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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P11557 | DAMX_ECOLI | MDEFKPEDELKPDPSDRRTGRSRQSSERSERTERGEPQINFDDIELDDTDDRRPTRAQKERNEEPEIEEEIDESEDETVDEERVERRPRKRKKAASKPASRQYMMMGVGILVLLLLIIGIGSALKAPSTTSSDQTASGEKSIDLAGNATDQANGVQPAPGTTSAENTQQDVSLPPISSTPTQGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPATVAPVRNGNASRDTAKTQTAERPSTTRPARQQAVIEPKKPQATVKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASP... | null | null | cytokinetic process [GO:0032506] | cell division site [GO:0032153]; cell septum [GO:0030428]; plasma membrane [GO:0005886] | enzyme activator activity [GO:0008047]; peptidoglycan binding [GO:0042834] | PF05036; | 3.30.70.1070; | DamX family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02021}. Note=Localizes at the septal ring (PubMed:19684127, PubMed:19880599, PubMed:23290046). Recruitment to the septal ring requires FtsZ (PubMed:19880599). {ECO:0000269|PubMed:19684127, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Non-essential cell division protein. {ECO:0000255|HAMAP-Rule:MF_02021, ECO:0000269|PubMed:19684127, ECO:0000269|PubMed:19880599}. | Escherichia coli (strain K12) |
P11558 | MCRA_METTM | MADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKRGIPQYNPDIGTPLGQRVLMPYQVSTTDTYVEGDDLHFVNNAAMQQMWDDIRRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMVETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVGDGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDFAYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPVRVSLDVVATGAMLYDQIWL... | 2.8.4.1 | COFACTOR: Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is act... | methanogenesis [GO:0015948] | cytoplasm [GO:0005737] | coenzyme-B sulfoethylthiotransferase activity [GO:0050524]; metal ion binding [GO:0046872] | PF02249;PF02745; | 3.30.70.470;1.20.840.10; | Methyl-coenzyme M reductase alpha subunit family | PTM: The alpha subunit contains six modified amino acids near the active site region (PubMed:27467699). Is methylated on His-257, Arg-271, Gln-400 and Cys-452, probably by the action of specific S-adenosylmethionine-dependent methyltransferases. Also contains a thioglycine at position 445, forming a thiopeptide bond (P... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}. | CATALYTIC ACTIVITY: Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for coenzyme B {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018}; KM=4 mM for methyl-coenzyme M {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018}; KM=169 uM for coenzyme B (at 25 degrees Celsius, under conditions in which the heterodisulfide pro... | PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. | null | null | FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of... | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
P11560 | MCRB_METTM | MAKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLEGIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDTNVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMYDANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVVAATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNLVFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAMWNAYAAAGLMAATMVNQGA... | 2.8.4.1 | COFACTOR: Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is act... | methanogenesis [GO:0015948] | cytoplasm [GO:0005737] | coenzyme-B sulfoethylthiotransferase activity [GO:0050524] | PF02241;PF02783; | 3.30.70.470;1.20.840.10; | Methyl-coenzyme M reductase beta subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}. | CATALYTIC ACTIVITY: Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO... | null | PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. | null | null | FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of... | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
P11562 | MCRG_METTM | MAQYYPGTTKVAQNRRNFCNPEYELEKLREISDEDVVKILGHRAPGEEYPSVHPPLEEMDEPEDAIREMVEPIDGAKAGDRVRYIQFTDSMYFAPAQPYVRSRAYLCRYRGADAGTLSGRQIIETRERDLEKISKELLETEFFDPARSGVRGKSVHGHSLRLDEDGMMFDMLRRQIYNKDTGRVEMVKNQIGDELDEPVDLGEPLDEETLMEKTTIYRVDGEAYRDDVEAVEIMQRIHVLRSQGGFNLE | 2.8.4.1 | COFACTOR: Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is act... | methanogenesis [GO:0015948] | cytoplasm [GO:0005737] | coenzyme-B sulfoethylthiotransferase activity [GO:0050524] | PF02240; | 3.90.320.20; | Methyl-coenzyme M reductase gamma subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}. | CATALYTIC ACTIVITY: Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO... | null | PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. | null | null | FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of... | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
P11568 | HGDC_ACIFV | MSIYTLGIDVGSTASKCIILKDGKEIVAKSLVAVGTGTSGPARSISEVLENAHMKKEDMAFTLATGYGRNSLEGIADKQMSELSCHAMGASFIWPNVHTVIDIGGQDVKVIHVENGTMTNFQMNDKCAAGTGRFLDVMANILEVKVSDLAELGAKSTKRVAISSTCTVFAESEVISQLSKGTDKIDIIAGIHRSVASRVIGLANRVGIVKDVVMTGGVAQNYGVRGALEEGLGVEIKTSPLAQYNGALGAALYAYKKAAK | 3.6.1.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:11106419, ECO:0000269|PubMed:11243821, ECO:0000269|PubMed:7607244}; Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000269|PubMed:11106419, ECO:0000269|PubMed:11243821, ECO:0000269|PubMed:7607244}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHE... | glutamate catabolic process via 2-hydroxyglutarate [GO:0019552] | null | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872] | PF01869; | 3.30.420.40; | HgdC family | null | null | 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; Evidence={ECO:0000305|PubMed:3691501, ECO:0000305|PubMed:7607244}; | null | PATHWAY: Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 4/5. {ECO:0000305|PubMed:7607244}. | null | null | FUNCTION: Involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity, whose the role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic am... | Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4) |
P11574 | VATB1_ARATH | MGTNDLDIEEGTLEIGMEYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGSTRRGQVLEVDGEKAVVQVFEGTSGIDNKFTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLVKRLEKTVDLLEDHGEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGR... | null | null | actin filament bundle assembly [GO:0051017]; actin filament capping [GO:0051693]; ATP metabolic process [GO:0046034]; glucose mediated signaling pathway [GO:0010255]; negative regulation of actin filament depolymerization [GO:0030835]; regulation of transcription by RNA polymerase II [GO:0006357]; vacuolar acidificatio... | Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; protein-containing complex [GO:0032991]; proton-transporting V-type ATPase, V1 domain [GO:0033180]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874; | 3.40.50.12240; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. | Arabidopsis thaliana (Mouse-ear cress) |
P11584 | ITBX_DROME | MILERNRRCQLALLMIAILAAIAGQTDAQKAAKLTAVSTCASKEKCHTCIQTEGCAWCMQPDFKGQSRCYQNTSSLCPEEFAYSPITVEQILVNNKLTNQYKAELAAGGGGSAMSGSSSSSYSSSSSSSSFYSQSSSGSSSASGYEEYSAGEIVQIQPQSMRLALRVNEKHNIKISYSQAEGYPVDLYYLMDLSKSMEDDKAKLSTLGDKLSETMKRITNNFHLGFGSFVDKVLMPYVSTIPKKLEHPCENCKAPYGYQNHMPLNNNTESFSNEVKNATVSGNLDAPEGGFDAIMQAIACRSQIGWREQARRLLVFSTDA... | null | null | actin filament organization [GO:0007015]; axon guidance [GO:0007411]; border follicle cell migration [GO:0007298]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; calcium-dependent cell-matrix adhesion [GO:0016340]; cell adhesion mediated by integrin [GO:0033627]; cell-cel... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; cell leading edge [GO:0031252]; cell surface [GO:0009986]; costamere [GO:0043034]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lateral plasma membrane [GO:0016328]; muscle tendon junction [GO:0005927]; plasma... | integrin binding [GO:0005178]; protein heterodimerization activity [GO:0046982] | PF07974;PF08725;PF07965;PF00362; | 4.10.1240.30;1.20.5.100;2.10.25.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Lateral cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Basal cell membrane {ECO:0000269|PubMed:19035354}; Single-p... | null | null | null | null | null | FUNCTION: Integrin alpha-PS1/beta-PS is a receptor for laminin (PubMed:7972082). Integrin alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m (PubMed:7924982, PubMed:7972082, PubMed:9660786). Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle (PubMed:154... | Drosophila melanogaster (Fruit fly) |
P11586 | C1TC_HUMAN | MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKPGKWMIQYNNLNLKTPVPSDI... | 1.5.1.5; 3.5.4.9; 6.3.4.3 | null | 10-formyltetrahydrofolate biosynthetic process [GO:0009257]; embryonic neurocranium morphogenesis [GO:0048702]; embryonic viscerocranium morphogenesis [GO:0048703]; heart development [GO:0007507]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; neural tube closure [GO:0001843]; ... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]; methylenetetrahydrofolate dehydroge... | PF01268;PF00763;PF02882; | 1.10.8.770;3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:3053686}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:18767138, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.3 uM for ATP {ECO:0000269|PubMed:10828945}; KM=364 uM for (6S)-5,6,7,8-tetrahydrofolate {ECO:0000269|PubMed:10828945}; KM=36.7 mM for formate {ECO:0000269|PubMed:10828945}; Vmax=13.2 umol/min/mg enzyme for the methylenetetrahydrofolate dehydrogenase activity {EC... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:18767138, ECO:0000269|PubMed:1881876}. | null | null | FUNCTION: Trifunctional enzyme that catalyzes the interconversion of three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and (6S)-10-formyltetrahydrofolate (PubMed:10828945, PubMed:18767138, PubMed:1881876). These derivatives of tetrahydrof... | Homo sapiens (Human) |
P11588 | MUP1_MOUSE | MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEKHGILRENIIDLSNANRCLQARE | null | null | aerobic respiration [GO:0009060]; cellular response to food [GO:0071240]; cellular response to lipid [GO:0071396]; cellular response to starvation [GO:0009267]; cellular response to testosterone stimulus [GO:0071394]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone activity [GO:0005186]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. | Mus musculus (Mouse) |
P11589 | MUP2_MOUSE | MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLEKSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAKLCEEHGILRENIIDLSNANRCLQARE | null | null | aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. | Mus musculus (Mouse) |
P11590 | MUP4_MOUSE | MKLLLCLGLTLVCIHAEEATSKGQNLNVEKINGEWFSILLASDKREKIEEHGSMRVFVEHIHVLENSLAFKFHTVIDGECSEIFLVADKTEKAGEYSVMYDGFNTFTILKTDYDNYIMFHLINEKDGKTFQLMELYGRKADLNSDIKEKFVKLCEEHGIIKENIIDLTKTNRCLKARE | null | null | aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds pheromones, likely to displace pheromones complexed to urinary MUPs and transport them to the vomeronasal organ (VNO) where they associate with their neuronal receptor(s). MUP4 is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT). {ECO:0000269|PubMed:12192080, ECO:000026... | Mus musculus (Mouse) |
P11597 | CETP_HUMAN | MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITASYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNT... | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle remodeling [GO:0034375]; lipid homeostasis [GO:0055088]; lipid transport [GO:0006869]; low-density lipoprotein particle remodeling [GO:0034374]; negative regulation of ... | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; vesicle [GO:0031982] | cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; phosphatidylcholine binding [GO:0031210]; phospholipid transporter activity [GO:0005548]; triglyceride binding [GO:0017129] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24293641, ECO:0000269|PubMed:3281933}. Note=Secreted in plasma. {ECO:0000269|PubMed:3281933}. | CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898; Evidence={ECO:0000269|PubMed:24293641}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352,... | null | null | null | null | FUNCTION: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL ... | Homo sapiens (Human) |
P11598 | PDIA3_RAT | MRFSCLALLPGVALLLASALLASASDVLELTDENFESRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEDEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDNYRFAHTNVESLVKEYDDNGEGITIFRPLHLANKFEDKIVAYTEKKMTSGKIKKFIQESIFGLCPHMTEDNKDLIQGKDLLTAYYDVDYEKNTKGSNYWRNRVMMVAKTFLDAGHKLNFAVASRKTFSHELSDFGLESTT... | 5.3.4.1 | null | adaptive immune response [GO:0002250]; cellular response to interleukin-7 [GO:0098761]; cellular response to nonylphenol [GO:1904148]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to vitamin D [GO:0071305]; circadian rhythm [GO:0007623]; extrinsic apoptotic signaling pat... | acrosomal vesicle [GO:0001669]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; melanosome [GO:0042470]; MHC class I peptide loading complex [GO:0042824]; sm... | identical protein binding [GO:0042802]; MHC class I protein binding [GO:0042288]; peptidase activity [GO:0008233]; protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase (glutathione) activity [GO:0019153]; protein-disulfide reductase activity [GO:0015035] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Within the major histocompatibility complex class I (MHC I) peptide loading complex forms reversible disulfide-linked heterodimers with TAPBP as part of its protein folding chaperone activity. This is essential to assist the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic retic... | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:9399589}. Melanosome {ECO:0000250|UniProtKB:P30101}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P30101}; | null | null | null | null | FUNCTION: Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone. Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essent... | Rattus norvegicus (Rat) |
