Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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B1AS29 | GRIK3_MOUSE | MTAPWRRLRSLVWEYWAGFLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQSLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWAMERLQAAPRAESGLLDGVMM... | null | null | modulation of chemical synaptic transmission [GO:0050804]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; regulation of membrane potential [GO:0042391]; synaptic transmission, glutamatergic [GO:0035249] | axon [GO:0030424]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; glutamatergic synapse [GO:0098978]; kainate selective glutamate receptor complex [GO:0032983]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; terminal bouton ... | adenylate cyclase inhibiting G protein-coupled glutamate receptor activity [GO:0001640]; glutamate receptor activity [GO:0008066]; glutamate-gated receptor activity [GO:0004970]; kainate selective glutamate receptor activity [GO:0015277]; ligand-gated monoatomic ion channel activity involved in regulation of presynapti... | PF01094;PF00060;PF10613; | 1.10.287.70;3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, GRIK3 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Receptor for glutamate that functions as a ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by ... | Mus musculus (Mouse) |
B1ATG9 | TIKI2_MOUSE | MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRHPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTHVYFELDLTDPYTISALASCQLLPHGENLQDVLPRELYWRLKRHLDYVKLMIPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTETDVRSRGVPVLDLYLAQQAEKMKKSTGAVERVEEQCHPLNGLNFSQVLFALNQTLLQHESVRAGSLQAPYTTEDLIKHYNCGDLNAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLQENQDK... | 3.4.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000250}; | negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of protein oxidation [GO:1904808]; positive regulation of protein-containing complex assembly [GO:0031334]; proteolysis [GO:0006508]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; Wnt-protein binding [GO:0017147] | PF01963; | null | TIKI family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23152936}; Single-pass type I membrane protein {ECO:0000269|PubMed:23152936}. | null | null | null | null | null | FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5... | Mus musculus (Mouse) |
B1AUH1 | PTPRU_MOUSE | MARAQALVLALTFQFCAPETETPAAGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRK... | 3.1.3.48 | null | animal organ regeneration [GO:0031100]; cell differentiation [GO:0030154]; dephosphorylation [GO:0016311]; homotypic cell-cell adhesion [GO:0034109]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferat... | cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | beta-catenin binding [GO:0008013]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF00629;PF00102; | 2.60.120.200;2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2B subfamily | PTM: The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylated ... | SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1AVY7 | KI16B_MOUSE | MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAANPLVKKKQVFVPYRDSVLTWLLK... | null | null | cellular response to type II interferon [GO:0071346]; early endosome to late endosome transport [GO:0045022]; endoderm development [GO:0007492]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; formation of primary germ layer [GO:0001704]... | cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; phagocytic vesicle [GO:0045335]; spindle [GO:0005819] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate bindin... | PF00498;PF00225;PF00787; | 2.60.200.20;3.40.850.10;3.30.1520.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96L93}. Early endosome membrane {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96L93}. Note=It is unclear whether association with endosomes is mediated via phosphati... | null | null | null | null | null | FUNCTION: Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golg... | Mus musculus (Mouse) |
B1AWL2 | ZN462_MOUSE | MEVLQCDGCDFRAPSYEDLKAHIQDVHTAFLQPTDVAEDNDDEPLSGSMNASNQTEVEFSSIKDEFVIAEDLPGQSATALGSGGYYGHSPGYYGQHITPNPKPTNKFFQCKFCVRYFRSKNLLIEHTRKVHGAQAEESPTGPPVPGSLNYNIMMHEGFGKVFSCQFCTYKSPRRARIIKHQKMYHKNSLKESTAPPPAPAPLPDPLVPPVSLQDPCKELPAEVVERSILESMVKPLTKSRGNFCCEWCSYQTPRRERWCDHMMKKHRSMVKILSSIRQQEGPNVSEAQNDNEPSPTSNSTYLSMNAASREMPNANVSNFR... | null | null | chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | null | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965}. | null | null | null | null | null | FUNCTION: Zinc finger nuclear factor involved in transcription by regulating chromatin structure and organization (PubMed:20219459, PubMed:21570965). Involved in the pluripotency and differentiation of embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG (PubMed:21570965). By binding PBX1, prevents the heter... | Mus musculus (Mouse) |
B1AWN4 | AT10B_MOUSE | MTCSLDFSWLRWKWRTQDGFSQSPSETTPLLSPETDRQSHNTAEQRVVYPNNSMCHQDWKKVCRRYPGNSICTTKYTLLTFLPQNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITIFPLATVLLIIMVKDGIEDFKRYCFDREMNSASIQIYERKEQRYMLKRWQDVRVGDFVQMQCNEIVPADILLLFSSDPSGVCHLETANLDGETNLKQRRVVKGFSQPEVQFQPEHFHSTIVCEKPNNHLSKFKGYMEHPDQTRTGFGSESLLLRGCTIRNTEVAAGIVIYAGHETKAMLNNSGPRYKRSKIERRINTDIFFC... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | lysosomal membrane organization [GO:0097212]; phospholipid translocation [GO:0045332] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345] | PF13246;PF16212;PF16209; | 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 IV subfamily | PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000250|UniProtKB:O94823}. | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O94823}; Multi-pass membrane protein {ECO:0000255}. Not... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O94823}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + pho... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes (By similarity). Plays an important role in the maintenance of lysosome membrane integrity and function in ... | Mus musculus (Mouse) |
B1AWN6 | SCN2A_MOUSE | MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTMNMFNWDEYI... | null | null | cellular response to hypoxia [GO:0071456]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; intrinsic apoptotic signaling pathway in response to osmotic stress [GO:0008627]; membrane depolarization during action potential [GO:0086010]; memory [GO:0007613]; nerve development [GO:0021... | axon [GO:0030424]; axon initial segment [GO:0043194]; glutamatergic synapse [GO:0098978]; intercalated disc [GO:0014704]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; T-tubule [GO:0030315]; voltage-gated sodiu... | calmodulin binding [GO:0005516]; leucine zipper domain binding [GO:0043522]; sodium channel activity [GO:0005272]; sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.2/SCN2A subfamily | PTM: Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases voltage-gated sodium current and mediates the early response to acute hypoxia in neurons. Sumoylated SCN2A is located at the cell membrane. {ECO:0000250|UniProtKB:P04775}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827969}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10827969, ECO:0000269|PubMed:11166117, ECO:0000269|PubMed:28137877}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (Pu... | Mus musculus (Mouse) |
B1AXD8 | AKIR2_MOUSE | MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPASAAASPAAATAAAAASAAAASPQKYLRMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLEASFQQADPGCTSDSQPHAFLISGPASPGTSSATSSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYDAFVKFTHDQIMRRYGEQPASYVS | null | null | adaptive immune response [GO:0002250]; cerebral cortex development [GO:0021987]; defense response to bacterium [GO:0042742]; embryo development ending in birth or egg hatching [GO:0009792]; innate immune response [GO:0045087]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; transcription coregulator activity [GO:0003712] | null | null | Akirin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25107474, ECO:0000269|PubMed:30116001, ECO:0000269|PubMed:30801883}. Cytoplasm {ECO:0000269|PubMed:30801883}. Membrane {ECO:0000269|PubMed:30801883}. Note=Present mainly in the nuclear fraction, and at much lower level in the cytoplasmic and membrane fractions. {ECO:000... | null | null | null | null | null | FUNCTION: Molecular adapter that acts as a bridge between a variety of multiprotein complexes, and which is involved in embryonic development, immunity, myogenesis and brain development (PubMed:25107474, PubMed:26041538, PubMed:27871306, PubMed:30116001, PubMed:30801883). Plays a key role in nuclear protein degradation... | Mus musculus (Mouse) |
B1AY10 | NFX1_MOUSE | MAEAPPVSGTFKFNTDAAEFIPQERKTSGLNCGTQRRLDSSRIGRRNYSSSPPCHLPRHIPYEDISAVHQHSYASGSKPKSPQGFFQSSNKSLKNHGLQNQPWQKARNEKHQNRNKKAQGLSEQTSDTSSLESVARSESGTNPREHSPSESEKEVVIADPRGAKPKKAAQLTYNYGRGPKAKGRLRSEWGNRMSPKSEDENTRPVAISHTDSSDASCRKPVVDPCVCRRNEQRRYPQKRPPWEVEGARPRPGRNPPKQESQRHINAGPKTNMSPIPKDNLRERPTKSACDTGNLAVVSKSSRRVNQEKTAVRRQDPQVLS... | 2.3.2.- | null | negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein autoubiquitination [GO:0051865] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; ubiquitin protein ligase activity [GO:0061630]; zinc io... | PF01424;PF01422; | 3.30.1370.50; | NFX1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Together with PABPC1 or PABPC4, acts as a coactivator for TER... | Mus musculus (Mouse) |
B1AY15 | UBP51_MOUSE | MRGTQGAQEMKPELWPEPKPTSENLTSRGSGSYEKVLPSIPAACHTSSSSVCPRRKPRPRPQPRSRSRGGRGLKAPPPPPAKPPPPPPAPPPPPLPKQRSVAWRNSRRRSRPGPRPQTRKSYSSDHGSSRDSDGSENSLLEVGSNKGPTGCCHVESFKVAKNWQRNLRMIYQRFIWSGTPETRKRKAKSCICQICSTHKNRLHSCLSCVFFGCFTDKHIHIHAETTQHNLAVDLCHGVIYCFMCRDYVYDKDIEKIAKETKEKILGLLSSPTGDASYQQLMASEVEENQLTCESKDQETSLVKPKKKRRKKTMYYTVGFR... | 3.4.19.12 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; proteolysis [GO:0006508]; regulation of cell cycle process [GO:0010564]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of double-strand break repair via non... | chromosome [GO:0005694] | chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843]; histone binding [GO:0042393]; histone H2A deubiquitinase activity [GO:0140950]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q70EK9}. Note=Dissociates from chromatin immediately after DNA damage and reassociates with chromatin following DNA repair. {ECO:0000250|UniProtKB:Q70EK9}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:27083998}; | null | null | null | null | FUNCTION: Specifically deubiquitinates 'Lys-14' (H2AK13Ub) and 'Lys-16'(H2AK15Ub) of histone H2A regulating the DNA damage response at double-strand breaks (DSBs). USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1 (PubMed:27083998). Functions in DNA dou... | Mus musculus (Mouse) |
B1AYL1 | SCN7A_MOUSE | MLTSPEPKGLVPFTTESLELIENHIAKKCNEDPEEEEGLKPSRNLEAGKRLPIPYGTLPRGTVSEPLEDVDPYYYVKRNTFMVLNRSRVIFRFNAVSIFCTLSPLNSLRRAAIKALVHPLFRLLILISVLTDSILMCMSNLPEWILAIENTLLGIYAFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRFSPLSSFLMLKTIRTFRILKIIPLNHGLQSIVMTLAQCLKKLFGAIALALFFLAVFSLLGMGLFMGNLKHKCLRWPEENENETLHNRTGSLNYSPERINFYYMEGAKYALLCGNRTDAGQCPEG... | null | null | cellular homeostasis [GO:0019725]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; osmosensory signaling pathway [GO:0007231]; response to bacterium [GO:0009617]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725] | axon [GO:0030424]; glial cell projection [GO:0097386]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518] | osmolarity-sensing monoatomic cation channel activity [GO:1990760]; sodium channel activity [GO:0005272]; transmembrane transporter binding [GO:0044325]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, SCN7A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17408578}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:11992118, ECO:0000269|PubMed:17408578}; | null | null | null | null | FUNCTION: Sodium leak channel functioning as an osmosensor regulating sodium ion levels in various tissues and organs. While most sodium channels are voltage-gated, SCN7A is not and lets sodium flow through membrane along its concentration gradient (PubMed:11027237, PubMed:11992118, PubMed:17408578, PubMed:27252474). I... | Mus musculus (Mouse) |
