKRVIMRVDFNVPMKNNQITNNQRIKAAIPSIKHCLDNGAKSVVLMSHLGRPDGIPMPDKYSLEPVADELKSLLNKDVIFLKDCVGPEVEQACANPDNGSIILLENLRFHVEEEGKGKDSSGKKISADPAKVEAFQASLSKLGDVYVNDAFGTAHRAHSSTVGVNLPQKASGFLMKKELDYFSKALEKPERPFLAILGGAKVKDKIQLIKNMLDKVNFMIIGGGMAYTFLKELKNMQIGASLFDEEGATIVKEIMEKAEKNGVKIVFPVDFVTGDKFDENAKVGQATIESGIPSGWMGLDCGPES... | 2.7.2.3 | null | flagellated sperm motility [GO:0030317]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310] | cilium [GO:0005929]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; sperm fibrous sheath [GO:0035686] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; Evidence={ECO:0000305|PubMed:2823118}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. | null | null | FUNCTION: Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis (PubMed:19759366). {ECO:0000269|PubMed:19759366}. | Mus musculus (Mouse) |
P09052 | VASA1_DROME | MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDINNNNNIVEDVERKREFYIPPEPSNDAIEIFSSGIASGIHFSKYNNIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRPQ... | 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8026330}; | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; germ cell development [GO:0007281]; oogenesis [GO:0048477]; protein localization [GO:0008104]; secondary piRNA processing [GO:0140965] | cytoplasm [GO:0005737]; germ cell nucleus [GO:0043073]; nucleus [GO:0005634]; P granule [GO:0043186]; posterior cell cortex [GO:0061803] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX4/VASA subfamily | PTM: Ubiquitinated during oogenesis. Deubiquitinated by faf, which protects this protein from proteasome-mediated degradation. {ECO:0000269|PubMed:14588248}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:16949822, ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:8026330}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meios... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:8026330}; | null | null | null | null | FUNCTION: Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or struct... | Drosophila melanogaster (Fruit fly) |
P09055 | ITB1_MOUSE | MNLQLVSWIGLISLICSVFGQTDKNRCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIA... | null | null | axon extension [GO:0048675]; basement membrane organization [GO:0071711]; bicellular tight junction assembly [GO:0070830]; calcium-independent cell-matrix adhesion [GO:0007161]; cardiac cell fate specification [GO:0060912]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [... | acrosomal vesicle [GO:0001669]; adherens junction [GO:0005912]; basement membrane [GO:0005604]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; dendritic spine [GO:0043197]; external side of plasma membrane [GO:0009897]; filopodium [GO:0030175... | actin binding [GO:0003779]; alpha-actinin binding [GO:0051393]; C-X3-C chemokine binding [GO:0019960]; calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; integrin binding involv... | 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 | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... | Mus musculus (Mouse) |
P09056 | LIF_MOUSE | MKVLAAGIVPLLLLVLHWKHGAGSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFPNNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNPTAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQRKKLGCQLLGTYKQVISVVVQAF | null | null | animal organ regeneration [GO:0031100]; astrocyte differentiation [GO:0048708]; blood vessel remodeling [GO:0001974]; cell morphogenesis [GO:0000902]; cell population proliferation [GO:0008283]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; fibroblast proliferation [GO:0048144]; gene expression [GO:00... | cytosol [GO:0005829]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; leukemia inhibitory factor receptor binding [GO:0005146] | PF01291; | 1.20.1250.10; | LIF/OSM family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. | Mus musculus (Mouse) |
P09057 | DCOR_RAT | MGSFTKEEFDCHILDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDVLKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPPERIIYANPCKQVSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMGTEVGFSMYLLDIGGGFPGSEDTKLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKTVWKEQTGSDDEDESNEQTLMYYVND... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926}; | cell population proliferation [GO:0008283]; kidney development [GO:0001822]; polyamine metabolic process [GO:0006595]; positive regulation of cell population proliferation [GO:0008284]; putrescine biosynthetic process [GO:0009446]; putrescine biosynthetic process from ornithine [GO:0033387]; regulation of protein catab... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471] | ornithine decarboxylase activity [GO:0004586]; protein homodimerization activity [GO:0042803] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926}; | null | PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. | null | null | FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.... | Rattus norvegicus (Rat) |
P09064 | IF2B_YEAST | MSSDLAAELGFDPALKKKKKTKKVIPDDFDAAVNGKENGSGDDLFAGLKKKKKKSKSVSADAEAEKEPTDDIAEALGELSLKKKKKKTKDSSVDAFEKELAKAGLDNVDAESKEGTPSANSSIQQEVGLPYSELLSRFFNILRTNNPELAGDRSGPKFRIPPPVCLRDGKKTIFSNIQDIAEKLHRSPEHLIQYLFAELGTSGSVDGQKRLVIKGKFQSKQMENVLRRYILEYVTCKTCKSINTELKREQSNRLFFMVCKSCGSTRSVSSIKTGFQATVGKRRRM | null | null | formation of cytoplasmic translation initiation complex [GO:0001732]; formation of translation preinitiation complex [GO:0001731]; translational initiation [GO:0006413] | cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic translation initiation factor 2 complex [GO:0005850]; multi-eIF complex [GO:0043614]; ribosome [GO:0005840] | metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369] | PF01873; | 3.30.30.170; | EIF-2-beta/eIF-5 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}. | null | null | null | null | null | FUNCTION: Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09065 | HME1_MOUSE | MEEQQPEPKSQRDSGLGAVAAAAPSGLSLSLSPGASGSSGSDGDSVPVSPQPAPPSPPAAPCLPPLAHHPHLPPHPPPPPPPPPPPPQHLAAPAHQPQPAAQLHRTTNFFIDNILRPDFGCKKEQPLPQLLVASAAAGGGAAAGGGSRVERDRGQTGAGRDPVHSLGTRASGAASLLCAPDANCGPPDGSQPATAVSAGASKAGNPAAAAAAAAAAAAAAVAAAAAAASKPSDSGGGSGGNAGSPGAQGAKFPEHNPAILLMGSANGGPVVKTDSQQPLVWPAWVYCTRYSDRPSSGPRTRKLKKKKNEKEDKRPRTAFT... | null | null | adult locomotory behavior [GO:0008344]; cerebellum development [GO:0021549]; dopaminergic neuron differentiation [GO:0071542]; dorsal/ventral pattern formation [GO:0009953]; drinking behavior [GO:0042756]; embryonic brain development [GO:1990403]; embryonic forelimb morphogenesis [GO:0035115]; embryonic limb morphogene... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF10525;PF00046; | 1.10.10.60; | Engrailed homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Required for proper formation of the apical ectodermal ridge and correct dorsal-ventral patterning in the limb. {ECO:0000269|PubMed:8684466}. | Mus musculus (Mouse) |
P09066 | HME2_MOUSE | MEEKDSKPSETAAEAQRQPEPSSGGGSGGGSSPSDSDTGRRRALMLPEVLQAPGNHQHPHRITNFFIDNILRPEFGRRKDAGTCCAGAGGARGGEGGAGTTEGGGGGAGGAEQLLGARESRPNPACAPSAGGTLSAAAGDPAVDGEGGSKTLSLHGGAKKPGDPGGSLDGVLKARGLGGGDLSVSSDSDSSQASATLGAQPMLWPAWVYCTRYSDRPSSGPRSRKPKKKNPNKEDKRPRTAFTAEQLQRLKAEFQTNRYLTEQRRQSLAQELSLNESQIKIWFQNKRAKIKKATGNKNTLAVHLMAQGLYNHSTTAKEGK... | null | null | dopaminergic neuron differentiation [GO:0071542]; embryonic brain development [GO:1990403]; hindbrain development [GO:0030902]; midbrain development [GO:0030901]; negative regulation of neuron apoptotic process [GO:0043524]; neuron development [GO:0048666]; neuron differentiation [GO:0030182]; positive regulation of tr... | fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF10525;PF00046; | 1.10.10.60; | Engrailed homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | null | Mus musculus (Mouse) |
P09067 | HXB5_HUMAN | MSSYFVNSFSGRYPNGPDYQLLNYGSGSSLSGSYRDPAAMHTGSYGYNYNGMDLSVNRSSASSSHFGAVGESSRAFPAPAQEPRFRQAASSCSLSSPESLPCTNGDSHGAKPSASSPSDQATSASSSANFTEIDEASASSEPEEAASQLSSPSLARAQPEPMATSTAAPEGQTPQIFPWMRKLHISHDMTGPDGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSLATAGSAFQP | null | null | anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; endothelial cell differentiation [GO:0045446]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P09077 | SCR_DROME | MDPDCFAMSSYQFVNSLASCYPQQMNPQQNHPGAGNSSAGGSGGGAGGSGGVVPSGGTNGGQGSAGAATPGANDYFPAAAAYTPNLYPNTPQAHYANQAAYGGQGNPDMVDYTQLQPQRLLLQQQQQQQQQQHAHAAAAVAAQQQQQLAQQQHPQQQQQQQQANISCKYANDPVTPGGSGGGGVSGSNNNNNSANSNNNNSQSLASPQDLSTRDISPKLSPSSVVESVARSLNKGVLGGSLAAAAAAAGLNNNHSGSGVSGGPGNVNVPMHSPGGGDSDSESDSGNEAGSSQNSGNGKKNPPQIYPWMKRVHLGTSTVNA... | null | null | anterior/posterior pattern specification [GO:0009952]; midgut development [GO:0007494]; positive regulation of transcription by RNA polymerase II [GO:0045944]; salivary gland boundary specification [GO:0007432]; sex comb development [GO:0045498] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-s... | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Controls the segmental transformation of the first to the second thoracic segment (prothorax to mesothorax) and of the labial palps ... | Drosophila melanogaster (Fruit fly) |
P09079 | HXB5_MOUSE | MSSYFVNSFSGRYPNGPDYQLLNYGSGSSLSGSYRDPAAMHTGSYGYNYNGMDLSVNRSSASSSHFGAVGESSRAFPASAQEPRFRQATSSCSLSSPESLPCTNGDSHGAKPSASSPSDQATPASSSANFTEIDEASASSEPEEAASQLSSPSLARAQPEPMATSTAAPEGQTPQIFPWMRKLHISHDMTGPDGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSLATAGSAFQP | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system development [GO:0048706]; embryonic skeletal system morphogenesis [GO:0048704]; endothelial cell differentiation [GO:0045446]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcriptio... | cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09081 | BCD_DROME | MAQPPPDQNFYHHPLPHTHTHPHPHSHPHPHSHPHPHHQHPQLQLPPQFRNPFDLLFDERTGAINYNYIRPYLPNQMPKPDVFPSEELPDSLVMRRPRRTRTTFTSSQIAELEQHFLQGRYLTAPRLADLSAKLALGTAQVKIWFKNRRRRHKIQSDQHKDQSYEGMPLSPGMKQSDGDPPSLQTLSLGGGATPNALTPSPTPSTPTAHMTEHYSESFNAYYNYNGGHNHAQANRHMHMQYPSGGGPGPGSTNVNGGQFFQQQQVHNHQQQLHHQGNHVPHQMQQQQQQAQQQQYHHFDFQQKQASACRVLVKDEPEADY... | null | null | anterior region determination [GO:0007355]; anterior/posterior axis specification [GO:0009948]; anterior/posterior axis specification, embryo [GO:0008595]; maternal determination of anterior/posterior axis, embryo [GO:0008358]; negative regulation of translation [GO:0017148]; oogenesis [GO:0048477]; positive regulation... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; mRNA 3'-UTR binding [GO:0003730]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; translation repres... | PF00046; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Segment polarity transcription factor that provides positional cues for the development of head and thoracic segments (PubMed:24637116, PubMed:2901954, PubMed:35363606). Forms a protein concentration gradient that patterns the anterior-posterior axis during embryogenesis and promotes the expression of anterio... | Drosophila melanogaster (Fruit fly) |
P09082 | GSB_DROME | MAVSALNMTPYFGGYPFQGQGRVNQLGGVFINGRPLPNHIRRQIVEMAAAGVRPCVISRQLRVSHGCVSKILNRFQETGSIRPGVIGGSKPRVATPDIESRIEELKQSQPGIFSWEIRAKLIEAGVCDKQNAPSVSSISRLLRGSSGSGTSHSIDGILGGGAGSVGSEDESEDDAEPSVQLKRKQRRSRTTFSNDQIDALERIFARTQYPDVYTREELAQSTGLTEARVQVWFSNRRARLRKQLNTQQVPSFAPTSTSFGATPTTSAAPAPNMGMSLYSSQSWPSSGAYENHAAYGGSVASMSPASSTSGTSSAAHSPVQ... | null | null | chemical synaptic transmission [GO:0007268]; neurogenesis [GO:0022008]; regulation of synaptic activity [GO:0060025]; regulation of transcription by RNA polymerase II [GO:0006357]; salivary gland morphogenesis [GO:0007435]; segment polarity determination [GO:0007367]; ventral cord development [GO:0007419] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; synapse [GO:0045202] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046;PF00292; | 1.10.10.60;1.10.10.10; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Expressed in segmentally repeating pattern to define the polarity of embryonic segments. {ECO:0000269|PubMed:3123319}. | Drosophila melanogaster (Fruit fly) |