P11602 | LIPL_CHICK | MERGRGMGKTALLAVLCLCLRGAAGSDPEAEMNFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVDWLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIHLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRV... | 3.1.1.32; 3.1.1.34 | null | cholesterol homeostasis [GO:0042632]; chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle mediated signaling [GO:0055096]; positive regulation of adipose ... | catalytic complex [GO:1902494]; chylomicron [GO:0042627]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; phosphatidylse... | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | PTM: N-glycan at Asn-70 is a triantennary complex oligosaccharide containing sialic acid, galactose, mannose, and N-acetylglucosamine, the reducing GlcNAc being sulfated at C6. {ECO:0000269|PubMed:1985932}.; PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:000025... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synth... | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; Evidence={ECO:0000250|UniProtKB:P11151}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3... | null | null | null | null | FUNCTION: Key enzyme in triglyceride metabolism (By similarity). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (By similarity). Although it has ... | Gallus gallus (Chicken) |
P11605 | NIA1_TOBAC | MAASVENRQFSHIEAGLSRSFKPRSDSPVRGCNFPPPNSTNFQKKPNSTIFLDYSSSEDDDDDDEKNEYLQMIKKGNSELEPSVHDSRDEGTADNWIERNFSLIRLTGKHPFNSEPPLNRLMHHGFITPVPLHYVRNHGPVPKGTWDDWTVEVTGLVKRPMKFTMDQLVNEFPSRELPVTLVCAGNRRKEQNMVKQTIGFNWGAAAVSTTVWRGVPLRALLKRYGVFSKNKGALNVCFEGADVLPGGGGSKYGTSIKKEFAMDPARDIIIAYMQNGEKLAPDHGFPVRMIIPGFIGGRMVKWIKRIIVTTQESDSYYHFK... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 heme group per subunit. {ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=... | nitrate assimilation [GO:0042128]; nitric oxide biosynthetic process [GO:0006809]; sulfur compound metabolic process [GO:0006790] | mitochondrion [GO:0005739] | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase (NADPH) activity [GO:0050464]; sulfite oxidase activity [GO:0008482] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; | null | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | Nicotiana tabacum (Common tobacco) |
P11607 | AT2A2_PIG | MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 7.2.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30777856}; | autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; organelle localization by membrane tethering [GO:0140056]; regulati... | sarcoplasmic reticulum membrane [GO:0033017] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000269|PubMed:30777856}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:30777856}; Multi-pass membrane protein {ECO:0000269|PubMed:30777856}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER c... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:30777856}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome ... | Sus scrofa (Pig) |
P11609 | CD1D1_MOUSE | MRYLPWLLLWAFLQVWGQSEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATVQMLLNDTCPLFVRGLLEAGKSDLEKQEKPVAWLSSVPSSADGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWDARQAPVGLIVFIVLIMLVVVGA... | null | null | antigen processing and presentation [GO:0019882]; antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]; innate immune response [GO:0045087]; NK T cell differen... | early endosome [GO:0005769]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764] | endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723]; T cell receptor binding [GO:0042608] | PF07654;PF16497; | 2.60.40.10;3.30.500.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:11754812, ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11754812}; Single-pass type I membrane protein {ECO:0000269|PubMed:11754812}. Endosome membrane {ECO:0000269|PubMed:11754812}. Lysosome membrane {ECO:0000269|PubMed:11754812}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysos... | null | null | null | null | null | FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:11754812, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439}. | Mus musculus (Mouse) |
P11610 | CD1D2_MOUSE | MRYLPCLLLWAFLQVWGQSEVQQKNYTFRCLQTSSFANISWSRTDSLILLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSTGCEMYPGNASESFFHVAFQGKYAVRFRGTSWQRVLGAPSWLDLPIKVLNADQGTSATVQTLLNDTWPQFARGLLEAGKSDLEKQEKPVAWLSSVPSSAHGHLQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWDARQAPVGLIVFIVLIMLVVVGA... | null | null | antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of interleukin-2 production [GO:0032743]; positi... | endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765] | endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723] | PF07654;PF16497; | 2.60.40.10;3.30.500.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11609}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11609}. Endosome membrane {ECO:0000250|UniProtKB:P11609}. Lysosome membrane {ECO:0000250|UniProtKB:P11609}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and l... | null | null | null | null | null | FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. | Mus musculus (Mouse) |
P11613 | ACKR3_CANLF | MDLHLFDYAEPGNFSDISWPCNSSDCIVVDTVLCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVVTIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLTCMSVDRYLSITYFASTSSRRKKVVRRAVCVLVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSVKEWLISMELVSVVLGFAIPFCVIAVFYCLLARAISASSDQEKQSSRKIIFSYVVVFLVCWLPYHVVVLLDIFSILHYIPFTCQLENFLFTALHVTQCLSLVHCCVNPVLYSFINR... | null | null | angiogenesis [GO:0001525]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:190223... | cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine binding [GO:0019958]; C-X-C chemokine receptor activity [GO:0016494]; coreceptor activity [GO:0015026]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. {ECO:0000250|UniProtKB:P25106}.; PTM: Ubiquitinated at the Lys residues in its C-terminal cytoplasmic tail and is essential for correct trafficking from and to the cell membrane. Deubiquitinated by CXCL12-stimulation in a reversible man... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25106}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000250|UniProtKB:P25106}. Recycling endosome {ECO:0000250|UniProtKB:P25106}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clat... | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... | Canis lupus familiaris (Dog) (Canis familiaris) |
P11617 | AA2AR_CANLF | MSTMGSWVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHNCLFFACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAVCWVLSFAIGLTPMLGWNNCSQPKEGRNYSQGCGEGQVACLFEDVVPMNYMVYYNFFAFVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPECSHAPLWLMYLTIVLSHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRRREPFKAGGTS... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic signaling pathway [GO:0097190]; eating behavior [GO:0042755]; G protein-coupled adenosine receptor signaling pathway [GO:0001973]; inhibitory postsynaptic potential [GO:0060080]; locomotory behavior [GO:0007626]; negative ... | plasma membrane [GO:0005886]; postsynapse [GO:0098794] | calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; G protein-coupled adenosine receptor activity [GO:0001609]; identical protein binding [GO:0042802]; lipid binding [GO:0008289] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Ubiquitinated. Deubiquitinated by USP4; leading to stabilization and expression at the cell surface (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30543}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30543}. Note=Colocalizes with GAS2L2 at neuronal processes. {ECO:0000250|UniProtKB:P30543}. | null | null | null | null | null | FUNCTION: Receptor for adenosine (PubMed:2125216). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (PubMed:2125216). {ECO:0000269|PubMed:2125216}. | Canis lupus familiaris (Dog) (Canis familiaris) |
P11620 | YPT1_SCHPO | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTFELEGKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDQDSFNNVKQWLQEIDRYAVEGVNRLLVGNKSDMVDKKVVEYSVAKEFADSLNIPFLETSAKDSTNVEQAFLTMSRQIKERMGNNTFASSNAKSSVKVGQGTNVSQSSSNCC | null | null | autophagosome assembly [GO:0000045]; endocytic recycling [GO:0032456]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886] | cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P01123}; Peripheral membrane protein {ECO:0000250|UniProtKB:P01123}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P01123}; Peripheral membrane protein {ECO:0000250|UniProtKB:P01123}. Cytoplasm {ECO:0000250|UniProtKB:P01123}. Preautophagosoma... | null | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P11627 | L1CAM_MOUSE | MVVMLRYVWPLLLCSPCLLIQIPDEYKGHHVLEPPVITEQSPRRLVVFPTDDISLKCEARGRPQVEFRWTKDGIHFKPKEELGVVVHEAPYSGSFTIEGNNSFAQRFQGIYRCYASNKLGTAMSHEIQLVAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAAPPRIYWMNSKIFDIKQDERVSMGQNGDLYFANVLTSDNHSDYICNAHFPGTRTIIQKEPIDLRVKPTNSMIDRKPRLLFPTNSSSRLVALQGQSLILECIAEGFPTPTIKWLHPSDPMPTDRVIYQNHNKTLQLLNVGEEDDGEYTCLAENSLGSA... | null | null | axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:0007160]; heterophilic... | axon [GO:0030424]; axonal growth cone [GO:0044295]; cell surface [GO:0009986]; dendrite [GO:0030425]; dendritic growth cone [GO:0044294]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:... | axon guidance receptor activity [GO:0008046]; cell-cell adhesion mediator activity [GO:0098632]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; PDZ domain binding [GO:0030165]; protein self-association [GO:0043621]; sialic acid binding [GO:0033691] | PF13882;PF00041;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, L1/neurofascin/NgCAM family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05695}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q05695}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q05695}. Note=Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonalne growth cones... | null | null | null | null | null | FUNCTION: Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain,... | Mus musculus (Mouse) |
P11632 | NHP6A_YEAST | MVTPREPKKRTTRKKKDPNAPKRALSAYMFFANENRDIVRSENPDITFGQVGKKLGEKWKALTPEEKQPYEAKAQADKKRYESEKELYNATLA | null | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; maintenance of transcriptional fidelity during transcription elongation by RNA polymerase III [GO:0001195]; negative regulation of DNA binding [GO:0043392]; protein-DNA complex assembly [GO:0065004]; RNA polymerase II prein... | chromosome [GO:0005694]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993] | DNA binding, bending [GO:0008301]; MutSalpha complex binding [GO:0032407]; nucleic acid binding [GO:0003676]; nucleosome binding [GO:0031491] | PF00505; | 1.10.30.10; | NHP6 family | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with both RNA polymerase II and some regions that are not transcribed on chromatin. | null | null | null | null | null | FUNCTION: DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11633 | NHP6B_YEAST | MAATKEAKQPKEPKKRTTRRKKDPNAPKRGLSAYMFFANENRDIVRSENPDVTFGQVGRILGERWKALTAEEKQPYESKAQADKKRYESEKELYNATRA | null | null | chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; maintenance of transcriptional fidelity during transcription elongation by RNA polymerase III [GO:0001195]; RNA polymerase III preinitiation complex assembly [GO:0070898]; transcription by RNA polymerase II [GO:0006366] | chromosome [GO:0005694]; nucleus [GO:0005634] | DNA binding, bending [GO:0008301]; sequence-specific DNA binding [GO:0043565] | PF00505; | 1.10.30.10; | NHP6 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:14562095}. Chromosome {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11653 | MUTB_PROFR | MSTLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNEDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFYRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRELFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILKEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLRAARMLWAKLVHQFGPKNP... | 5.4.99.2 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541, ECO:0000269|PubMed:9772164}; | propionate metabolic process, methylmalonyl pathway [GO:0019678] | null | cobalamin binding [GO:0031419]; metal ion binding [GO:0046872]; methylmalonyl-CoA mutase activity [GO:0004494] | PF02310;PF01642; | 3.40.50.280;3.20.20.240; | Methylmalonyl-CoA mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888, ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2; Evidence={ECO:0000269|PubMed:9772164}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22890; Evidence={ECO:0000305}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=96 uM for succinyl-CoA {ECO:0000269|PubMed:9772164}; Note=kcat is 48 sec(-1) with succinyl-CoA as substrate. {ECO:0000269|PubMed:9772164}; | null | null | null | FUNCTION: Catalyzes the reversible conversion of succinyl-CoA to (R)-methylmalonyl-CoA through a radical mechanism (PubMed:9772164). Is involved in the fermentation of pyruvate to propanoate that occurs in Propionibacteria (Probable). {ECO:0000269|PubMed:9772164, ECO:0000305|PubMed:2569861}. | Propionibacterium freudenreichii subsp. shermanii |
P11654 | PO210_RAT | MARASLIQPGLWALLLLQAVGPAVAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWSSTRPEVASIEPLGSSEQQCSQKAVVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHGIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFDWTIVKDTEANGFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLILENILLNPAYDVYLLVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPDPQGDPARPVAVLTQDTSRVTAMQMGQSNL... | null | null | mRNA transport [GO:0051028]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003] | endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643] | structural constituent of nuclear pore [GO:0017056] | PF02368; | null | NUP210 family | PTM: N-glycosylated, but not all potential glycosylation sites may be used. Contains high-mannose type oligosaccharides. {ECO:0000269|PubMed:2738089}.; PTM: Phosphorylated at Ser-1880 in mitosis specifically; not phosphorylated in interphase. {ECO:0000269|PubMed:8672508}. | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. {ECO:0000250}. | Rattus norvegicus (Rat) |