B1AZ99 | OTUD3_MOUSE | MSRKQAAKSRPGSGGRRAEAERKRDERAARRALAKERRNRPDPGGSGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLSKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAPAHLLTDFQMLHQDGANKKEKMKTKGVDVKDGLRDDVEDAVHKVGSATGCTDFNLIVQNLEAENYNIKSAITALLQVNQGTGNDAEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGRMETSE... | 3.4.19.12 | null | cellular response to nutrient levels [GO:0031669]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; protein K11-linked deubiquitination [GO:0035871]; protein K6-linked deubiquitination [GO:0044313]; protein stabilization [GO:0050821]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF02338; | 3.90.70.80; | null | PTM: Glucose and fatty acids stimulate CREBBP-dependent acetylation, promoting its nuclear translocation. {ECO:0000269|PubMed:35675826}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35675826}. Nucleus {ECO:0000269|PubMed:35675826}. Note=Glucose or fatty acid promote nuclear translocation upon acetylation. {ECO:0000269|PubMed:35675826}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000305|PubMed:35675826}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin (PubMed:35675826). Also hydrolyzes heterotypic (mixed and branched) and homotypic chains (PubMed:35675826). Important regulator of energy metabolism (PubMed:35675826). Glucose and fatty acids trigger its nuclear translocation b... | Mus musculus (Mouse) |
B1AZI6 | THOC2_MOUSE | MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGNLKHEQASSVLNDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSDTVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELGQDLSGNITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCEPQTLCHILGFKFKFYQEPSGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEYKREIVEAKQIVRKLTMVVLSS... | null | null | blastocyst development [GO:0001824]; cell morphogenesis [GO:0000902]; generation of neurons [GO:0048699]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; negative regulation of neuron projection development [GO:0010977]; neuron development [GO:0048666]; poly(A)+ mRNA export from nucleus [GO:0016973... | chromosome, telomeric region [GO:0000781]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; THO complex part of transcription export complex [GO:0000445] | mRNA binding [GO:0003729] | PF11262;PF11732;PF16134; | null | THOC2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as a component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruit... | Mus musculus (Mouse) |
B1AZP2 | DLGP4_MOUSE | MKGLGDSRPRHLSDSLDPPHEPLFAGPDRNPYLLSPTEAFAREARFPGQNTLPGDGLFPLNNQLPPPSSTFPRIHYNSHFEVPEESPFPSHAQATKINRLPANLLDQFEKQLPIHRDGFSTLQFPRGEAKARGESPGRIRHLVHSVQRLFFTKAPSMEGTAGKVGGNGSKKGGLEDGKGRRAKSKERAKAGEPKRRSRSNISGWWSSDDNLDGEGGAFRSGPASGLMTLGRQQERTQPRYFMHAYNTISGHMLKTTKNTTTELTAPPPPPAPPATCPSLGVGTDTNYVKRGSWSTLTLSHAHEVCQKTSATLDKSLLKSK... | null | null | signaling [GO:0023052] | cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; postsynaptic specialization [GO:0099572]; synapse [GO:0045202] | molecular adaptor activity [GO:0060090]; protein domain specific binding [GO:0019904] | PF03359; | null | SAPAP family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1B0V2 | EZHIP_MOUSE | MASSSSPERGLEALRDTDESEGEAPGPSGPRGRGGPSGAGSALRLRSLEAEMAAACVTSTAGEDLGTFSEPGSQHGDPEGGGGPDLELGHARPMMRSQRELGLTPKGGGKADQGGKGRKGGSGSPPHTKSSRKREQPNPNRSLMAQGAAGPPLPGARGSPAMPQPESSLSPRPDQSHHFDFPVGNLEAPGPTLRSSTSQGSGSTPVPEALRCAESSRAESDQSSPAGRELRQQASPRAPDDDDDGDGGPDPRGSGTPEGWVLRSGVVPFGRRSSASEVSPEEVRPEAQCTGWNLRPRPRSSASAVSPEARPKAQSAGRNL... | null | null | chromatin organization [GO:0006325]; oocyte development [GO:0048599] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | protein-containing complex binding [GO:0044877] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86X51}. Cytoplasm {ECO:0000250|UniProtKB:Q86X51}. | null | null | null | null | null | FUNCTION: Inhibits PRC2/EED-EZH1 and PRC2/EED-EZH2 complex function by inhibiting EZH1/EZH2 methyltransferase activity, thereby causing down-regulation of histone H3 trimethylation at 'Lys-27' (H3K27me3) (PubMed:31086175). Probably inhibits methyltransferase activity by limiting the stimulatory effect of cofactors such... | Mus musculus (Mouse) |
B1B534 | EHD2_ORYSJ | MLLSDLSSDQEATGSNSHGGGGGDRMVVGSHGAAHVVLSNLFLPPAAAAAATMLLPAAPVMVRPAAMAAAQEPRAKKKRSLPGNPDPEAEVIALSPRALVATNRFVCEVCNKGFQRDQNLQLHRRGHNLPWKLRHRAAAVSAVTTAAPAPRKRVYVCPEPTCVHHDPARALGDLTGIKKHFSRKHGEKRWRCERCGKRYAVHSDWKAHVKNCGTREYRCDCGILFSRKDSLLTHRAFCDALAEESARLLAAANNSSSITTTTCNNSNISSNNNNNNINSISNSNNLLITSSSSSPPLFLPFSTTPAENPNPNQLLFLQQH... | null | null | long-day photoperiodism, flowering [GO:0048574]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; short-day photoperiodism, flowering [GO:0048575] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF12874; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969, ECO:0000269|PubMed:24280027}. | null | null | null | null | null | FUNCTION: Transcription activator that acts as a flowering master switch in both long and short days, independently of the circadian clock (PubMed:18725639, PubMed:18774969, PubMed:18790997, PubMed:19304997, PubMed:24280027). Promotes flowering upstream of HD1 by up-regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT... | Oryza sativa subsp. japonica (Rice) |
B1H134 | FLRT3_XENTR | MSTETWNLFVAWAQLLLLFRISPQYVNAKPCPSVCRCDGGFIYCNDRDLTSIPSGIPDDATTLYLQNNQINNAGIPSDLRGLDKVERIYLYRNSLDEFPINLPKNVKELHLQENNIRTITYDALSQIPSIEELHLDDNSVSAVSIEDGAFRDNIFLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTIAEISLQDLTNLKRLVLDGNLLNNNGLGERVFMNLINLTELSLVRNSLTSPPANLPGTNLRKLYLQENHMNYVPPNAFADLTQLYRLDMSNNNITALPQGIFDDLDNLTQLFLRNNPWYCGCKMKWVRDWL... | null | null | cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; embryonic morphogenesis [GO:0048598]; fibroblast growth factor receptor signaling pathway [GO:0008543]; head development [GO:0060322]; heart development [GO:0007507]; neuron projection development [GO:0031175]; neuron projection extension [GO:19901... | axon terminus [GO:0043679]; axonal growth cone [GO:0044295]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060] | null | PF13855; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BGT1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon {EC... | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (By similarity). Modulates cadherin-dependent cell-cell adhesion and cell sorting (By similarity). Plays a role in the spatial organization of brain neurons. Plays ... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1H1X1 | FXL17_XENLA | MGHVAPHASKKEHVAPHAAEKDHVAPHASKKEHVAPHAAEKGQVAPYAAGEGQVAPNAAGERPVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEAQVAPHAAGEGRVAPHAAGDGQVEHCTVEDREEGHIGTTEQGHMSHYTSKLEHMAPPSAQTEAVVSYVAGERHAPPDCTVSGPAMCCSAEARQTTPDWTTTGPEISQGTLPGLTVLHVGGTWQTFAAEDEPCVTTLLSPVKPLSSSRKYAPYNLQIPSYSESEPQAHKGLSSETFGPCEPLHINQLPSSLLLKIFSNLSLNERCILASL... | null | null | nervous system development [GO:0007399]; neural crest cell differentiation [GO:0014033]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein ubiquitinatio... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | null | PF12937;PF13516; | 3.80.10.10; | FBXL17 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UF56}. Nucleus {ECO:0000250|UniProtKB:Q9UF56}. Note=Present in the cytoplasm and nucleus; more abundant in the cytoplasm. {ECO:0000250|UniProtKB:Q9UF56}. | null | null | null | null | null | FUNCTION: Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved ... | Xenopus laevis (African clawed frog) |
B1H234 | FLRT3_RAT | MISPAWSLFLIGTKIGLFFQVAPLSVMAKSCPSVCRCDAGFIYCNDRSLTSIPVGIPEDATTLYLQNNQINNVGIPSDLKNLLKVQRIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPGGLPRTIEELRLDDNRISTISSPSLHGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTSLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWL... | null | null | axon guidance [GO:0007411]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; embryonic morphogenesis [GO:0048598]; fibroblast growth factor receptor signaling pathway [GO:0008543]; head development [GO:0060322]; heart development [GO:0007507]; neuron projection development [GO:0031175]; neuron pr... | axon terminus [GO:0043679]; axonal growth cone [GO:0044295]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; gro... | chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104]; protein homodimerization activity [GO:0042803] | PF13855; | 3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Synapse, synaptosome {ECO:0000269|PubMed:22405201}. Postsynaptic density {ECO:0000269|PubMed:22405201}. Cell projection, dendrite {ECO:0000269|PubMed:22405201}. Sy... | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion v... | Rattus norvegicus (Rat) |
B1H267 | SNX5_RAT | MAAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYE... | null | null | epidermal growth factor catabolic process [GO:0007174]; intracellular protein transport [GO:0006886]; negative regulation of blood pressure [GO:0045776]; pinocytosis [GO:0006907]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of insulin receptor signaling pathway [GO:0046628]; ret... | brush border [GO:0005903]; cytoplasmic side of early endosome membrane [GO:0098559]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endosome [GO:0005768]; macropinocytic cup [GO:0070685]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; retromer complex [GO:0030904]; r... | D1 dopamine receptor binding [GO:0031748]; dynactin binding [GO:0034452]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314] | PF00787;PF09325; | 1.20.1270.60;3.30.1520.10; | Sorting nexin family | null | SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|Un... | null | null | null | null | null | FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi netw... | Rattus norvegicus (Rat) |
B1H278 | TRI11_RAT | MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECREVSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPTCERSEHWAHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALVSELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDS... | 2.3.2.27 | null | innate immune response [GO:0045087]; negative regulation of AIM2 inflammasome complex assembly [GO:0140972]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neurogenesis [GO:0050768]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral tra... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | protein domain specific binding [GO:0019904]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | TRIM/RBCC family | PTM: Autoubiquitinated upon DNA stimulation; autoubiquitination promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes. {ECO:0000250|UniProtKB:Q96F44}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F44}. Nucleus {ECO:0000250|UniProtKB:Q96F44}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96F44}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q96F44}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PA... | Rattus norvegicus (Rat) |
B1H3E1 | NLK2_XENTR | MAFQGPGRSLPGQLCAGVFGGLIQPPLGQKFYCPNGGSGGGGVPAVPSPLPQALSAPQCNGDGRGEPEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPQIDCFEEIYVITELMQTDLHKVIVSPQPLSSDHIKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESQHMTQEVVTQYYRAPEILMGSRHYRSAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPPLTAMRSACEGARAHILRGPHKPPSLSVLYM... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | anterior/posterior pattern specification [GO:0009952]; mesoderm formation [GO:0001707]; nervous system development [GO:0007399]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of protein ubiquitination [GO:0031398]; serine phosphorylation of STAT prote... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. | 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=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q8QGV6}; CATALYT... | null | null | null | null | FUNCTION: Negatively regulates Wnt/beta-catenin-signaling during development. Plays a role together with sox11 in neural induction during early embryogenesis. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 to phosphorylate stat3. Augments the rnf138/narf-directed ubiq... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1INP5 | BXB_CLOBK | MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIY... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P10844}; Note=Binds 1 zinc ion per subunit (By similarity). {ECO:0000250|UniProtKB:P10844}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | lipid binding [GO:0008289]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | SUBCELLULAR LOCATION: [Botulinum neurotoxin type B]: Secreted {ECO:0000250|UniProtKB:P10844}. Host synapse, host presynaptic cell membrane {ECO:0000250|UniProtKB:P10844}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin B light chain]: Secreted {ECO:0000250|UniProtKB:P10844}. Host cytoplasm, host cytosol {ECO:0000250|UniPr... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000250|UniProtKB:P10844}; | null | null | null | null | FUNCTION: [Botulinum neurotoxin type B]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotox... | Clostridium botulinum (strain Okra / Type B1) |