P09083 | GSBN_DROME | MDMSSANSLRPLFAGYPFQGQGRVNQLGGVFINGRPLPNHIRLKIVEMAASGVRPCVISRQLRVSHGCVSKILNRYQETGSIRPGVIGGSKPKVTSPEIETRIDELRKENPSIFSWEIREKLIKEGFADPPSTSSISRLLRGSDRGSEDGRKDYTINGILGGRDSDISDTESEPGIPLKRKQRRSRTTFTAEQLEALERAFSRTQYPDVYTREELAQTTALTEARIQVWFSNRRARLRKHSGGSNSGLSPMNSGSSNVGVGVGLSGATAPLGYGPLGVGSMAGYSPAPGTTATGAGMNDGVHHAAHAPSSHHSAATAAAA... | null | null | neurogenesis [GO:0022008]; regulation of transcription by RNA polymerase II [GO:0006357]; segment polarity determination [GO:0007367] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046;PF00292; | 1.10.10.60;1.10.10.10; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Expressed in a segmentally repeating pattern to define the polarity of embryonic segments. {ECO:0000269|PubMed:3123319}. | Drosophila melanogaster (Fruit fly) |
P09084 | PAX1_MOUSE | MKFTLGLGSRAWRVSWERAAAAAAGPGAGGALGSGSLRVSSRRGPRLARALPLCLSGGGGARALPDCAGPSPRRSGARQLAGPRAMEQTYGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPNVVKHIRDYKQGDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGSLAQPGPYEASKQPPPQPALPYNHIYQYPYPSPVSPTGTKMGTHPGVPGSAGHVSIPRSWPSAHSVSNILGIRTFMEQTGALAGSEGAAYSPKMEDWAGVNRA... | null | null | animal organ morphogenesis [GO:0009887]; bone morphogenesis [GO:0060349]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; CD8-positive, alpha-beta T cell differentiation [GO:0043374]; cell population proliferation [GO:0008283]; parathyroid gland development [GO:0060017]; pattern specification process [GO:... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00292; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column. | Mus musculus (Mouse) |
P09085 | CAD_DROME | MVSHYYNTLPYTQKHSAANLAYASAAGQPWNWTPNYHHTPPNHQFLGDVDSSHAAHHAAAAHQMYYNSHHMFHSAAAASAGEWHSPASSTADNFVQNVPTSAHQLMQQHHHHHAHASSSSASSGSSSSGGAPGAPQLNETNSSIGVGGAGGGGGVGGATDGGPGSAPPNHQQHIAEGLPSPPITVSGSEISSPGAPTSASSPHHHLAHHLSAVANNNNNNNNNNNSPSTHNNNNNNNSVSNNNRTSPSKPPYFDWMKKPAYPAQPQPGKTRTKDKYRVVYTDFQRLELEKEYCTSRYITIRRKSELAQTLSLSERQVKIW... | null | null | analia development [GO:0007487]; animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; blastoderm segmentation [GO:0007350]; cell differentiation [GO:0030154]; gastrulation involving germ band extension [GO:0010004]; genital disc anterior/posterior pattern formation [GO:0035224]; ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046; | 1.10.10.60; | Caudal homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:2433048}. | null | null | null | null | null | FUNCTION: Caudal (cad) is one of a number of transcription factors controlling segmentation of the embryo. Further transcriptional regulation via a 5' flanking region containing DNA replication-related elements (DRE) and by dref also regulated by trh and tgo via the CNS midline element. Alongside Bicoid (bcd), caudal f... | Drosophila melanogaster (Fruit fly) |
P09086 | PO2F2_HUMAN | MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAVTRPTLPDPHLSHPQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQ... | null | null | cellular response to virus [GO:0098586]; humoral immune response [GO:0006959]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:19... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3') (PubMed:2904654, PubMed:7859290). Regulates IL6 expression in B cells with POU2AF1 (By similarity). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression (PubMed:2901913, PubMed... | Homo sapiens (Human) |
P09087 | ABDB_DROME | MQQHHLQQQQQQQQQQEQQHLQEQQQHLQQLHHHAHHHLPQPLHTTSHHHSAHPHLQQQQQQQQHAVVASSPSSVLQQQQQQSTPTTHSTPTHAVMYEDPPPVPLVAVQQQHLPAPQQQQQLQQQQQQQQQQLATTPVAGALSPAQTPTGPSAQQQQHLTSPHHQQLPQQQTPNSVASGASSNLQQQQQQQNAAVAPGQTQIVAPTTASVSPSSVSSQKEDINMSIQLAPLHIPAIRAGPGFETDTSAAVKRHTAHWAYNDEGFNQHYGSGYYDRKHMFAYPYPETQFPVGQYWGPNYRPDQTTSAAAAAAYMNEAERHV... | null | null | determination of genital disc primordium [GO:0035225]; external genitalia morphogenesis [GO:0035261]; female genitalia development [GO:0030540]; genital disc anterior/posterior pattern formation [GO:0035224]; genital disc sexually dimorphic development [GO:0035263]; germ cell migration [GO:0008354]; gonadal mesoderm de... | nucleus [GO:0005634]; polytene chromosome band [GO:0005704] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00046; | 1.10.10.60; | Abd-B homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Drosophila melanogaster (Fruit fly) |
P09088 | MEC3_CAEEL | MEMLESKPLSAISMVIDSIGVDHENQNKCNCCNEQIYDRYIYRMDNRSYHENCVKCTICESPLAEKCFWKNGRIYCSQHYYKDHSIHRCAGCKKGVSPTDMVYKLKAGLVFHVECHCCSLCGRHLSPGEQILVDDTMMTVSCMSHYPPQMDDNAPGAIGSAVDIPSCSTENPIAPYPIDESFSSAFQVKKEVDAYGYNFEHYSFSDFCDDDSRMLKRRGPRTTIKQNQLDVLNEMFSNTPKPSKHARAKLALETGLSMRVIQVWFQNRRSKERRLKHLCNYLRHYEQRGLIPPPIHFRNEEMDTTDFNAFCGNFEEEDDE... | null | null | mechanosensory behavior [GO:0007638]; neuron differentiation [GO:0030182]; neuron projection organization [GO:0106027]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response ... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF00046;PF00412; | 2.10.110.10;1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:10899123, PubMed:26096732). Specifies differentiation of the set of six touch receptor neurons (TRNs) (PubMed:2898300). May positively modulate expression of both its own gene and also of homeobox ARX homolog alr-1 in TRNs, forming a positive feedback loop with alr-1, thereby rest... | Caenorhabditis elegans |