P11655 | SEC12_YEAST | MKFVTASYNVGYPAYGAKFLNNDTLLVAGGGGEGNNGIPNKLTVLRVDPTKDTEKEQFHILSEFALEDNDDSPTAIDASKGIILVGCNENSTKITQGKGNKHLRKFKYDKVNDQLEFLTSVDFDASTNADDYTKLVYISREGTVAAIASSKVPAIMRIIDPSDLTEKFEIETRGEVKDLHFSTDGKVVAYITGSSLEVISTVTGSCIARKTDFDKNWSLSKINFIADDTVLIAASLKKGKGIVLTKISIKSGNTSVLRSKQVTNRFKGITSMDVDMKGELAVLASNDNSIALVKLKDLSMSKIFKQAHSFAITEVTISPD... | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein secretion [GO:0009306]; regulation of COPII vesicle coating [GO:0003400] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794] | GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085] | null | 2.130.10.10; | WD repeat SEC12 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type II membrane protein. Note=Cycling between endoplasmic reticulum and the early Golgi. | null | null | null | null | null | FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy. {ECO:0000269|PubMed:11694599, ECO:000026... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11667 | ARGO_ECOLI | MFSYYFQGLALGAAMILPLGPQNAFVMNQGIRRQYHIMIALLCAISDLVLICAGIFGGSALLMQSPWLLALVTWGGVAFLLWYGFGAFKTAMSSNIELASAEVMKQGRWKIIATMLAVTWLNPHVYLDTFVVLGSLGGQLDVEPKRWFALGTISASFLWFFGLALLAAWLAPRLRTAKAQRIINLVVGCVMWFIALQLARDGIAHAQALFS | null | null | amino acid transport [GO:0006865]; L-arginine transmembrane transport [GO:1903826] | plasma membrane [GO:0005886] | amino acid transmembrane transporter activity [GO:0015171]; L-arginine transmembrane transporter activity [GO:0061459] | PF01810; | null | LysE/ArgO transporter (TC 2.A.75) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:27645388}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000269|PubMed:27645388}. | CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000269|PubMed:15150242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32144; Evidence={ECO:0000255|HAMAP-Rule:MF_01901, ECO:0000269|PubMed:15150242}; | null | null | null | null | FUNCTION: Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine. May also be involved in the export of canavanine (a plant-derived antimetabolite). {ECO:0000269|PubMed:15150242}. | Escherichia coli (strain K12) |
P11672 | NGAL_MOUSE | MALSVMCLGLALLGVLQSQAQDSTQNLIPAPSLLTVPLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQDQGCRYWIRTFVPSSRAGQFTLGNMHRYPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTDQCIDN | null | null | cellular response to hydrogen peroxide [GO:0070301]; defense response to bacterium [GO:0042742]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; innate immune response [GO:0045087]; long-term memory [GO:0007616]; negative regulation of hippocampal neuron apoptotic process [GO:0110091]; positive... | cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | enterobactin binding [GO:1903981]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; iron ion sequestering activity [GO:0140315]; protease binding [GO:0002020] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | PTM: N-glycosylated. {ECO:0000269|PubMed:21911364, ECO:0000269|PubMed:8687399}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:20550936, ECO:0000269|PubMed:8687399}. Cytoplasmic granule lumen {ECO:0000250|UniProtKB:P80188}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P80188}. Note=Upon binding to the SLC22A17 (24p3R) receptor, it is internalized (PubMed:163775... | null | null | null | null | null | FUNCTION: Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413). Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes i... | Mus musculus (Mouse) |
P11678 | PERE_HUMAN | MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVS... | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) covalently through ester linkages to hydroxylat... | defense response to bacterium [GO:0042742]; defense response to nematode [GO:0002215]; eosinophil migration [GO:0072677]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of ... | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule lumen [GO:0034774] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of eosinophils. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | null | null | null | null | FUNCTION: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. {ECO:0000269|PubMed:12540536, ECO:0000269|PubMed:18694936}. | Homo sapiens (Human) |
P11679 | K2C8_MOUSE | MSIRVTQKSYKMSTSGPRAFSSRSFTSGPGARISSSSFSRVGSSSSSFRGSMGTGVGLGGFGGAGVGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNI... | null | null | cell differentiation involved in embryonic placenta development [GO:0060706]; extrinsic apoptotic signaling pathway [GO:0097191]; hepatocyte apoptotic process [GO:0097284]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; response to hydrostatic pressure [GO:0051599]; response to other orga... | apicolateral plasma membrane [GO:0016327]; cell periphery [GO:0071944]; cell-cell junction [GO:0005911]; costamere [GO:0043034]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucl... | protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-80 phosphorylation plays an important role in keratin filament reorganization (By similarity). {ECO:0000250}.; PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing prot... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}. | null | null | null | null | null | FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000250}. | Mus musculus (Mouse) |
P11684 | UTER_HUMAN | MKLAVTLTLVTLALCCSSASAEICPSFQRVIETLLMDTPSSYEAAMELFSPDQDMREAGAQLKKLVDTLPQKPRESIIKLMEKIAQSSLCN | null | null | embryo implantation [GO:0007566]; female pregnancy [GO:0007565]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-4 production [GO:0032713]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of T cell proliferation [GO:0042130]; negative r... | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nuclear envelope [GO:0005635]; secretory granule [GO:0030141] | phospholipase A2 inhibitor activity [GO:0019834]; polychlorinated biphenyl binding [GO:0097160] | PF01099; | 1.10.210.10; | Secretoglobin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. | Homo sapiens (Human) |
P11685 | PSPC_RAT | MDMGSKEVLMESPPDYSTGPRSQFRIPCCPVHLKRLLIVVVVVVLVVVVIVGALLMGLHMSQKHTEMVLEMSIGGAPETQKRLALSEHTDTIATFSIGSTGIVLYDYQRLLTAYKPAPGTYCYIMKMAPESIPSLEALARKFKNFQAKSSTPTSKLGQEEGHSAGSDSDSSGRDLAFLGLAVSTLCGELPLYYI | null | null | cellular response to mechanical stimulus [GO:0071260]; cellular response to nitric oxide [GO:0071732]; circadian rhythm [GO:0007623]; respiratory gaseous exchange by respiratory system [GO:0007585]; response to cAMP [GO:0051591]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to gro... | alveolar lamellar body [GO:0097208]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; multivesicular body [GO:0005771] | identical protein binding [GO:0042802] | PF04089;PF08999; | 3.30.390.150; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, surface film. | null | null | null | null | null | FUNCTION: Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. | Rattus norvegicus (Rat) |
P11686 | PSPC_HUMAN | MDVGSKEVLMESPPDYSAAPRGRFGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGLHMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALTRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVSTLCGEVPLYYI | null | null | respiratory gaseous exchange by respiratory system [GO:0007585] | alveolar lamellar body [GO:0097208]; clathrin-coated endocytic vesicle [GO:0045334]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lamellar body [GO:0042599]; multivesicular body lumen [GO:0097486] | identical protein binding [GO:0042802] | PF04089;PF08999; | 3.30.390.150; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, surface film. | null | null | null | null | null | FUNCTION: Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. | Homo sapiens (Human) |
P11688 | ITA5_MOUSE | MGSWTPRSPRSPLHAVLLRWGPRRLPPLLPLLLLLWPPPLQVGGFNLDAEAPAVLSGPPGSLFGFSVEFYRPGRDGVSVLVGAPKANTSQPGVLQGGAVYVCPWGTSPIQCTTIQFDSKGSRILESSLYSAKGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKDPQNDPVGTCYLSTENFTRILEYAPCRSDFGSAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQISESYYPEYLINPVQGQLQTRQASSVYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTVLNGSDIHSLYNV... | null | null | angiogenesis [GO:0001525]; CD40 signaling pathway [GO:0023035]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; endodermal... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; integrin alpha5-beta1 complex [GO:0034674]; inte... | calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; epidermal growth factor receptor binding [GO:0005154]; integrin binding [GO:0005178] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: Proteolytic cleavage by PCSK5 mediates activation of the precursor. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08648}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P08648}. | null | null | null | null | null | FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen (PubMed:36812915). It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational cha... | Mus musculus (Mouse) |
P11708 | MDHC_PIG | MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEEIAFKDLDVAILVGSMPRRDGMERKDLLKANVKIFKCQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTSDDVKNVIIWGNHSSTQYPDVNHAKVKLQAKEVGVYEAVKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGIISDGNSYGVPDDLLYSFPVTIKDKTWKIVEGLPINDFSREKMDLTAKEL... | 1.1.1.37; 1.1.1.96 | null | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | hydroxyphenylpyruvate reductase activity [GO:0047995]; L-malate dehydrogenase activity [GO:0030060]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | PTM: ISGylated. {ECO:0000250|UniProtKB:P40925}.; PTM: Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation. {ECO:0000250|UniProtKB:P40925}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:8682322}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433; Evidence={... | null | null | null | null | FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation. Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading t... | Sus scrofa (Pig) |
P11709 | BIK1_YEAST | MDRYQRKIGCFIQIPNLGRGQLKYVGPVDTKAGMFAGVDLLANIGKNDGSFMGKKYFQTEYPQSGLFIQLQKVASLIEKASISQTSRRTTMEPLSIPKNRSIVRLTNQFSPMDDPKSPTPMRSFRITSRHSGNQQSMDQEASDHHQQQEFGYDNREDRMEVDSILSSDRKANHNTTSDWKPDNGHMNDLNSSEVTIELREAQLTIEKLQRKQLHYKRLLDDQRMVLEEVQPTFDRYEATIQEREKEIDHLKQQLELERRQQAKQKQFFDAENEQLLAVVSQLHEEIKENEERNLSHNQPTGANEDVELLKKQLEQLRNIE... | null | null | 2-micrometer plasmid partitioning [GO:0030543]; cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle orientation [GO:0000132]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; mitotic spindle elongation [GO:0000022]; negative regulation of m... | cell cortex [GO:0005938]; cell tip [GO:0051286]; kinetochore [GO:0000776]; mating projection tip [GO:0043332]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]; spindle pole body [GO:00... | microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010] | PF01302; | 2.30.30.190; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Note=And mitotic spindle. | null | null | null | null | null | FUNCTION: Required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11710 | FUS1_YEAST | MVATIMQTTTTVLTTVAAMSTTLASNYISSQASSSTSVTTVTTIATSIRSTPSNLLFSNVAAQPKSSSASTIGLSIGLPIGIFCFGLLILLCYFYLKRNSVSISNPPMSATIPREEEYCRRTNWFSRLFWQSKCEDQNSYSNRDIEKYNDTQWTSGDNMSSKIQYKISKPIIPQHILTPKKTVKNPYAWSGKNISLDPKVNEMEEEKVVDAFLYTKPPNIVHIESSMPSYNDLPSQKTVSSKKTALKTSEKWSYESPLSRWFLRGSTYFKDYGLSKTSLKTPTGAPQLKQMKMLSRISKGYFNESDIMPDERSPILEYNN... | null | null | cytogamy [GO:0000755]; maintenance of protein location in cell cortex [GO:0032065] | cell cortex [GO:0005938]; endoplasmic reticulum [GO:0005783]; mating projection tip [GO:0043332]; plasma membrane [GO:0005886] | null | PF00018; | 2.30.30.40; | null | PTM: O-glycosylated. {ECO:0000269|PubMed:2690078}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for cell fusion. Negatively regulates Sho1p signaling to ensure efficient cell fusion. {ECO:0000269|PubMed:15020407}.; FUNCTION: Interacts with SHO1. {ECO:0000269|PubMed:15020407}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11711 | CP2A1_RAT | MLDTGLLLVVILASLSVMLLVSLWQQKIRGRLPPGPTPLPFIGNYLQLNTKDVYSSITQLSERYGPVFTIHLGPRRVVVLYGYDAVKEALVDQAEEFSGRGEQATYNTLFKGYGVAFSSGERAKQLRRLSIATLRDFGVGKRGVEERILEEAGYLIKMLQGTCGAPIDPTIYLSKTVSNVISSIVFGERFDYEDTEFLSLLQMMGQMNRFAASPTGQLYDMFHSVMKYLPGPQQQIIKVTQKLEDFMIEKVRQNHSTLDPNSPRNFIDSFLIRMQEEKNGNSEFHMKNLVMTTLSLFFAGSETVSSTLRYGFLLLMKHPD... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | coumarin metabolic process [GO:0009804]; epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as on... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Highly active in the 7-alpha-hydroxylation of testosterone, progesterone and androstenedione. | Rattus norvegicus (Rat) |
P11712 | CP2C9_HUMAN | MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVT... | 1.14.14.1; 1.14.14.51; 1.14.14.52; 1.14.14.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | amide metabolic process [GO:0043603]; cholesterol metabolic process [GO:0008203]; epoxygenase P450 pathway [GO:0019373]; estrogen metabolic process [GO:0008210]; icosanoid biosynthetic process [GO:0046456]; long-chain fatty acid biosynthetic process [GO:0042759]; monocarboxylic acid metabolic process [GO:0032787]; mono... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | (R)-limonene 6-monooxygenase activity [GO:0052741]; (S)-limonene 6-monooxygenase activity [GO:0018675]; (S)-limonene 7-monooxygenase activity [GO:0018676]; arachidonic acid 11,12-epoxygenase activity [GO:0008405]; arachidonic acid 14,15-epoxygenase activity [GO:0008404]; arachidonic acid epoxygenase activity [GO:000839... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.2 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (epoxygenation) {ECO:0000269|PubMed:15766564}; KM=14.3 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (epoxygenation) {ECO:0000269|PubMed:15766564}; KM=1.25 mM for S-mephenytoin {ECO:0000269|PubMed:3079764}; KM=46.24 uM f... | PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000269|PubMed:15766564, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:7574697, ECO:0000269|PubMed:9435160}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:21576599}.; PATHWAY: Terpene metabolism; (4R)-limonene degradation. {ECO:00002... | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids (PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599, PubMed:7574697, PubMed:9435160, PubMed:9866708). Mechanistically, uses molecular oxygen inserting one oxygen atom... | Homo sapiens (Human) |