B1IZU5 | HCHA_ECOLC | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) |
B1LQP2 | HCHA_ECOSM | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli (strain SMS-3-5 / SECEC) |
B1MK49 | PHY_MYCA9 | MHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEVFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLPDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPWCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDPLDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQEFGPR | 3.7.1.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30784195}; | null | null | metal ion binding [GO:0046872]; phloretin hydrolase activity [GO:0050180] | PF18089; | null | DAPG/phloretin hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate; Xref=Rhea:RHEA:23396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16204, ChEBI:CHEBI:16331, ChEBI:CHEBI:17276; EC=3.7.1.4; Evidence={ECO:0000269|PubMed:30784195}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=81.2 uM for phloretin {ECO:0000269|PubMed:30784195}; KM=2590 uM for MAPG {ECO:0000269|PubMed:30784195}; Note=kcat is 0.85 sec(-1) with phloretin as substrate. kcat is 49.6 sec(-1) with MAPG as substrate. {ECO:0000269|PubMed:30784195}; | null | null | null | FUNCTION: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG). {ECO:0000269|PubMed:30784195}. | Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium abscessus) |
B1MTB0 | HMGB1_PLEMO | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; ... | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (N... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P6315... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch) |
B1NF18 | C719B_PAPSO | MAPINIEGNDFWMIACTVIIVFALVKFMFSKISFYQSANTTEWPAGPKTLPIIGNLHQLGGGVPLQVALANLAKVYGGAFTIWIGSWVPMIVISDIDNAREVLVNKSADYSARDVPDILKIITANGKNIADCDSGPFWHNLKKGLQSCINPSNVMSLSRLQEKDMQNLIKSMQERASQHNGIIKPLDHAKEASMRLLSRVIFGHDFSNEDLVIGVKDALDEMVRISGLASLADAFKIAKYLPSQRKNIRDMYATRDRVYNLIQPHIVPNLPANSFLYFLTSQDYSDEIIYSMVLEIFGLGVDSTAATAVWALSFLVGEQE... | 1.14.19.67 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1}; | hormone biosynthetic process [GO:0042446]; morphine biosynthetic process [GO:0097295]; progesterone metabolic process [GO:0042448] | endoplasmic reticulum membrane [GO:0005789] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; salutaridine synthase activity [GO:0047055]; steroid 17-alpha-monooxygenase activity [GO:0004508] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(R)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + salutaridine; Xref=Rhea:RHEA:17713, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:580... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.2 uM for (R)-reticuline {ECO:0000269|PubMed:19567876}; Note=kcat is 1.64 min(-1) for (R)-reticuline.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:19567876}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19567876}; | FUNCTION: Cytochrome P450 monooxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:19567876, PubMed:22098111). Catalyzes the formation of the morphinan alkaloid salutaridine by intramolecular phenol oxidation of (R)-reticuline without the incorporation of... | Papaver somniferum (Opium poppy) |
B1NF19 | C719D_ARGME | MEEKIMTNNSPWILTSSTTTTTTILLSLLFTIFIILRRNKSSSSKMVWPTGPKTLPIIGNMNILGGTALHVVLHNLAKTYGNVMTIWIGSWRPVIVVSDIDRAWEVLVNKSSDYSARDMPEITKLATADWKTISSSDSGPFWTNLRKGLQNVALSPQNLSSQSKFQERDIIKTIQNLKEEAKMNNGIVKPLDHLKKAMVRLISRLIYGQDFDNDEYVEEMHHTIEELIRVSGYARLAEAFYYAKYLPSHKKAVREVLQANQRVQNLVRPLLSLNSPTNTYLHFLRSQNYEDEVIIFAIFEAYLLGVDSTSSTTAWALAYL... | 1.14.19.64; 1.14.19.68; 1.14.19.73 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | isoquinoline alkaloid biosynthetic process [GO:0033075] | endoplasmic reticulum membrane [GO:0005789] | (S)-canadine synthase activity [GO:0047056]; (S)-nandinine synthase activity [GO:0102632]; (S)-stylopine synthase activity [GO:0047052]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-cheilanthifoline + O2 + reduced [NADPH--hemoprotein reductase] = (S)-stylopine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:13773, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16233, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 13.8 min(-1) for (S)-cheilanthifoline. {ECO:0000269|PubMed:21094631}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:21094631}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-35 degrees Celsius. {ECO:0000269|PubMed:21094631}; | FUNCTION: Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (S)-cheilanthifoline to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-tetrahydrocolumbamine to (S)-canadine. Can be involved in both sanguinarine and berberine biosynthesis. Catalyzes an oxi... | Argemone mexicana (Mexican prickly poppy) |
B1NWR6 | NA228_NEMVE | MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00706; | 2.20.20.10; | Sea anemone sodium channel inhibitory toxin family, Type II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18538344}. | null | null | null | null | null | FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity ... | Nematostella vectensis (Starlet sea anemone) |
B1NWS4 | NA225_NEMVE | MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00706; | 2.20.20.10; | Sea anemone sodium channel inhibitory toxin family, Type II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18538344}. | null | null | null | null | null | FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity ... | Nematostella vectensis (Starlet sea anemone) |
B1NY81 | CAS31_MEDTR | MSQYQQGYGDQTRRVDEYGNPLTSQGQVDQYGNPISGGGMTGATGHGHGHHQQHHGVGVDQTTGFGSNTGTGTGYGTHTGSGGTHTGGVGGYGTTTEYGSTNTGSGYGNTDIGGTGYGTGTGTGTTGYGATGGGTGVGYGGTGHDNRGVMDKIKEKIPGTDQNASTYGTGTGYGTTGIGHQQHGGDNRGVMDKIKEKIPGTDQNQYTHGTGTGTGTGYGTTGYGASGVGHQQHGEKGVMDKIKEKIPGTEQNTYGTGTGTGHGTTGYGSTGTGHGTTGYGDEQHHGEKKGIMEKIKEKLPGTGSCTGHGQGH | null | null | cold acclimation [GO:0009631]; nodulation [GO:0009877]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | metal ion binding [GO:0046872] | PF00257; | null | Plant dehydrin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29868087}. | null | null | null | null | null | FUNCTION: Intrinsically disordered protein acting as a chaperone (By similarity). Ensures leghemoglobins (e.g. LB120-1) protection from denaturation under thermal and drought stresses to delay root nodule nitrogenase inactivation and subsequent nodule senescence, thus supporting symbiotic nitrogen fixation (SNF) (PubMe... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
B1P1D9 | JZ11F_CHIGU | MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E0 | JZ11C_CHIGU | MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFRSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E1 | JZ11B_CHIGU | MKVSVVITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E2 | JZ11D_CHIGU | MKASVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E3 | JZ11E_CHIGU | MKVSVLITLAVLGVMFVWTSAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1F5 | JZT32_CHIGU | KASVLITLAVLGVMFVWTSAAELEERGSDQRDSPALIKSMAKVFQSEERECTKLLGGCTKDSECCPHLGCRKKWPYHCGWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 47 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17476710}. | null | null | null | null | null | FUNCTION: Inhibits TTX-sensitive and TTX-insensitive sodium currents (IC(50) is 0.6 uM and 0.95 uM respectively) on rat dorsal root ganglion (DRG) neurons (PubMed:18581053, PubMed:19409400). Inhibits muscular subtypes sodium channels Nav1.4/SCN4A and Nav1.5/SCN5A transiently transfected in to HEK293 cells (IC(50) is 5.... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1PRL5 | CAVN4_RAT | MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVATVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDVPCPASLSVVKDRSLPENEEEAEEVFDPPIDLSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSKENMQKTRQNFDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISNATPSKEAFKIRSLRKPKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDGFSETEKEVT... | null | null | cell differentiation [GO:0030154]; muscle organ development [GO:0007517]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | null | PF15237; | null | CAVIN family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:A2AMM0}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:A2AMM0}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Cell membrane {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes... | Rattus norvegicus (Rat) |
B1PVZ9 | KARG_METEN | MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKKTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSMQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEG... | 2.7.3.3 | null | female gonad development [GO:0008585]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | null | arginine kinase activity [GO:0004054]; ATP binding [GO:0005524]; creatine kinase activity [GO:0004111] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine; Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3; Evidence={ECO:0000269|PubMed:12496430, ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.33 mM for ATP (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:19341812}; KM=1.59 mM for L-arginine (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:19341812}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:19341812}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19341812}; | FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine. {ECO:0000269|PubMed:12496430, ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330, ECO:0000269|PubMed:21645540}. | Metapenaeus ensis (Greasyback shrimp) (Penaeus ensis) |
B1Q005 | MBOA4_RAT | MDWLQFFFLHPVSLYQGAAFPFALLFNYLCITESFPTRARYLFLLAGGGVLALAAMGPYALLIFIPALCAVAMISSLSPQEVHGLTFFFQMGWQTLCHLGLHYKEYYLCEPPPVRFYITLSSLMLLTQRVTSLSLDISEGKVEAAWRGTRSRSSLCEHLWDALPYISYLLFFPALLGGSLCSFQRFQACVQRPRSLYPSISFWALTWRGLQILGLECLKVALRRVVSAGAGLDDCQRLECIYIMWSTAGLFKLTYYSHWILDDSLLHAAGFGSEAGQRPGEERYVPDVDIWTLETTHRISLFARQWNRSTAQWLKRLVFQ... | 2.3.1.- | null | lipid modification [GO:0030258]; peptidyl-serine octanoylation [GO:0018191] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; serine O-acyltransferase activity [GO:0016412] | PF03062; | null | Membrane-bound acyltransferase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity) (PubMed:18443287). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that a... | Rattus norvegicus (Rat) |
B1Q006 | MBOA4_DANRE | MIDLLWISSDGHPQLFYQFINIPFAFLFHCLSSQGHLSIINRYVYLAMGGFMLAIATMGPYSSLLFLSAIKLLLLIHYIHPMHLHRWILGLQMCWQTCWHLYVQYQIYWLQEAPDSRLLLAISALMLMTQRISSLSLDFQEGTISNQSILIPFLTYSLYFPALLGGPLCSFNAFVQSVERQHTSMTSYLGNLTSKISQVIVLVWIKQLFSELLKSATFNIDSVCLDVLWIWIFSLTLRLNYYAHWKMSECVNNAAGLGVYFHKHSGQTSWDELSDGSVLVTEASSRPSVFARKWNQTTVDWLRKIVFNRTSRSPLFMTFG... | 2.3.1.- | null | lipid modification [GO:0030258]; peptidyl-serine octanoylation [GO:0018191]; response to food [GO:0032094] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | serine O-acyltransferase activity [GO:0016412] | PF03062; | null | Membrane-bound acyltransferase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity) (PubMed:18443287). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that a... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B1Q236 | SYG1_CAEEL | MVRWQTWPLLLLFQLVTCQQLQQRIVEAPKDTLAAVGETAILTCRVEHQQGPVQWMKDDFGLGTDRDKPLPGNKRYRMVGSAANGEYNLEISNVTLFDDDDFACQISESDHAKAVVSSKAKLTVLVRPTPPKIVKSHHSLKAIAGDPITQSCLSRKGKPPPTIGWAIASDEHGKHIVSWLGESRSKFGGIHAKPEISQETVIAHVNETTQVEEGGNNSREDSSIYSIMSNLSFIPRPEDDHKYLICISQHMTFPNKIEVDSVKLSLRYAPQINLTVASKLPLRENGSALLACNVNAKPLDNVKISWYKGNQKLRETGDTL... | null | null | actin filament bundle assembly [GO:0051017]; branching morphogenesis of a nerve [GO:0048755]; cell-cell adhesion [GO:0098609]; cell-cell signaling [GO:0007267]; collateral sprouting [GO:0048668]; synapse assembly [GO:0007416]; synapse organization [GO:0050808]; synaptic target recognition [GO:0008039] | axon [GO:0030424]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636]; synapse [GO:0045202]; synaptic membrane [GO:0097060] | cell adhesion molecule binding [GO:0050839]; protein-containing complex binding [GO:0044877] | PF08205;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:15035988, ECO:0000269|PubMed:17626846}. Synapse {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:24485456}. | null | null | null | null | null | FUNCTION: Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). A... | Caenorhabditis elegans |