P09099 | XYLB_ECOLI | MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA... | 2.7.1.-; 2.7.1.17 | null | D-xylose catabolic process [GO:0042843]; xylulose catabolic process [GO:0005998] | null | 1-deoxy-D-xylulose kinase activity [GO:0103020]; ATP binding [GO:0005524]; D-xylulokinase activity [GO:0004856]; protein homodimerization activity [GO:0042803] | PF02782;PF00370; | 3.30.420.40; | FGGY kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+); Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140, ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216; EC=2.7.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_02220, ECO:0000269|PubMed:17123542}; CATALYTIC ACTIVITY: Reaction=1-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for D-xylulose {ECO:0000269|PubMed:17123542}; KM=14 mM for D-ribulose {ECO:0000269|PubMed:17123542}; KM=127 mM for xylitol {ECO:0000269|PubMed:17123542}; KM=141 mM for D-arabitol {ECO:0000269|PubMed:17123542}; Note=kcat is 255 sec(-1) with D-xylulose as sub... | null | null | null | FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate (PubMed:17123542). Also catalyzes the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency (PubMed:11168365). Can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the ot... | Escherichia coli (strain K12) |
P09102 | PDIA1_CHICK | MAVVRVRAIVALLCLVAALGLAEPLEEEDGVLVLRAANFEQALAAHRHLLVEFYAPWCGHCKALAPEYAKAAAQLKAEGSEIRLAKVDATEEAELAQQFGVRGYPTIKFFRNGDKAAPREYTAGREADDIVSWLKKRTGPAATTLTDAAAAETLVDSSEVVVIGFFKDVTSDAAKEFLLAAESVDDIPFGISSSADVFSKYQLSQDGVVLFKKFDEGRNNFEGDLTKDNLLNFIKSNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLDNFKTAAGNFKGKILFIFIDSDHSDNQRILEFFGLKKEECPAV... | 5.3.4.1 | null | 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] | protein disulfide isomerase activity [GO:0003756] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; | 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... | Gallus gallus (Chicken) |
P09103 | PDIA1_MOUSE | MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFEEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDVESDSAKQFLLAAEAIDDIPFGITSNSGVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSSFKRAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLI... | 5.3.4.1 | null | cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; insulin processing [GO:0030070]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of viral entry into ho... | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; lamellipodium [GO:0030027... | actin binding [GO:0003779]; enzyme binding [GO:0019899]; integrin binding [GO:0005178]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; protein-disulfide reducta... | 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:0000269|PubMed:21670307}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be... | 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... | Mus musculus (Mouse) |
P09104 | ENOG_HUMAN | MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; perikaryon [GO:0043204]; phosphopyruvate hydratase complex [GO:0000015]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. | null | null | FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
P09105 | HBAT_HUMAN | MALSAEDRALVRALWKKLGSNVGVYTTEALERTFLAFPATKTYFSHLDLSPGSSQVRAHGQKVADALSLAVERLDDLPHALSALSHLHACQLRVDPASFQLLGHCLLVTLARHYPGDFSPALQASLDKFLSHVISALVSEYR | null | null | hydrogen peroxide catabolic process [GO:0042744]; oxygen transport [GO:0015671] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
P09108 | RAPSN_TETCF | MGQDQTKQQIEKGLQLYQANETGKALEIWQQVVERSTELPGRFRALGCLITAHSEMGKYEDMLRFAVAQSEAARQMGDPERVTEAYLNLARGHEKLCEFSEAVAYCRTCLGAEGGPLRLQFNGQVCLSMGNAFLGLSAFQKALECFEKALRYAHGNDDKMLECRVCCSLGAFYVQLKDYEKALFFPCKSAELVADYGRGWSLKYKAMSRYHMAAAYRKLGRMDDAMECCEESMKIALQHQDRPLQALCLLCFADIHRHRSDIGKALPRYESSLNIMTEIGNRLGQAHVLLNIAKCWMTEKKLDKTLGVVQKAEELADAVG... | null | null | positive regulation of neuromuscular synaptic transmission [GO:1900075]; synaptic transmission, cholinergic [GO:0007271] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211] | acetylcholine receptor binding [GO:0033130]; metal ion binding [GO:0046872]; protein-membrane adaptor activity [GO:0043495] | PF10579;PF13424;PF13639; | 1.25.40.10;3.30.40.10; | RAPsyn family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of postsynaptic membranes. | null | null | null | null | null | FUNCTION: Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin (By similarity). {ECO:0000250}. | Tetronarce californica (Pacific electric ray) (Torpedo californica) |
P09110 | THIK_HUMAN | MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIG... | 2.3.1.155; 2.3.1.16; 2.3.1.9 | null | alpha-linolenic acid metabolic process [GO:0036109]; bile acid metabolic process [GO:0008206]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; phenylacetate catabolic process [GO:0010124]; very long-chain fatty acid metabolic process [GO:0000038] | cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; specific granule lumen [GO:0035580] | acetate CoA-transferase activity [GO:0008775]; acetyl-CoA C-acetyltransferase activity [GO:0003985]; acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]; palmitoyl-CoA oxidase activity [GO:0016401] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Ev... | null | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}. | null | null | FUNCTION: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) (PubMed:11734571, PubMed:2882519). Plays an important role in fatty acid peroxisomal beta-oxidation (PubMed:11734571, PubMed:2882519). Catalyzes the cleavage of short, medium, long, and very long straight chain 3-... | Homo sapiens (Human) |
P09114 | ILVB2_TOBAC | MAAAAAAPSPSFSKTLSSSSSKSSTLLPRSTFPFPHHPHKTTPPPLHLTPTHIHSQRRRFTISNVISTTQKVSETQKAETFVSRFAPDEPRKGSDVLVEALEREGVTDVFAYPGGASMEIHQALTRSSIIRNVLPRHEQGGVFAAEGYARATGFPGVCIATSGPGATNLVSGLADALLDSVPIVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVVREAFFLARSGRPGPVLIDVPKDIQQQLVIPDWDQPMRLPGYMSRLPKLPNEMLLEQIVRLISESKKPVLYVGGGCSQSSEELRRFVELTGI... | 2.2.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; response to herbicide [GO:0009635]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; chloroplast [GO:0009507]; mitochondrion [GO:0005739] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. | null | null | null | Nicotiana tabacum (Common tobacco) |