P11714 | CP2D9_MOUSE | MELLTGTDLWPVAIFTVIFILLVDLTHQRQRWTSRYPPGPVPWPVLGNLLQVDLGNMPYSLYKLQNRYGDVFSLQMAWKPMVVINGLKAMKEMLLTCGEDTADRPPVPIFEYLGVKPGSQGVVLAPYGPEWREQRRFSVSTLRNFGLGKKSLEDWVTKEANHLCDAFTAQAGQPINPNPMLNKSTCNVIASLIFARRFEYEDPFLIRMLKVLEQSLTEVSGLIPEVLNAFPILLRIPRLADKALQGQKSFIAILDNLLTENRTTWDPVQAPRNLTDAFLAEIEKAKGNPESSFNDENLLMVVRDLFGAGMLTTSTTLSWA... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Mus musculus (Mouse) |
P11715 | CP17A_RAT | MWELVGLLLLILAYFFWVKSKTPGAKLPRSLPSLPLVGSLPFLPRRGHMHVNFFKLQEKYGPIYSLRLGTTTTVIIGHYQLAREVLIKKGKEFSGRPQMVTQSLLSDQGKGVAFADAGSSWHLHRKLVFSTFSLFKDGQKLEKLICQEAKSLCDMMLAHDKESIDLSTPIFMSVTNIICAICFNISYEKNDPKLTAIKTFTEGIVDATGDRNLVDIFPWLTIFPNKGLEVIKGYAKVRNEVLTGIFEKCREKFDSQSISSLTDILIQAKMNSDNNNSCEGRDPDVFSDRHILATVGDIFGAGIETTTTVLKWILAFLVHN... | 1.14.14.19; 1.14.14.32 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P05093}; | adrenal gland development [GO:0030325]; androgen biosynthetic process [GO:0006702]; biphenyl metabolic process [GO:0018879]; cellular response to antibiotic [GO:0071236]; cellular response to gonadotropin stimulus [GO:0071371]; cellular response to lipopolysaccharide [GO:0071222]; dibenzo-p-dioxin metabolic process [GO... | axon [GO:0030424]; cell projection [GO:0042995]; endoplasmic reticulum membrane [GO:0005789]; neuronal cell body [GO:0043025] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05093}. Microsome membrane {ECO:0000250|UniProtKB:P05093}. | CATALYTIC ACTIVITY: Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, C... | null | PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P05093}.; PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000250|UniProtKB:P05093}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of ... | Rattus norvegicus (Rat) |
P11716 | RYR1_RABIT | MGDGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFTLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSK... | null | null | calcium ion transmembrane transport [GO:0070588]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; intracellular calcium ion homeostasis [GO:0006874]; muscle contraction [GO:0006936]; ossification involved in bone maturation [GO:0043931]; outflow tract morphogenesis [GO:0003151... | membrane [GO:0016020]; organelle membrane [GO:0031090]; ryanodine receptor complex [GO:1990425]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; terminal cisterna [GO:0014802]; Z disc [GO:0030018] | ATP binding [GO:0005524]; ATP-gated ion channel activity [GO:0035381]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:001... | PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR1 subfamily | PTM: The N-terminus is blocked.; PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2843 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2843. {ECO:0000250|UniProtKB:P21817}.; PTM: Activated by reversible S-nitrosylation (PubMed:22036948). Rep... | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12486242, ECO:0000269|PubMed:12732639, ECO:0000269|PubMed:18713863, ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:2725677, ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175, ECO:0000269|PubMed:27662087, ECO:0000269|PubMed:3722165}; Multi... | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12732639, ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:26245150, ECO:0000269|PubMed:27662087}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:10097181, PubMed:10388749, PubMed:12732639, PubMed:22036948, PubMed:26245... | Oryctolagus cuniculus (Rabbit) |
P11717 | MPRI_HUMAN | MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKNNVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQGTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEELRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGHQAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRYEIEWITEYACHR... | null | null | animal organ regeneration [GO:0031100]; G protein-coupled receptor signaling pathway [GO:0007186]; liver development [GO:0001889]; lysosomal transport [GO:0007041]; positive regulation by host of viral process [GO:0044794]; positive regulation of apoptotic process [GO:0043065]; post-embryonic development [GO:0009791]; ... | cell surface [GO:0009986]; clathrin coat [GO:0030118]; clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794... | enzyme binding [GO:0019899]; G-protein alpha-subunit binding [GO:0001965]; identical protein binding [GO:0042802]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor II binding [GO:0031995]; insulin-like growth factor receptor activity [GO:0005010]; mannose binding [GO:0005537]; phosphoprotein ... | PF00878;PF00040; | 2.10.10.10;2.70.130.10; | MRL1/IGF2R family | PTM: Palmitoylated (PubMed:18817523). Undergoes cysteine S-palmitoylation which promotes interaction with the retromer cargo-selective complex which mediates its retrograde trafficking to the Golgi apparatus (PubMed:18817523). {ECO:0000269|PubMed:18817523}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein {ECO:0000269|PubMed:2957598}. Endosome membrane {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein {ECO:0000269|PubMed:2957598}. Note=Mainly localized in the Golgi at steady state and not de... | null | null | null | null | null | FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes (PubMed:18817523, PubMed:2963003). Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand ... | Homo sapiens (Human) |
P11720 | TRPI_PSEAE | MSRDLPSLNALRAFEAAARLHSISLAAEELHVTHGAVSRQVRLLEDDLGVALFGKDGRGVKLTDSGVRLRDACGDAFERLRGVCAELRRQTAEAPFVLGVPGSLLARWFIPRLDQLNRALPDLRLQLSTSEGEFDPRRPGLDAMLWFAEPPWPADMQVFELAPERMGPVVSPRLAQETGLAQAPAARLLQEPLLHTASRPQAWPAWAASQGLAAEALRYGQGFEHLYYLLEAAVAGLGVAIAPEPLVRDDLAAGRLAAPWGFIETDARLALWVPARLHDPRAGRLAQWLREQLAG | null | null | DNA-templated transcription [GO:0006351]; positive regulation of amino acid biosynthetic process [GO:2000284]; regulation of DNA-templated transcription [GO:0006355]; tryptophan biosynthetic process [GO:0000162] | protein-DNA complex [GO:0032993] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF00126;PF03466; | 3.40.190.10;1.10.10.10; | LysR transcriptional regulatory family | null | null | null | null | null | null | null | FUNCTION: Activates the expression of the trpBA genes, which encode the two tryptophan synthase subunits, and represses initiation at its own promoter. Acts by binding to two adjacent sites in the intergenic region. In the absence of the inducer indoleglycerol phosphate (InGP), TrpI binds to site I. In the presence of ... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P11722 | FINC_CHICK | MPGRGGLRLALLALCLGAAAAGGGDGQRRGGKNRRQAQTASVPQATPAQGKQTCFDNGRYYQINQQWERIYLGNTLVCTCYGGSRGFNCESKPEPEETCFDKYTGSTYRVGETYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGKSYKIGDTWRRPHETGGYLLECVCLGNGKGEWTCKPLAERCYDNTAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTKTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSLHTTSTGSGSPSFTNVQTALYQPQPQQPQPQPHGHCVTDNGVV... | null | null | acute-phase response [GO:0006953]; apical protein localization [GO:0045176]; axis elongation involved in somitogenesis [GO:0090245]; biological process involved in interaction with symbiont [GO:0051702]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell... | apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; basement membrane [GO:0005604]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracell... | DNA binding [GO:0003677]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]; proteoglycan binding [GO:0043394] | PF00039;PF00040;PF00041; | 2.10.70.10;2.10.10.10;2.60.40.10; | null | PTM: Sulfated. {ECO:0000250}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrilloge... | Gallus gallus (Chicken) |
P11725 | OTC_MOUSE | MLSNLRILLNNAALRKGHTSVVRHFWCGKPVQSQVQLKGRDLLTLKNFTGEEIQYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPSFLTTQDIHLGVNESLTDTARVLSSMTDAVLARVYKQSDLDTLAKEASIPIVNGLSDLYHPIQILADYLTLQEHYGSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDPNIVKLAEQYAKENGTKLSMTNDPLEAARGGNVLITDTWISMGQEDEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPR... | 2.1.3.3 | null | ammonium homeostasis [GO:0097272]; arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240]; liver development [GO:0001889]; midgut development [GO:0007494]; monoatomic anion homeostasis [GO:0055081]; ornithine catabolic process [GO:0006593]; ornithine metabolic process [GO... | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; ornithine carbamoyltransferase activity [GO:0004585]; phosphate ion binding [GO:0042301]; phospholipid binding [GO:0005543] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, OTCase family | PTM: Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. {ECO:0000250|UniProtKB:P00480}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P00480}. | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000250|UniProtKB:P00480}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA... | null | PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine and carbamoyl phosphate: step 1/1. {ECO:0000250|UniProtKB:P00480}. | null | null | FUNCTION: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion. {ECO:0000250|UniProtKB:P00480}. | Mus musculus (Mouse) |
P11730 | KCC2G_RAT | MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQS... | 2.7.11.17 | null | calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; G1/S transition of mitotic cell cycle [GO:0000082]; nervous system development [GO:0007399]; phosphorylation [GO:0016310]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of neuron projection development [GO:0010975]; r... | calcium- and calmodulin-dependent protein kinase complex [GO:0005954]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; postsynaptic density [GO:0014069]; sarcoplasmic reticulum membrane [GO:0033017] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF08332;PF00069; | 3.10.450.50;6.10.140.620;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity). {ECO:0000250|UniProtKB:Q13555}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (By similarity). In s... | Rattus norvegicus (Rat) |
P11745 | RNA1_YEAST | MATLHFVPQHEEEQVYSISGKALKLTTSDDIKPYLEELAALKTCTKLDLSGNTIGTEASEALAKCIAENTQVRESLVEVNFADLYTSRLVDEVVDSLKFLLPVLLKCPHLEIVNLSDNAFGLRTIELLEDYIAHAVNIKHLILSNNGMGPFAGERIGKALFHLAQNKKAASKPFLETFICGRNRLENGSAVYLALGLKSHSEGLKVVKLYQNGIRPKGVATLIHYGLQYLKNLEILDLQDNTFTKHASLILAKALPTWKDSLFELNLNDCLLKTAGSDEVFKVFTEVKFPNLHVLKFEYNEMAQETIEVSFLPAMEKGNL... | null | null | nucleocytoplasmic transport [GO:0006913]; protein import into nucleus [GO:0006606]; ribosomal subunit export from nucleus [GO:0000054]; RNA import into nucleus [GO:0006404]; subtelomeric heterochromatin formation [GO:0031509]; tRNA export from nucleus [GO:0006409] | chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267] | PF13516; | 3.80.10.10; | RNA1 family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein GSP1 (Ran), converting it to the putatively inactive GDP-bound state. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11746 | MCM1_YEAST | MSDIEEGTPTNNGQQKERRKIEIKFIENKTRRHVTFSKRKHGIMKKAFELSVLTGTQVLLLVVSETGLVYTFSTPKFEPIVTQQEGRNLIQACLNAPDDEEEDEEEDGDDDDDDDDDGNDMQRQQPQQQQPQQQQQVLNAHANSLGHLNQDQVPAGALKQEVKSQLLGGANPNQNSMIQQQQHHTQNSQPQQQQQQQPQQQMSQQQMSQHPRPQQGIPHPQQSQPQQQQQQQQQLQQQQQQQQQQPLTGIHQPHQQAFANAASPYLNAEQNAAYQQYFQEPQQGQY | null | null | arginine metabolic process [GO:0006525]; cell cycle [GO:0007049]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of arginine metabolic process [GO:0000821]; regulation of mating type switching [GO:0031494]; regul... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; RNA polymerase II transcription repressor complex [GO:0090571] | DNA replication origin binding [GO:0003688]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; molecular sequest... | PF00319; | 3.40.1810.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are tran... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11747 | TAF13_YEAST | MSRKLKKTNLFNKDVSSLLYAYGDVPQPLQATVQCLDELVSGYLVDVCTNAFHTAQNSQRNKLRLEDFKFALRKDPIKLGRAEELIATNKLITEAKKQFNETDNQNSLKRYREEDEEGDEMEEDEDEQQVTDDDEEAAGRNSAKQSTDSKATKIRKQGPKNLKKTKK | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription by RNA polymerase II [GO:0006366] | nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669] | protein heterodimerization activity [GO:0046982]; transcription coactivator activity [GO:0003713] | PF02269; | 1.10.20.10; | TAF13 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through differen... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11759 | ALGD_PSEAE | MRISIFGLGYVGAVCAGCLSARGHEVIGVDVSSTKIDLINQGKSPIVEPGLEALLQQGRQTGRLSGTTDFKKAVLDSDVSFICVGTPSKKNGDLDLGYIETVCREIGFAIREKSERHTVVVRSTVLPGTVNNVVIPLIEDCSGKKAGVDFGVGTNPEFLRESTAIKDYDFPPMTVIGELDKQTGDLLEEIYRELDAPIIRKTVEVAEMIKYTCNVWHAAKVTFANEIGNIAKAVGVDGREVMDVICQDHKLNLSRYYMRPGFAFGGSCLPKDVRALTYRASQLDVEHPMLGSLMRSNSNQVQKAFDLITSHDTRKVGLLG... | 1.1.1.132 | null | alginic acid biosynthetic process [GO:0042121]; cellular response to cell envelope stress [GO:0036460]; response to osmotic stress [GO:0006970]; single-species biofilm formation [GO:0044010] | null | GDP-mannose 6-dehydrogenase activity [GO:0047919]; NAD binding [GO:0051287] | PF00984;PF03720;PF03721; | 1.20.5.170;3.40.50.720; | UDP-glucose/GDP-mannose dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:21728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:84886; EC=1.1.1.132; Evidence={ECO:0000269|PubMed:12135385, ECO:0000269|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.9 uM for GDP-D-mannose {ECO:0000269|PubMed:2470755}; KM=4.1 uM for GDP-D-mannose {ECO:0000269|PubMed:12135385}; KM=185 uM for NAD(+) {ECO:0000269|PubMed:2470755}; KM=92 uM for NAD(+) {ECO:0000269|PubMed:12135385}; Vmax=581.4 nmol/min/mg enzyme {ECO:0000269|PubMe... | PATHWAY: Glycan biosynthesis; alginate biosynthesis. {ECO:0000305|PubMed:12705829, ECO:0000305|PubMed:3108855}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.7. {ECO:0000269|PubMed:2470755}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Stable at 57.5 degrees Celsius, pH 5.0 for 10 minutes, used to purify protein. {ECO:0000269|PubMed:2470755}; | FUNCTION: Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (Probable). Other sugars are not used as subst... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P11762 | LEG1_RAT | MACGLVASNLNLKPGECLKVRGELAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDDGTWGTEQRETAFPFQPGSITEVCITFDQADLTIKLPDGHEFKFPNRLNMEAINYMAADGDFKIKCVAFE | null | null | apoptotic process [GO:0006915]; cell-cell adhesion [GO:0098609]; cellular response to glucose stimulus [GO:0071333]; cellular response to organic cyclic compound [GO:0071407]; myoblast differentiation [GO:0045445]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of neuron projection dev... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; galectin complex [GO:1990724] | carbohydrate binding [GO:0030246]; galactoside binding [GO:0016936]; identical protein binding [GO:0042802]; lactose binding [GO:0030395]; laminin binding [GO:0043236] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm {ECO:0000250|UniProtKB:P09382}. Secreted {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in p... | null | null | null | null | null | FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000250|UniPro... | Rattus norvegicus (Rat) |