B1Q257 | GCY10_CAEEL | MLKSLLIIVIVFLHRELCDGIQLILFDNWPSAQNVCASAVADATANGQCTTKSIQKHLELLTVIILLKLFGVFHRINQQHGCSGDNSVKSASYAINAVASRTSGELDFVFVGPTCTTDIRTIGDFAEIWKSPVIGYEPVFEARGVQELTSVINVAQFSVGGVAETLVFLMKELEQVEITLVGSVKVLPNGLSLSNDLRSYNEIMNSFKIREYVEVDENDVDWTKVDQKIKRGARMIVVCADFYDIYSAFYNIGIRSLSGFRFIIVVILNKPPDEILNQPNVKNLLYGSNAFIISPLQEQYSDAFSIMQDVIPNLADDQFT... | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; chemosensory behavior [GO:0007635]; intracellular signal transduction [GO:0035556]; negative chemotaxis [GO:0050919]; negative regulation of multicellular organism growth [GO:0040015]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; phototransduction [GO:0007602... | non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF00069; | 3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:10774726}. Note=Localizes in cilium of sensory neurons. {ECO:0000269|PubMed:10774726}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187}; | null | null | null | null | FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward volatile odorants in AWC sensory neurons and their avoidance in AWB sensory neurons (PubMed:10774726, PubMed:8348618). May be involved in sensitivity to quinine by regulating egl-4 ... | Caenorhabditis elegans |
B1Q2B6 | OLIS_CANSA | MNHLRAEGPASVLAIGTANPENILLQDEFPDYYFRVTKSEHMTQLKEKFRKICDKSMIRKRNCFLNEEHLKQNPRLVEHEMQTLDARQDMLVVEVPKLGKDACAKAIKEWGQPKSKITHLIFTSASTTDMPGADYHCAKLLGLSPSVKRVMMYQLGCYGGGTVLRIAKDIAENNKGARVLAVCCDIMACLFRGPSESDLELLVGQAIFGDGAAAVIVGAEPDESVGERPIFELVSTGQTILPNSEGTIGGHIREAGLIFDLHKDVPMLISNNIEKCLIEAFTPIGISDWNSIFWITHPGGKAILDKVEEKLHLKSDKFVD... | 2.3.1.206; 4.4.1.- | null | cannabinoid biosynthetic process [GO:1901696]; polyketide biosynthetic process [GO:0030639]; terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; lyase activity [GO:0016829] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=3 H(+) + hexanoyl-CoA + 3 malonyl-CoA = 3,5,7-trioxododecanoyl-CoA + 3 CO2 + 3 CoA; Xref=Rhea:RHEA:34119, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:62620, ChEBI:CHEBI:66957; EC=2.3.1.206; Evidence={ECO:0000269|PubMed:19454282, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60.8 uM for hexanoyl-CoA {ECO:0000269|PubMed:19454282}; KM=88.9 uM for butyryl-CoA {ECO:0000269|PubMed:19454282}; KM=99.1 uM for isovaleryl-CoA {ECO:0000269|PubMed:19454282}; KM=81.7 uM for octanoyl-CoA {ECO:0000269|PubMed:19454282}; Note=kcat is 2.96 min(-1) with ... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:18323613, PubMed:19454282, PubMed:19581347, PubMed:22802619). Polyketide synthase responsible for olivetol biosynthesis, from a C(12)-polyketide, probably 3,5,7-trioxododecanoyl-C... | Cannabis sativa (Hemp) (Marijuana) |
B1Q3J6 | DNM1B_ORYSJ | MVKSPCSPVTTGKKRCRAKPQKKDEDTTDKGKLDEGPLDATKEMNGVGKGDSRAACKRPRRAAACSDFKEKSVRLSDKSSVVATNGNKMEEEEMDAVKLTKLGPEVQRPCRKLIDFILHDADGKLQPFEMSEIDDFFITALIMPMDDDLEKDRQKGVRCEGFGRIEDWAISGYDEGTAVVWVSTEVADYECVKPAGNYKSYYDHFYEKAQVCVEVYRKLARSVGGNPNLGLEELLASVVRSINAIKGYSGTLSKDFVISNGEFVYNQLIGLDETANTDDEKFATLPVLLALRDGCKSRVEVSKLQPNISNGSLKINDAEC... | 2.1.1.37 | null | embryo development ending in seed dormancy [GO:0009793]; genomic imprinting [GO:0071514]; methylation [GO:0032259]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677] | PF01426;PF00145;PF12047; | 2.30.30.490;3.90.120.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.... | null | null | null | null | FUNCTION: Major CG methylase that methylates chromatin CpG residues and maintains DNA methylation (PubMed:24535433, PubMed:25002488). Plays a major role in genomic imprinting, regulation of embryogenesis and seed viability (PubMed:24535433, PubMed:25002488). Maintains DNA methylation at the FIE1 gene locus in the embry... | Oryza sativa subsp. japonica (Rice) |
B1V8A0 | SH3GH_CAEEL | MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQ... | null | null | clathrin-dependent endocytosis [GO:0072583]; necroptotic process [GO:0070266]; synaptic vesicle uncoating [GO:0016191] | glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; presynapse [GO:0098793]; synaptic vesicle [GO:0008021] | null | PF03114;PF07653; | 1.20.1270.60;2.30.30.40; | Endophilin family | null | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Membrane {ECO:0000305|PubMed:21029864}; Peripheral membrane protein {ECO:0000305|Pub... | null | null | null | null | null | FUNCTION: Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis (PubMed:14622579, PubMed:21029864). By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion (PubMed:21029864). In a s... | Caenorhabditis elegans |
B1VB63 | PDUB_CITFR | MSSNELVDQIMAQVIARVATPEQQAIPENNPPTRETAMAEKSCSLTEFVGTAIGDTVGLVIANVDSALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTFGDVYANEAGHIEMQYTARASYALEKAFGAPIGRACGVIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVISAREIGKTVLGTLGSEPKNDRPSYI | null | null | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469] | structural molecule activity [GO:0005198] | PF00936; | 3.30.70.1710; | EutL/PduB family | PTM: In purified BMCs seen as a 30.0 kDa and 25.0 kDa form; the smaller form is called PduB'. {ECO:0000269|PubMed:18332146}. | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}. | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) shell dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of the gene gives large amorphous intracellular structures; when only PduB is overexpressed large circular bodies are observed which cont... | Citrobacter freundii |
B1VB77 | PDUS_CITFR | MKTAMTAESTLYDAQTIRERVRAAGVVGAGGAGFPAHVKLQAQVDTFLVNAAECEPMLKVDQQLMAVQAERLIRGVQYAMTATGARAGIIALKEKYQRAINALTPLLPAGIRLHILPDVYPAGDEVLTIWMATGRRVPPAALPVSVGVVVNNVQTVLNITRAVEQQYPVTRRTLTVNGAVARPITLTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDTPVSKTTGGLLVLPKSHALIQRRMQDERTVLSVAKTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNYQQAATPQLLLTALTCSECNVCESVAC... | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|PROSITE-ProRule:PRU00711, ECO:0000269|PubMed:21103360}; Note=Binds 2 [4Fe-4S] clusters (By similarity) (PubMed:21103360). The two centers are coupled but must possess different redox potentials (PubMed:21103360). {ECO:0000255|PROSITE-ProRule... | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469]; membrane [GO:0016020] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872] | PF01512;PF13534;PF13375;PF10531; | 3.10.20.600;1.10.1060.10;3.40.50.11540; | PduS cobalamin reductase family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000250|UniProtKB:Q9XDM9}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for aquacob(III)alamin {ECO:0000269|PubMed:21103360}; KM=24.7 uM for NADH {ECO:0000269|PubMed:21103360}; | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: A bifunctional cobalamin reductase that converts cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC (PubMed:21103360). Cobalamin re... | Citrobacter freundii |
B1VTI5 | GRIF_STRGG | MVHVRKNHLTMTAEEKRRFVHAVLEIKRRGIYDRFVKLHIQINSTDYLDKETGKRLGHVNPGFLPWHRQYLLKFEQALQKVDPRVTLPYWDWTTDHGENSPLWSDTFMGGNGRPGDRRVMTGPFARRNGWKLNISVIPEGPEDPALNGNYTHDDRDYLVRDFGTLTPDLPTPQELEQTLDLTVYDCPPWNHTSGGTPPYESFRNHLEGYTKFAWEPRLGKLHGAAHVWTGGHMMYIGSPNDPVFFLNHCMIDRCWALWQARHPDVPHYLPTVPTQDVPDLNTPLGPWHTKTPADLLDHTRFYTYDQ | 1.10.3.15; 1.10.3.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:16282322}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:16282322}; | antibiotic biosynthetic process [GO:0017000]; melanin biosynthetic process [GO:0042438]; pigmentation [GO:0043473] | null | copper ion binding [GO:0005507]; o-aminophenol oxidase activity [GO:0050149]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 3-amino-4-hydroxybenzoate + H(+) + N-acetyl-L-cysteine + 2 O2 = CO2 + grixazone B + 4 H2O; Xref=Rhea:RHEA:41420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:60005, ChEBI:CHEBI:73483, ChEBI:CHEBI:78236; EC=1.10.3.15; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for alpha-aminophenol {ECO:0000269|PubMed:16282322}; KM=0.58 mM for 3,4-AHBAL {ECO:0000269|PubMed:16282322}; KM=0.75 mM for 2-amino-4-methylphenol {ECO:0000269|PubMed:16282322}; KM=0.41 mM for 3,4-dihydroxybenzaldehyde {ECO:0000269|PubMed:16282322}; KM=19 mM... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8.5 and 10.5. {ECO:0000269|PubMed:16282322}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:16282322}; | FUNCTION: Involved in the biosynthesis of the parasiticide antibiotic grixazone. Catalyzes the oxidation of 3-amino-4-hydroxybenzoate (3,4-AHBOA) to yield the corresponding quinone imine which is then non-enzymatically conjugated with the thiol group of N-acetylcysteine. The resultant compound is oxidized to its quinon... | Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
B1W019 | GCOA_STRGG | MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDL... | 4.2.1.138; 4.2.3.89 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21693706}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21693706}; Note=Binds 3 Mg(2+) ions per subunit. To a lesser extent, can also use Mn(2+) instead of Mg(2+). Cannot use Fe(2+), Co(2+), Zn(2+), Ni(2+), or Cu(2+). {ECO:... | sesquiterpene biosynthetic process [GO:0051762]; sesquiterpenoid biosynthetic process [GO:0016106] | null | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances [GO:0016823]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; sesquiterpene synthase activity [GO:0010334] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:31815, ChEBI:CHEBI:33019, ChEBI:CHEBI:63190, ChEBI:CHEBI:175763; EC=4.2.3.89; Evidence={ECO:0000269|PubMed:21693706}; CATALYTIC ACTIVITY: Reaction=(+)-(E)-beta-caryophyllene + H2O = (+)-caryolan-1-ol; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=95.6 nM for farnesyl diphosphate (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:21693706}; Note=kcat is 0.025 sec(-1) for (+)-caryolan-1-ol formation (at pH 7.5 and 30 degrees Celsius).; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for (+)-caryolan-1-ol synthesis. {ECO:0000269|PubMed:21693706}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for (+)-caryolan-1-ol synthesis. {ECO:0000269|PubMed:21693706}; | FUNCTION: Sesquiterpene cyclase that first catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-caryophyllene intermediate, and then its conversion to (+)-caryolan-1-ol via a second cyclization and the addition of a water molecule. {ECO:0000269|PubMed:21693706}. | Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
B1WAR9 | GWL_XENTR | MGVVVAETSQNGDISLLSEKKFTVPQPPSIEEFSIVKPISRGAFGKVYLARRKNNNKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLIMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLKRELSMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPVGGRTQGSIAQQTEGMRGNASTPLLMKKKENSVKGNKLMISCPEAGLSSPSMPVKCLTPNLLKCRTPFTTSSTSSQSRICLSSLESECGMSPRWENC... | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-752 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and e... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1WBP0 | MPPD2_RAT | MAHGIPSQGKVTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDKEFMADLVKQDYYRFPSVSKLKPEDFDNVQSLLTNSIYLQDSEVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGTDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGTMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19004815, ECO:0000269|PubMed:21824479}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:19004815}; | null | null | AMP binding [GO:0016208]; GMP binding [GO:0019002]; manganese ion binding [GO:0030145]; phosphoric diester hydrolase activity [GO:0008081] | PF00149; | 3.60.21.10; | UPF0046 family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for p-nitrophenyl phenyphosphonate {ECO:0000269|PubMed:19004815}; KM=1.5 mM for manganese {ECO:0000269|PubMed:19004815}; Vmax=8 umol/min/mg enzyme with p-nitrophenyl phenyphosphonate as substrate {ECO:0000269|PubMed:19004815}; | null | null | null | FUNCTION: Displays low metallophosphoesterase activity (in vitro) (PubMed:19004815, PubMed:21824479). May play a role in the development of the nervous system (Probable). {ECO:0000269|PubMed:19004815, ECO:0000269|PubMed:21824479, ECO:0000305}. | Rattus norvegicus (Rat) |