P09117 | ALDOC_RAT | MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDN... | 4.1.2.13 | null | animal organ regeneration [GO:0031100]; epithelial cell differentiation [GO:0030855]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; response to hypoxia [GO:0001666]; response to organic cyclic compound [GO:0014070]; response to organonitrogen co... | axon [GO:0030424]; cytosol [GO:0005829]; 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 | Rattus norvegicus (Rat) |
P09118 | URIC_RAT | MAHYHDDYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKFKGIKSIETFAMNICEHFLSSFSHVTRAHVYVEEVPWKRFEKNGVKHVHAFIHTPTGTHFCDVEQVRNGPPIIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYQNRDVDFEATWGAVRDIVLKKFAGPYDRGEYSPSVQKTLYDIQVLTLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVRRKLPSRL | 1.7.3.3 | null | purine nucleobase catabolic process [GO:0006145]; urate catabolic process [GO:0019628] | peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | urate oxidase activity [GO:0004846] | PF01014; | 3.10.270.10; | Uricase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:3194410}. | CATALYTIC ACTIVITY: Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2; Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3; Evidence={ECO:0000269|PubMed:1520291}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.33 uM for urate {ECO:0000269|PubMed:1520291}; | PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. {ECO:0000305|PubMed:1520291}. | null | null | FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. {ECO:0000269|PubMed:1520291}. | Rattus norvegicus (Rat) |
P09119 | CDC6_YEAST | MSAIPITPTKRIRRNLFDDAPATPPRPLKRKKLQFTDVTPESSPEKLQFGSQSIFLRTKALLQKSSELVNLNSSDGALPARTAEYEQVMNFLAKAISEHRSDSLYITGPPGTGKTAQLDMIIRQKFQSLPLSLSTPRSKDVLRHTNPNLQNLSWFELPDGRLESVAVTSINCISLGEPSSIFQKIFDSFQDLNGPTLQIKNMQHLQKFLEPYHKKTTFVVVLDEMDRLLHANTSETQSVRTILELFLLAKLPTVSFVLIGMANSLDMKDRFLSRLNLDRGLLPQTIVFQPYTAEQMYEIVIQKMSSLPTIIFQPMAIKFA... | null | null | cell division [GO:0051301]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic DNA replication checkpoint signaling [GO:0033314]; pre-replicative complex assembly involved in nuclear cell cycle DNA replication [GO:0006267]; regulation of DNA-templated DNA replication in... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; DNA replication preinitiation complex [GO:0031261]; nuclear pre-replicative complex [GO:0005656]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF13401; | 1.10.8.60;3.40.50.300;1.10.10.10; | CDC6/cdc18 family | PTM: Ubiquitinated by the E3 ubiquitin ligase complex SCF(CDC4), DIA2, and TOM1; and targeted to the 26S proteasome for degradation.; PTM: Phosphorylated by CDC28. Phosphorylation is a prerequisite to ubiquitination and degradation. {ECO:0000269|PubMed:10512865, ECO:0000269|PubMed:10734126}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Plays a crucial role in forming the pre-replicative complexes. Interacts with the origin recognition complex (ORC) and MCM2-7 helicase complex leading to the linking of those complexes and loading of the replicative helicase MCM2-7 onto the pre-replicative complexes. Required for the initiation of DNA replica... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09124 | G3P1_BACSU | MAVKVGINGFGRIGRNVFRAALNNPEVEVVAVNDLTDANMLAHLLQYDSVHGKLDAEVSVDGNNLVVNGKTIEVSAERDPAKLSWGKQGVEIVVESTGFFTKRADAAKHLEAGAKKVIISAPANEEDITIVMGVNEDKYDAANHDVISNASCTTNCLAPFAKVLNDKFGIKRGMMTTVHSYTNDQQILDLPHKDYRRARAAAENIIPTSTGAAKAVSLVLPELKGKLNGGAMRVPTPNVSLVDLVAELNQEVTAEEVNAALKEAAEGDLKGILGYSEEPLVSGDYNGNKNSSTIDALSTMVMEGSMVKVISWYDNESGYS... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096] | cytoplasm [GO:0005737] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: In response to oxidative stress, the active site Cys likely reacts with bacillithiol (BSH) to form mixed disulfides to protect the Cys residue against overoxidation. S-bacillithiolation presumably leads to loss of catalytic activity. Debacillithiolation by monothiol bacilliredoxin BrxC restores the activity. {ECO:... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10658653}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000269|PubMed:10799476}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:10799476}. | null | null | FUNCTION: Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is t... | Bacillus subtilis (strain 168) |
P09130 | TRAD1_ECOLI | MSFNAKDMTQGGQIASMRIRMFSQIANIMLYCLFIFFWILVGLVLWIKISWQTFVNGCIYWWCTTLEGMRDLIKSQPVYEIQYYGKTFRMNAAQVLHDKYMIWCSEQLWSAFVLAAVVALVICLITFFVVSWILGRQGKQQSENEVTGGRQLTDNPKDVARMLKKDGKDSDIRIGDLPIIRDSEIQNFCLHGTVGAGKSEVIRRLANYARQRGDMVVIYDRSGEFVKSYYDPSIDKILNPLDARCAAWDLWKECLTQPDFDNTANTLIPMGTKEDPFWQGSGRTIFAEAAYLMRNDPNRSYSKLVDTLLSIKIEKLRTYL... | null | null | unidirectional conjugation [GO:0009291] | plasma membrane [GO:0005886] | ATP binding [GO:0005524] | PF12615;PF10412; | 1.10.8.80;3.40.50.300; | TrwB coupling protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9324263}; Multi-pass membrane protein {ECO:0000269|PubMed:9324263}. | null | null | null | null | null | FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Couples the transferosome to a type IV secretion system. Probably forms a p... | Escherichia coli (strain K12) |
P09132 | SRP19_HUMAN | MACAAARSPADQDRFICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREWNRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK | null | null | cotranslational protein targeting to membrane [GO:0006613]; SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition [GO:0006617] | cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; signal recognition particle [GO:0048500]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786] | 7S RNA binding [GO:0008312]; RNA binding [GO:0003723] | PF01922; | 3.30.56.30; | SRP19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10618370, ECO:0000269|PubMed:11682607}. Nucleus, nucleolus {ECO:0000269|PubMed:10618370, ECO:0000269|PubMed:11682607}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11682607}. Note=Although the signal recognition particle complex acts in the cytoplasm, it assembles at leas... | null | null | null | null | null | FUNCTION: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). Binds directly to 7SL RNA (By similarity). Mediates binding of SRP54 to the SRP complex (By ... | Homo sapiens (Human) |