P11766 | ADHX_HUMAN | MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFG... | 1.1.1.-; 1.1.1.1; 1.1.1.284 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:3365377}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:3365377}; | ethanol oxidation [GO:0006069]; fatty acid omega-oxidation [GO:0010430]; formaldehyde catabolic process [GO:0046294]; positive regulation of blood pressure [GO:0045777]; respiratory system process [GO:0003016]; response to lipopolysaccharide [GO:0032496]; response to nitrosative stress [GO:0051409]; response to redox s... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739] | alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; electron transfer activity [GO:0009055]; fatty acid binding [GO:0005504]; formaldehyde dehydrogenase activity [GO:0018467]; identical protein binding [GO:0042802]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; S-(hydroxymethyl)glutathione ... | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:8460164}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a keton... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for 20-HETE {ECO:0000269|PubMed:16081420}; | null | null | null | FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z... | Homo sapiens (Human) |
P11792 | SCH9_YEAST | MMNFFTSKSSNQDTGFSSQHQHPNGQNNGNNNSSTAGNDNGYPCKLVSSGPCASSNNGALFTNFTLQTATPTTAISQDLYAMGTTGITSENALFQMKSMNNGISSVNNNNSNTPTIITTSQEETNAGNVHGDTGGNSLQNSEDDNFSSSSTTKCLLSSTSSLSINQREAAAAAYGPDTDIPRGKLEVTIIEARDLVTRSKDSQPYVVCTFESSEFISNGPESLGAINNNNNNNNNNQHNQNQHINNNNENTNPDAASQHHNNNSGWNGSQLPSIKEHLKKKPLYTHRSSSQLDQLNSCSSVTDPSKRSSNSSSGSSNGPK... | 2.7.11.1 | null | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of hydrogen sulfide biosynthetic process [GO:1904828]; positive regulation of ribosomal protein gene transcription by RNA polymerase II [GO:0060963]; positive regulation of transcription by RNA polymerase I [GO:0045943]; p... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00168;PF00069;PF00433; | 2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Phosphorylated by TORC1 in nutrient-replete conditions and during mechanical stress. {ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway. Regulates both BCY1 phosphorylation and MPK1 activity (PubMed:20702584). Regulates ribosome biogenesis, translation initiation, and entry into stationary phase in a TORC1-dependent manner (PubMed... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11798 | KCC2A_MOUSE | MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGG... | 2.7.11.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UQM7}; | calcium ion transport [GO:0006816]; calmodulin dependent kinase signaling pathway [GO:0099004]; cellular response to interferon-beta [GO:0035458]; dendrite morphogenesis [GO:0048813]; dendritic spine development [GO:0060996]; G1/S transition of mitotic cell cycle [GO:0000082]; ionotropic glutamate receptor signaling pa... | axon [GO:0030424]; calcium- and calmodulin-dependent protein kinase complex [GO:0005954]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; glutamatergic postsynaptic density [GO:0099573]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; neuron ... | ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; glutamate receptor binding [GO:0035254]; GTPase activating protein binding [GO:0032794]; metal ion binding [GO:0046872]; protein ... | PF08332;PF00069; | 3.10.450.50;6.10.140.620;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state. {ECO:0000269|PubMed:28130356}.; PTM: Palmitoylated. Probably palmitoylated by ZDHHC3 and ZDHHC7. {ECO:0000250|UniProtKB:P11275}. | SUBCELLULAR LOCATION: [Isoform Alpha KAP]: Cytoplasm {ECO:0000305|PubMed:8524307}.; SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:28642476}. Postsynaptic density {ECO:0000250|UniProtKB:P11275}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9UQM7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9UQM7}.... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:15994560, ECO:00002... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (By similarity). Member of the NMDAR signaling complex in exci... | Mus musculus (Mouse) |
P11799 | MYLK_CHICK | MGDVKLVTSTRVSKTSLTLSPSVPAEAPAFTLPPRNIRVQLGATARFEGKVRGYPEPQITWYRNGHPLPEGDHYVVDHSIRGIFSLVIKGVQEGDSGKYTCEAANDGGVRQVTVELTVEGNSLKKYSLPSSAKTPGGRLSVPPVEHRPSIWGESPPKFATKPNRVVVREGQTGRFSCKITGRPQPQVTWTKGDIHLQQNERFNMFEKTGIQYLEIQNVQLADAGIYTCTVVNSAGKASVSAELTVQGPDKTDTHAQPLCMPPKPTTLATKAIENSDFKQATSNGIAKELKSTSTELMVETKDRLSAKKETFYTSREAKDG... | 2.7.11.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | muscle structure development [GO:0061061]; phosphorylation [GO:0016310]; tonic smooth muscle contraction [GO:0014820] | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; stress fiber [GO:0001725] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; myosin light chain kinase activity [GO:0004687] | PF16620;PF00041;PF07679;PF00069; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: The C-terminus is deglutamylated, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The C-terminus is variable, with one to five C-terminal glutamyl residues being removed producing five forms differring in their number of C-terminal glutamyl residues. {ECO:0000269|PubMed:9... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12176732}. Membrane {ECO:0000269|PubMed:12176732}. Note=Telokin is cytosolic and can translocate to the membrane upon stimulation. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals. | Gallus gallus (Chicken) |
P11801 | KPSH1_HUMAN | MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEP... | 2.7.11.1 | null | determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Autophosphorylated on serine residues. {ECO:0000269|PubMed:11087665}.; PTM: Myristoylated. Required for membrane association. Prerequisite for palmitoylation to occur. {ECO:0000269|PubMed:14644153}.; PTM: Palmitoylated. {ECO:0000269|PubMed:14644153}. | SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus speckle. Endoplasmic reticulum membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Cytoplasm. Note=Localized in the brefeldin A-sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat ... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing. {ECO:0000269|PubMed:12466556}. | Homo sapiens (Human) |
P11802 | CDK4_HUMAN | MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE | 2.7.11.22 | null | cell division [GO:0051301]; cellular response to interleukin-4 [GO:0071353]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; G1/S transition of mitotic cell cycle [GO:0000082]; positive regulation of ce... | bicellular tight junction [GO:0005923]; chromatin [GO:0000785]; cyclin D1-CDK4 complex [GO:0097128]; cyclin D2-CDK4 complex [GO:0097129]; cyclin D3-CDK4 complex [GO:0097130]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nuc... | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine ph... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18827403}. Nucleus {ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:20399237, ECO:0000269|PubMed:9106657}. Nucleus membrane {ECO:0000269|PubMed:18827403}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:19075005, ECO:00002... | null | null | null | null | FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and... | Homo sapiens (Human) |
P11827 | GLCAP_SOYBN | MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEECEEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREHPRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLFKNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDALRVPAGTTYYVVNPDNDENL... | null | null | null | aleurone grain [GO:0033095]; endoplasmic reticulum [GO:0005783]; protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 7S seed storage protein family | null | SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage vacuole {ECO:0000269|PubMed:12787246, ECO:0000269|PubMed:15447650, ECO:0000269|PubMed:16900322, ECO:0000269|PubMed:17181539}. Note=Localizes in protein storage vacuoles in cotyledons of deve... | null | null | null | null | null | FUNCTION: Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling. {ECO:0000305}. | Glycine max (Soybean) (Glycine hispida) |
P11831 | SRF_HUMAN | MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANG... | null | null | actin cytoskeleton organization [GO:0030036]; angiogenesis involved in wound healing [GO:0060055]; associative learning [GO:0008306]; axon extension [GO:0048675]; bicellular tight junction assembly [GO:0070830]; branching involved in blood vessel morphogenesis [GO:0001569]; bronchus cartilage development [GO:0060532]; ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; 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]; DNA-binding transcription factor binding [GO:0140297]; hi... | PF00319; | 3.40.1810.10; | null | PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:1547771, ECO:0000269|PubMed:8375385, ECO:0000269|PubMed:8407951}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:19350017}. | null | null | null | null | null | FUNCTION: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton ... | Homo sapiens (Human) |
P11832 | NIA1_ARATH | MATSVDNRHYPTMNGVAHAFKPPLVPSPRSFDRHRHQNQTLDVILTETKIVKETEVITTVVDSYDDSSSDDEDESHNRNVPYYKELVKKSNSDLEPSILDPRDESTADSWIQRNSSMLRLTGKHPFNAEAPLPRLMHHGFITPVPLHYVRNHGAVPKANWSDWSIEITGLVKRPAKFTMEELISEFPSREFPVTLVCAGNRRKEQNMVKQTIGFNWGSAGVSTSLWKGIPLSEILRRCGIYSRRGGALNVCFEGAEDLPGGGGSKYGTSIKKEMAMDPARDIILAYMQNGELLTPDHGFPVRVIVPGFIGGRMVKWLKRI... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 heme group per subunit. {ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=... | nitrate assimilation [GO:0042128]; nitric oxide biosynthetic process [GO:0006809]; response to herbicide [GO:0009635]; response to light stimulus [GO:0009416]; sulfur compound metabolic process [GO:0006790] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase (NADPH) activity [GO:0050464]; nitrate reductase activity [GO:0008940]; sulfite oxidase activity [GO:0008482] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; | null | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | Arabidopsis thaliana (Mouse-ear cress) |
P11835 | ITB2_MOUSE | MLGLRPSLLLALAGLFFLGSAVSQECTKYKVSSCRDCIQSGPGCSWCQKLNFTGPGEPDSLRCDTRAQLLLKGCPADDIMDPRSIANPEFDQRGQRKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLNNVKKLGGDLLQALNEITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKACQPPFAFRHVLKLTDNSNQFQTEVGKQLISGNLDAPEGGLDAIMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNMYKRSNEFDYPSVGQLAHKLSESNIQPI... | null | null | activated T cell proliferation [GO:0050798]; amyloid-beta clearance [GO:0097242]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cellular extravasation [GO:0045123]; cellular response to low-density lipoprotein particle st... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; integrin alphaM-beta2 complex [GO:0034688]; integrin complex [GO:0008305]; membrane [GO:0016020]; membrane raft [GO:0045121]; receptor complex [GO:0043235] | amyloid-beta binding [GO:0001540]; complement component C3b binding [GO:0001851]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | PF08725;PF07965;PF00362;PF17205; | 6.20.50.10;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Both Ser-747 and Ser-758 become phosphorylated when T-cells are exposed to phorbol esters. Phosphorylation on Thr-760 (but not on Ser-758) allows interaction with 14-3-3 proteins. {ECO:0000250|UniProtKB:P05107}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}. Membrane raft {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}. | null | null | null | null | null | FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (By similarity). Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third comp... | Mus musculus (Mouse) |