B1WC10 | FRITZ_RAT | MSFCLTELHLWSLKSTLHIADRDIGVYQYYDKKDLPVSAAEHGNLEEKQRLAESRDYPWTLKNRRPEKLRDSLKELEELMQNSQCVLCQWKSKHICQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFAKKMDSLDVNKRLEKLSALDYKISYHDIPGPATRTVDRHLAINSTQDLAVCWWPLLSDDAWPWTPIASEKDRANMLLLGFTQGGLEVLSSVRTEWNPLDVHFGTRQPYQVFTVECSFSVDQEPMADSCIYESVRNKLHCVSVTRIPLRSKAISCCKNSTEDK... | null | null | auditory receptor cell morphogenesis [GO:0002093]; camera-type eye development [GO:0043010]; cilium assembly [GO:0060271]; cilium organization [GO:0044782]; circulatory system development [GO:0072359]; digestive system development [GO:0055123]; embryonic digit morphogenesis [GO:0042733]; embryonic organ development [GO... | axonemal basal plate [GO:0097541]; axoneme [GO:0005930]; plasma membrane [GO:0005886] | null | PF11768; | 2.130.10.10; | WD repeat fritz family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q32NR9}. | null | null | null | null | null | FUNCTION: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recr... | Rattus norvegicus (Rat) |
B1WC40 | NCBP2_RAT | MSGGLLKALRSDSYVELSEYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYREDYDAGRGGYGKLAQKQ | null | null | histone mRNA metabolic process [GO:0008334]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA export from nucleus [GO:0006406]; mRNA metabolic process [GO:0016071]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transcription by RNA polymerase II [GO:0042789]; nuclear-transcribed mRNA catabolic process, nonsens... | cytoplasm [GO:0005737]; nuclear cap binding complex [GO:0005846]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA cap binding complex [GO:0034518] | DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA cap binding [GO:0000339]; snRNA binding [GO:0017069] | PF00076; | 3.30.70.330; | RRM NCBP2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm {ECO:0000250|UniProtKB:P52298}. | null | null | null | null | null | FUNCTION: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC comple... | Rattus norvegicus (Rat) |
B1WC58 | CTIP_RAT | MSISGSSCGSPNSTDISSDFKELWTKLKEYHDKEVQGLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRLITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELECEENIIPDSPITSFSFSGINRLRRKENLHVRYVEQTHTKLEHSACTSELRKFSKGSTPAPVNSEEHEILVADTCDQSHSPLSKICGTSSYPADKLSSNLDAVVAETLGLDGQEESEPQGPVSPLGNELYHCLKEDHKKQPFMESAIRNEDNVRFSDSASKAPPREL... | 3.1.-.- | null | blastocyst hatching [GO:0001835]; cell division [GO:0051301]; DNA double-strand break processing involved in repair via single-strand annealing [GO:0010792]; double-strand break repair via homologous recombination [GO:0000724]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic cell cycle [GO:0051321]; respons... | BRCA1-C complex [GO:0070533]; chromosome [GO:0005694]; transcription repressor complex [GO:0017053] | damaged DNA binding [GO:0003684]; identical protein binding [GO:0042802]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]; transcription corepressor activity [GO:0003714] | PF10482;PF08573; | null | COM1/SAE2/CtIP family | PTM: Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylation at Thr-843 and Thr-855 promote interaction with NBN and recruitment to double-strand breaks (DSBs). Phosphorylated... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chr... | null | null | null | null | null | FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork ... | Rattus norvegicus (Rat) |
B1WC61 | ACAD9_RAT | MSGYVLFSRGATAAAAAARASRVLRVFTERRRTLHTSLQSCSFAKELFLGHIQQKGVFPFPEVSQEELSEINQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLK... | 1.3.8.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9H845}; | leucine catabolic process [GO:0006552]; long-chain fatty acid metabolic process [GO:0001676]; medium-chain fatty acid metabolic process [GO:0051791]; mitochondrial respiratory chain complex I assembly [GO:0032981] | dendrite [GO:0030425]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991] | PF21343;PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H845}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H845}; Matrix side {ECO:0000250|UniProtKB:Q9H845}. Note=Essentially associated with membranes. {ECO:0000250|UniProtKB:Q9H845}. | CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691... | null | null | null | null | FUNCTION: As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation. This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-Co... | Rattus norvegicus (Rat) |
B1WC68 | HDAC8_RAT | MEIPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTG... | 3.5.1.-; 3.5.1.98 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q9BY41}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q9BY41}; | cellular response to forskolin [GO:1904322]; cellular response to trichostatin A [GO:0035984]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein modification process [GO:0031... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; deacetylase activity [GO:0019213]; histone deacetylase activity [GO:0004407]; histone decrotonylase activity [GO:0160009]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; metal ion binding [GO:0046872]; protein lysine deacetylase activity [GO:0033558] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 (By similarity). {ECO:0000250|UniProtKB:Q9BY41}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BY41}. Chromosome {ECO:0000250|UniProtKB:Q9BY41}. Cytoplasm {ECO:0000250|UniProtKB:Q9BY41}. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation. {ECO:0000250|UniProtKB:Q9BY41}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000250|UniProtKB:Q9BY41}; PhysiologicalDirection=left-t... | null | null | null | null | FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. His... | Rattus norvegicus (Rat) |
B1X6B7 | HCHA_ECODH | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli (strain K12 / DH10B) |
B1XJV9 | CRTE_PICP2 | MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN | 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | null | metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:32523588}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.; PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl... | null | null | FUNCTION: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids. {ECO:0000269|PubMed:32523588}. | Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
B1YAL1 | FBPAP_PYRNV | MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEVTDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDPSMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVRAQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDL... | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21983965}; | gluconeogenesis [GO:0006094] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287] | PF01950; | 6.10.250.1180; | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965}; CATALYTIC ACTIVITY: Reaction=... | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906}. | null | null | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965}. | Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus) |
B2AXJ5 | HETQ1_PODAN | MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA | null | null | programmed cell death [GO:0012501] | plasma membrane [GO:0005886] | wide pore channel activity [GO:0022829] | null | null | Gasdermin family | PTM: [Gasdermin-like protein het-Q1]: The precursor form is cleaved by het-Q2, generating the pore-forming protein (Gasdermin-like protein het-Q1, N-terminal). {ECO:0000269|PubMed:35135876}. | SUBCELLULAR LOCATION: [Gasdermin-like protein het-Q1, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:P57764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. | null | null | null | null | null | FUNCTION: [Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) (PubMed:35135876). In P.anserina, the het-q locus exists as 2 incom... | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2B223 | ARO1_PODAN | MTSSTGSGPTRISILGKDDIIVDHGIWLDFVTHDLLQNIPSSTYVLITDTNLHDTYVPAFQEVFERAAGQDARLLTYTIPPGEYSKGRETKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLETLPVREFINGMAEVIKTAAIWNETEFTALEDNAPAILEAIRSKPTGTGARLAPIRDILKRIVLGSAGVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQVLHGECVAIGMVREAELARFLGVLPPGAVARLTKCI... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2B3C0 | MANA_PODAN | MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRE... | 3.2.1.78 | null | mannan catabolic process [GO:0046355] | extracellular region [GO:0005576] | mannan endo-1,4-beta-mannosidase activity [GO:0016985] | PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | PTM: Not glycosylated. {ECO:0000269|PubMed:23558681}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:21037302}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mg/ml for konjac glucomannan {ECO:0000269|PubMed:21037302}; KM=1.7 mg/ml for carob galactomannan {ECO:0000269|PubMed:21037302}; KM=4.7 mg/ml for locust bean gum galactomannan {ECO:0000269|PubMed:21037302}; KM=1.6 mg/ml for ivory nut mannan {ECO:0000269|PubMed:2... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:21037302}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:21037302}; | FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucoman... | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2C4D0 | TS23B_MAIZE | MAADEARSVSRLHSEEDMHGKHHSTLWGDFFLHHVPCRPGQYLIMKDNVEIMKEEVKKMLLDVGSSDLSHKLDCIDTLERLGLDYHYTKEIDELMCNVFEARDQDLDLTTTSQLFYLLRKHGYHISSDVFLKFRDDKGDIVTNDARCLLRMYEAAHVRVNGEEILDNILIHTKRQLQCIVDDLEPTLQEEVRYALETPLFRRLNRVQARQFISTYEKSTTRINMLLEFSKLDFNILLTLYCEELKDLTLWWKEFQAQANTTIYARDRMVEMHFWMMGVFFEPQYSYSRKMLTQLFMIVSVLDDLYDSHCTTEEGNAFTAA... | 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18296628}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18296628}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q5GJ60}; | beta-caryophyllene biosynthetic process [GO:1901937]; defense response to insect [GO:0002213]; diterpenoid biosynthetic process [GO:0016102]; farnesyl diphosphate catabolic process [GO:0045339]; response to herbivore [GO:0080027]; response to insect [GO:0009625]; sesquiterpene biosynthetic process [GO:0051762]; terpeno... | cytoplasm [GO:0005737] | (-)-E-beta-caryophyllene synthase activity [GO:0080016]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:18296628}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for farnesyl diphosphate (in the presence of MgCl(2)) {ECO:0000269|PubMed:18296628}; KM=1.1 uM for farnesyl diphosphate (in the presence of MnCl(2)) {ECO:0000269|PubMed:18296628}; Note=kcat is 0.00191 sec(-1) with farnesyl diphosphate (in the presence of MgC... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000250|UniProtKB:Q84ZW8}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9.5. {ECO:0000269|PubMed:18296628}; | null | FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Sesquiterpene synthase that converts farnesyl diphosphate to (E)-beta-caryophyllene (PubMed:18296628). Involved in indirect defense by producing volatile signals that attract natural enemies of leaf herbivores such as Chilo partellus ... | Zea mays (Maize) |
B2C4J0 | GLYC_CHAVB | MGQLVSFFQEIPNIIQEAINIALIAVSLIAILKGLVNLWKSGLFQLLVFLILAGRSCSFKIGRSTELQNITINMLKVFEDHPISCTVNKTLYYIRESENATWCVEIAALDMSVLLSPHDPRVMGNLSNCVHPDIKHRSELLGLLEWILRALKYDFLNYPPLLCEKVTSSVNETRIQINVSDSAGSHDFKETMLQRLAILFGTKLMFDKTPKQFIVIRNQTWVNQCKSNHVNTLHLMMANAGHAVKLRRLQGVFTWTITDAAGNDMPGGYCLERWMLVTSDLKCFGNTALAKCNLNHDSEFCDMLKLFEFNKKAIESLNDN... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Chapare mammarenavirus (isolate Human/Bolivia/810419/2003) |