P09139 | AGT1_RAT | MFRMLAKASVTLGSRAASWVRNMGSHQLLVPPPEALSKPLSIPKRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMFQIMDEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLVGTNGIWGIRAAEIAERIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDILYSGSQKVLNAPPGISLISFNDKAKSKVYSRKTKPVSFYTDITYLSKLWGCEGKTRVIHHTLPVISLYCLRESLALISEQGLENSWRRHREATAHL... | 2.6.1.44; 2.6.1.51 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P21549}; | glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glyoxylate catabolic process [GO:0009436]; glyoxylate metabolic process [GO:0046487]; L-alanine catabolic process [GO:0042853]; L-cysteine catabolic process [GO:0019448]; L-serine metabolic process [GO:0006563]; Notch signaling pathway [GO:0007... | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | alanine-glyoxylate transaminase activity [GO:0008453]; amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621]; pyridoxal phosphate binding [GO:0030170]; serine-pyruvate transaminase activity [GO:0004760]; transaminas... | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome {ECO:0000250|UniProtKB:P21549}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix {ECO:0000269|PubMed:6725236}. | CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine; Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51; Evidence={ECO:0000269|PubMed:10347151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853; Ev... | null | null | null | null | FUNCTION: [Isoform Peroxisomal]: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification. {ECO:0000250|UniProtKB:P21549}.; FUNCTION: [Isoform Mitochondrial]: Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-ser... | Rattus norvegicus (Rat) |
P09143 | SUCD_THETH | MILVNRETRVLVQGITGREGQFHTKQMLDYGTKIVAGVTPGKGGTEVLGVPVYDTVKEAVAHHEVDASIIFVPAPAAADAALEAAHAGIPLIVLITEGIPTLDMVRAVEEIKALGSRLIGGNCPGIISAEETKIGIMPGHVFKRGRVGIISRSGTLTYEAAAALSQAGLGTTTTVGIGGDPVIGTTFKDLLPLFNEDPETEAVVLIGEIGGSDEEEAAAWVKDHMKKPVVGFIGGRSAPKGKRMGHAGAIIMGNVGTPESKLRAFAEAGIPVADTIDEIVELVKKALG | 6.2.1.4 | null | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; succinate-CoA ligase complex (ADP-forming) [GO:0009361] | nucleotide binding [GO:0000166]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776] | PF02629;PF00549; | 3.40.50.720;3.40.50.261; | Succinate/malate CoA ligase alpha subunit family | null | null | CATALYTIC ACTIVITY: Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000269|PubMed:22751660}; PhysiologicalDirection=right-to-left; Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=121 uM for ATP {ECO:0000269|PubMed:22751660}; KM=24 uM for GTP {ECO:0000269|PubMed:22751660}; KM=1.4 mM for succinate {ECO:0000269|PubMed:22751660}; KM=5.5 uM for CoA {ECO:0000269|PubMed:22751660}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000305|PubMed:22751660}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.4. {ECO:0000269|PubMed:22751660}; | null | FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... | Thermus thermophilus |
P09144 | PSAB_CHLRE | MATKLFPKFSQGLAQDPTTRRIWYGLAMAHDFESHDGMTEENLYQKIFASHFGQLSIIFLWTSGNLFHVAWQGNFEQWVTDPVHIRPIAHAIWDPHFGQPAVEAFTRGGASGPVNISTSGVYQWWYTIGMRTNQDLYVGSVFLALVSAIFLFAGWLHLQPNFQPSLSWFKDAESRLNHHLSGLFGVSSLAWTGHLVHVAIPESRGQHVGWDNFLSVLPHPQGLTPFFTGNWAAYAQSPDTASHVFGTAQGSGQAILTFLGGFHPQTQSLWLTDMAHHHLAIAVIFIVAGHMYRTNFGIGHRMQAILEAHTPPSGSLGAGH... | 1.97.1.12 | COFACTOR: Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center. {ECO:0000250}; | photosynthesis [GO:0015979] | chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522] | 4 iron, 4 sulfur cluster binding [GO:0051539]; chlorophyll binding [GO:0016168]; electron transfer activity [GO:0009055]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491] | PF00223; | 1.20.1130.10; | PsaA/PsaB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChE... | null | null | null | null | FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair ... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P09147 | GALE_ECOLI | MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKNFIFSSSATVYGDQPKIPYVESFPTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNLMPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKLANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDE... | 5.1.3.2 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:12019271, ECO:0000269|PubMed:8241178, ECO:0000269|PubMed:8611497, ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8652544, ECO:0000269|PubMed:8931134, ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9708982}; | carbohydrate metabolic process [GO:0005975]; colanic acid biosynthetic process [GO:0009242]; galactose catabolic process via UDP-galactose [GO:0033499]; galactose metabolic process [GO:0006012] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; NAD+ binding [GO:0070403]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]; UDP-glucose 4-epimerase activity [GO:0003978] | PF01370; | 3.40.50.720;3.90.25.10; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; Evidence={ECO:0000269|PubMed:14235524}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for UDP-Gal (at pH 8.5) {ECO:0000269|PubMed:14235524, ECO:0000269|PubMed:8241178, ECO:0000269|PubMed:9271498}; KM=160 uM for UDP-Gal (at pH 8.5 and 27 degrees Celsius) {ECO:0000269|PubMed:14235524, ECO:0000269|PubMed:8241178, ECO:0000269|PubMed:9271498}; KM=2... | PATHWAY: Carbohydrate metabolism; galactose metabolism. | null | null | FUNCTION: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose. {ECO:0000269|PubMed:14235524}. | Escherichia coli (strain K12) |