P11836 | CD20_HUMAN | MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLGILSVMLIFAFFQELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP | null | null | B cell activation [GO:0042113]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; calcium ion import into cytosol [GO:1902656]; cell surface receptor signaling pathway [GO:0007166]; humoral immune response [GO:0006959]; positive regulation of calcium... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853] | epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802]; immunoglobulin binding [GO:0019865]; MHC class II protein complex binding [GO:0023026] | PF04103; | null | MS4A family | PTM: Phosphorylated on serines and threonines in resting B-cells. Protein kinase C/PKC can use CD20 as substrate. {ECO:0000269|PubMed:2472394}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12920111, ECO:0000269|PubMed:22615937}; Multi-pass membrane protein {ECO:0000269|PubMed:22615937}. Cell membrane {ECO:0000269|PubMed:22615937}; Lipid-anchor {ECO:0000269|PubMed:22615937}. Note=Constitutively associated with membrane rafts. {ECO:0000269|PubMed:1292... | null | null | null | null | null | FUNCTION: B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:12920111, PubMed:3925015, PubMed:7684739). Functions as a store-operated calcium (SOC) channel component promoting calci... | Homo sapiens (Human) |
P11837 | NIMA_EMENI | MAIALAEADKYEVLEKIGCGSFGIIRKVKRKSDGFILCRKEINYIKMSTKEREQLTAEFNILSSLRHPNIVAYYHREHLKASQDLYLYMEYCGGGDLSMVIKNLKRTNKYAEEDFVWRILSQLVTALYRCHYGTDPAEVGSNLLGPAPKPSGLKGKQAQMTILHRDLKPENIFLGSDNTVKLGDFGLSKLMHSHDFASTYVGTPFYMSPEICAAEKYTLRSDIWAVGCIMYELCQREPPFNARTHIQLVQKIREGKFAPLPDFYSSELKNVIASCLRVNPDHRPDTATLINTPVIRLMRREVELNNLSRAARKREEATMQ... | 2.7.11.1 | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; positive regulation of mitotic nuclear division [GO:0045840]; protein phosphorylation [GO:0006468] | cortical microtubule [GO:0055028]; cytoplasm [GO:0005737]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634] | ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Recessive mutations of NIMA cause a specific cell cycle block in G2 at restrictive temperature due to lack of phosphorylation that normally activates the G2-kinase. {ECO:0000269|PubMed:7629122}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Protein kinase that plays an important role in mitotic regulation. Seems to be phosphorylated and thereby activated by CDC2/cyclin B during mitotic activation. It is also required for spindle formation and for nuclear envelope breakdown. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P11845 | IPP2_RABIT | MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS | null | null | glycogen metabolic process [GO:0005977]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; regulation of signal transduction [GO:0009966] | protein phosphatase type 1 complex [GO:0000164]; skeletal muscle myofibril [GO:0098723] | protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864] | PF04979; | 6.10.250.1050; | Protein phosphatase inhibitor 2 family | PTM: Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex (By similarity). Phosphorylation on Thr-73 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex. {ECO:0000250, ECO:0000269|PubMed:3036252, ECO:0000269|PubMed:6091765, ECO:0000269|PubMed:6297978}. | null | null | null | null | null | null | FUNCTION: Inhibitor of protein-phosphatase 1. | Oryctolagus cuniculus (Rabbit) |
P11859 | ANGT_MOUSE | MTPTGAGLKATIFCILTWVSLTAGDRVYIHPFHLLYHNKSTCAQLENPSVETLPESTFEPVPIQAKTSPVNEKTLHDQLVLAAEKLEDEDRKRAAQVAMIANFVGFRMYKMLNEAGSGASGAILSPPALFGTLVSFYLGSLDPTASQLQTLLDVPVKEGDCTSRLDGHKVLAALRAVQGLLVTQGGSSSQTPLLQSIMVGLFTAPGFRLKHSFVQSLALFTPALFPRSLDLSTDPVLATEKINRFIKAVTGWKMNLPLEGVSTDSTLLFNTYVHFQGTMRGFSQLPGVHEFWVDNSISVSVPMISGTGNFQHWSDAQNNF... | null | null | aldosterone secretion [GO:0035932]; angiotensin-mediated drinking behavior [GO:0003051]; angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure [GO:0001998]; artery smooth muscle contraction [GO:0014824]; associative learning [GO:0008306]; astrocyte activation [GO:0048143]; blo... | extracellular space [GO:0005615] | hormone activity [GO:0005179]; serine-type endopeptidase inhibitor activity [GO:0004867]; type 1 angiotensin receptor binding [GO:0031702]; type 2 angiotensin receptor binding [GO:0031703] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01019}. | null | null | null | null | null | FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. {ECO:0000250|UniProtKB:P01019}.; FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate... | Mus musculus (Mouse) |
P11862 | GAS2_MOUSE | MMCTALSPKVRSGPGLSDMHQYSQWLASRHEANLLPMKEDLALWLTNLLGKEITAETFMEKLDNGALLCQLAATVQEKFKESMDANKPAKTLPLKKIPCKASAPSGSFFARDNTANFLSWCRDLGVDETCLFESEGLVLHKQPREVCLCLLELGRIAARYGVEPPGLIKLEKEIEQEETLSAPSPSPSPSSKSSGKKSTGNLLDDAVKRISEDPPCKCPTKFCVERLSQGRYRVGEKILFIRMLHNKHVMVRVGGGWETFAGYLLKHDPCRMLQISRVDGKTSPVQSKSPTLKDMNPDNYLVVSATYKAKKEIK | null | null | actin crosslink formation [GO:0051764]; antral ovarian follicle growth [GO:0001547]; apoptotic process [GO:0006915]; basement membrane organization [GO:0071711]; cell cycle [GO:0007049]; initiation of primordial ovarian follicle growth [GO:0001544]; ovulation [GO:0030728]; regulation of cell cycle [GO:0051726]; regulat... | actin filament [GO:0005884]; cytoplasm [GO:0005737]; membrane [GO:0016020]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; cytoskeletal anchor activity [GO:0008093]; microtubule binding [GO:0008017] | PF00307;PF02187; | 1.10.418.10;3.30.920.20; | GAS2 family | PTM: Cleaved, during apoptosis, on a specific aspartic residue by caspases. {ECO:0000250}.; PTM: Phosphorylated on serine residues during the G0-G1 transition phase. {ECO:0000269|PubMed:8120096}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:8120096}. Membrane {ECO:0000269|PubMed:8120096}; Peripheral membrane protein {ECO:0000269|PubMed:8120096}. Note=Component of the microfilament system (PubMed:1607387). Colocalizes with actin fibers at the cell border and along the stress fi... | null | null | null | null | null | FUNCTION: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May play a role in chondrocyte proliferation and differentiation, and... | Mus musculus (Mouse) |
P11868 | TDCD_ECOLI | MNEFPVVLVINCGSSSIKFSVLDASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSYEGALKAIAFELEKRNLNDSVALIGHRIAHGGSIFTESAIITDEVIDNIRRVSPLAPLHNYANLSGIESAQQLFPGVTQVAVFDTSFHQTMAPEAYLYGLPWKYYEELGVRRYGFHGTSHRYVSQRAHSLLNLAEDDSGLVVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMSWVASQTNQSLGDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERAQLAIKTFVHRIARHIAGHAASLRRLDG... | 2.7.2.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01881}; | acetate metabolic process [GO:0006083]; anaerobic amino acid catabolic process [GO:0019665]; L-threonine catabolic process to propionate [GO:0070689]; phosphorylation [GO:0016310]; threonine catabolic process [GO:0006567] | cytosol [GO:0005829] | acetate kinase activity [GO:0008776]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; propionate kinase activity [GO:0008980] | PF00871; | 3.30.420.40; | Acetokinase family, TdcD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + propanoate = ADP + propanoyl phosphate; Xref=Rhea:RHEA:23148, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:58933, ChEBI:CHEBI:456216; EC=2.7.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01881}; | null | PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 4/4. {ECO:0000255|HAMAP-Rule:MF_01881}. | null | null | FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor. {ECO:0000255|HAMAP-Rule:MF_01881, ECO:0000269|PubMed:9484901}. | Escherichia coli (strain K12) |
P11880 | MURF_ECOLI | MISVTLSQLTDILNGELQGADITLDAVTTDTRKLTPGCLFVALKGERFDAHDFADQAKAGGAGALLVSRPLDIDLPQLIVKDTRLAFGELAAWVRQQVPARVVALTGSSGKTSVKEMTAAILSQCGNTLYTAGNLNNDIGVPMTLLRLTPEYDYAVIELGANHQGEIAWTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNADNNDWLNWQSVIGSRKVWRFSPNAANSDFTATNIHVTSHGTEFTLQTPTGSVDVLLPLPGRHNIANALAAAALSMSVGATLDAIKAGLANLKAVPGRLFPI... | 6.3.2.10 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytosol [GO:0005829] | ATP binding [GO:0005524]; UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity [GO:0047480]; UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity [GO:0008766] | PF01225;PF02875;PF08245; | 3.90.190.20;3.40.1190.10;3.40.1390.10; | MurCDEF family, MurF subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}. | CATALYTIC ACTIVITY: Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374, ChEBI:CHEBI:15378, ChEBI:CHE... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}. | null | null | FUNCTION: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}. | Escherichia coli (strain K12) |
P11881 | ITPR1_MOUSE | MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP... | null | null | calcium ion transport [GO:0006816]; cell morphogenesis [GO:0000902]; cellular response to cAMP [GO:0071320]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; epithelial fluid transport [GO:0042045]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; ion channel mo... | calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; GABA-ergic synapse [GO:0098982]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; n... | calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; inositol 1,4,5 trisphosphate binding [GO:0070679]; inositol 1,4,5-trisphosphate receptor activity involved in regulation of postsynaptic cytosolic calcium levels [GO:0098695]; inositol 1,4,5-trisph... | PF08709;PF00520;PF02815;PF08454;PF01365; | 1.10.287.70;2.80.10.50;1.25.10.30; | InsP3 receptor family | PTM: Polyubiquitinated (PubMed:35568199). Polyubiquitination targets ITPR1 for proteasomal degradation (PubMed:35568199). Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (By similarity). {ECO:0000250|UniProtKB:P29994, ECO:0000269|PubMed:355... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28416699, ECO:0000305|PubMed:24374158, ECO:0000305|PubMed:25368151}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P29994, ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane prote... | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11955285, ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:28416699, ECO:0000269|PubMed:35568199}; | null | null | null | null | FUNCTION: Inositol 1,4,5-trisphosphate-gated calcium channel that, upon inositol 1,4,5-trisphosphate binding, mediates calcium release from the endoplasmic reticulum (ER) (PubMed:11955285, PubMed:12442173, PubMed:20813840, PubMed:2554142, PubMed:28416699, PubMed:35568199). Undergoes conformational changes upon ligand b... | Mus musculus (Mouse) |
P11883 | AL3A1_RAT | MSSISDTVKRAREAFNSGKTRSLQFRIQQLEALQRMINENLKSISGALASDLGKNEWTSYYEEVAHVLEELDTTIKELPDWAEDEPVAKTRQTQQDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAVAAGNAVILKPSEVSGHMADLLATLIPQYMDQNLYLVVKGGVPETTELLKERFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKDFYGEDAKQSRDYGRIINDRHFQRVKGLIDNQKVAHGGTWDQSSRYIAPTI... | 1.2.1.5 | null | cellular aldehyde metabolic process [GO:0006081]; lipid metabolic process [GO:0006629]; positive regulation of cell population proliferation [GO:0008284]; response to cAMP [GO:0051591]; response to glucocorticoid [GO:0051384]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]; response to organic cycl... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor [... | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47739}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.5; Evidence={ECO:0000269|PubMed:2831537}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + ... | null | null | null | null | FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:2831537). Prefere... | Rattus norvegicus (Rat) |
P11884 | ALDH2_RAT | MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQC... | 1.2.1.3 | null | acetaldehyde metabolic process [GO:0006117]; aldehyde catabolic process [GO:0046185]; apoptotic mitochondrial changes [GO:0008637]; behavioral response to ethanol [GO:0048149]; cellular detoxification of aldehyde [GO:0110095]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:00328... | mitochondrial matrix [GO:0005759] | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; carboxylesterase activity [GO:0106435]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; identical protein binding [GO:0042802]; NADH binding [GO:0070404]; nitroglycerin reductase activity [GO:0018547]; phenylacetaldehyde d... | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. | null | null | FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage. {ECO:0000250|UniProtKB:P05091}. | Rattus norvegicus (Rat) |
P11885 | COLI_AQUCT | MLQPVWHACILAILGVFIFHVGEVRSQCWESNKCTDLSSEDGILECIKACKMDLSAESPVFPGNGHIQPLSENIRKYVMSHFRWNKFGRRNSTSNDNNNNNGGYKREDIANYPILNLFLGSDNQNTQEGIMEDDALDRQDSKRSYSMEHFRWGKPVGKKRRPIKVFPTDAEEESSESFPIELRRELSLEFDYPDTNSEEELDNGELLEGPVKKGRKYKMHHFRWEGPPKDKRYGGFMTPERSQTPLMTLFKNAIIKNAHKKGQ | null | null | neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852] | extracellular space [GO:0005615]; secretory granule [GO:0030141] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184] | PF00976;PF08384;PF08035; | null | POMC family | PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}. | null | null | null | null | null | FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin ... | Aquarana catesbeiana (American bullfrog) (Rana catesbeiana) |
P11908 | PRPS2_HUMAN | MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGCGEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTSIADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL | 2.7.6.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; nucleobase-containing compound metabolic process [GO:0006139]; pentose-phosphate shunt [GO:0006098]; phosphorylation [GO:0016310]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; ribose phosphate diphosphokinase complex [GO:0002189] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; ribose phosphate diphosphokinase activity [GO:0004749] | PF14572;PF13793; | 3.40.50.2020; | Ribose-phosphate pyrophosphokinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; | null | PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. | null | null | FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. | Homo sapiens (Human) |