B2C6R6 | TAFCL_ARATH | MAEPIPSSSLSPKSLQSPNPMEPSPASSTPLPSSSSQQQQLMTAPISNSVNSAASPAMTVTTTEGIVIQNNSQPNISSPNPTSSNPPIGAQIPSPSPLSHPSSSLDQQTQTQQLVQQTQQLPQQQQQIMQQISSSPIPQLSPQQQQILQQQHMTSQQIPMSSYQIAQSLQRSPSLSRLSQIQQQQQQQQHQGQYGNVLRQQAGLYGTMNFGGSGSVQQSQQNQQMVNPNMSRAALVGQSGHLPMLNGAAGAAQMNIQPQLLAASPRQKSGMVQGSQFHPGSSGQQLQGMQAMGMMGSLNLTSQMRGNPALYAQQRINPGQ... | null | null | RNA polymerase II preinitiation complex assembly [GO:0051123] | SAGA complex [GO:0000124]; SLIK (SAGA-like) complex [GO:0046695]; transcription factor TFIID complex [GO:0005669] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; TBP-class protein binding [GO:0017025] | PF03847; | 1.10.20.10; | TAF12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21357579}. | null | null | null | null | null | FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Required for the expression of a subset of ethylene-responsive genes (By similarity). Involved in the negative regulation of cytokinin sensitivity. {ECO:0000250, ECO:... | Arabidopsis thaliana (Mouse-ear cress) |
B2D6K9 | PPH6R_CAEEL | MFWAKEEEENSLMRLLKTDNFTLEDVLLNEFVVQESRYGKAELVQYITSRENMKALLELSLNPKINTDLPMKQQYRLSFIASEILTIRGTDVFQKQIVTTEETRKCLVDFLNDKTPLNHLVAGFFAKIMECLLSRHFDLFQTFSLLQETKFFDKCLRNINLGAIECLLENLVRIPTTSEGTRIVKEWMISENLFEKIVDRMRESETDDEKECLAEVYCEILRELRDKLYIMESKVDELHAKSMDETLIAKIADNLIVEEGCPAEELVKKSALISASAKILEAFIKTNFVSNAPAQQLEEIERNLIEERHYSYGLMRPCMD... | null | null | actomyosin contractile ring contraction [GO:0000916]; cortical actin cytoskeleton organization [GO:0030866]; establishment of mitotic spindle localization [GO:0040001]; first cell cycle pseudocleavage [GO:0030590]; positive regulation of mitotic cell cycle [GO:0045931]; spindle localization [GO:0051653] | astral microtubule [GO:0000235]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; phosphatase complex [GO:1903293]; spindle pole [GO:0000922] | protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888] | PF04499; | null | SAPS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20040490}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes mainly to the cytoplasm and to a lesser extent with ... | null | null | null | null | null | FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6) (Probable). In complex with pph-6, promotes actomyosin contractility during cytokinesis by regulating the organization of cortical non-muscle myosin II nmy-2 and thus contributing to correct spindle positioning (PubMed:20040490). Also required for the proper g... | Caenorhabditis elegans |
B2D6M2 | LIN61_CAEEL | MLKLVILCFALFYNTVSSTRFLFGVEVKCDFDEVFQLTVSHWEDDGNTFWDRDEDITGRMTMFARKKIFFYQDGHHGFEFGKLEPYGWFLHNCTKNGNFREYRHGLSSTSGSNGLEYIEYTMSEFLKIVRANKKSDRKLDKTYLWESYLHQFEKGKTSFIPVEAFNRNLTVNFNECVKEGVIFETVVHDYDKNCDSIQVRWFARIEKVCGYRVLAQFIGADTKFWLNILSDDMFGLANAAMSDPNMDKIVYAPPLAINEEYQNDMVNYVNNCIDGEIVGQTSLSPKFDEGKALLSKHRFKVGQRLELLNYSNSTEIRVAR... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; vulval development [GO:0040025] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; methylated histone binding [GO:0035064] | PF02820; | 2.30.30.140; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409073}. Chromosome {ECO:0000269|PubMed:17409073}. | null | null | null | null | null | FUNCTION: Synthetic multivulva class B (synMuvB) protein required to repress the induction of vulval development by Ras signaling. Unlike other synMuv proteins it does not associate with the multiprotein DRM complex and the NuRD-like complex. Interaction with methylated histone H3 is essential for vulva development. It... | Caenorhabditis elegans |
B2D6P4 | TBPL1_CAEEL | MQMGDHQMMGNQRYYRTYVQKVMPAQAGGAVSQNATYVQTAGIRTVHHDGNGQQRIVQLPPGVRQIQQNGVGPAYVRQVPGGQPMQVNFGHPGTIAGRNVAVGVQMRPVQGHNVQQGYQRQQVANQIQQQNRAVFMAQNQQGQQQISYAQAQHRQQQQNQQQHHQQPQHFNHPSQQNQMIMQHRQPQMHHNQQHQMVQPQMTRHQMAQHHAQQPHPQIYVPRDMNLAVPLREPSPEPIPVKIEVPDVPPEGTSAANEEPMPDDGDIDIQIRNVVCNYTLPLHIDLRKLAMNTHNVTYEREKGVMMKQKRSPGCYIKVYSS... | null | null | DNA-templated transcription initiation [GO:0006352]; embryo development ending in birth or egg hatching [GO:0009792]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA binding [GO:0003677]; general transcription initiation factor activity [GO:0140223] | PF00352; | 3.30.310.10; | TBP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11030349, ECO:0000269|PubMed:11030350, ECO:0000269|PubMed:14726532}. | null | null | null | null | null | FUNCTION: May be a general transcription factor (PubMed:11030349, PubMed:11030350). Plays an essential role for RNA polymerase II/ama-1 transcription in early embryos whereby it activates a subset of RNA polymerase II promoters and facilitates the reestablishment of transcription after mitosis (PubMed:14726532). {ECO:0... | Caenorhabditis elegans |
B2DBE9 | GGS4_PHOAM | MDFPIRSQARLYPAQCVTFCLYVRVPPLSEWNFLKMQTDARPSATWPSVPKVHKRNRSTSLSDQQTAKKAHANHARLHLPQPIEPVYESQNGSVSQSEEKSSAVEINNSAAGDPQRFAVADLNFSWAEEEEKVVLAPYDYVASNSGKEFRTLILNAFNAWFRVPPESLTIICDVVRMLHTSSLLIDDIQDNSLLRRGRPVAHSIYGVAQTINTGNYVYFLAAKELNKLRNAASALEVFTAEMLNLHRGQGQELYWRDTLKCPTEDEYLKMVSNKTGGLFRMAVKLMQAESPAGPMAPVCDKLVQLLGLVYQIADDYKNLT... | 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | alcohol biosynthetic process [GO:0046165]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone... | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:18391465}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diph... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGDP). {ECO:0000269|PubMed:18391465}. | Phomopsis amygdali (Fusicoccum amygdali) |
B2DCZ9 | ARHG2_PIG | MKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTTRERPSSAIYPSDSFRQSLLGSRRGRSPLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEGAEVIYNELMSDFEMGEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELQLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSPRNFVIHRLGDLLITQFSGPSADQMRKTYSEFCSRHT... | null | null | actin filament organization [GO:0007015]; asymmetric neuroblast division [GO:0055059]; cell cycle [GO:0007049]; cell morphogenesis [GO:0000902]; cellular response to muramyl dipeptide [GO:0071225]; innate immune response [GO:0045087]; negative regulation of microtubule depolymerization [GO:0007026]; positive regulation... | bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; protein-containing complex [GO:0032991]; ruffle membrane [GO:0032587]; spindle [GO:0005819]; vesicle [GO:0031982] | guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; small GTPase binding [GO:0031267] | PF17838;PF00621; | 3.30.60.20;1.20.900.10;2.30.29.30; | null | PTM: Phosphorylation of Ser-860 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosp... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cytoplasm {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Golgi apparatus {ECO:0000250|UniProtKB:Q92974}. ... | null | null | null | null | null | FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but... | Sus scrofa (Pig) |
B2DD29 | BRSK1_RAT | MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVL... | 2.7.11.1; 2.7.11.26 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | associative learning [GO:0008306]; axonogenesis [GO:0007409]; centrosome duplication [GO:0051298]; DNA damage response [GO:0006974]; establishment of cell polarity [GO:0030010]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule cytoskeleton organization involved in establishment of planar polarity [GO:009... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; distal axon [GO:0150034]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynaptic active zone [GO:0048786]; synaptic vesicle [GO:0008021] | ATP binding [GO:0005524]; gamma-tubulin binding [GO:0043015]; magnesium ion binding [GO:0000287]; molecular function inhibitor activity [GO:0140678]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0... | PF21122;PF00069;PF21115; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-189 by PP2C. May be autophosphorylated. {ECO:0000... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Synapse {ECO:0000269|PubMed:16630837}. Presynaptic active zone {ECO:0000269|PubMed:16630837}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubM... | 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: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by m... | Rattus norvegicus (Rat) |
B2DEU7 | MSHMT_PARSX | MNELTRTFFNSSVHDTDPLIAQALDDERARQKNQIELIASENIVSQAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLVKPGDRILSLDLAAGGHLSHGMKGNLSGRWFEAHNYNVDPQNEVINYDEMERIAEEVKPKLLITGGSAYPRELDFARMAQIAKKVGAFFMVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQTAVFPGVQGSLHSNVLAAKAICLGEALRPEFRDYVAQVVKNAKVLAETLTSRGIRIVSGGTDT... | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.1}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=540 uM for alpha-methyl-L-serine {ECO:0000269|Ref.1}; KM=73 uM for tetrahydrofolate {ECO:0000269|Ref.1}; Vmax=8.15 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|Ref.1}; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-8.0. {ECO:0000269|Ref.1}; | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|Ref.1}. | Paracoccus sp |
B2DEU8 | MSHMT_AMISX | MTEQTKAYFNTPVHERDPLVAQALDNERKRQQDQIELIASENIVSRAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKELFGCAYANVQPHSGTQANLAVFFLLLKPGDKVLSLDLAAGGHLSHGMKGNLSGRWFESHNYNVDPETEVIDYDEMERIAEEVRPTLLITGGSAYPRELDFERMGKIAKKVGAWFLVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEAWFKKLQSAVFPGVQGSLHSNVLAAKAVCLGEALRPDFKVYAAQVKANARVLAETLIARGVRIVSGGTDT... | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1500 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407}; KM=90 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407}; Vmax=22.1 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|PubMed:18997407}; Vmax=7.75 umol/min/mg enzyme with D-ala... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | null | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|PubMed:18997407}. | Aminobacter sp |
B2DEV1 | MSHMT_ENSSX | MDHATRAHFTMTVGEVDPLLADALASERGRQQNQIELIASENIVSRAVLDALGHEITNKTLEGYPGNRFHGGGQFVDIAEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLLKPGEKVLSLDLAAGGHLSHGMKANLSGRWFDATNYNVNPQNEVIDLDEMERLAEEIRPKLLITGGSAYPRELDFERMSRIAKKVGAYFLVDMAHIAGLVAGGVHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQAAVFPGVQGSLHSNVLAAKAICLGEAMLDDFKVYARQVVANAKVLANTLAERGVRIVSGGTDT... | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1880 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407}; KM=228 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407}; Vmax=15.4 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|PubMed:18997407}; Vmax=5.48 umol/min/mg enzyme with D-al... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | null | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|PubMed:18997407}. | Ensifer sp |
B2DFG5 | DTHAD_DELSH | MQDTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHVKTSKSVPVAAAQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRLPQALQLRRRGCDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRSGVGADDTPLLLAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERERAGCVQAAEALRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFDLVMRNIGVCAAEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQKQDFGYGQVCDLQGRVMPGFVLTGANQE... | 4.3.1.27 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20843822}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20843822}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:20843822}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0... | D-serine catabolic process [GO:0036088] | null | ammonia-lyase activity [GO:0016841]; D-serine ammonia-lyase activity [GO:0008721]; pyridoxal phosphate binding [GO:0030170] | PF01168;PF14031; | 3.20.20.10;2.40.37.20; | DSD1 family | null | null | CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxy-D-aspartate = NH4(+) + oxaloacetate; Xref=Rhea:RHEA:27942, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:60898; EC=4.3.1.27; Evidence={ECO:0000269|PubMed:20843822}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 mM for D-THA {ECO:0000269|PubMed:20843822}; KM=6.16 mM for L-THA {ECO:0000269|PubMed:20843822}; KM=0.16 mM for L-EHA {ECO:0000269|PubMed:20843822}; KM=0.15 mM for D-serine {ECO:0000269|PubMed:20843822}; Note=kcat is 10.93 sec(-1) for D-THA. kcat is 3.03 sec(-1... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:20843822}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20843822}; | FUNCTION: Catalyzes the deamination of D-threo-3-hydroxyaspartate (D-THA). Also exhibits dehydratase activity towards L-threo-3-hydroxyaspartate (L-THA), L-erythro-3-hydroxyaspartate (L-EHA) and D-serine. {ECO:0000269|PubMed:20843822}. | Delftia sp. (strain HT23) |