P09148 | GAL7_ECOLI | MTQFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQVLPAHDPDCFLCAGNVRVTGDKNPDYTGTYVFTNDFAALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQKEYFAEQKSPMLVDYVQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAHVLRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLA... | 2.7.7.12 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869}; Note=Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role. {ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869}; | galactose catabolic process via UDP-galactose [GO:0033499] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ferrous iron binding [GO:0008198]; galactokinase activity [GO:0004335]; UDP-glucose:hexose-1-phosphate uridylyltransferase activity [GO:0008108]; zinc ion binding [GO:0008270] | PF02744;PF01087; | 3.30.428.10; | Galactose-1-phosphate uridylyltransferase type 1 family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989, ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=2.7.7.12; Evidence={ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:10820011, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for uridine 5'-diphosphate glucose {ECO:0000269|PubMed:10820011}; KM=0.303 mM for galactose-1-phosphate {ECO:0000269|PubMed:10820011}; KM=0.121 mM for uridine 5'-diphosphate galactose {ECO:0000269|PubMed:10820011}; KM=0.157 mM for glucose-1-phosphate {ECO:00... | PATHWAY: Carbohydrate metabolism; galactose metabolism. | null | null | null | Escherichia coli (strain K12) |
P09152 | NARG_ECOLI | MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHL... | 1.7.5.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; COFACTOR: Name=Mo-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60539; Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126] | membrane [GO:0016020]; NarGHI complex [GO:0044799] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase activity [GO:0008940] | PF00384;PF01568;PF14710; | 3.40.50.12440;4.10.1200.10; | Prokaryotic molybdopterin-containing oxidoreductase family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; | null | null | null | null | FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. | Escherichia coli (strain K12) |
P09158 | SPEE_ECOLI | MAEKKQWHETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVTRHKNVESITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFKLVIDDGVNFVNQTSQTFDVIISDCTDPIGPGESLFTSAFYEGCKRCLNPGGIFVAQNGVCFLQQEEAIDSHRKLSHYFSDVGFYQAAIPTYYGGIMTFAWATDNDALRHLSTEIIQARFLASGLKCRYYNPAIHTAAFALPQYLQDALASQPS | 2.5.1.-; 2.5.1.16; 2.5.1.22; 2.5.1.79 | null | spermidine biosynthetic process [GO:0008295] | cytosol [GO:0005829] | cadaverine aminopropyltransferase activity [GO:0043918]; protein homodimerization activity [GO:0042803]; spermidine synthase activity [GO:0004766]; spermine synthase activity [GO:0016768]; thermospermine synthase activity [GO:0010487] | PF17284;PF01564; | 2.30.140.10;3.40.50.150; | Spermidine/spermine synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}. | CATALYTIC ACTIVITY: Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 uM for S-adenosylmethionine {ECO:0000269|PubMed:4572733}; KM=12 uM for putrescine {ECO:0000269|PubMed:4572733}; KM=77.77 uM for putrescine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:23001854}; KM=84.98 uM for S-adenosylmethionine (at pH 7.5 and 37 d... | PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00198}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23001854}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:23001854}; | FUNCTION: Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer (ping-pong mechanism) of a propylamine group from the amino donor S-adenosyl... | Escherichia coli (strain K12) |
P09167 | AERA_AERHY | MQKIKLTGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIEL... | null | null | null | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | identical protein binding [GO:0042802]; toxin activity [GO:0090729] | PF01117;PF03440; | 3.10.40.10;3.30.412.10;2.170.15.10; | Aerolysin family | PTM: Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. | SUBCELLULAR LOCATION: Secreted. Host cell membrane. Note=Secreted as a soluble precursor. | null | null | null | null | null | FUNCTION: Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. {ECO:0000269|PubMed:104... | Aeromonas hydrophila |
P09169 | OMPT_ECOLI | MRAKLLGIVLTTPIAISSFASTETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF | 3.4.23.49 | null | proteolysis [GO:0006508] | cell outer membrane [GO:0009279] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF01278; | 2.40.128.90; | Peptidase A26 family | null | SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.; EC=3.4.23.49; | null | null | null | null | FUNCTION: Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues. {ECO:0000269|PubMed:9683502}. | Escherichia coli (strain K12) |
P09172 | DOPO_HUMAN | MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFG... | 1.14.17.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:8546710, ECO:0000305|PubMed:27152332}; Note=Binds 2 copper ions per subunit. {ECO:0000305|PubMed:27152332}; | behavioral response to ethanol [GO:0048149]; blood vessel remodeling [GO:0001974]; chemical synaptic transmission [GO:0007268]; dopamine catabolic process [GO:0042420]; fear response [GO:0042596]; glucose homeostasis [GO:0042593]; homoiothermy [GO:0042309]; leukocyte mediated immunity [GO:0002443]; leukocyte migration ... | centriolar satellite [GO:0034451]; chromaffin granule lumen [GO:0034466]; chromaffin granule membrane [GO:0042584]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020... | catalytic activity [GO:0003824]; copper ion binding [GO:0005507]; dopamine beta-monooxygenase activity [GO:0004500]; L-ascorbic acid binding [GO:0031418] | PF03712;PF01082;PF03351; | 2.60.120.230;2.60.120.310; | Copper type II ascorbate-dependent monooxygenase family | PTM: N-glycosylated. {ECO:0000269|PubMed:27152332, ECO:0000269|PubMed:8546710}.; PTM: Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form. {ECO:0000250|UniProtKB:P15101}. | SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:7961964}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000269|PubMed:7961964}. Secreted {ECO:0000269|PubMed:7961964, ECO:0000269|PubMed:8546710}.; SUBCELLULAR LOCATION: C... | CATALYTIC ACTIVITY: Reaction=dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:19117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:59905, ChEBI:CHEBI:72587; EC=1.14.17.1; Evidence={ECO:0000269|PubMed:3443096, ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for tyramine {ECO:0000269|PubMed:8546710}; | PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1. {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:3443096, ECO:0000269|PubMed:8546710}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.2. {ECO:0000269|PubMed:8546710}; | null | FUNCTION: Catalyzes the hydroxylation of dopamine to noradrenaline (also known as norepinephrine), and is thus vital for regulation of these neurotransmitters. {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:3443096, ECO:0000269|PubMed:7961964, ECO:0000269|PubMed:8546710}. | Homo sapiens (Human) |
P09174 | CNRG_MOUSE | MNLEPPKGEIRSATRVIGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII | 3.1.4.35 | null | positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of MAPK cascade [GO:0043410]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886] | 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; spectrin binding [GO:0030507] | PF04868; | 4.10.1120.10; | Rod/cone cGMP-PDE gamma subunit family | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; | null | null | null | null | FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. | Mus musculus (Mouse) |
P09186 | LOX3_SOYBN | MLGGLLHRGHKIKGTVVLMRKNVLHVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRPVSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDGSGILGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKSDRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERVYDYDVYNDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYLPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVHGLYSGGIKLPTD... | 1.13.11.58 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. Iron is tightly bound. {ECO:0000255|PROSITE-ProRule:PRU00726}; | fatty acid biosynthetic process [GO:0006633]; lipid oxidation [GO:0034440]; oxylipin biosynthetic process [GO:0031408] | cytoplasm [GO:0005737] | linoleate 9S-lipoxygenase activity [GO:1990136]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; | null | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726}. | null | null | FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. | Glycine max (Soybean) (Glycine hispida) |
P09190 | PSBE_SYNY3 | MSGTTGERPFSDIVTSIRYWVIHSITIPMLFIAGWLFVSTGLAYDAFGTPRPDEYFTQTRQELPILQERYDINQEIQEFNQ | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:1904816}; Note=With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:34937700}... | photosynthetic electron transport chain [GO:0009767] | photosystem II reaction center [GO:0009539]; plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00283;PF00284; | 1.20.5.860; | PsbE/PsbF family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:34937700}. | null | null | null | null | null | FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core an... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
P09191 | PSBF_SYNY3 | MATQNPNQPVTYPIFTVRWLAVHTLAVPSVFFVGAIAAMQFIQR | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:34937700}; Note=With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:34937700}; | photosynthetic electron transport chain [GO:0009767] | photosystem II reaction center [GO:0009539]; plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506] | PF00283; | null | PsbE/PsbF family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:34937700}. | null | null | null | null | null | FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core an... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
P09192 | PSBD_SYNY3 | MTIAVGRAPVERGWFDVLDDWLKRDRFVFIGWSGLLLFPCAFMALGGWLTGTTFVTSWYTHGLASSYLEGANFLTVAVSSPADAFGHSLLFLWGPEAQGNLTRWFQIGGLWPFVALHGAFGLIGFMLRQFEISRLVGIRPYNAIAFSGPIAVFVSVFLMYPLGQSSWFFAPSFGVAGIFRFILFLQGFHNWTLNPFHMMGVAGILGGALLCAIHGATVENTLFEDGEDSNTFRAFEPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSSVGIVGLALNLRAYDFVSQELRAAEDPEFETFYTKNIL... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which... | photosynthetic electron transport in photosystem II [GO:0009772] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxygen evolving activity [GO:0010242] | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000269|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:34937700}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01383}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
P09193 | PSBC_SYNY3 | MVTLSNTSMVGGRDLPSTGFAWWSGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFEVAHFIPEKPMYEQGLILLPHIATLGWGVGPAGEVTDIFPFFVVGVLHLISSAVLGLGGIYHALRGPEVLEEYSSFFGYDWKDKNQMTNIIGYHLILLGCGALLLVFKAMFFGGVYDTWAPGGGDVRVITNPTLNPAIIFGYLLKAPFGGEGWIISVNNMEDIIGGHIWIGLICISGGIWHILTKPFGWARRALIWSGEAYLSYSLGALSLMGFIASVFVWFNNTAYPSEFYGPTGMEASQSQAFTFLVRDQRLGANIASAQG... | null | COFACTOR: Note=Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0... | photosynthetic electron transport in photosystem II [GO:0009772] | plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; metal ion binding [GO:0046872] | PF00421; | 1.10.10.670; | PsbB/PsbC family, PsbC subfamily | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000269|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:34937700, ECO:0000269|PubMed:9512353}. Note=PsbQ binds to the large ... | null | null | null | null | null | FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton ... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
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