P11909 | GPX1_RABIT | MCAARMAAAAQSVYSFSAHPLAGGEPVNLGSLRGKVLLIENVASLUGTTVRDYTQMNELQERLGPRALVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFQKCEVNGAKASPLFAFLREALPPPSDDPTALMTDPKFITWCPVCRNDVSWSFEKFLVGPDGVPVRRYSRRFPTIDIEPDIQALLSKGSGGA | 1.11.1.12; 1.11.1.9 | null | arachidonic acid metabolic process [GO:0019369]; glutathione metabolic process [GO:0006749]; hydrogen peroxide catabolic process [GO:0042744]; lipoxygenase pathway [GO:0019372]; response to hydrogen peroxide [GO:0042542]; response to selenium ion [GO:0010269] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066] | PF00255; | 3.40.30.10; | Glutathione peroxidase family | PTM: During periods of oxidative stress, Sec-46 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250|UniProtKB:P11352}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000250|UniProtKB:P11352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. In platelets catalyzes the redu... | Oryctolagus cuniculus (Rabbit) |
P11911 | CD79A_MOUSE | MPGGLEALRALPLLLFLSYACLGPGCQALRVEGGPPSLTVNLGEEARLTCENNGRNPNITWWFSLQSNITWPPVPLGPGQGTTGQLFFPEVNKNHRGLYWCQVIENNILKRSCGTYLRVRNPVPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKFGVDMPDDYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGNLHIGDAQLEKP | null | null | adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853] | B cell receptor complex [GO:0019815]; external side of plasma membrane [GO:0009897]; IgM B cell receptor complex [GO:0071755]; membrane raft [GO:0045121]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF00047;PF02189; | 2.60.40.10; | null | PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases, including LYN, is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass type I membrane protein {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}. Note=Following antigen binding, the BCR has been shown to translocate ... | null | null | null | null | null | FUNCTION: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and ... | Mus musculus (Mouse) |
P11912 | CD79A_HUMAN | MPGGPGVLQALPATIFLLFLLSAVYLGPGCQALWMHKVPASLMVSLGEDAHFQCPHNSSNNANVTWWRVLHGNYTWPPEFLGPGEDPNGTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQPPPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKLGLDAGDEYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGSLNIGDVQLEKP | null | null | adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853] | B cell receptor complex [GO:0019815]; external side of plasma membrane [GO:0009897]; IgM B cell receptor complex [GO:0071755]; membrane raft [GO:0045121]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF00047;PF02189; | 2.60.40.10; | null | PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activa... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and ... | Homo sapiens (Human) |
P11913 | MPPB_NEUCR | MASRRLALNLAQGVKARAGGVINPFRRGLATPHSGTGIKTQTTTLKNGLTVASQYSPYAQTSTVGMWIDAGSRAETDETNGTAHFLEHLAFKGTTKRTQQQLELEIENMGAHLNAYTSRENTVYFAKALNEDVPKCVDILQDILQNSKLEESAIERERDVILRESEEVEKQLEEVVFDHLHATAYQHQPLGRTILGPRENIRDITRTELVNYIKNNYTADRMVLVGAGGVPHEQLVEMADKYFSKLPATAPVSSASILSKKKPDFIGSDIRIRDDTIPTANIAIAVEGVSWSDDDYFTGLVTQAIVGNYDKALGNAPHQG... | 3.4.24.64 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:2967109}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507}; | protein processing involved in protein targeting to mitochondrion [GO:0006627] | mitochondrial inner membrane [GO:0005743]; mitochondrial processing peptidase complex [GO:0017087]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:2967109}. Mitochondrion inner membrane {ECO:0000269|PubMed:226365}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07256}; Matrix side {ECO:0000250|UniProtKB:P07256}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000269|PubMed:2967109, ECO:0000269|PubMed:8106471}; | null | null | null | null | FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2967109). Preferentially, cleaves after an arginine at position P2 (PubMed:8106471). {ECO:0000269|PubMed:2967109, ECO:0000269|PubMed:8106471}.; FU... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P11914 | MPPA_YEAST | MLRNGVQRLYSNIARTDNFKLSSLANGLKVATSNTPGHFSALGLYIDAGSRFEGRNLKGCTHILDRLAFKSTEHVEGRAMAETLELLGGNYQCTSSRENLMYQASVFNQDVGKMLQLMSETVRFPKITEQELQEQKLSAEYEIDEVWMKPELVLPELLHTAAYSGETLGSPLICPRELIPSISKYYLLDYRNKFYTPENTVAAFVGVPHEKALELTEKYLGDWQSTHPPITKKVAQYTGGESCIPPAPVFGNLPELFHIQIGFEGLPIDHPDIYALATLQTLLGGGGSFSAGGPGKGMYSRLYTHVLNQYYFVENCVAFN... | null | null | protein processing involved in protein targeting to mitochondrion [GO:0006627]; proteolysis [GO:0006508] | mitochondrial matrix [GO:0005759]; mitochondrial processing peptidase complex [GO:0017087]; mitochondrion [GO:0005739] | endopeptidase activator activity [GO:0061133]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:2007593}. | null | null | null | null | null | FUNCTION: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. {ECO:0000269|PubMed:9299349}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11915 | SCP2_RAT | MPSVALNSPRLPRVFVVGVGMTKFMKPGGENSRDYPDLAKEAGQKALADRQIPYSAVEQACVGYVYGESTCGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAQQLVQGGLANCVLALGFEKMEKGSLGTKYSDRSNPLEKHIDVLINKYGMSACPFAPQLFGSAGKEHMETYGTKVEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEIMKSRPVFDFLTVLQCCPTSDGAAAAIVSSEEFVQKHGLQSKAVEIVAQEMVTDMPSTFEEKSVIKMVGYDMSKEAARKCYEKSGLGPSDVDVIELHDCFSTNELLTYEALG... | 2.3.1.155; 2.3.1.16; 2.3.1.176 | null | bile acid metabolic process [GO:0008206]; cellular response to cholesterol [GO:0071397]; fatty acid beta-oxidation [GO:0006635]; intracellular cholesterol transport [GO:0032367]; lipid hydroperoxide transport [GO:1901373]; phospholipid transport [GO:0015914]; positive regulation of apoptotic process [GO:0043065]; posit... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; fatty-acyl-CoA binding [GO:0000062]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA binding [GO:0036042]; oleic ac... | PF02036;PF02803;PF00108; | 3.40.47.10;3.30.1050.10; | Thiolase-like superfamily, Thiolase family | PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about 15 kDa, is processed into its mature form (SCP2) by proteolytic cleavage of a 20 residue leader sequence after translocation into peroxisomes. {ECO:0000250|UniProtKB:O62742}. | SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000250|UniProtKB:P22307}. Mitochondrion {ECO:0000250|UniProtKB:P22307}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {ECO:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339}. | CATALYTIC ACTIVITY: [Isoform SCPx]: 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:8063752, ECO:0000305|PubMed:9325339}; PhysiologicalDirection=right-to-left; Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for 3-oxooctanoyl-CoA {ECO:0000269|PubMed:9325339}; KM=4 uM for 3-oxohexadecanoyl-CoA {ECO:0000269|PubMed:9325339}; KM=2.9 uM for 3-oxohexadecanedioyl-CoA {ECO:0000269|PubMed:9325339}; KM=3 uM for 3-oxo-2-methylpalmitoyl-CoA {ECO:0000269|PubMed:9325339}; KM=... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6 with 3-oxooctanoyl-CoA and 3-oxo-2-methylpalmitoyl-CoA as substrates (PubMed:9325339). Optimum pH is 9.5 with 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA as substrate (PubMed:10706581). {ECO:0000269|PubMed:10706581, ECO:0000269|PubM... | null | FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids (PubMed:8063752, PubMed:9325339). Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA ... | Rattus norvegicus (Rat) |
P11916 | RNASO_AQUCT | MCAKSLLLVFGILLGLSHLSLSQNWATFQQKHIINTPIINCNTIMDNNIYIVGGQCKRVNTFIISSATTVKAICTGVINMNVLSTTRFQLNTCTRTSITPRPCPYSSRTETNYICVKCENQYPVHFAGIGRCP | 3.1.27.- | null | angiogenesis [GO:0001525]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; endonuclease activity [GO:0004519]; nucleic acid binding [GO:0003676]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Preferentially cleaves single-stranded RNA at pyrimidine residues with a 3'flanking guanine. Hydrolyzes poly(U) and poly(C) as substrates, and prefers the former. The S-lectins in frog eggs may be involved in the fertilization and development of the frog embryo. This lectin agglutinates various animal cells, ... | Aquarana catesbeiana (American bullfrog) (Rana catesbeiana) |
P11926 | DCOR_HUMAN | MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVND... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26443277}; | 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 from ornithine [GO:0033387]; regulation of protein catabolic process [GO:0042176]; response to virus [... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ornithine decarboxylase activity [GO:0004586]; protein homodimerization activity [GO:0042803] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | PTM: S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues. {ECO:0000269|PubMed:10462479, ECO:0000269|PubMed:11461922}. | 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:0000269|PubMed:17407445}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.08 mM for L-ornithine {ECO:0000269|PubMed:17407445}; Note=kcat is 3.3 sec(-1) with L-ornithine as substrate. {ECO:0000269|PubMed:17407445}; | 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.... | Homo sapiens (Human) |
P11928 | OAS1A_MOUSE | MEHGLRSIPAWTLDKFIEDYLLPDTTFGADVKSAVNVVCDFLKERCFQGAAHPVRVSKVVKGGSSGKGTTLKGKSDADLVVFLNNLTSFEDQLNRRGEFIKEIKKQLYEVQHERRFRVKFEVQSSWWPNARSLSFKLSAPHLHQEVEFDVLPAFDVLGHVNTSSKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKLGKPLPPQYALELLTVFAWEQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRR... | 2.7.7.84 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00973}; | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of viral genome replication [GO:0045071]; negative regulation of viral process [GO:0048525]; purine nucleotide biosynthetic process [GO:0006164]; response to virus [GO:0009615] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872] | PF01909;PF10421; | 1.10.1410.20;3.30.460.10; | 2-5A synthase family | PTM: C-terminal prenylated. {ECO:0000305|PubMed:34581622}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}. Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus {ECO:0000250|UniProtKB:P00973}. Microsome {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00973}. Note=Associated with different subcellular fractions such as mitochondrial,... | CATALYTIC ACTIVITY: Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence={ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:2171206, ECO:0000305|PubMed:... | null | null | null | null | FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2... | Mus musculus (Mouse) |
P11929 | NINL_DROME | MEVSADPYEQKLYQMFRSCETQCGLLDEKSLLKLCSLLELRDQGSALIASLGGSHQLGVSFGQFKEALLNFLGSEFDGNTSSGFIERSLVITDEPLNNTYIESPPESSDREVSPKLVVGTKKYGRRSRPQQGIYELSVTDSDNTDEDQLQQQQNQRSLNGCDELGVQVQRSSSQSDLPGSRRLRSVHTSGSKLKRCASLPARRKMNSNTTGATTSPTAAAKLKQLSIQSQAQHSSSVESLDTVTPQQLETISVHSIMEAWELASIPNTRNLLHVLGFDEEEEVNLQQLTKALEEELRGIDGDHEQSNMLRALAALQATEL... | null | null | microtubule anchoring at centrosome [GO:0034454]; microtubule organizing center attachment site organization [GO:0034994] | centrosome [GO:0005813]; pericentriolar material [GO:0000242]; perinuclear region of cytoplasm [GO:0048471] | microtubule binding [GO:0008017] | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27053665, ECO:0000269|PubMed:27422905}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:27053665, ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:320669... | null | null | null | null | null | FUNCTION: Required for the positioning and anchorage of the microtubule minus-ends in various cells (PubMed:27422905, PubMed:30626718, PubMed:32066907). In fat body cells, part of perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) which function to accommodate the organization of microtubule (MT) netw... | Drosophila melanogaster (Fruit fly) |
P11930 | NUD19_MOUSE | MSSSSSWRRAATVMLAAGWTHSSPAGFRLLLLQRAQNQRFLPGAHVFPGGVLDAADSSPDWVRLFAPRHTPPRFGLGPEPPRQPPFPGLSHGDADPAALPDDVALRICAIREAFEEAGVLLLRPRDAAPASQEPSQALSPPAGLAEWRSRVRSDPRCFLQLCAHLDCTPDIWALHDWGGWLTPYGRTIRRFDTTFFLCCLRDIPRVEPDVAEVVGYQWLSPSEATECFLSKEIWLAPPQFYEMRRLENFASLSALYRFCSDRPSEVPEKWLPIILLTSDGTIHLLPGDELYVKDSDFLEKNMSTDKKTEEIVKEGKVLNR... | 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16185196}; | butyryl-CoA catabolic process [GO:0044580]; coenzyme A catabolic process [GO:0015938]; malonyl-CoA catabolic process [GO:2001294]; medium-chain fatty-acyl-CoA catabolic process [GO:0036114]; propionyl-CoA metabolic process [GO:1902858]; succinyl-CoA catabolic process [GO:1901289] | mitochondrion [GO:0005739]; peroxisome [GO:0005777] | coenzyme A diphosphatase activity [GO:0010945]; magnesium ion binding [GO:0000287] | null | 3.90.79.10; | Nudix hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343, ChEBI:CHEBI:132023; Evidence={ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}; Physiological... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for CoA {ECO:0000269|PubMed:16185196}; KM=0.58 mM for oxidized CoA {ECO:0000269|PubMed:16185196}; KM=0.08 mM for lauroyl-CoA {ECO:0000269|PubMed:16185196}; KM=0.01 mM for palmitoyl-CoA {ECO:0000269|PubMed:16185196}; KM=0.1 mM for choloyl-CoA {ECO:0000269|Pub... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:16185196}; | null | FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (PubMed:16185196, PubMed:29378847). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low sub... | Mus musculus (Mouse) |