B2FDA8 | SMC3_CAEEL | MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRE... | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; establishment of mitotic sister chromatid cohesion [GO:0034087]; mitotic sister chromatid cohesion [GO:0007064] | chromatin [GO:0000785]; cohesin complex [GO:0008278]; MIS12/MIND type complex [GO:0000444]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC3 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158, ECO:0000269|PubMed:21957461}. Chromosome {ECO:0000269|PubMed:12827206}. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues. {ECO:0000269|PubMed:12827206}. | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair (PubMed:21957461). Involved in the repair of double strand breaks during mitosis and meiosis (PubMed:21957461). Required for chromosome segregation during mitosis (PubMed:12808038). Central component of cohesin complex (PubMed:12808038, PubMe... | Caenorhabditis elegans |
B2FHL8 | PL_STRMK | MSLPLRLALLPTLLASASAFAACPAPPPGQPDIRAIGYYTDKAGSVIDPALQQQNKDATAPLDRYAADVARMSDDYLRNGDPAAAQCTLSWLGAWADDGAMLGQMIRVNNDQSFYMRQWMLDAVAMAYLKVHDQANPQQRARIDPWLQKLARANLAYWDNPKRRRNNHYYWGGLGVLATGLATDDDALWQAGHAAFQKGIDDIQDDGSLPLEMARGQRALHYHDYALAPLVMMAELARLRGQDWYASRNHAIDRLARRVIEGSRDPAWFNQHTGAAQLPLQASGWVEFYRLRSPDGGVFDAAHARGPFHSPRLGGDLTLM... | 4.2.2.-; 4.2.2.1; 4.2.2.14; 4.2.2.3 | null | polysaccharide catabolic process [GO:0000272] | cell outer membrane [GO:0009279]; periplasmic space [GO:0042597] | glucuronan lyase activity [GO:0033994]; hyaluronate lyase activity [GO:0030340]; poly(beta-D-mannuronate) lyase activity [GO:0045135] | PF05426; | 1.50.10.100; | Polysaccharide lyase 5 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:24257754}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:24257754}. | CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.; EC=4.2.2.3; Evidence={ECO:0000269|PubMed:24257754}; CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) = n 3-(4-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mg/ml for poly-GlcA {ECO:0000269|PubMed:24257754}; KM=0.26 mg/ml for poly-ManA {ECO:0000269|PubMed:24257754}; KM=0.55 mg/ml for hyaluronan {ECO:0000269|PubMed:24257754}; KM=0.17 mM for poly-GlcA (at pH 7) {ECO:0000269|PubMed:24808176}; KM=0.35 mM for poly-ManA... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for enzymatic activity is substrate-dependent, with optimal hyaluronate degradation at pH 5, poly-beta-D-glucuronate degradation at pH 7, and alginate degradation at pH 9. {ECO:0000269|PubMed:24257754}; | null | FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of several anionic polysaccharides via a beta-elimination mechanism. Exhibits broad substrate specificity, catalyzing the degradation of not only alginate and poly-beta-D-mannuronate (poly-ManA), but poly-beta-D-glucuronate (poly-GlcA or poly-GlcUA) and... | Stenotrophomonas maltophilia (strain K279a) |
B2FSW8 | EALGL_STRMK | MRLQPLFVSLALAAPCALLPTASLSAAPAAAARQADTAPVLVTAAQWQQMASEGRRYPWFAKEQARTEATLKKMMKAGIDVPVPRDKGGGRTHEQHKRNYQALLAAGTLYRLTGDRAYVDYARDMLLQYAQLYPTLGPHPEGRGQIPGRVFWQVLNDSVWLVNAIQGYDAIRDALSAEDRNTIESKVFRPMAEFLVSEPKNYDQIHNHATWAVAATGMTGYVLRDQELVEKSLRGSQKDDKFGFLRQIDLLFSPDGYYEEGPYYQRYALAPFLLFANAIERNEPQRKIFARRDGVLLKAVDVLVQSSYGGLFFPINDAIL... | 4.2.2.26 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q21FJ0}; Note=The zinc ion likely plays a structural role. {ECO:0000250|UniProtKB:Q21FJ0}; | polysaccharide catabolic process [GO:0000272] | periplasmic space [GO:0042597] | exo-oligoalginate lyase activity [GO:0052764]; metal ion binding [GO:0046872] | PF05426;PF07940; | 2.70.98.70;1.50.10.100; | Polysaccharide lyase 17 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Cleavage of 4-deoxy-alpha-L-erythro-hex-4-enopyranuronoside oligosaccharides into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides.; EC=4.2.2.26; Evidence={ECO:0000305|PubMed:26913076}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 mM for alginate {ECO:0000269|PubMed:26913076}; KM=0.41 mM for poly-ManA {ECO:0000269|PubMed:26913076}; KM=5.99 mM for poly-GulA {ECO:0000269|PubMed:26913076}; KM=0.57 mM for poly-MG {ECO:0000269|PubMed:26913076}; KM=1.4 mM for poly-GlcA {ECO:0000269|PubMed:269... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26913076}; | null | FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Sh... | Stenotrophomonas maltophilia (strain K279a) |
B2G331 | VKT2B_HETCR | MKGTFLICLILIAGFSFKSTQAGSICLEPKVVGPCTAYFRRFYFDSETGKCTVFIYGGCEGNGNNFETLRACRAICRA | null | null | modulation of sensory perception of pain in another organism [GO:0044465] | extracellular region [GO:0005576]; nematocyst [GO:0042151] | ion channel inhibitor activity [GO:0008200]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729] | PF00014; | 4.10.410.10; | Venom Kunitz-type family, Sea anemone type 2 potassium channel toxin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18579526}. Nematocyst {ECO:0000269|PubMed:18579526}. | null | null | null | null | null | FUNCTION: This protease inhibitor shows two different activities, it inhibits both the capsaicin receptor TRPV1 and serine proteases. It partially (max 50%) and reversibly inhibits capsaicin-induced response of TRPV1 (IC(50)=54 nM), a receptor of the pain pathway (PubMed:18579526, PubMed:24351908). The second activity ... | Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus) |
B2GM84 | ALL21_DERFA | MKFIIFCAIVMAVSVSGFIVDVDTEDKWRNAFDHMLMEEFEEKMDQIEHGLLMLSEQYKELEKTKSKELKEQILRELTIAENYLRGALKFMQQEAKRTDLNMFERYNFETAVSTIEILVKDLAELAKKVKAVKSDD | null | null | null | null | protein homodimerization activity [GO:0042803] | PF11642; | 1.20.58.970; | Mite group 5 allergen family | null | null | null | null | null | null | null | null | Dermatophagoides farinae (American house dust mite) |
B2GUB3 | TTLL3_XENTR | MAHHTAVNPDRLKHAKALVEKAIKQKKIFAIHGPYPVIRSCLRSRGWVEKKFPKSGKAKQKKEKASDEDMEDDDGDGSSNDDDDGENSDEEENGDPDGTCDLMSRLLRNEDPNFFWTTKRDAVDCRFLKKDQMLNHYAKAGSFTTKVGLCLNLRNLHWFDDADPDSFFPRCYRLGAEDEKQSFKEDFWHTAARSILKRVANRRDICSPAATGGAKASHREPGANNGAQLLAKRGSRKRAESVPVQIILTALEACERYLNSLEHNDIDMETEATPAMTDTQWEEFLHGYYQVIHDGATIEHSEYYVDQCSEVLHKLEAVNP... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; microtubule [GO:0005874]; motile cilium [GO:0031514] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28576883}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}. | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:45621... | null | null | null | null | FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (PubMed:28576883). Preferentially... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B2GUT4 | WNT11_XENTR | MKIYFLLGIFLTFLLHTRICQGIKWLALAKTPLSLALNQSQHCKQLEGLVSSQMQLCRSNLELMQTIIHAAKEVKKTCIKAFTDMRWNCSSIELAPTFHQDLERGTRESAFVYALSAAAISHTIARACTTGDIPGCSCAPIPGESPGPGYRWGGCADNLNYGILMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWRGLQELREIALDLKTKYLSATKVVHRPMGTRKQLVPKDIDIRPVQETEMIYLQSSPDYCLKNEKMGSHGTHERQCNKTSNGSDSCDLMCCGRGYNPYM... | null | null | canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell migration involved in gastrulation [GO:0042074]; dorsal fin development [GO:0033337]; embryonic viscerocranium morphogenesis [GO:0048703]; heart looping [GO:0001947]; heart morphogenesis [GO:0003007]; negative regulation of canonical ... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein kinase activator activity [GO:0030295] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Glycosylation is required for protein secretion. {ECO:0000250|UniProtKB:P49893}.; PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q670P5}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N-terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural cres... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B2GUV7 | IF2P_RAT | MGKKQKNKSEDSTKDDTDLGALAAEIEGAGAAKEQEPQKGKGKKKKEKKKQDFDENDILRELEELSLEAQGIGADRDAATVKPTENNEEESASKQDKKKKGQKGKKTSFDENDSEELEDKDSKSKKPARPNSEVLLSGSEDADDPNKLSKKGKKAQKSTKKRDGSEEDEDNSKRSKERSRVNSSGESGGESDEFLQSRKGQKKNQKNKSVPTIDSGNEDDDSSFKIKTVAQKKAEKKERERKKREEEKAKLRKVKEKEELEKGRKEQSKQREPQKRPDEEVLVLRGTPDAGAASEEKGDIAATLEDDNEGDKKKKDKKKK... | 3.6.5.3 | COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250|UniProtKB:G0S8G9}; Note=Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction. {ECO:0000250|UniProt... | regulation of translational initiation [GO:0006446]; ribosome assembly [GO:0042255]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; synapse [GO:0045202] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; translation initiation factor activity [GO:0003743]; tRNA binding [GO:0000049] | PF00009;PF14578;PF11987; | 3.40.50.300;2.40.30.10;3.40.50.10050; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, IF-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; Evidence={ECO:0000250|UniProtKB:O60841}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Plays a role in translation initiation. Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. Together with eIF1A (EIF1AX), actively orie... | Rattus norvegicus (Rat) |
B2GUY0 | MA1B1_RAT | MYPPPPAPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLQVSDQWKALSGSRAEVEKMKLEVLPVLPAPQKESAEPEGFADILSQKRQRHLRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATEPPSKRAEASIKPLFLASRIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKEARKWVSENLDFQKNVDVNLFESTIRILGGLLSAYHLSGDSLFLSKAEDFGNRL... | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; | carbohydrate metabolic process [GO:0005975]; ERAD pathway [GO:0036503]; mannoprotein catabolic process [GO:0006058]; protein glycosylation [GO:0006486] | cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; endosome [GO:0005768]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trim... | Rattus norvegicus (Rat) |
B2GUY1 | PLK4_RAT | MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSESEARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSTKSKDLGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRRLLVGQPLPN... | 2.7.11.21 | null | centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast gi... | centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]; spindle pole [GO:0000922]; XY body [GO:0001741] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB... | 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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpres... | Rattus norvegicus (Rat) |
B2GUZ1 | UBP4_RAT | MAEGRGTHERPDVETQKTELGALMGTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSSKPSASPYSSMSASLIANGDSTNSSGMHNSGVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCL... | 3.4.19.12 | null | negative regulation of protein ubiquitination [GO:0031397]; positive regulation of TORC1 signaling [GO:1904263]; protein deubiquitination [GO:0016579]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647]; spliceosomal tri-snRNP complex assembly [GO:0... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | adenosine receptor binding [GO:0031685]; cysteine-type deubiquitinase activity [GO:0004843]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06337;PF14836;PF00443; | 3.90.70.10;3.30.2230.10; | Peptidase C19 family, USP4 subfamily | PTM: Phosphorylated at Ser-445 by PKB/AKT1 in response to EGF stimulus, promoting its ability deubiquitinate RHEB. {ECO:0000250|UniProtKB:Q13107}.; PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Nucleus {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alph... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q13107}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. Deubiquitinates RHEB in response to EGF signaling, promot... | Rattus norvegicus (Rat) |
B2GV06 | SCOT1_RAT | MAALKLLSSGLRLCASARNSRGALHKGCACYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFRGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGEGKAKSGKPGEDVRERIIKRAALEFEDGMYAN... | 2.8.3.5 | null | adipose tissue development [GO:0060612]; cellular ketone body metabolic process [GO:0046950]; heart development [GO:0007507]; ketone body catabolic process [GO:0046952]; ketone catabolic process [GO:0042182]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; respon... | mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; succinyl-CoA:3-oxo-acid CoA-transferase activity [GO:0008260] | PF01144; | 3.40.1080.10; | 3-oxoacid CoA-transferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19343716}. | CATALYTIC ACTIVITY: Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate; Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973, ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5; Evidence={ECO:0000250|UniProtKB:P55809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565; Evidence={ECO:0000250... | null | PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P55809}. | null | null | FUNCTION: Key enzyme for ketone body catabolism. Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further... | Rattus norvegicus (Rat) |