P11936 | DNAS1_PIG | MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQDDPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPSDAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAGPLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA | 3.1.21.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:3782104}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3782104}; Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+). {ECO:0000269|PubMed:3782104}; | apoptotic process [GO:0006915]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948] | extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; zymogen granule [GO:0042588] | actin binding [GO:0003779]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677] | PF03372; | 3.60.10.10; | DNase I family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:3782104}; | null | null | null | null | FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:3782104). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:3782104). Binds s... | Sus scrofa (Pig) |
P11938 | RAP1_YEAST | MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVN... | null | null | establishment of protein localization to chromatin [GO:0071169]; establishment of protein localization to telomere [GO:0070200]; G-quadruplex DNA formation [GO:0071919]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ribosomal protein gene transcription by RNA polymerase ... | chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; shelterin complex [GO:0070187]; transcription regulator complex [GO:0005667] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding, bending [GO:0008301]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [G... | PF16589;PF00249;PF09197;PF11626; | 1.10.10.2170;1.20.120.1480;3.40.50.10190;1.10.10.60; | RAP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96TL7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q96TL7}. | null | null | null | null | null | FUNCTION: Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements: promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regula... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11939 | FOS_CHICK | MMYQGFAGEYEAPSSRCSSASPAGDSLTYYPSPADSFSSMGSPVNSQDFCTDLAVSSANFVPTVTAISTSPDLQWLVQPTLISSVAPSQNRGHPYGVPAPAPPAAYSRPAVLKAPGGRGQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEEEKSALQAEIANLLKEKEKLEFILAAHRPACKMPEELRFSEELAAATALDLGAPSPAAAEEAFALPLMTEAPPAVPPKEPSGSGLELKAEPFDELLFSAGPREASRSVPDMDLPGASSFYASDWEPLGAGSGGELEPLCTPVVTCTPC... | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to calcium ion [GO:0071277]; cellular response to extracellular stimulus [GO:0031668]; cellular response to reactive oxygen species [GO:0034614]; nervous system development [GO:0007399]; osteoclast differentiation [GO:0030316]; positive regulation of miRN... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription factor AP-1 complex [GO:0035976] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: May be Tyr-phosphorylated in quiescent cells and dephosphorylated upon cell growth induction. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, may be present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and later to the nucleus (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. FOS has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation... | Gallus gallus (Chicken) |
P11940 | PABP1_HUMAN | MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTI... | null | null | CRD-mediated mRNA stabilization [GO:0070934]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; mRNA stabilization [GO:0048255]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; negative regulation of nuclear-transcribed mRNA ca... | catalytic step 2 spliceosome [GO:0071013]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; mCRD-mediated... | mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; translation activator activity [GO:0008494] | PF00658;PF00076; | 3.30.70.330;1.10.1900.10; | Polyadenylate-binding protein type-1 family | PTM: Phosphorylated by MAPKAPK2. {ECO:0000269|PubMed:12565831}.; PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000269|PubMed:11850402, ECO:0000269|Ref.6, ECO:0000269|Ref.7}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:23077296, ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:31649314, ECO:0000269|PubMed:7908267, ECO:0000269|PubMed:9582337}. Cytoplasm, Stress granule {ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150, ... | null | null | null | null | null | FUNCTION: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability (PubMed:11051545, PubMed:17212783, PubMed:25480299). Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by... | Homo sapiens (Human) |
P11941 | LYSC2_ONCMY | MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCDDGRTPGAKNVCGIRCSQLLTADLTVAIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVAGCGV | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | extracellular space [GO:0005615] | lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|PubMed:15142536}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.5. No activity above pH 8.8. {ECO:0000269|PubMed:15142536}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33-49 degrees Celsius. Retains 25% of its maximal activity after heating 10 minutes at 80 degrees Celsius. {ECO:0000269|PubMed:15142536}; | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bac... | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) |
P11942 | CD3G_MOUSE | MEQRKGLAGLFLVISLLQGTVAQTNKAKNLVQVDGSRGDGSVLLTCGLTDKTIKWLKDGSIISPLNATKNTWNLGNNAKDPRGTYQCQGAKETSNPLQVYYRMCENCIELNIGTISGFIFAEVISIFFLALGVYLIAGQDGVRQSRASDKQTLLQNEQLYQPLKDREYDQYSHLQGNQLRKK | null | null | adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; establishment or maintenance of cell polarity [GO:0007163]; positive thymic T cell selection [GO:0045059]; protein transport [GO:0015031]; regulation of lymphocyte apoptotic process [GO:0070228] | alpha-beta T cell receptor complex [GO:0042105]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF16680;PF02189; | 2.60.40.10; | null | PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. Phosphorylated also by PKC; leading to the TCR complex down-regulation. {ECO:0000250|UniProtKB:P09693}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... | Mus musculus (Mouse) |
P11943 | ACPM_NEUCR | MFRTAALTAARVARPAVASAVRAGVARPAFVQAVPKVAAFQAVRFYSAGGHLKKDEVFSRIAQVLSGFDKVNDPKNITETAHFANDLGLDSLDTVEVVMAIEEEFSIEIPDKDADQIHSVDKAVEYILSQPDAN | null | null | iron-sulfur cluster assembly [GO:0016226]; lipoate biosynthetic process [GO:0009107] | mitochondrial iron-sulfur cluster assembly complex [GO:0099128]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | acyl binding [GO:0000035]; acyl carrier activity [GO:0000036] | PF00550; | 1.10.1200.10; | Acyl carrier protein (ACP) family | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion. | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons ... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P11954 | TDCB_SALTY | MHITYDLPVAIEDILEAKKRLAGKIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTEAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVETEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAIAIKSINPTIKVIGVQAENVHGMAASYYTGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVITEGAGALACAALLSGKLDSHIQNRKTVSIISGGNIDLSRV... | 4.3.1.17; 4.3.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; L-threonine catabolic process to propionate [GO:0070689]; threonine catabolic process [GO:0006567] | null | L-serine ammonia-lyase activity [GO:0003941]; nucleotide binding [GO:0000166]; pyridoxal phosphate binding [GO:0030170]; threonine deaminase activity [GO:0004794] | PF00291; | 3.40.50.1100; | Serine/threonine dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 mM for L-threonine (in the presence of 5 mM of AMP at 25 dregrees Celsius and at pH 8) {ECO:0000269|PubMed:17046821}; KM=32 mM for L-threonine (in the presence of 5 mM of CMP at 25 dregrees Celsius and at pH 8) {ECO:0000269|PubMed:17046821}; KM=123 mM for L-thre... | PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 1/4. | null | null | FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and sh... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P11960 | ODBA_RAT | SAAKIWRPSRGLRQAALLLLGRPGARGLARFHPSRQQQQQFPSLDDKPQFPGASAEFVDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPQEEVLKLYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMAQCYGNVSDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANQIVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPF... | 1.2.4.4 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P12694}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P12694}; | branched-chain amino acid catabolic process [GO:0009083]; response to cAMP [GO:0051591]; response to glucocorticoid [GO:0051384]; response to nutrient [GO:0007584] | mitochondrial branched-chain alpha-keto acid dehydrogenase complex [GO:0160120]; mitochondrial oxoglutarate dehydrogenase complex [GO:0009353] | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity [GO:0003863]; branched-chain alpha-keto acid dehydrogenase activity [GO:0047101]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877] | PF00676; | 3.40.50.970; | BCKDHA family | PTM: Phosphorylated at Ser-333 by BCKDK and dephosphorylated by protein phosphatase PPM1K. {ECO:0000269|PubMed:29779826}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P12694}. | CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]; Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rh... | null | null | null | null | FUNCTION: Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producin... | Rattus norvegicus (Rat) |
P11961 | ODP2_GEOSE | MAFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGYENMTFKGQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEAGPNRRVIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGAKPAPAAAEEKAAPAAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAHRKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTSIDDETEEIIQKHYYNIGIAADTDRGLLVPVIKHADRKPIFALAQ... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently.; | null | cytoplasm [GO:0005737] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; lipoic acid binding [GO:0031405] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P11962 | GLHA_RAT | MDCYRRYAAVILVMLSMVLHILHSLPDGDLIIQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKSFTKATVMGNARVENHTDCHCSTCYYHKS | null | null | cellular response to hormone stimulus [GO:0032870]; developmental growth [GO:0048589]; follicle-stimulating hormone secretion [GO:0046884]; G protein-coupled receptor signaling pathway [GO:0007186]; gonad development [GO:0008406]; luteinizing hormone secretion [GO:0032275]; negative regulation of organ growth [GO:00466... | extracellular space [GO:0005615]; follicle-stimulating hormone complex [GO:0016914]; pituitary gonadotropin complex [GO:0061696] | follicle-stimulating hormone activity [GO:0016913]; hormone activity [GO:0005179] | PF00236; | 2.10.90.10; | Glycoprotein hormones subunit alpha family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01215}. | null | null | null | null | null | FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. {ECO:0... | Rattus norvegicus (Rat) |
P11972 | SST2_YEAST | MVDKNRTLHELSSKNFSRTPNGLIFTNDLKTVYSIFLICLDLKEKKHSSDTKSFLLTAFTKHFHFTFTYQEAIKAMGQLELKVDMNTTCINVSYNIKPSLARHLLTLFMSSKLLHTPQDRTRGEPKEKVLFQPTPKGVAVLQKYVRDIGLKTMPDILLSSFNSMKLFTFERSSVTDSIIHSDYLIHILFIKMMGAKPNVWSPTNADDPLPCLSSLLEYTNNDDTFTFEKSKPEQGWQAQIGNIDINDLERVSPLAHRFFTNPDSESHTQYYVSNAGIRLFENKTFGTSKKIVIKYTFTTKAIWQWIMDCTDIMHVKEAVS... | null | null | cellular response to pheromone [GO:0071444]; intracellular signal transduction [GO:0035556]; negative regulation of signal transduction [GO:0009968]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096] | PF00610;PF00615; | 1.10.167.10;1.10.10.10; | null | PTM: Phosphorylated by FUS3 and KSS1. {ECO:0000269|PubMed:10593933}. | null | null | null | null | null | null | FUNCTION: Desensitization to alpha-factor pheromone. Is involved in regulating the signaling pathway for responding to mating pheromone. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11974 | KPYM_RABIT | MSKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMIIGRCNRA... | 2.7.1.40; 2.7.10.2; 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9308890}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:9308890}; | cellular response to insulin stimulus [GO:0032869]; phosphorylation [GO:0016310]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of sprouting angiogenesis [GO:1903672] | nucleus [GO:0005634]; rough endoplasmic reticulum [GO:0005791] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; mRNA binding [GO:0003729]; potassium ion binding [GO:0030955]; protein tyrosine kinase activity [GO:0004713]; pyruvate kinase activity [GO:0004743] | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P14618}.; PTM: Under hypoxia, hydroxylated by EGLN3. {ECO:0000250|UniProtKB:P14618}.; PTM: Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:00002... | SUBCELLULAR LOCATION: [Isoform M2]: Cytoplasm {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli. {ECO:0000250|UniProtKB:P14618}.; SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm {ECO... | CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P14618}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:1... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P14618}. | null | null | FUNCTION: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic proc... | Oryctolagus cuniculus (Rabbit) |
P11978 | SIR4_YEAST | MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVAS... | null | null | double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of protein-containing complex localization to telomere [GO:0097695]; heterochromatin formation [GO:0031507]; positive regulation of heterochromatin formation [GO:0031453]; silent mating-type cassette heterochromatin formation [GO:00304... | chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781] | double-stranded DNA binding [GO:0003690]; molecular adaptor activity [GO:0060090]; nucleosome binding [GO:0031491] | PF16991; | 6.10.140.1820;1.20.5.730; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR (PubMed:18039933). The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure (PubMed:18039933). Involves the compaction of chromatin fiber into a more condensed f... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
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