B2GV17 | CBPC5_RAT | MELRCGGLLFSSRFDSGNLAHVEKVETVPSDGEGVGGAATAPTSGSASSPDYEFNVWTRPDCAETEYENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPSRPRWERIRERPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLSQLDQRFPENYSAHSSPLDSIYYHRELLCYSLDGLRVDLLTITSCHGLRDDREPRLEQLFPDVGTPRPFRFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDA... | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed. Colocalizes with alpha-tubuli... | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=le... | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tu... | Rattus norvegicus (Rat) |
B2GV24 | UFL1_RAT | MADAWEEIRRLAADFQRAQFAESTQRLSERNCIEIVNKLISQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLTHIENRVGDIIKSEKHVQMVLGQLVDENYLDRLSEEVNDKLQESGQVTVSELCKTYDLPGDFLTQALTQRLGRIINGHLDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLVSKYGFQEQLLYSVLEELVSTGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVNYIKKRYKNTPLLFLKATCVGQGLVDQVEASVEEAISSG... | 2.3.2.- | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of apoptotic process [GO:0043066]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation o... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of double-strand break [GO:0035861] | protein kinase binding [GO:0019901]; UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568] | PF09743; | null | UFL1 family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome. {ECO:0000250|UniProtKB:O94874}.; PTM: Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and promoting ATM activation in a positi... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20531390}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O94874}. Nucleus {ECO:0000250|UniProtKB:O94874}. Chromosome {ECO:0000250|UniProtKB:O94874}. Note=Recruited to double-strand breaks by the MRE11-RAD50-NBN (MRN) complex following DNA damage. {ECO... | null | null | null | null | null | FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. In response to endoplasmic reticulum stress, re... | Rattus norvegicus (Rat) |
B2GV46 | FFAR3_RAT | MDTSFFPGNHWLFFSVDLLVFLVGLPLNVMALVVFVNKLRRRPVAVDLLLLNLTISDLLLLLFLPFRIVEAACGMKWILPFIFCPLSGFLFFTTIYLTSLFLMTVSIERFLSVAYPLWYKTRPRLAQAGLVSGICWFLASAHCSVIYVTEYWGNATYSQGTNGTCYLEFREDQLAILLPVRLEMAVVLFMVPLCITSYCYSRLVWILSQGASRRRRKRVMGLLVATLLIFFVCFGPYNMSHVVGYVRGESPTWRSYVLLLSTLNSCIDPLVFYFSSSKFQADFHQLLSRLIRACVPWTQEVSLELKVKNGEEPSKECPS | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to fatty acid [GO:0071398]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; inflammatory response [GO:0006954]; mucosal immune response [GO:0002385]; negative regulation... | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyr... | Rattus norvegicus (Rat) |
B2GV50 | RFX2_RAT | MQNSEGGADSPATVALRPAAQPVPASPQRVLVQAAGSTPKGTPMQTLTLPRVQPVPPQVQHVYPAQVQYVEGGDAVYANGAIRAAYTYNPDPQLYAPSSAASYFETPGGAQVTVAASSPPAVPSHGMVGITMDVSGTPIVSGAGTYLIHGGMDSTRHSLAHTARSSPATLQWLLDNYETAEGVSLPRSSLYNHYLRHCQEHKLEPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRLQEDTQYMAMRQQPTHQKPRYRPAQKSDSLGDGSAHSNMHSTPEQAMAAQGQHHQQYIDVSHVFPEFPAP... | null | null | acrosome assembly [GO:0001675]; cellular response to leukemia inhibitory factor [GO:1990830]; cilium assembly [GO:0060271]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatid development [GO:0007286] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polym... | PF04589;PF02257; | 1.10.10.10; | RFX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:16676351}. Cytoplasm {ECO:0000269|PubMed:16676351}. Note=Mainly expressed in the nucleus and at lower level in cytoplasm. {ECO:0000269|PubMed:16676351}. | null | null | null | null | null | FUNCTION: Transcription factor that acts as a key regulator of spermatogenesis (By similarity). Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (By similarity). Recognizes and binds the X-box, a regulatory motif with DN... | Rattus norvegicus (Rat) |
B2GV72 | CRB3_RAT | MSSCSRVALVTGANKGIGFAITRDLCRKFSGDVVLTARDEARGRAAVKQLQAEGLSPRFHQLDIDNPQSIRALRDFLRKEYGGLNVLVNNAGIAFRMDDPTPFDVQAEVTLKTNFFATRNVCTELLPIMKPHGRVVNVSSLQGLKALENCSEDLQERFRCDTLTEGDLVDLMKKFVEDTKNEVHEREGWPDSAYGVSKLGVTVLTRILARQLDEKRKADRILLNACCPGWVKTDMARDQGSRTVEEGAETPVYLALLPPDATEPHGQLVRDKVVQTW | 1.1.1.184; 1.6.5.10 | null | cognition [GO:0050890]; phylloquinone catabolic process [GO:0042376] | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | 3-keto sterol reductase activity [GO:0000253]; carbonyl reductase (NADPH) activity [GO:0004090]; NADPH binding [GO:0070402]; NADPH dehydrogenase (quinone) activity [GO:0008753] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75828}. | CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:18983987}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259; Evi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 nM for 4-benzoylpyridine {ECO:0000269|PubMed:18983987}; Note=kcat is 14 min(-1) with 4-benzoylpyridine as substrate (PubMed:18983987). kcat is 0.030 min(-1) with menadione as substrate (PubMed:18983987). {ECO:0000269|PubMed:18983987}; | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity (PubMed:18983987). Acts on several orthoquinones, as well as on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2... | Rattus norvegicus (Rat) |
B2GV87 | PTPRE_RAT | MEPFCPLLLASFSLSLATAGQGNDTTPTESNWTSTTAGPPDPGTSQPLLTWLLLPLLLLLFLLAAYFFRFRKQRKAVVNSNDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK... | 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of insulin receptor signaling pathway [GO:0046627]; regulation of mast cell activation [GO:0033003]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 4 subfamily | PTM: A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3. {ECO:0000250}.; PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}. Note=Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin can induce translocation to the membrane ... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity). Acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism... | Rattus norvegicus (Rat) |
B2HIL7 | MSL7_MYCMM | MTTSGESADQQNDKLFRYLKKVAVELDEARARLREYEQRATEPVAVVGIGCRFPGGADGPEGLWDLVSQGRDAVTEFPNDRGWDTEGLFDPDPDAEGKTYTRWGAFVENATNFDAGFFGIPPSEVLAMDPQQRLMLEVSWEALEHAGIDPMSLRGSSTGVFTGIFAPSYGGKDVGALQGYGLTGSPVSVASGRVAYVLGLEGPALSVDTACSSSLVAIHWAMASLRSGECDMALAGGVTVMGLPSIFVGFSRQRGLAADGRCKAFAAAADGTGWGEGAGVLVLERLSDAQRNGHNVLAVVRGSAINQDGASNGLTAPNGL... | 2.3.1.41 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000250}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000250}; | Actinobacterium-type cell wall biogenesis [GO:0071766]; DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610] | plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.30.70.3290;3.40.47.10;6.10.40.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family | null | null | CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:C... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). {ECO:0000269|PubMed... | Mycobacterium marinum (strain ATCC BAA-535 / M) |
B2HN69 | CAR_MYCMM | MSPITREERLERRIQDLYANDPQFAAAKPATAITAAIERPGLPLPQIIETVMTGYADRPALAQRSVEFVTDAGTGHTTLRLLPHFETISYGELWDRISALADVLSTEQTVKPGDRVCLLGFNSVDYATIDMTLARLGAVAVPLQTSAAITQLQPIVAETQPTMIAASVDALADATELALSGQTATRVLVFDHHRQVDAHRAAVESARERLAGSAVVETLAEAIARGDVPRGASAGSAPGTDVSDDSLALLIYTSGSTGAPKGAMYPRRNVATFWRKRTWFEGGYEPSITLNFMPMSHVMGRQILYGTLCNGGTAYFVAKS... | 1.2.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000305|PubMed:23248280}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000305|PubMed:23248280}; | organonitrogen compound biosynthetic process [GO:1901566] | membrane [GO:0016020] | ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor [GO:0016620]; phosphopantetheine binding [GO:0031177] | PF00501;PF07993;PF00550; | 1.10.1200.10;3.40.50.12780;3.40.50.720; | ATP-dependent AMP-binding enzyme family, Carboxylic acid reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde + diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=362 uM for benzoate {ECO:0000269|PubMed:23248280}; KM=48 uM for NADPH {ECO:0000269|PubMed:23248280}; KM=115 uM for ATP {ECO:0000269|PubMed:23248280}; Vmax=2.32 umol/min/mg enzyme with benzoate as substrate {ECO:0000269|PubMed:23248280}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23248280}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Displays in vitro half-lives of 73, 70, and 48 hours at 26, 30, and 37 degrees Celsius, respectively, indicating it is a relatively stable enzyme. {ECO:0000269|PubMed:23248280}; | FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (PubMed:23248280). Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as... | Mycobacterium marinum (strain ATCC BAA-535 / M) |
B2IZD3 | BDLP_NOSP7 | MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLN... | 3.6.5.5 | null | mitochondrial fusion [GO:0008053] | plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289] | PF21808;PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:17122778}; Peripheral membrane protein {ECO:0000305|PubMed:17122778}. Note=Probably inserts into the outer leaflet of the membrane only (Probable). Forms foci localized in the cell periphery, and occasionally in the cell interior. {ECO:0000305|PubMed:2006437... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:17122778}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=68.6 uM for GTP {ECO:0000269|PubMed:17122778}; Note=kcat is 0.53 min(-1). {ECO:0000269|PubMed:17122778}; | null | null | null | FUNCTION: Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bi... | Nostoc punctiforme (strain ATCC 29133 / PCC 73102) |
B2J528 | PAL_NOSP7 | MNITSLQQNITRSWQIPFTNSSDSIVTVGDRNLTIDEVVNVARHGTQVRLTDNADVIRGVQASCDYINNAVETAQPIYGVTSGFGGMADVVISREQAAELQTNLIWFLKSGAGNKLSLADVRAAMLLRANSHLYGASGIRLELIQRIETFLNAGVTPHVYEFGSIGASGDLVPLSYITGALIGLDPSFTVDFDGKEMDAVTALSRLGLPKLQLQPKEGLAMMNGTSVMTGIAANCVYDAKVLLALTMGVHALAIQGLYGTNQSFHPFIHQCKPHPGQLWTADQMFSLLKDSSLVREELDGKHEYRGKDLIQDRYSLRCLA... | 4.3.1.24 | null | aromatic amino acid metabolic process [GO:0009072]; cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559]; phenylpropanoid biosynthetic process [GO:0009699]; protein homotetramerization [GO:0051289] | cytoplasm [GO:0005737] | phenylalanine ammonia-lyase activity [GO:0045548] | PF00221; | 1.20.200.10;1.10.275.10; | PAL/histidase family | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000269|PubMed:17240984}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.24; Evidence={ECO:0000269|PubMed:17240984}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.045 mM for phenylalanine {ECO:0000269|PubMed:17240984}; Note=kcat is 1.96 sec(-1) for phenylalanine. {ECO:0000269|PubMed:17240984}; | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.7-8.5. {ECO:0000269|PubMed:17240984}; | null | FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway. {ECO:0000269|PubMed:17240984}. | Nostoc punctiforme (strain ATCC 29133 / PCC 73102) |
B2KF05 | BRPF3_MOUSE | MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPAKSKKPSSKGKRKESCSKHASGTSFHLPQPSFRVVDTGSQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDIAWLDMVNEKRRADGHSSVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCVLCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPAR... | null | null | positive regulation of DNA replication [GO:0045740]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357] | histone acetyltransferase complex [GO:0000123]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleus [GO:0005634] | histone H3K14 acetyltransferase activity [GO:0036408]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K5 acetyltransferase activity [GO:0043995]; histone H4K8 acetyltransferase activity [GO:0043996]; metal ion binding [GO:0046872] | PF00439;PF10513;PF13831;PF00855;PF13832; | 2.30.30.140;1.20.920.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULD4}. | null | null | null | null | null | FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity. Plays a role in DNA replication initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby facilitat... | Mus musculus (Mouse) |
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